TITLE: Transgenic Animals
PUBLICATION DATE: June, 1994
ENTRY DATE: June, 1994
EXPIRATION DATE: None
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Transgenic Animals
January 1991 - February 1994
QB 94-34
Quick Bibliographies
Raymond Dobert
Transgenic Animals
SEARCH STRATEGY
SET ITEMS DESCRIPTION
S150739 ANIMAL?/TI,DE
S2 407317 SH=L? OR SH=S100
S3419691 S1 OR S2
S42168 TRANSGEN?
S54256 (GENETIC OR GENE)(W)(TRANSFORMATION OR
TRANSFER)/TI,DE
S65241 S4 OR S5
S7823S3 AND S6
S8577 S7 NOT (DROSOPHILA OR COLI)
S9 264 S8 AND PY=1991:9999
S10 261 S9/ENG
1 NAL Call. No.: QR360.J6
Activator-dependent and activator-independent defective recombinant
retroviruses from bovine leukemia virus.
Milan, D.; Nicolas, J.F.
Washington, D.C. : American Society for Microbiology; 1991 Apr.
Journal of virology v. 65 (4): p. 1938-1945; 1991 Apr. Includes
references.
Language: English
Descriptors: Bovine oncovirus; Retroviral vectors; Gene transfer;
Recombinant
DNA; Gene expression; Reporter genes; Dna; Beta-galactosidase;
Enzyme
activity; Transfection; Host range; Cell lines; Sheep; Fowls;
Mammals
Abstract: The replication-competent bovine leukemia virus (BLV)
has been
modified for use as a vector for foreign genes. The gag, pol, env,
and pX
regions of the virus were replaced by an exogenous nuclear location
signal
LacZ (nlsLacZ) or SVnlsLacZ gene. Transfection of the ovine cell
line FLK-BLV,
which expresses all BLV proteins from a wild-type provirus, with
this viral
DNA resulted in a viral titer of 10(4) CFU/ml. The inclusion of a
large
portion of the gag region did not significantly increase the titer.
Both
activator-dependent and activator-independent retroviruses were
constructed.
In activator-dependent vectors, the expression of the insert was
dependent on
the presence of the Tax protein, which activated the BLV long
terminal repeat.
In activator-independent vectors, the expression of the insert was
constitutive because of the presence of an internal promoter.
Infections with
the recombinant retrovirus were inhibited by specific neutralizing
antibodies.
The structure of the transduced genetic material was not
rearranged. BLV
vectors encoding a reporter nlsLacZ gene, the product of which can
be detected
in single cells, greatly simplified studies of their biological
properties.
Determination of the host range of BLV vectors established that
BLV-based
recombinant retroviruses are effective in the transduction of genes
in a
variety of species and cell types.
2 NAL Call. No.: TX341.F662
Alteration of carcass composition in transgenic swine.
Pursel, V.G.; Solomon, M.B.
New York, N.Y. : Marcel Dekker, c1985-; 1993.
Food reviews international v. 9 (3): p. 423-439; 1993. Presented
at a
symposium on "Novel Production Practices and Food Quality," Nov.
15-18, 1992,
The Hague, The Netherlands. Includes references.
Language: English
Descriptors: Pigs; Genetic engineering; Transgenics; Carcass
composition;
Modification; Literature reviews
3 NAL Call. No.: 100 IL64
Animal and plant transformation: the application of transgenic
organisms in
agriculture.
Wheeler, M.B.; Farrand, S.K.; Widholm, J.M.
Urbana, Ill. : The Station; 1991.
Illinois research - Illinois Agricultural Experiment Station v. 33
(1/2): p.
20-22; 1991.
Language: English
Descriptors: Illinois; Animals; Plants; Transgenics
4 NAL Call. No.: 1.90 C2OU8
Animal biotechnology on the horizon.
Rexroad, C.E. Jr
Washington, D.C. : U.S. Dept. of Agriculture; 1993 Mar.
Outlook. p. 644-651; 1993 Mar. Paper presented at the conference
"Agriculture's changing horizon," December 1-3, 1992, Washington,
DC.
Includes references.
Language: English
Descriptors: Biotechnology; Transgenic animals
5 NAL Call. No.: TA166.T72
Animal genetics--of pigs, oncomice and men.
Webster, J.
New York, N.Y. : Elsevier Science Publishing Co; 1993 Jan.
Trends in biotechnology v. 11 (1): p. 1-2; 1993 Jan.
Language: English
Descriptors: Pigs; Transgenics; Biotechnology; Animal welfare
6 NAL Call. No.: 284.28 W15
Animals altered to make drugs in their milk.
Stipp, D.
New York, N.Y. : Dow Jones; 1991 Aug27.
The Wall Street journal. p. B1, B5; 1991 Aug27.
Language: English
Descriptors: Animal products; Proteins; Genetic engineering;
Biological
production; Transgenics
7 NAL Call. No.: A00064
Animals altered to make medicinal proteins.
Haney, D.Q.
Charlotte, N.C. : Observer Co; 1991 Aug27.
The Charlotte observer. p. 2A; 1991 Aug27.
Language: English
Descriptors: Transgenics; Proteins; Biological production
8 NAL Call. No.: 442.8 J8222
Assessment of functional gametes in chickens after transfer of
primordial germ
cells.
Petitte, J.N.; Clark, M.E.; Etches, R.J.
Colchester : The Journal; 1991 May.
Journal of reproduction and fertility v. 92 (1): p. 225-229; 1991
May.
Includes references.
Language: English
Descriptors: Fowls; Gametes; Germ cells; Embryos; Germ line;
Transfer;
Transgenics; Genotypes
9 NAL Call. No.: QP251.M64
Association of exogenous DNA with cattle and insect spermatozoa in
vitro.
Atkinson, P.W.; Hines, E.R.; Beaton, S.; Matthaei, K.I.; Reed,
K.C.; Bradley,
M.P.
New York, N.Y. : Wiley-Liss, Inc; 1991 May.
Molecular reproduction and development v. 29 (1): p. 1-5; 1991 May.
Includes
references.
Language: English
Descriptors: Cattle; Lucilia cuprina; Apis mellifera; Spermatozoa;
Dna;
Uptake; Binding; Vectors; Genetic transformation
10 NAL Call. No.: 41.8 C163
An attempt at sperm-mediated gene transfer in mice and chickens.
Gavora, J.S.; Benkel, B.; Sasada, H.; Cantwell, W.J.; Fiser, P.;
Teather,
R.M.; Nagai, J.; Sabour, M.P.
Ottawa : Agricultural Institute of Canada; 1991 Jun.
Canadian journal of animal science v. 71 (2): p. 287-291; 1991 Jun.
Includes
references.
Language: English
Descriptors: Fowls; Mice; Gene transfer; Spermatozoa; Genetic
transformation;
Transgenics; Artificial insemination; Fertilization
11 NAL Call. No.: aT223.V4A4
Avian herpesvirus amplicon as a eucaryotic expression vector.
Carter, J.K.; Silva, R.F.
Washington, D.C.? : The Department; 1991 Feb26.
United States Department of Agriculture patents (4,996,152): 1 p.;
1991 Feb26.
Copies of USDA patents are available for a fee from the
Commissioner of
Patents and Trademarks, U.S. Patents and Trademarks Office,
Washington, D.C.
20231. Includes references.
Language: English
Descriptors: U.S.A.; Poultry diseases; Marek's disease virus; Avian
herpesvirus; Dna amplification; Vectors; Gene transfer; Gene
expression;
Genes; Animal breeding; Usda; Patents
Abstract: DNA fragments (seeds) having the characteristics of
amplicons,
which are useful for amplifying genes of interest, have been
isolated from
Marek's disease viruses of poultry. Concatmers of the seeds and the
associated
genes have potential as vaccines or delivery vectors when
cotransfected and
replicated in the presence of helper viruses. The amplicons are
also useful
for inserting associated genes into the helper viruses, which in
turn could be
used as expression vectors. Candidate genes for use with the
subject amplicons
include those which encode immunogenic proteins and other
beneficial economic
traits desired in commercial poultry lines.
12 NAL Call. No.: SF492.M36 1993
Avian leukosis retroviruses and gene transfer into the avian
genome.
Salter, D.W.; Payne W.S.; Crittenden, L.B.; Federspiel, M.J.;
Petropoulos,
C.J.; Bradac, J.A.; Hughes, S.
Boca Raton : CRC Press; 1993.
Manipulation of the avian genome / edited by Robert J. Etches, Ann
M.
Verrinder Gibbins. p. 135-150; 1993. Includes references.
Language: English
Descriptors: Chickens; Avian oncovirus; Gene transfer; Germ line
13 NAL Call. No.: QR360.J6
An avian retrovirus expressing chicken pp59(c-myc) possesses weak
transforming
activity distinct from v-myc that may be modulated by adjacent
normal cell
neighbors.
Filardo, E.J.; Humphries, E.H.
Washington, D.C. : American Society for Microbiology; 1991 Dec.
Journal of virology v. 65 (12): p. 6621-6629; 1991 Dec. Includes
references.
Language: English
Descriptors: Fowls; Avian oncovirus; Gene expression; Oncogenes;
Genetic
transformation; Fibroblasts; Quails
Abstract: We demonstrate that EF168, an avian retrovirus that
expresses the
chicken pp59c-myc proto-oncogene, transforms quail embryo
fibroblasts in
vitro. An EF168-transformed quail clone, EF168-28, containing a
single
provirus, synthesizes several hundred copies of c-myc RNA and
expresses
elevated levels of the pp59c-myc gene product. The EF168 provirus
in EF168-28
was isolated as a molecular clone, and the nucleotide sequence of
its c-myc
allele was confirmed as identical to that of exons 2 and 3 of the
chicken
c-myc proto-oncogene. Extended infection of quail embryo fibroblast
cultures
with EF168 induced a number of in vitro transformation-associated
parameters
similar to those elicited by the oncogenic v-myc-encoding
retrovirus MC29,
including alteration of cellular morphology, anchorage-independent
growth, and
induction of immortalized cell lines. Despite the fact that EF168
and MC29
shared these biological activities, further analysis revealed that
EF168
initiated transformation in quail embryo fibroblasts, bone marrow,
or adherent
peripheral blood cultures 100- to 1,000-fold less efficiently than
did MC29.
Further, in contrast to MC29-induced foci, EF168 foci were smaller,
morphologically diffuse, and less prominent. Analysis of newly
infected cells
demonstrated efficient expression of EF168 viral RNA in the absence
of
transformation. These differences suggest that while the pp59v-myc
gene
product can exert dominant transforming activity on quail embryo
fibroblasts,
its ability to initiate transformation is distinct from that of the
pp110gag-v-myc gene product encoded by MC29 and may be suppressed
by adjacent
nontransformed cell neighbors.
14 NAL Call. No.: 1 AG84Y Barnyard biotechnology may soon produce new medical therapeutics. Purcel, V.G.; Rexroad, C.E. Jr; Wall, R.J. Washington, D.C. : U.S. Department of Agriculture; 1992. The ... Yearbook of agriculture. p. 189-193; 1992.
Language: English
Descriptors: U.S.A.; Biotechnology; Transgenics; Medical research;
Proteins;
Mammary glands; Bioreactors; Animals; Hemoglobin
15 NAL Call. No.: 442.8 J8222 SUPPL.
Basic techniques for transgenesis.
Wilmut, I.; Clark, A.J.
Cambridge, U.K. : The Journals of Reproduction and Fertility Ltd;
1991.
Journal of reproduction and fertility: Supplement (43): p. 265-275;
1991. In
the series analytic: Reproduction in domestic ruminants II / edited
by G.E.
Lamming, A.P.F. Flint, B.J. Weir. Proceedings of a symposium held
March 1990,
Nice, France. Includes references.
Language: English
Descriptors: Transgenics; Gene transfer; Gene expression
16 NAL Call. No.: SF140.B54A55
The binding of exogenous DNA fragments to bovine spermatozoa.
Bird, J.M.; Powell, R.; Horan, R.; Gannon, F.; Houghton, J.A.
New York, N.Y. : Marcel Dekker; 1992.
Animal biotechnology v. 3 (2): p. 181-200; 1992. Includes
references.
Language: English
Descriptors: Cattle; Spermatozoa; Gene transfer
17 NAL Call. No.: SB925.B5
Biological control of arthropods: genetic engineering and
environmental risks.
Hoy, M.A.
Orlando, Fla. : Academic Press; 1992 Jun.
Biological control v. 2 (2): p. 166-170; 1992 Jun. Literature
review.
Includes references.
Language: English
Descriptors: Arthropod pests; Biological control; Insect control;
Natural
enemies; Research; Genetic engineering; Transgenics; Genetic
improvement;
Risk; Literature reviews
18 NAL Call. No.: QH585.A1I58
Bovine cell lines for collaborative gene mapping studies.
Troyer, D.; Hertzke, D.
Columbia, Md. : The Association; 1991 Jun.
In vitro cellular & development biology : journal of the Tissue
Culture
Association v. 27A (6): p. 435-438; 1991 Jun. Includes references.
Language: English
Descriptors: Cattle; Genetic transformation; Fibroblasts; Cell
lines;
Plasmids; Reporter genes; Phosphotransferases; Simian polyomavirus;
Genes; Dna
binding proteins; Gene mapping; Marker genes
19 NAL Call. No.: ViBlbVLD5655.V856 1992.S6715
Bovine embryo microinjection, culture, microsurgery, and DNA
analysis by the
polymerase chain reaction technique.
Sparks, Amy Elizabeth Thuemmel,
1992; 1992.
x, 146 leaves : ill. ; 28 cm. Vita. Abstract. Bibliography:
leaves 135-143.
Language: English
Descriptors: Cattle; Transgenic animals; Gene amplification
20 NAL Call. No.: QR360.J6
The bovine papillomavirus constitutive enhancer is essential for
viral
transformation, DNA replication, and the maintenance of latency.
Vande Pol, S.B.; Howley, P.M.
Washington, D.C. : American Society for Microbiology; 1992 Apr.
Journal of virology v. 66 (4): p. 2346-2358; 1992 Apr. Includes
references.
Language: English
Descriptors: Bovine papillomavirus; Genetic transformation; Dna
replication;
Transcription
Abstract: Bovine papillomavirus type 1 (BPV-1) has served as the
prototype
papillomavirus for the study of viral transcription, DNA
replication, and
latency. However, no cis essential transcription control regions
which are
necessary for both transformation and replication of BPV-1 or any
other
papillomavirus have yet been defined. We have found that BPV-1
mutants with
deletions in the long control region were defective for
transformation and
replication, with the essential region in the 5' long control
region
corresponding to the previously defined BPV-1 constitutive enhancer
(S.B.
Vande Pol and P.M. Howley, J. Virol. 64:5420-5429, 1990). BPV-1
mutants
deleted of the constitutive enhancer could be complemented in trans
by the
full-length virally encoded E2 transactivator and replication
factor (E2TA)
and in cis by the simian virus 40 enhancer. The constitutive
enhancer induced
the production of E2TA by activating all the major viral early
promoters
upstream of the E2 open reading frame. Complementation experiments
using a
temperature-sensitive E2TA mutant indicated that the constitutive
enhancer was
necessary for the maintenance of viral DNA replication within
latently
infected cells and implied that viral transcription under the
regulation of
the constitutive enhancer may be controlled during the cell cycle.
The
constitutive enhancer is a master regulatory control region for
establishing
and maintaining BPV-1 latency, and its characteristics reveal some
analogies
with cell type-specific enhancer elements recognized in the human
papillomaviruses.
21 NAL Call. No.: QP251.A1T5
Bovine spermatozoa in vitro: a review of storage, fertility
estimation and
manipulation.
Coulter, G.H.
Stoneham, Mass. : Butterworth-Heinemann; 1992 Aug.
Theriogenology v. 38 (2): p. 197-207; 1992 Aug. Paper presented at
the
research symposium on "Reproduction in Farm Animals: Science,
Application and
Models," August 13, 1992, Ithaca, New York. Includes a list of his
publications. Literature review. Includes references.
Language: English
Descriptors: Cattle; Spermatozoa; Semen characters; Semen
preservation; Male
fertility; Ai bulls; In vitro; Literature reviews
Abstract: In vitro storage of bovine spermatozoa virtually
indefinitely has
provided the opportunity to distribute conveniently and widely germ
plasm from
superior sires and benefit the productivity of cattle around the
world.
Techniques developed in our laboratories are well on their way to
being able
to predict accurately the fertility of young, prospective sires
without the
inconvenience and expense of large field trials. Manipulation of
spermatozoa
provides opportunities for the predetermination of sex of resulting
offspring,
the introduction of foreign DNA into oocytes, and the formation of
transgenic
individuals. Many other possibilities are limited only by the
ingenuity of
those conducting research in this exciting field.
22 NAL Call. No.: HV4701.A35
Brave new animals: the genetic engineering of the animal kingdom.
Kimbrell, A.
Englewood, Colo. : American Humane Association, Animal Protection
Division;
1993.
Advocate v. 11 (2): p. 6-9; 1993.
Language: English
Descriptors: Transgenic animals; Genetic engineering
23 NAL Call. No.: 389.9 N953
Breeding and transgenesis as means of decreasing adiposity in farm
animal
species: practice and promise.
Griffin, H.D.; Cameron, N.D.; Bulfield, G.
Cambridge : Cambridge University Press; 1992 Dec.
Proceedings of the Nutrition Society v. 51 (3): p. 441-446; 1992
Dec.
Presented at a symposium on "The manipulation of adiposity" held
April 2-3,
1992 at Craigie College of Education, Ayr, Scotland. Includes
references.
Language: English
Descriptors: Meat animals; Obesity; Carcass composition; Control;
Animal
breeding; Transgenics
24 NAL Call. No.: S1.S68
Cell culture from lung tissue of transgenic rabbit-producer of
bovine growth
hormone.
Musienko, M.I.; Makarevich, A.V.; Ernst, L.K.; Gol'dman, I.L.;
D'yakonov,
L.P.; Strel'chenko, N.S.; Semenova, V.A.; Smirnov, O.K.; Matveev,
V.A.
New York, N.Y. : Allerton Press; 1991.
Soviet agricultural sciences (1): p. 33-36; 1991. Translated from:
Vsesoiuznaia akademiia sel'skokhoziaistvennykh nauk. Doklady, (1),
1991, p.
32-35. (20 AK1). Includes references.
Language: English; Russian
Descriptors: Rabbits; Transgenics; Lungs; Animal tissues; Cell
culture;
Bovidae; Somatotropin; Transfer; Biotechnology; Genetic engineering
25 NAL Call. No.: QR360.A1J6
Cell transformation by animal papillomaviruses.
Saveria Campo, M.
Reading : Society for General Microbiology; 1992 Feb.
The Journal of general virology v. 73 (pt.2): p. 217-222; 1992 Feb.
Literature review. Includes references.
Language: English
Descriptors: Cattle; Rabbits; Monkeys; Bovine papillomavirus;
Rabbit
papillomavirus; Cells; Transformation; Genetic transformation;
Literature
reviews
26 NAL Call. No.: 47.8 AM33P
Characterization and comparison of avian and murine helper cell
lines for
production replication-defective retroviruses for avian
transformation.
Highkin, M.K.; Krivi, G.G.; Hippenmeyer, P.J.
Champaign, Ill. : Poultry Science Association; 1991 Apr.
Poultry science v. 70 (4): p. 970-981; 1991 Apr. Includes
references.
Language: English
Descriptors: Cell lines; Avian oncovirus; Genetic transformation;
Retroviral
vectors; Plasmids; Transfection; Efficiency; Fowls
Abstract: Several approaches were taken to identify improved
helper cell
lines for the production of replication-defective avian retroviral
vectors for
avian transformation. Both QT6 and D17 cells were engineered to
become helper
cell lines for the production of reticuloendotheliosis virus
vectors. The
results showed that the majority of fines from the D17, QT6, and
D17C3 cells
produced titers in the 10(2) to 10(3) cfu/mL range, with one QT6
line
producing 10(5) cfu/mL. This high producer line was relatively free
of helper
virus when restricted to low passage. An amphotropic murine cell
line produced
a 6- to 10-fold higher amount of virus and had a comparable higher
titer on
chicken cells, suggesting possible application to avian
transformation.
27 NAL Call. No.: 47.8 AM33P
Chimeric chickens and their use in manipulation of the chicken
genome.
Etches, R.J.; Carsience, R.S.; Clark, M.E.; Fraser, R.A.; Toner,
A.; Verrinder
Gibbins, A.M.
Champaign, Ill. : Poultry Science Association; 1993 May.
Poultry science v. 72 (5): p. 882-889; 1993 May. Paper presented
at the
symposium "Current Advances in Reproduction", August 3, 1992 at the
81st
Annual Meeting of the Poultry Science Association. Includes
references.
Language: English
Descriptors: Chickens; Chimeras; Transgenics; Genetic engineering
Abstract: Germline chimeric chickens can be made by injecting
dispersed cells
from Stage X blastoderms into recipient embryos at an equivalent
stage of
development. Colonization of the chimera by donor-derived cells is
facilitated
when the recipient embryo is compromised by exposure to irradiation
prior to
injection of the donor cells. Donor cells can be genetically
manipulated by
lipofection-mediated gene transfer before they are introduced into
the
recipient. The genetic modification is expressed in the ectoderm,
mesoderm,
and endoderm of the chimera after incubation for 96 h. Donor cells
can also be
cultured as dispersed cells in a monolayer or as whole-embryo
explants for at
least 48 h before transfer into recipients and retain the ability
to enter
both somatic and germline tissues in the resulting chimera. A
strategy is
proposed for the production of transgenic chickens using
lipofection-mediated
gene transfer to blastoderm cells isolated from Stage X embryos,
which are
subsequently injected into compromised recipients to yield a
germline chimera.
28 NAL Call. No.: SF492.M36 1993
CHox-cad characterization and rooster sperm perservation as a first
step in
the generation of transgenic chickens with modified homeobox genes.
Greunbaum, Y.; Frumkin, A.; Rangini, Z.; Revel, E.; Yarus, S.;
Margalit, Y.;
Khatib, H.; Darvsi, A.; Fainsod, A.
Boca Raton : CRC Press; 1993.
Manipulation of the avian genome / edited by Robert J. Etches, Ann
M.
Verrinder Gibbins. p. 151-164; 1993. Includes references.
Language: English
Descriptors: Chickens; Transgenics; Genetic engineering
29 NAL Call. No.: QH442.A1G4
Cloning of the goat beta-casein-encoding gene and expression in
transgenic
mice.
Roberts, B.; DiTullio, P.; Vitale, J.; Hehir, K.; Gordon, K.
Amsterdam : Elsevier Science Publishers; 1992.
Gene v. 121 (2): p. 255-262; 1992. Includes references.
Language: English
Descriptors: Goats; Mice; Transgenics; Genetic transformation;
Structural
genes; Beta-casein; Nucleotide sequences; Cloning; Gene transfer;
Gene
expression; Introns; Exons; Mammary glands; Amino acid sequences
Abstract: The goat beta-casein-encoding gene (CSN2), which encodes
the most
abundant protein of goat milk, has been cloned and sequenced. The
intron/exon
organization of the 9.0-kb goat CSN2 gene is similar to that of
other CSN2
genes. Expression of the goat gene was principally restricted to
the mammary
gland of lactating transgenic animals. A low level of expression
was also
observed in skeletal muscle and skin. In contrast to a rat CSN2
transgene [Lee
et al., Nucleic Acids Res. 16 (1988) 1027-1041], the goat gene was
expressed
to a high degree in the lactating mammary gland. Differences in the
content or
context of regulatory elements may account for the enhanced
performance of the
goat relative to the rat CSN2 gene in transgenic mice.
30 NAL Call. No.: BJ52.5.J68
The concept of intrinsic value and transgenic animals.
Verhoog, H.
Guelph, Ontario, Canada : University of Guelph; 1992.
Journal of agricultural & environmental ethics v. 5 (2): p.
147-160; 1992.
Includes references.
Language: English
Descriptors: Transgenics; Animal breeding; Genetic engineering;
Animal
welfare; Ethics
31 NAL Call. No.: QR360.J6
Conserved functional organization of the human immunodeficiency
virus type 1
and visna virus Rev proteins.
Tiley, L.S.; Malim, M.H.; Cullen, B.R.
Washington, D.C. : American Society for Microbiology; 1991 Jul.
Journal of virology v. 65 (7): p. 3877-3881; 1991 Jul. Includes
references.
Language: English
Descriptors: Visna maedi virus; Human immunodeficiency virus; Viral
proteins;
Amino acid sequences; Induced mutations; Hybrids; Chimeras; Binding
site; Gene
expression; Genetic regulation
Abstract: Visna virus encodes a posttranscriptional regulatory
protein that
is functionally analogous to the Rev trans activator of human
immunodeficiency
virus type 1. Here, we demonstrate that the known functional
organization of
the human immunodeficiency virus type 1 Rev trans activator is
shared by the
distantly related visna virus Rev protein. In particular, both Rev
proteins
contain an N-terminal domain marked by a highly basic core motif
that
determines RNA sequence specificity, as well as a second C-terminal
domain
containing an essential leucine-rich motif that functions as an
activation
domain. Chimeric proteins consisting of the binding domain of one
Rev protein
fused to the activation domain of the other were fully functional
in the viral
sequence context cognate for the binding domain. We also describe
derivatives
of visna virus Rev bearing a defective activation domain that
displayed a
trans-dominant negative phenotype in transfected cells. These visna
virus Rev
mutants may prove useful in the derivation of transgenic animals
resistant to
this agriculturally important retroviral pathogen.
32 NAL Call. No.: 443.8 H42
The control of insect-borne diseases through recombinant DNA
technology.
Eggleston, P.
Oxford : Blackwell Scientific Publications; 1991 Apr.
Heredity v. 66 (pt.2): p. 161-172; 1991 Apr. Includes references.
Language: English
Descriptors: Aedes aegypti; Genetic control; Genetic
transformation;
Transgenics; Transposable elements; Recombinant DNA; Genetic
engineering;
Genomes; Disease control; Mosquito-borne diseases
33 NAL Call. No.: ViBlbVLD5655.V856 1992.D539
Correlation of predicted breeding values across environments in the
presence
of selection for direct and maternal breeding values.
Diaz-Martin, Clara,
1992; 1992.
xii, 163 leaves : ill. ; 28 cm. Vita. Abstract. Bibliography:
leaves
145-162.
Language: English
Descriptors: Hereford cattle; Genetic transformation
34 NAL Call. No.: QH442.G393
The CRG says no to patenting life forms.
Newman, S.; Wilker, N.
Boston, Mass. : Council for Responsible Genetics; 1992 Jul.
Genewatch v. 8 (2): p. 8-9; 1992 Jul.
Language: English
Descriptors: Crops; Livestock; Genetic engineering; Recombinant
DNA;
Transgenics; Patents; Organizations
35 NAL Call. No.: 442.8 Z8
Decreased frequency of the rat growth hormone transgene in mouse
populations
with or without selection for increased adult body weight.
Sabour, M.P.; Ramsey, U.; Nagai, J.
Berlin, W. Ger. : Springer International; 1991.
Theoretical and applied genetics v. 81 (3): p. 327-332; 1991.
Includes
references.
Language: English
Descriptors: Animal breeding; Genetic engineering; Mice; Rats;
Transgenics;
Somatotropin; Genes; Line differences; Inheritance; Gene frequency;
Selection
responses; Species differences; Segregation; Body weight
Abstract: Frequencies of mice with the rat growth hormone (rGH)
transgene
were examined in lines derived from two genetic bases (P/W and
(P/C). The
genetic bases were developed from males (P) with the rGH transgene,
mated with
non-transgenic females of different origin: a line previously
selected for
large body size (W) and a corresponding unselected control line
(C). They were
maintained for six generations under random mating with or without
selection
for increased 42-day body weight. The frequencies of P/W and P/C
males with
the rGH transgene wer 0.075 and 0.300, respectively at generation
0 of the
genetic bases. They were significantly (P<0.05) lower than the
expected
frequency (about 0.5). At generation 6, the frequencies had
decreased further
both in selected and unselected lines (ranging from 0.025 to
0.125). Decreased
frequencies of mice with the transgene were confirmed in a separate
experiment
testing segregation of the transgene. The reasons for these
decreases are not
clear. The results suggest that transgenes need to be monitored
when
transgenic animals are mated with animals of different origin.
36 NAL Call. No.: 44.8 J822
Designing animals: ethical issues for genetic engineers.
Thompson, P.B.
Champaign, Ill. : American Dairy Science Association; 1992 Aug.
Journal of dairy science v. 75 (8): p. 2294-2303; 1992 Aug.
Includes
references.
Language: English
Descriptors: Transgenics; Genetic engineering; Ethics; Patents
Abstract: Two general philosophical approaches to ethical issues
in property
rights are described. Instrumental approaches take property rights
to be means
for achieving goals such as social efficiency or economic growth.
Labor
approaches take property rights to be fundamental human rights that
protect
liberty or that assign ownership of goods based on criteria of
desert. A
thought experiment is used to illustrate the relevance of these
theories to
intellectual property. Alternative strategies for application of
ethical
theory to animal biotechnology are surveyed. The choice of an
approach
determines a burden of proof that must be met before property
claims can be
ethically sanctioned, but the question of which approach should be
applied to
animal biotechnology technology remains open. Ethical issues raised
by
unwanted consequences of biotechnology technology and religious
objections to
gene transfer are briefly summarized with emphasis on how these
issues have
influenced public debate on animal patents.
37 NAL Call. No.: 41.8 R312
Detection of foreign DNA in transgenic chicken embryos using the
polymerase
chain reaction.
Savva, D.; Vick, L.; Simkiss, K.
London : British Veterinary Association; 1991 Mar.
Research in veterinary science v. 50 (2): p. 131-133. ill; 1991
Mar. Includes
references.
Language: English
Descriptors: Chick embryos; Transgenics; Detection; Dna; Genes;
Polymerase
chain reaction; Retroviridae
38 NAL Call. No.: 448.3 AR23
Development and testing of a packaging cell line for avian
retroviral vectors.
Meyers, N.L.; Booth, S.C.; Bumstead, N.; Vick, L.; Simkiss, K.
Wien : Springer-Verlag; 1991.
Archives of virology v. 119 (3/4): p. 257-264; 1991. Includes
references.
Language: English
Descriptors: Fowls; Germ cells; Cell lines; Retroviridae;
Retroviral vectors;
Replication; Plasmids; Transgenics; Gene transfer
Abstract: A new helper cell line designated L3.07, has been used
to package
spleen necrosis virus (SNV)-based vectors, resulting in the
production of high
titres of replication defective retroviruses. One of these vectors,
vSNO21 has
been shown to infect avian primordial germ cells (PGCs).
39 NAL Call. No.: 49 J82
Development of a recombinant bovine leukemia virus vector for
delivery of a
synthetic bovine growth hormone-releasing factor gene into bovine
cells.
Mehigh, C.S.; Elias, V.D.; Mehigh, R.J.; Helferich, W.G.; Tucker,
H.A.
Champaign, Ill. : American Society of Animal Science; 1993 Mar.
Journal of animal science v. 71 (3): p. 687-693; 1993 Mar.
Includes
references.
Language: English
Descriptors: Dairy cattle; Gene transfer; Somatoliberin; Bovine
oncovirus;
Vectors; Messenger RNA; Transfection; Cell cultures
Abstract: Continuous intravenous infusion of bovine growth
hormone-releasing
factor (bGRF) increases milk synthesis in dairy cattle by as much
as 46%. We
have begun to develop a system for delivery and expression of a
synthetic bGRF
gene in cultured bovine cells using the provirus of the bovine
leukemia virus
(BLV). The gene encoding synthetic bGRF, constructed from eight
overlapping
oligonucleotides, was fused to the whey acidic protein promoter
(WAP) or the
mouse mammary tumor virus promoter (MMTV). These plasmids, termed
pWAP.GRF and
pMMTV.GRF, were able to induce transcription of bGRF upon
transfection into
Madin-Darby bovine kidney (MDBK) cells and induction with a
lactogenic
hormonal milieu (prolactin, hydrocortisone, triiodothyronine,
insulin) or
dexamethasone. When these constructs were cloned into a BLV vector
in place of
its oncogenic region, and transfected into MDBK cells, bGRF was
expressed.
Virus particles were prepared from these cultures and used to
deliver the bGRF
gene by viral infection into fresh MDBK cells. Northern blot
analysis of MDBK
total RNA revealed a fivefold higher level of expression of bGRF
mRNA in
transfected cultures than in virally infected cells, and no
expression was
detected in control cultures. The bGRF peptide was detected in both
cell
extracts and media samples from transfected cultures but was not
detected in
cell extracts or media samples from virally infected cells. This
provirus
construct may prove useful as a delivery system for peptides into
cattle.
40 NAL Call. No.: QD341.A2N8
Development of baculovirus triple and quadruple expression vectors:
co-expression of three or four bluetongue virus proteins and the
synthesis of
bluetongue virus-like particles in insect cells.
Belyaev, A.S.; Roy, P.
Oxford : IRL Press; 1993 Mar11.
Nucleic acids research v. 21 (5): p. 1219-1223; 1993 Mar11.
Includes
references.
Language: English
Descriptors: Autographa californica; Nuclear polyhedrosis viruses;
Gene
transfer; Bluetongue virus
Abstract: Baculovirus multiple gene transfer vectors pAcAB3 and
pAcAB4 have
been developed to facilitate the insertion of three or four foreign
genes
respectively into the Autographa californica nuclear polyhedrosis
virus
(AcNPV) genome by a single co-transfection experiment. The pAcAB3
vector
contains a polyhedrin promoter and two p10 promoters on either side
of the
polyhedrin promoter but in opposite orientations. The pAcAB4 vector
has an
additional polyhedrin promoter in opposite orientation to the first
copy that
is in juxtaposition to the first p10 promoter. Each of these
derived vectors
(pAcAB3, pAcAB4) have been used for the simultaneous expression of
three or
four bluetongue virus (BTV) genes respectively. When Spodoptera
frugiperda
cells were infected with the recombinant virus (AcBT-3/2/7/5)
expressing the
four major structural genes of BTV, double-capsid, virus-like
particles
consisting of VP2, VP3, VP5 and VP7 of BTV were assembled.
41 NAL Call. No.: 410.9 P94
Development of mouse oocytes superovulated at different ages.
Sugiyama, F.; Kajiwara, N.; Hayashi, S.; Sugiyama, Y.; Yagami, K.
Cordova, Tenn. : American Association for Laboratory Animal
Science; 1992 Jun.
Laboratory animal science v. 42 (3): p. 297-298; 1992 Jun.
Includes
references.
Language: English
Descriptors: Mice; Oocytes; Superovulation; Age differences; Age;
Strain
differences; In vitro; Fertilization; Embryo culture; Embryo
transfer;
Embryonic development; Viability
Abstract: The development of oocytes superovulated at 25, 50, or
90 days in
four mouse strains (C57BL/6N, DBA/2N, ICR, and B6D2F1) was examined
using the
techniques of in vitro fertilization, culture, and transfer of
two-cell
embryos to pseudopregnant recipients. The highest number of ova
were obtained
from superovulated 25-day-old mice in all strains. Approximately
80% of
oocytes developed to the two-cell stage after in vitro
fertilization. Of these
living oocytes, 60% developed to weanling stage through the
recipient. These
results suggested that donor age among 25, 50, or 90-day-old mice
has no
influence on the viability of superovulated oocytes. Consequently,
we conclude
that superovulated 25-day-old mice offer an economical and
efficient source of
viable oocytes for the production of transgenic mice.
42 NAL Call. No.: S494.5.B563N33
The development of sheep expressing growth promoting transgenes.
Murray, J.D.; Rexroad, C.E. Jr
Ithaca, N.Y. : National Agricultural Biotechnology Council; 1991.
NABC report / (3): p. 251-263; 1991. In the series analytic:
Agricultural
biotechnology at the crossroads: biological, social and
institutional
concerns. Proceedings of the National Agricultural Biotechnology
Council's
third annual meeting, May 1991.
Language: English
Descriptors: Sheep; Transgenics; Gene expression; Growth promoters
43 NAL Call. No.: 475 EX7
Disease resistance in farm animals.
Muller, M.; Brem, G.
Basel : Birkhauser; 1991 Sep15.
Experientia v. 47 (9): p. 923-939; 1991 Sep15. Literature review.
Includes
references.
Language: English
Descriptors: Livestock; Disease resistance; Genetic variation;
Transgenics;
Monoclonal antibodies; Antisense RNA; Genes; Literature reviews
44 NAL Call. No.: QR360.A1J6
Dissimilar expression of Autographa californica multiple
nucleocapsid nuclear
polyhderosis virus polyhedrin and p10 genes.
Roelvink, P.W.; Meer, M.M.M. van; Kort, C.A.D. de; Possee, R.D.;
Hammock,
B.D.; Vlak, J.M.
Reading : Society for General Microbiology; 1992 Jun.
The Journal of general virology v. 73 (pt.6): p. 1481-1489; 1992
Jun.
Includes references.
Language: English
Descriptors: Autographa californica; Nuclear polyhedrosis viruses;
Spodoptera
frugiperda; Cell culture; Heliothis virescens; Gene expression;
Gene transfer
Abstract: The temporal expression of the Autographa californica
multiple
nucleocapsid nuclear polyhedrosis virus polyhedrin and p10 genes in
Spodoptera
frugiperda cells was studied using virus recombinants in which
either gene was
replaced by the juvenile hormone esterase (JHE) gene of Heliothis
virescens.
The JHE served as a highly specific and sensitive reporter for gene
expression. Activation of the p10 gene followed a pattern different
to that of
polyhedrin. The p10 gene was activated a few hours earlier than the
polyhedrin
gene, but its expression reached a lower maximum level. Northern
blot analysis
complemented and confirmed the results obtained from the JHE
assays.
Co-infection of sense recombinants and those containing an
antisense copy of
the JHE gene in place of the polyhedrin or p10 gene resulted in
reduced levels
of JHE gene expression. These experiments independently supported
the
hypothesis that the p10 gene promoter is more active at earlier
times
post-infection than that of the polyhedrin gene. The results also
highlight
the potential of the antisense strategy as an experimental approach
for the
study of baculovirus gene regulation and possibly insect
metabolism.
45 NAL Call. No.: QP251.A1T5
DNA probes to repetitive sequences for the analysis of porcine
genomic DNA
with reference to DNA methylation.
Kronnie, G. te; Samallo, J.
Stoneham, Mass. : Butterworth-Heinemann; 1993 Jun.
Theriogenology v. 39 (6): p. 1313-1320; 1993 Jun. Includes
references.
Language: English
Descriptors: Pigs; Dna probes; Dna methylation
Abstract: The aim of this study was to isolate probes to
repetitive sequences
of porcine (Great Yorkshire X Landrace) genomic DNA. The production
of
transgenic animals involves the isolation of stem cell lines and
the
understanding of DNA methylation modifications. Probes to
repetitive sequences
enable the analysis of DNA methylation in the tissues of various
embryonic
stages of the pig. A primary library of porcine genomic DNA was
screened with
labeled fragments of porcine DNA, and 6 clones containing
repetitive DNA were
isolated and analyzed for the presence of potential methylation
moieties (CCGG
sites). Probes of all 6 clones were tested in a hybridization
analysis of
HpaII and MspI digests of porcine sperm DNA, and it was found that
methylation
was not present in the methylation moieties of the repetitive
sequences.
46 NAL Call. No.: 472 N42
Dutch lack appetite for genectically 'altered' foods.
Coghlan, A.
London, Eng. : New Science Publications; 1991 Aug17.
New scientist v. 131 (1782): p. 9; 1991 Aug17.
Language: English
Descriptors: Netherlands; Food processing; Genetic engineering; Transgenics
47 NAL Call. No.: QL868.D6
Effect of bovine growth hormone gene expression, sex and age on
plasma
gonadotropins, estrone and testosterone in prepuberal pigs.
Guthrie, H.D.; Pursel, V.G.; Miller, K.F.; Bolt, D.J.; Palmiter,
R.D.;
Brinster, R.L.
Stoneham, Mass. : Butterworth-Heinemann; 1991 Jul.
Domestic animal endocrinology v. 8 (3): p. 423-429; 1991 Jul.
Includes
references.
Language: English
Descriptors: Gilts; Boars; Transgenics; Somatotropin; Blood plasma;
Gonadotropins; Estrone; Testosterone; Gene expression; Hormone
secretion;
Sexual maturity; Lh
48 NAL Call. No.: ViBlbVLD5655.V855 1993.H346
Effect of culture conditions, donor source, and injection site on
in vitro
development of deoxyribonucleic acid microinjected porcine zygotes.
Hajdu, Melissa Anne,
1993; 1993.
vii, 68 leaves : ill. ; 28 cm. Vita. Abstract. Bibliography:
leaves 49-57.
Language: English
Descriptors: Transgenic animals; Embryology; Swine
49 NAL Call. No.: 448.3 Ap5
Effect of promoter modification on mosquitocidal cryIVB gene
expression in
Synechococcus sp. strain PCC 7942.
Soltes-Rak, E.; Kushner, D.J.; Williams, D.D.; Coleman, J.R.
Washington : American Society for Microbiology; 1993 Aug.
Applied and environmental microbiology v. 59 (8): p. 2404-2410;
1993 Aug.
Includes references.
Language: English
Descriptors: Synechococcus; Bacillus thuringiensis subsp.
israelensis;
Structural genes; Endotoxins; Bacterial toxins; Genetic
transformation; Gene
expression; Promoters; Recombinant DNA; Genetic regulation;
Plasmid vectors;
Insecticidal properties; Culex restuans; Larvae
Abstract: The impact of promoter modification on the expression of
the
mosquitocidal Bacillus thuringiensis subsp. israelensis cryIVB gene
when used
to transform the cyanobacterium Synechococcus sp. strain PCC 7942
has been
examined. Maximal transcript and protein abundances were achieved
by the
addition of the lacZ promoter upstream of the cryIVB sequence.
Replacement of
the endogenous corresponding Bacillus sequences with the
Synechococcus petF1
promoter, ribosome binding site, and initiation codon also resulted
in
increased expression of the cryIVB gene relative to the expression
obtained
with the Bacillus promoter alone but decreased expression relative
to the
expression achieved with the tandem array of the Bacillus and lacZ
promoters.
Synechococcus cells carrying plasmids in which the expression of
the cryIVB
gene was regulated by either the lacZ or the petF1 promoter were
readily
consumed by first-instar Culex restuans larvae and proved to be
toxic for
these organisms.
50 NAL Call. No.: 442.8 P94
Effects of an acute in vivo application of concanavalin A on the
migration of
avian primordial germ cells.
Al-Thani, R.; Simkiss, K.
Wien : Springer-Verlag; 1991.
Protoplasma v. 161 (1): p. 52-57; 1991. Includes references.
Language: English
Descriptors: Fowls; Chick embryos; Germ cells; Movement; Kinetics;
Concanavalin a; Cell membranes; Receptors; Animal breeding;
Transgenics; Germ
line; Sterilization; Animal breeding methods
51 NAL Call. No.: TP248.13.B54
Efforts to commercialize transgenic pigs don't fly; rabbits in the
wings.
New York : McGraw-Hill :.; 1991 Jan21.
Biotechnology newswatch v. 11 (2): p. 12; 1991 Jan21.
Language: English
Descriptors: Pigs; Transgenics; Genetic engineering; Usda; Markets
52 NAL Call. No.: QP251.M64
Electroporation of bovine spermatozoa to carry foreign DNA in
oocytes.
Gagne, M.B.; Pothier, F.; Sirard, M.A.
New York, N.Y. : Wiley-Liss, Inc; 1991 May.
Molecular reproduction and development v. 29 (1): p. 6-15; 1991
May. Includes
references.
Language: English
Descriptors: Cattle; Spermatozoa; Oocytes; Plasmids; Dna;
Fertilization;
Nucleotide sequences; Vectors; Transgenics; Electroporation
53 NAL Call. No.: Q320.B56
Enhanced growth performance in transgenic swine.
Pinkert, C.A.; Kooyman, D.L.; Dyer, T.J.
Stoneham, Mass. : Butterworth Publishers; 1991.
Biotechnology (16): p. 251-258; 1991. In the series analytic:
Transgenic
Animals / Edited by Neal L. First; Florence P. Haseltime. Includes
references.
Language: English
Descriptors: Transgenics; Pigs; Gene transfer; Growth; Performance
54 NAL Call. No.: QH511.G6
The epigenetic influence of growth hormone on skeletal development.
Vogl, C.; Atchley, W.R.; Cowley, D.E.; Crenshaw, P.; Murray, J.D.;
Pomp, D.
Bar Harbor, Me. : Growth Publishing Company; 1993.
Growth, development, and aging : GDA v. 57 (3): p. 163-182; 1993.
Includes
references.
Language: English
Descriptors: Mice; Transgenic animals; Sheep; Somatotropin;
Structural genes;
Recombinant DNA; Metallothionein; Promoters; Genetic
transformation;
Epigenetics; Gene expression; Skeletal development; Mandible; Limb
bones;
Skull; Cartilage; Epiphyses
55 NAL Call. No.: QD341.A2N8
Estrogen-inducible and liver-specific expression of the chicken
Very Low
Density Apolipoprotein II gene locus in transgenic mice.
Wijnholds, J.; Philipsen, S.; Pruzina, S.; Fraser, P.; Grosveld,
F.; AB, G.
Oxford : IRL Press; 1993 Apr11.
Nucleic acids research v. 21 (7): p. 1629-1635; 1993 Apr11.
Includes
references.
Language: English
Descriptors: Chickens; Mice; Transgenic animals; Structural genes;
Apolipoproteins; Very low density lipoprotein; Gene expression;
Genetic
regulation; Inhibitor genes; Estradiol; Liver; Messenger RNA; Rna
editing
Abstract: We have examined the chicken Very Low Density
apolipoprotein II
(apoVLDL II) gene locus in transgenic mice. A DNA fragment composed
of the
transcribed region, 16 kb of 5' flanking and 400 bp of 3' flanking
sequences
contained all the information sufficient for estrogen-inducible,
liver-specific expression of the apoVLDL II gene. The far-upstream
region
contains a Negative Regulating Element coinciding with a
DNaseI-hypersensitive
site at -11 kb. In transgenic mice, the NRE at -11 kb is used for
downregulating the expression to a lower maximum level. The NRE
might be used
for modulating apoVLDL II gene expression, and may be involved in
the rapid
shut-down of the expression after hormone removal.
56 NAL Call. No.: QH332.E83 1992
Ethics and patenting of transgenic organisms.
National Agricultural Biotechnology Council (U.S.),Texas A & M
University,
Center for Biotechnology Policy and Ethics
Ithaca, NY : National Agricultural Biotechnology Council,; 1992.
iv, 101 p. ; 28 cm. (NABC occasional papers : no. 1). This NABC 4
optional
symposium was co-sponsored by the National Agricultural
Biotechnology Council
and the Center for Biotechnology Policy and Ethics at Texas A&M
University.
Special funding was provided by the Institute for Biosciences and
Technology,
Texas A&M University. Includes bibliographical references.
Language: English
Descriptors: Bioethics; Transgenic animals; Animal biotchnology
57 NAL Call. No.: 472 N42
Europe wrangles over Herman's sex life.
Cremers, H.C.; MacKenzie, D.
London, Eng. : New Science Publications; 1992 Nov28.
New scientist v. 136 (1849): p. 8; 1992 Nov28.
Language: English
Descriptors: Netherlands; Transgenics; Cattle; Mastitis; Disease resistance
58 NAL Call. No.: QP251.A1T5
Evaluation of systems for collection of porcine zygotes for DNA
microinjection
and transfer.
Williams, B.L.; Sparks, A.E.T.; Canesco, R.S.; Knight, J.W.;
Johnson, J.L.;
Velander, W.H.; Page, R.L.; Drohan, W.N.; Kornegay, E.T.; Pearson,
R.E.
Stoneham, Mass. : Butterworth-Heinemann; 1992 Sep.
Theriogenology v. 38 (3): p. 501-511; 1992 Sep. Includes
references.
Language: English
Descriptors: Sows; Gilts; Superovulation; Estrus; Synchronization;
Zygotes;
Transgenics; Ovulation rate; Dna; Injection; Embryo transfer;
Fertilization;
Pregnancy rate
Abstract: Crossbred gilts and sows (n = 116) were used for the
collection of
1-cell zygotes for DNA microinjection and transfer.
Retrospectively, estrus
synchronization and superovulation schemes were evaluated to assess
practicality for zygote collection. Four synchronization and
superovulation
procedures were used: 1) sows were observed for natural estrous
behavior; 1000
IU human chorionic gonadotrophin (hCG) was administered at the
onset of estrus
(NAT); 2) cyclic gilts were synchronized with 17.6 mg altrenogest
(Alt)/day
for 15 to 19 days followed by superovulation with 1500 IU pregnant
mares serum
gonadotropin (PMSG) and 500 IU hCG (LALT): 3) gilts between 11 and
16 days of
the estrous cycle received 17.6 mg ALT for 5 to 9 days and PMSG and
hCG were
used to induce superovulation (SALT); and 4) precocious ovulation
was induced
in prepubertal gilts with PMSG and hCG (PRE). A total of 505 DNA
microinjected
embryos transferred into 17 recipients produced 7 litters and 50
piglets, of
which 8 were transgenic. The NAT sows had less (P < 0.05) ovarian
activity
than gilts synchronized and superovulated by all the other
procedures.
Synchronization treatments with PMSG did not differ (P > 0.05) in
the number
of corpora hemorrhagica or unovulated follicles, but SALT and PRE
treatments
had higher ovulation rates than LALT (24.7 +/- 2.9, 24.3 +/- 1.8 vs
11.6 2.7
ovulations; mean +/- SEM). The SALT and PRE treatments yielded 12.3
+/- 2.6
and 17.7 +/- 1.7 zygotes. Successful transgenesis was accomplished
with SALT
and PRE procedures for estrus synchronization and superovulation.
59 NAL Call. No.: 47.8 W89
Evaluation of the potentials of new scientific developments for
commercial
poultry breeding.
Hartmann, W.
London : Butterworth; 1992 Mar.
World's poultry science journal v. 48 (1): p. 17-27; 1992 Mar.
Literature
review. Includes references.
Language: English
Descriptors: Broilers; Hens; Egg production; Breeding value;
Transgenics;
Selection criteria; Breeding methods; Crossbreds; Molecular
genetics;
Phenotypic selection; Accuracy; Best linear unbiased prediction;
Literature
reviews
60 NAL Call. No.: QP251.M64
Evidence for nuclear internalization of exogenous DNA into
mammalian sperm
cells.
Francolini, M.; Lavitrano, M.; Lamia, C.L.; French, D.; Frati, L.;
Cotelli,
F.; Spadafora, C.
New York, N.Y. : Wiley-Liss, Inc; 1993 Feb.
Molecular reproduction and development v. 34 (2): p. 133-139; 1993
Feb.
Includes references.
Language: English
Descriptors: Cattle; Spermatozoa; Direct DNAuptake; Nuclei;
Autoradiography;
Plasmids; Dna; Genetic transformation
61 NAL Call. No.: 381 J824
Evidence from transgenic mice that glucose transport is
rate-limiting for
glycogen deposition and glycolysis in skeletal muscle.
Ren, J.M.; Marshall, B.A.; Gulve, E.A.; Gao, J.; Johnson, D.W.;
Holloszy,
J.O.; Mueckler, M.
Baltimore, Md. : American Society for Biochemistry and Molecular
Biology; 1993
Aug05.
The Journal of biological chemistry v. 268 (22): p. 16113-16115;
1993 Aug05.
Includes references.
Language: English
Descriptors: Man; Mice; Glucose; Active transport; Skeletal muscle;
Animal
proteins; Plasma membranes; Glycogen; Carbohydrate metabolism;
Hexokinase;
Enzyme activity; Transgenic animals
Abstract: A line of transgenic mice was constructed in which the
human Glut1
glucose transporter is overexpressed in skeletal muscle.
Overexpression of
Glut1 protein was evident in epitrochlearis, extensor digitorum
longus (EDL),
and quadriceps muscles, and resulted in 6.6-7.4-fold elevations in
basal
glucose transport activity as measured in isolated muscles in
vitro. The
elevated glucose transporter activity in the skeletal muscles of
transgenic
mice was associated with a 10-fold increase in glycogen
concentration in EDL
and quadriceps muscles that was not due to an increase in muscle
glycogen
synthase activity or a decrease in glycogen phosphorylase activity.
The
increased glucose transport activity also resulted in a 2-fold
increase in
muscle lactate concentration, with no increase in muscle glucose
6-phosphate.
Despite a slight (10%) increase in muscle hexokinase activity,
there was a
4-fold increase in total muscle free glucose in transgenic mice,
indicating
that hexokinase becomes rate-limiting for glucose uptake when the
rate of
glucose transport is very high. These results demonstrate that the
muscle
glycogen content can be dramatically elevated by increasing the
muscle Glut1
protein level and that glucose transport is a rate-limiting step
for muscle
glucose disposal in normal, resting mice.
62 NAL Call. No.: QR360.J6
Experimentally introduced defective endogenous proviruses are
highly expressed
in chickens.
Federspiel, M.J.; Crittenden, L.B.; Provencher, L.P.; Hughes, S.H.
Washington, D.C. : American Society for Microbiology; 1991 Jan.
Journal of virology v. 65 (1): p. 313-319. ill; 1991 Jan. Includes
references.
Language: English
Descriptors: Fowls; Transgenics; Avian oncovirus; Gene expression
Abstract: We have previously described the experimental
introduction of
recombinant subgroup A avian leukosis viruses (ALV) with
Rous-associated virus
0 long terminal repeats into the germ line of line 0 chickens and
the
generation of 23 transgenic lines. Two of these transgenic lines,
alv6 and
alv11, do not produce infectious virus. Both of these lines contain
defective
proviruses but do express the gag and/or env protein. We have
measured viral
RNA expression in tissues derived from alv6, alv11, and the
parental line 0.
Total RNA was prepared from 9-day embryo, 16-day embryo, 1-day
chicken, and
28-day chicken tissues. Viral RNA was detected by Northern RNA
transfer
analysis. The results indicate that both alv6 and alv11 chickens
express viral
RNA in all tissues tested regardless of the stage of development.
No viral
transcripts were detected in any line 0 (C/E; ev-negative) tissue.
The levels
of biologically active env glycoprotein correlates with the env RNA
levels in
both lines. In an in vivo interference assay, alv6, alv11, and line
0 chickens
were infected with Rous-associated virus 1 and monitored for
viremia, antibody
against Rous-associated virus 1, and ALV-induced pathogenesis from
4 to 21
weeks. None of the 61 alv6 chickens contained detectable virus or
produced
antibody against subgroup A ALV. Virus and/or antibody against
subgroup A ALV
was detected in 34 of the 43 alv11 chickens, whereas 51 of 52 line
0 birds
were viremic and/or produced antibody. ALV-induced pathogenesis was
observed
predominantly in line 0 chickens (10 of 59), whereas very little
ALV-induced
pathogenesis was seen in either alv6 (1 of 62) or alv11 (1 of 44)
chickens.
Presumably the mechanism for the increased resistance of alv6 and
alv11
chickens was subgroup-specific receptor interference. These results
clearly
demonstrate that experimentally introduced endogenous proviruses
can be
expressed at high levels in the avian system.
63 NAL Call. No.: 442.8 J8222 SUPPL.
Expression and physiology of performance regulating genes in
transgenic sheep.
Nancarrow, C.D.; Marshall, J.T.A.; Clarkson, J.L.; Murray, J.D.;
Millard,
R.M.; Shanahan, C.M.; Wynn, P.C.; Ward, K.A.
Cambridge, U.K. : The Journals of Reproduction and Fertility Ltd;
1991.
Journal of reproduction and fertility: Supplement (43): p. 277-291;
1991. In
the series analytic: Reproduction in domestic ruminants II / edited
by G.E.
Lamming, A.P.F. Flint, B.J. Weir. Proceedings of a symposium held
March 1990,
Nice, France. Includes references.
Language: English
Descriptors: Sheep; Transgenics; Gene expression
64 NAL Call. No.: 381 J824
Expression of a whey acidic protein transgene during mammary
development.
Evidence for different mechanisms of regulation during pregnancy
and
lactation.
Burdon, T.; Sankaran, L.; Wall, R.J.; Spencer, M.; Hennighausen, L.
Baltimore, Md. : American Society for Biochemistry and Molecular
Biology; 1991
Apr15.
The Journal of biological chemistry v. 266 (11): p. 6909-6914; 1991
Apr15.
Includes references.
Language: English
Descriptors: Mouse milk; Whey protein; Gene expression; Cloning;
Genetic
regulation; Pregnancy; Lactation; Recombinant DNA; Mice
Abstract: Expression of the mouse whey acidic protein (WAP) gene
is specific
to the mammary gland, is induced several thousand-fold during
pregnancy, and
is under the control of steroid and peptide hormones. To study
developmental
regulation of the mouse WAP gene, a 7.2-kilobase (kb) WAP
transgene, including
2.6 kb of 5'- and 1.6 kb of 3'-flanking sequences, was introduced
into mice.
Of the 13 lines of mice examined, 6 expressed the transgenes during
lactation
at levels between 3 and 54% of the endogenous gene. Although
expression was
dependent on the site of integration, the transgenes within a given
locus were
expressed in a copy number-dependent manner and were coordinately
regulated.
The WAP transgenes were expressed specifically in the mammary
gland, but
showed a deregulated pattern of expression during mammary
development. In all
six lines of mice, induction of the WAP transgenes during pregnancy
preceded
that of the endogenous gene. During lactation, expression in two
lines
increased coordinately with the endogenous gene, and in three other
lines of
mice, transgene expression decreased to a basal level. These data
indicate
that the 7.2-kb gene contains some but not all of the elements
necessary for
correct developmental regulation. At a functional level it appears
as if a
repressor element, which inactivates the endogenous gene until late
pregnancy,
and an element necessary for induction during lactation are absent
from the
transgene. Complementary results from developmental and hormone
induction
studies suggest that WAP gene expression during pregnancy and
lactation is
mediated by different mechanisms.
65 NAL Call. No.: QH442.J69
Expression of recombinant calf prochymosin in mammalian cell
culture.
Kolmer, M.; Ord, T.; Ulmanen, I.
Amsterdam : Elsevier Science Publishers B.V.; 1991 Sep.
Journal of Biotechnology v. 20 (2): p. 131-140; 1991 Sep. Includes
references.
Language: English
Descriptors: Calves; Chymosin; Enzyme precursors; Cloning; Vectors;
Epstein-barr virus; Gene expression; Hela cells; Enzyme activity;
Milk; Gene
transfer
66 NAL Call. No.: QH506.A1M622
Extrachromosomal localization and hereditary transfer of a
recombinant plasmid
microinjected into silkworm eggs.
Nikolaev, A.I.; Chkoniya, T.T.; Kafiani-Eristavi, K.A.
New York, N.Y. : Consultants Bureau; 1992 Feb.
Molecular biology v. 25 (4,pt.2): p. 896-904; 1992 Feb. Translated
from:
Molekuliarnia biologiia, v.25 (4,pt.2), 1991, p. 1136-1145.
(QH506.A1M62).
Includes references.
Language: English; Russian
Descriptors: Bombyx mori; Rous sarcoma virus; Genetic
transformation;
Plasmids; Repetitive DNA; Direct DNAuptake; Transgenics;
Inheritance;
Embryos; Eggs
Abstract: The plasmid p1.5LTR, containing DNA copies of long
terminal repeats
of Rous sarcoma virus, was inserted into early silkworm embryos.
Three
generations of animals containing the introduced plasmid sequences
in their
total DNA were obtained. We demonstrated that exogenous DNA is
represented in
the form of extrachromosomal molecules, whose molecular weight
exceeds the
molecular weight of the original plasmid. In insects of the F0
generation, the
structure of extrachromosomal DNA differs from that of the injected
plasmid.
Further rearrangement of the transgenes occurred during the
hereditary
transmission.
67 NAL Call. No.: QP501.B642
The fate of female donor blastodermal cells in male chimeric
chickens.
Shaw, D.L.; Carsience, R.S.; Etches, R.J.; Verrinder Gibbins, A.M.
Ottawa : National Research Council of Canada; 1992 Oct.
Biochemistry and cell biology; Biochimie et biologie cellulaire v.
70 (10/11):
p. 1218-1229; 1992 Oct. Includes references.
Language: English
Descriptors: Chickens; Transgenics; Chimeras; Chromosomes; Hybridization
68 NAL Call. No.: QP251.M64
Fate of microinjected genes in preimplantation mouse embryos.
Burdon, T.G.; Wall, R.J.
New York, N.Y. : Wiley-Liss, Inc; 1992 Dec.
Molecular reproduction and development v. 33 (4): p. 436-442; 1992
Dec.
Includes references.
Language: English
Descriptors: Mice; Gene transfer; Direct DNAuptake; Dna; Genes;
Animal
proteins; Polymerase chain reaction; Embryos; Preimplantation
period;
Transgenics; Dna methylation; Dna conformation; Blastomere
69 NAL Call. No.: QH445.2.G45
Feline arylsulfatase B (ARSB): isolation and expression of the
cDNA,
comparison with human ARSB, and gene localization to feline
chromosome A1.
Jackson, C.E.; Yuhki, N.; Desnick, R.J.; Haskins, M.E.; O'Brien,
S.J.;
Schuchman, E.H.
Orlando, Fla. : Academic Press, Inc; 1992 Oct.
Genomics v. 14 (2): p. 403-411; 1992 Oct. Includes references.
Language: English
Descriptors: Cats; Structural genes; Dna; Arylsulfatase; Gene
location;
Chromosomes; Nucleotide sequences; Amino acid sequences; Polymerase
chain
reaction; Somatic hybridization; Mice; Hamsters; Cell lines;
Comparisons; Man;
Gene expression; Genetic transformation
70 NAL Call. No.: S494.5.B563N33
The food safety of transgenic animals.
Berkowitz, D.
Ithaca, N.Y. : National Agricultural Biotechnology Council; 1992.
NABC report / (4): p. 127-131; 1992. In the series analytic:
Animal
biotechnology: opportunities and challenges. Proceedings of the
fourth annual
NABC meeting, May 1992, College Station, Texas. Includes
references.
Language: English
Descriptors: Food safety; Transgenic animals; Genetic engineering
71 NAL Call. No.: S494.5.B563N33
Food safety perspectives on animal biotechnology.
Cross, H.R.
Ithaca, N.Y. : National Agricultural Biotechnology Council; 1992.
NABC report / (4): p. 121-126; 1992. In the series analytic:
Animal
biotechnology: opportunities and challenges. Proceedings of the
fourth annual
NABC meeting, May 1992, College Station, Texas.
Language: English
Descriptors: Food safety; Biotechnology; Transgenic animals; Regulations
72 NAL Call. No.: QH442.G4522 FSIS moving toward regulating slaughtered transgenic animals. Washington, D.C. : King Pub. Group; 1993 May03. Biotech daily v. 2 (176): p. 3; 1993 May03.
Language: English
Descriptors: U.S.A.; Meat inspection; Food safety; Transgenics; Usda
73 NAL Call. No.: 47.8 AM33P
Gene expression from heterologous promoters in a
replication-defective avian
retrovirus vector in quail cells.
Hippenmeyer, P.J.; Krivi, G.G.
Champaign, Ill. : Poultry Science Association; 1991 Apr.
Poultry science v. 70 (4): p. 982-992; 1991 Apr. Includes
references.
Language: English
Descriptors: Cell lines; Quails; Retroviral vectors; Gene transfer;
Genes;
Expressivity; Genetic regulation; Sequences; Transfection;
Methylation
Abstract: Avian retrovirus vectors, with potential for use in
avian
transformation, were constructed to evaluate the relative
efficiency of
promoters placed internal to the viral long terminal repeats (LTR).
The
vectors are replication-defective reticuloendotheliosis plasmids
that contain
the neomycin phosphotransferase gene under control of the 5' LTR ad
an
internal promoter that directs expression of the chloramphenicol
acetyltransferase gene. The internal promoters were the SV40 early,
the mouse
metallothionein I and the human cytomegalovirus immediate early
(HCMV-IE)
promoters. Under transient conditions in QT6 cells, the HCMV-IE
promoter
construct was by far the strongest. However, expression dropped
greatly from
the HCMV-IE promoter after integration into the quail cell genome.
Evidence
suggests that the HCMV-IE promoter is selectively suppressed by
methylation
after stable transfection but not after infection.
74 NAL Call. No.: 410.9 P94
Gene targeting technology for creating transgenic models of
lymphopoiesis.
Huang, M.T.F.
Cordova, Tenn. : American Association for Laboratory Animal
Science; 1993 Apr.
Laboratory animal science v. 43 (2): p. 156-159; 1993 Apr. Paper
presented at
a conference entitled "The Scid Mouse in Biomedical and
Agricultural
Research," August 5-7, 1992, Guelph, Canada. Includes references.
Language: English
Descriptors: Transgenic animals; Mice; Lymphocytes
Abstract: Naturally occurring immunodeficient mouse strains
express a variety
of genetic defects in myeloid and/or lymphoid cell development.
These strains
have served as valuable animal models for studying immune cell
differentiation
and mechanisms of transplant rejection. Some of the most commonly
used strains
carry mutations at the nude, scid, beige, and/or xid loci. Gene
targeting
technology can now be used to directly modify endogenous alleles
via
homologous recombination with exogenous DNA. By performing DNA
targeting in
embryonic stem (ES) cells, germline transmission of these
modifications can be
obtained by breeding chimeras generated from cloned ES cells. This
approach
can be used to target the inactivation, modification, or
replacement of
specific genes and has been used to examine the role of several
alleles in
hematopoiesis. This review describes the use of this technology to
generate
mutations that influence the development and function of T and B
lymphocytes.
75 NAL Call. No.: QH442.6.G45 1993
Gene transfer and expression in farmed fish.
Dunham, Rex Alan,
United States-Israel Binational Agricultural Research and
Development Fund
Bet Dagan, Israel : BARD,; 1993.
57 leaves : ill. ; 27 cm. Final report. Project no. US-1517-88.
Includes
bibliographical references (leaves 34-39).
Language: English
Descriptors: Fishes; Transgenic animals; Gene expression
76 NAL Call. No.: aZ5071.N3
Gene transfer in animal systems: January 1985-October 1991.
Warmbrodt, R.; Stone, V.
Beltsville, Md. : The Library; 1992 Jan.
Quick bibliography series - U.S. Department of Agriculture,
National
Agricultural Library (U.S.). (92-19): 70 p.; 1992 Jan. Updates QB
90-13.
Bibliography.
Language: English
Descriptors: Gene transfer; Genetic transformation; Genetic
engineering;
Animals; Bibliographies
77 NAL Call. No.: SF887.I82 1992
Gene transfer in farm animals.
Brem, G.
London : Portland Press on behalf of the Biochemical Society; 1992.
Embryonic development and manipulation in animal production trends
in research
and applications / editors, A. Lauria, F. Gondolfi. p. 147-164;
1992.
(Portland Press proceedings). Proceedings of the 1st Congress of
the Italian
Society of Embryo Transfer and the International Symposium on
Embryonic
Technology in Domestic Species, Milan. Includes references.
Language: English
Descriptors: Livestock; Animal breeding; Gene transfer
78 NAL Call. No.: SF140.B54A55
Gene transfer in fish: potential and practice.
McEvoy, T.G.; Gannon, F.; Sreenan, J.M.
New York, N.Y. : Marcel Dekker; 1992.
Animal biotechnology v. 3 (2): p. 221-243; 1992. Includes
references.
Language: English
Descriptors: Fishes; Gene transfer
79 NAL Call. No.: QP251.M64
Gene transfer in the chicken by sperm-mediated methods.
Nakanishi, A.; Iritani, A.
New York, N.Y. : Wiley-Liss, Inc; 1993 Oct.
Molecular reproduction and development v. 36 (2): p. 258-261; 1993
Oct. Paper
presented at an "International Symposium on Animal Biotechnology",
Oct. 15-17,
1991, Kyoto, Japan. Includes references.
Language: English
Descriptors: Chickens; Gene transfer; Spermatozoa
80 NAL Call. No.: SF140.B54A55
Gene transfer into bovine cells and embryos using
replication-defective
retroviral vectors encapsidated with xenotropic murine leukemia
virus
envelopes.
Kim, T.; Leifried-Rutledge, M.L.; First, N.L.
New York, N.Y. : Marcel Dekker; 1993.
Animal biotechnology v. 4 (1): p. 53-69; 1993. Includes
references.
Language: English
Descriptors: Cattle; Gene transfer; Genetic vectors
81 NAL Call. No.: 442.8 J8222 SUPPL.
Gene transfer studies in cattle.
Roschlau, K.
Cambridge, U.K. : The Journals of Reproduction and Fertility Ltd;
1991.
Journal of reproduction and fertility: Supplement (43): p. 293-295;
1991. In
the series analytic: Reproduction in domestic ruminants II / edited
by G.E.
Lamming, A.P.F. Flint, B.J Weir. Proceedings of a symposium held
March 1990,
Nice, France. Includes references.
Language: English
Descriptors: Cattle; Gene transfer
82 NAL Call. No.: QH442.B5
Generation of transgenic dairy cattle using 'in vitro' embryo
production.
Krimpenfort, P.; Rademakers, A.; Eyestone, W.; Schans, A. van der;
Broek, S.
van den; Kooiman, P.; Kootwijk, E.; Platenburg, G.; Pieper, F.;
Stijker, R.
New York, N.Y. : Nature Publishing Company; 1991 Sep.
Bio/technology v. 9 (9): p. 844-847; 1991 Sep. Includes
references.
Language: English
Descriptors: Dairy cattle; Transgenics; Gene transfer; In vitro;
Embryo
transfer; Binding proteins; Lactoferrin
83 NAL Call. No.: 475 EX7
The genetic engineering of production traits in domestic animals.
Ward, K.A.; Nancarrow, C.D.
Basel : Birkhauser; 1991 Sep15.
Experientia v. 47 (9): p. 913-922; 1991 Sep15. Literature review.
Includes
references.
Language: English
Descriptors: Domestic animals; Livestock; Animal production;
Genetic
engineering; Gene transfer; Somatotropin; Transgenics; Cysteine;
Milk
proteins; Literature reviews
84 NAL Call. No.: QR1.L47
Genetic transformation of the ruminal bacteria Butyrivibrio
fibrisolvens and
Streptococcus bovis by electroporation.
Whitehead, T.R.
Oxford : Blackwell Scientific Publications; 1992 Nov.
Letters in applied microbiology v. 15 (5): p. 186-189; 1992 Nov.
Includes
references.
Language: English
Descriptors: Streptococcus bovis; Butyrivibrio fibrisolvens;
Genetic
transformation; Electroporation; Plasmids
85 NAL Call. No.: 381 J824
Germline manipulation of glucose homeostasis via alteration of
glucose
transporter levels in skeletal muscle.
Marshall, B.A.; Ren, J.M.; Johnson, D.W.; Gibbs, E.M.; Lillquist,
J.S.;
Soeller, W.C.; Holloszy, J.O.; Mueckler, M.
Baltimore, Md. : American Society for Biochemistry and Molecular
Biology; 1993
Sep05.
The Journal of biological chemistry v. 268 (25): p. 18442-18445;
1993 Sep05.
Includes references.
Language: English
Descriptors: Mice; Glucose; Uptake; Active transport; Binding
proteins;
Receptors; Skeletal muscle; Gene expression; Man; Complementary
DNA; Gene
transfer; Genetic transformation; Transgenic animals; Insulin;
Hormonal
control; Blood sugar; Homeostasis; Carbohydrate metabolism
Abstract: Transgenic mice were constructed that overexpress the
human Glut1
glucose transporter in skeletal muscle. Transcription of the human
Glut1 cDNA
was driven by the rat myosin light chain 2 promoter. Soleus and
quadriceps
muscles from transgenic mice expressed increased levels of Glut1
protein
relative to muscles obtained from nontransgenic littermates, but
there was no
difference in the level of Glut4 protein between the two groups.
Skeletal
muscles isolated from the transgenic animals exhibited 3-4-fold
increases in
basal glucose uptake relative to muscles obtained from
nontransgenic
littermates. Muscles isolated from nontransgenic littermates
exhibited
2-3-fold increases in glucose transport after incubation in the
presence of
insulin, but no insulin-stimulated increase in transport was
observed in the
muscles of transgenic mice. Plasma glucose levels were reduced by
18 and 30%,
respectively, in fed and fasted transgenic mice relative to their
nontransgenic siblings, but insulin and glucagon levels were not
significantly
different between the two groups. Glucose disposal following an
oral glucose
load was markedly enhanced in the transgenic animals, and plasma
lactate and
beta-OH-butyrate levels were elevated in both fed and fasted
transgenic mice.
These data strongly support the hypothesis that glucose transport
plays a key
role in whole body glucose homeostasis. They also demonstrate that
the level
of a glucose transporter in skeletal muscle can significantly
influence the
blood glucose set point and alter the levels of other fuel
metabolites in the
blood.
86 NAL Call. No.: A00064
Goats altered to produce medicinal proteins.
Maugh, T.H. II
Charlotte, N.C. : Observer Co; 1991 Aug27.
The Charlotte observer. p. 2A; 1991 Aug27.
Language: English
Descriptors: Transgenics; Proteins; Biological production
87 NAL Call. No.: TP248.13.B54
Goats, sheep, cattle carry gene for human proteins.
New York : McGraw-Hill :.; 1991 Sep02.
Biotechnology newswatch v. 11 (17): p. 1, 3; 1991 Sep02.
Language: English
Descriptors: Massachusetts; Scotland; California; Transgenics;
Goats; Sheep;
Cattle; Proteins
88 NAL Call. No.: QH511.G6
Growth characteristics of metallothionein-human growth hormone
transgenic mice
as compared to mice selected for high eight-week body weight and
unselected
controls. I. Body weight gain and external body dimensions.
Wolf, E.; Wanke, R.; Hermanns, W.; Brem, G.; Pirchner, F.;
Butler-Wemken, I.
von
Bar Harbor, Me. : Growth Publishing Company; 1991.
Growth, development, and aging : GDA v. 55 (4): p. 225-235; 1991.
Includes
references.
Language: English
Descriptors: Mice; Transgenics; Genetic transformation; Gene
transfer; Man;
Somatotropin; Metallothionein; Growth rate; Growth curve;
Liveweight gain;
Dimensions; Artificial selection
89 NAL Call. No.: QH511.G6
Growth characteristics of metallothionein-human growth hormone
transgenic mice
as compared to mice selected for high eight-week body weight and
unselected
controls. II. Skeleton.
Wolf, E.; Rapp, K.; Wanke, R.; Hermanns, W.; Pirchner, F.;
Butler-Wemken, I.
von; Brem, G.
Bar Harbor, Me. : Growth Publishing Company; 1991.
Growth, development, and aging : GDA v. 55 (4): p. 237-248; 1991.
Includes
references.
Language: English
Descriptors: Mice; Transgenics; Genetic transformation; Gene
transfer; Man;
Somatotropin; Metallothionein; Artificial selection; Skeleton;
Dimensions;
Bones; Growth; Bone formation; Gigantism; Body weight
90 NAL Call. No.: SF407.M5H35 1991
Handbook on genetically standardized JAX mice.. Genetically
standardized JAX
mice JAX mice, 4th ed..
Green, Margaret C.; Witham, Barbara A.
Jackson Laboratory (Bar Harbor, Me.)
Bar Harbor, ME : Jackson Laboratory,; 1991.
96 p. : ill. ; 28 cm. Includes bibliographical references and
index.
Language: English
Descriptors: Mice as laboratory animals; Inbreeding; Mice, Inbred Strains
91 NAL Call. No.: 381 B522
Hepatic and renal expression of rat apolipoprotein E under control
of the
metallothionein promoter in transgenic mice.
Shimano, H.; Yamada, N.; Shimada, M.; Ohsawa, N.; Fukazawa, C.;
Yazaki, Y.;
Takaku, F.; Katsuki, M.
Amsterdam : Elsevier Science Publishers; 1991 Aug27.
Biochimica et biophysica acta : International journal of
biochemistry and
biophysics v. 1090 (1): p. 91-94; 1991 Aug27. Includes references.
Language: English
Descriptors: Apolipoproteins; Transgenics; Mice; Gene expression;
Metallothionein; Messenger RNA; Northern blotting; Liver; Kidneys;
Blood
plasma; Lipoproteins; Zinc; Bismuth
Abstract: We created three lines of transgenic mice with an
integrated rat
genomic apolipoprotein E gene fused with the mouse metallothinein
I promotor.
These lines transcribed rat apoE mRNA in the liver and/or in the
kidney and
expressed significant amounts of rat apoE in plasma. Enhancement of
the plasma
level by treatment with Zn ion or Bi ion was observed.
92 NAL Call. No.: 500 N21P
Heritable retroviral transgenes are highly expressed in chickens.
Briskin, M.J.; Hsu, R.Y.; Boggs, T.; Schultz, J.A.; Rishell, W.;
Bosselman,
R.A.
Washington, D.C. : The Academy; 1991 Mar01.
Proceedings of the National Academy of Sciences of the United
States of
America v. 88 (5): p. 1736-1740. ill; 1991 Mar01. Includes
references.
Language: English
Descriptors: Fowls; Disease vectors; Gene expression;
Reticuloendotheliosis
virus; Transgenics; Lines
Abstract: This report describes expression of heritable
reticuloendotheliosis
virus (REV) vector ME111 in 20 independent lines of transgenic
chickens. The
results are strikingly different from studies of Moloney virus in
transgenic
mice, where restricted expression of inherited proviruses has led
to their use
primarily as insertional mutagens rather than general agents for
gene
transfer. In contrast, the REV ME111 provirus is actively
transcribed in a
variety of tissues from transgenic chickens, is expressed from
transcriptional
control elements present in the long terminal repeat of the
provirus, and
codes for active neomycin phosphotransferase II. The REV vector
system as
applied to the chicken represents a departure from the
long-established
paradigm of retroviral transgenes in mice and provides a new
approach to the
study of avian biology.
93 NAL Call. No.: A00067
Herman's no monster.
Paris, France : Biofutur S.A.; 1991 Aug27.
European biotechnology newsletter (118): p. 3-4; 1991 Aug27.
Language: English
Descriptors: Netherlands; Transgenics; Calves; Micromanipulation; Lactoferrin
94 NAL Call. No.: QH442.B5
High level expression of active human alpha-1-antitrypsin in the
milk of
transgenic sheep.
Wright, G.; Carver, A.; Cottom, D.; Reeves, D.; Scott, A.; Simons,
P.; Wilmut,
I.; Garver, I.; Colman, A.
New York, N.Y. : Nature Publishing Company; 1991 Sep.
Bio/technology v. 9 (9): p. 830-834; 1991 Sep. Includes
references.
Language: English
Descriptors: Sheep; Transgenics; Gene expression; Antitrypsin; Ewe
milk;
Beta-lactoglobulin
95 NAL Call. No.: 500 N21P
High-level synthesis of a heterologous milk protein in the mammary
glands of
transgenic swine.
Wall, R.J.; Pursel, V.G.; Shamay, A.; McKnight, R.A.; Pittius,
C.W.;
Hennighausen, L.
Washington, D.C. : The Academy; 1991 Mar01.
Proceedings of the National Academy of Sciences of the United
States of
America v. 88 (5): p. 1696-1700. ill; 1991 Mar01. Includes
references.
Language: English
Descriptors: Gilts; Lines; Transgenics; Mammary glands; Milk
proteins; Protein
synthesis; Rna; Secretion; Gene expression; Mice; Whey protein
Abstract: The whey acidic protein (WAP) is a major milk protein in
mice,
rats, and rabbits but has not been found in milk of livestock
including swine.
To determine whether mammary gland regulatory elements from the WAP
gene
function across species boundaries and whether it is possible to
qualitatively
alter milk protein composition, we introduced the mouse WAP gene
into the
genome of swine. Three lines of transgenic swine were analyzed, and
mouse WAP
was detected in milk from all lactating females at concentrations
of about 1
g/liter; these levels are similar to those found in mouse milk.
Expression of
the corresponding RNA was specific to the mammary gland. Our
results suggest
that the molecular basis of mammary-specific gene expression is
conserved
between swine and mouse. In addition the WAP gene must share, with
other milk
protein genes, elements that target gene expression to the mammary
gland.
Mouse WAP accounted for about 3% of the total milk proteins in
transgenic
pigs, thus demonstrating that it is possible to produce high levels
of a
foreign protein in milk of farm animals.
96 NAL Call. No.: 41.8 P27
Histologic characterization of hepatic carcinogenesis in transgenic
mice
expressing SV40 T-antigens.
Cullen, J.M.; Sandgren, E.P.; Brinster, R.L.; Maronpot, R.R.
Lawrence, Kan. : American College of Veterinary Pathologists; 1993
Mar.
Veterinary pathology v. 30 (2): p. 111-118; 1993 Mar. Includes
references.
Language: English
Descriptors: Mice; Transgenic animals; Liver; Carcinogenesis
97 NAL Call. No.: QR360.J6
Improvement of avian leukosis virus (ALV)-based retrovirus vectors
by using
different cis-acting sequences from ALVs.
Cosset, F.L.; Legras, C.; Thomas, J.L.; Molina, R.M.; Chebloune,
Y.; Faure,
C.; Nigon, V.M.; Verdier, G.
Washington, D.C. : American Society for Microbiology; 1991 Jun.
Journal of virology v. 65 (6): p. 3388-3394; 1991 Jun. Includes
references.
Language: English
Descriptors: Avian oncovirus; Rous sarcoma virus; Retroviral
vectors;
Transduction; Reporter genes; Rna; Nucleotide sequences; Gene
expression; Cell
lines; Fowls; Infection; Gene transfer
Abstract: Production and expression of double-expression vectors
which
transduce both Neo(r) and lacZ genes and are based on the structure
of avian
leukosis virus were enhanced by using cis-acting sequences (long
terminal
repeats and noncoding sequences) from Rous-associated virus-1 and
Rous-associated virus-2 rather than those of avian erythroblastosis
virus
previously used in our constructs. Polyclonal producer cells
obtained after
transfection of these vectors into the Isolde packaging cell line
gave rise to
titers as high as 3 X 10(5) lacZ CFU/ml, whereas it was possible to
isolate
clones of producer cells giving rise to titers of more than 10(6)
resistance
focus-forming units per ml.
98 NAL Call. No.: QH442.6.I56 1992
In our back yard state action to govern release of genetically
engineered
organisms into the environment : a common sense guide for citizens
and policy
makers.
Stark, Margo D.
Biotechnology Working Group
St. Paul, MN : The Group, [1992?]; 1992.
52 p. : map ; 29 cm. Includes bibliographical references.
Language: English
Descriptors: Transgenic organisms
99 NAL Call. No.: 49 J82
In vitro development of zygotes from prepubertal gilts after
microinjection of
DNA.
Williams, B.L.; Sparks, A.E.T.; Canseco, R.S.; Knight, J.W.;
Johnson, J.L.;
Velander, W.H.; Page, R.L.; Drohan, W.N.; Young, J.M.; Pearson,
R.E.
Champaign, Ill. : American Society of Animal Science; 1992 Jul.
Journal of animal science v. 70 (7): p. 2207-2211; 1992 Jul.
Includes
references.
Language: English
Descriptors: Gilts; Zygotes; In vitro culture; Dna; Transgenics;
Embryos;
Cleavage
Abstract: The effect of pronuclear microinjection of DNA and
culture in
excised mouse oviducts on the development of porcine zygotes was
assessed in
this study. Precocious ovulation was induced in prepubertal gilts
with
pregnant mare's serum gonadotrophin and hCG. Zygotes received
either
pronuclear microinjection of buffer alone, buffer containing a DNA
construct,
or no microinjection. Zygotes were cultured in vitro in either
modified
Krebs-Ringer bicarbonate medium (KRB) for 144 h or in mouse oviduct
(MO)
explant culture with KRB for 48, 72, 96, or 120 h. Pronuclear
microinjection
of DNA resulted in a lower (P < .05) cleavage index (CI) than did
buffer or no
microinjection (CI 2.16 +/- .10 vs 2.80 +/- .13 and 2.93 +/- .10).
The CI loss
was greatest for DNA-injected zygotes at the two-cell stage of
development.
Coculture of zygotes in MO resulted in a higher CI (P < .01) than
did culture
in KRB. Culture in MO for 72 h was the most beneficial system
compared with MO
for 48, 96, or 120 h (P < .05; CI 3.25 +/- .12 vs 2.66 +/- .18,
2.79 +/- .14,
and 2.40 +/- .14, respectively). Microinjection of DNA, not merely
the
mechanical procedure, was detrimental to early zygote development
and may be
the cause of low pregnancy rates.
100 NAL Call. No.: QP251.M64
Inheritance and tissue-specific expression of transgenes in rabbits
and pigs.
Brem, G.
New York, N.Y. : Wiley-Liss, Inc; 1993 Oct.
Molecular reproduction and development v. 36 (2): p. 242-244; 1993
Oct. Paper
presented at an "International Symposium on Animal Biotechnology",
Oct. 15-17,
1991, Kyoto, Japan. Includes references.
Language: English
Descriptors: Rabbits; Pigs; Transgenic animals
101 NAL Call. No.: 442.8 J828
Inhibition of proliferation of primary avian fibroblasts through
expression of
histone H5 depends on the degree of phosphorylation of the protein.
Aubert, D.; Garcia, M.; Benchaibi, M.; Poncet, D.; Chebloune, Y.;
Verdier, G.;
Nigon, V.; Samarut, J.; Mura, C.V.
New York, N.Y. : Rockefeller University Press; 1991 May.
The Journal of cell biology v. 113 (3): p. 497-506; 1991 May.
Includes
references.
Language: English
Descriptors: Quails; Fowls; Fibroblasts; Histones; Gene expression;
Cell
division; Growth rate; Phosphorylation; Genes; Gene transfer;
Retroviral
vectors; Avian oncovirus; Genetic transformation; Transfection
Abstract: To obtain stable and constitutive expression of histone
H5 at
levels comparable to those observed in normal chicken erythrocytes,
an avian
self-inactivating retroviral vector was used to transfer the H5
gene into
cells which do not express this protein. The vector, pDAH5, was
obtained by
removing the CAAT and TATA boxes of the 3LTR of the avian leukosis
virus RAV-2
and inserting the H5 sequence. Infection of QT6 quail cells with
the
recombinant virus (DAH5) led to the stable integration of the
foreign H5 gene
at low copy number, to the formation of correctly initiated mRNA
transcripts
and to the production of H5 protein. The amount of H5 expressed was
equivalent
to that of a mature chicken erythrocyte. Expression of histone H5
in DAH5
transformed cells, such as QT6 or AEV-ES4, transformed chicken
embryo
fibroblasts had only slight effects on the growth rate and did not
inhibit
cell replication. Conversely, the effect of H5 expression on normal
quail and
chicken fibroblasts was dramatic: cells acquired the aspect of
quiescent
fibroblasts, grew very slowly, and nuclei looked compacted, often
extruded
from the cell. The H5 histone produced in QT6-transformed cells was
found to
be phosphorylated while in normal chicken fibroblasts the protein
lacked this
posttranslational modification. It is proposed that the
chromatincondensing
role of histone H5 is inhibited by its phosphorylation.
102 NAL Call. No.: Q320.B56
Insertion of a disease resistance gene into the chicken germline.
Salter, D.W.; Crittenden, L.B.
Stoneham, Mass. : Butterworth Publishers; 1991.
Biotechnology (16): p. 125-131; 1991. In the series analytic:
Transgenic
Animals / Edited by Neal L. First; Florence P. Haseltime. Includes
references.
Language: English
Descriptors: Fowls; Avian oncovirus; Disease resistance; Gene
transfer;
Transgenics; Gene expression; Sarcoma
103 NAL Call. No.: QD341.A2N8
Interaction of DNA-binding proteins with a milk protein gene
promoter in
vitro: identification of a mammary gland-specific factor.
Watson, C.J.; Gordon, K.E.; Robertson, M.; Clark, A.J.
Oxford : IRL Press; 1991 Dec11.
Nucleic acids research v. 19 (23): p. 6603-6610; 1991 Dec11.
Includes
references.
Language: English
Descriptors: Sheep; Beta-lactoglobulin; Genes; Interactions; Dna
binding
proteins; Binding site; Mammary glands; Extracts; Transcription;
Genetic
regulation; Transgenics; Mice
Abstract: The minimal 51 regulatory region of the sheep
beta-lactoglobulin
gene (BLG), as defined in transgenic mice, was used to identify
nuclear
factors which may be involved in milk protein gene expression in
the lactating
mammary gland. This 406bp promoter region was dissected into short,
overlapping, double-stranded oligonucleotides to facilitate
identification of
the bound proteins. A variety of sites, for both known and
previously
undescribed DNA-binding proteins, are occupied in vitro. Some of
these factors
were investigated in detail. Two forms of nuclear factor I (NFI),
which have
different recognition site affinities, are present in nuclear
extracts from
lactating mammary gland and bind to at least 5 sites in this BLG
control
element. In addition, a factor (milk protein binding factor, MPBF)
which is
specific to extracts from both mouse and sheep lactating mammary
gland binds
to 3 BLG promoter sites and may be a milk protein gene
transcription factor.
104 NAL Call. No.: TA166.T72
Intracellular immunization: a new strategy for producing
disease-resistant
transgenic livestock?.
Staeheli, P.
Cambridge : Elsevier Publications; 1991 Mar.
Trends in biotechnology v. 9 (3): p. 71-72; 1991 Mar. Includes
references.
Language: English
Descriptors: Livestock; Transgenics; Disease resistance;
Immunization;
Mutants; Viral proteins; Technology
105 NAL Call. No.: QR360.J6
Isolation of a chicken gene that confers susceptibility to
infection by
subgroup A avian leukosis and sarcoma viruses.
Young, J.A.T.; Bates, P.; Varmus, H.E.
Washington, D.C. : American Society for Microbiology; 1993 Apr.
Journal of virology v. 67 (4): p. 1811-1816; 1993 Apr. Includes
references.
Language: English
Descriptors: Chickens; Avian oncovirus; Rous sarcoma virus;
Structural genes;
Receptors; Loci; Transfection; Gene transfer; Gene expression;
Infection;
Susceptibility; Fibroblasts; Mice; Monkeys
Abstract: We used a genetic strategy to isolate the chicken gene
believed to
encode the receptor for subgroup A avian leukosis and sarcoma
viruses
(ALSV-A). Chicken genomic DNA was transfected into monkey COS-7
cells, and two
independent primary transfectants susceptible to ALSV-A infection
were
identified by using ALSV-A vectors containing a hygromycin B
resistance gene.
A second round of transfection and selection in mouse BALB/3T3
fibroblasts
again led to isolation of a transfectant susceptible to infection
by ALSV-A.
Plasmid DNA sequences linked to chicken DNA during the primary
transfection
segregated with chicken DNA in the secondary transfectant and
served as a
molecular tag to clone the gene conferring susceptibility.
Expression of the
cloned gene in mouse BALB/3T3 cells conferred susceptibility to
infection by
ALSV-A but not by ALSV-B. Therefore the cloned gene most probably
represents
the tv-a locus, the genetically defined receptor gene for ALSV-A.
106 NAL Call. No.: 448.8 V81
Isolation of the avian transforming retrovirus, AS42, carrying the
v-maf
oncogene and initial charaterization of its gene product.
Kawai, S.; Goto, N.; Kataoka, K.; Saegusa, T.; Shinno-Kohno, H.;
Nishizawa, M.
Orlando, Fla. : Academic Press; 1992 Jun.
Virology v. 188 (2): p. 778-784; 1992 Jun. Includes references.
Language: English
Descriptors: Fowls; Chick embryos; Fibroblasts; Retroviridae;
Oncogenic
viruses; Neoplasms; Oncogenes; Viral proteins; Clones; Dna;
Nucleotide
sequences; Genetic transformation; Histopathology
Abstract: A novel avian transforming retrovirus was isolated from
a chicken
musculoaponeurotic fibrosarcoma. This virus (called AS42) induces
tumors
histopathologically indistinguishable from the original sarcoma
after a long
latent period when inoculated into newborn chickens. AS42 also
exhibits a weak
transforming activity when infected into chicken embryo fibroblasts
(CEF).
This virus is replication-defective and associated with a helper
virus of
subgroup A (called ASAV). An AS42-specific protein of about 100 kDa
was
immunoprecipitated from lysates of AS42-transformed CEF with
antiserum
directed against avian retrovirus virion proteins. Molecular
analysis of the
genomic structure of the AS42 virus has revealed that this 10-kDa
protein
represents a novel oncogene, v-maf of cellular origin, which is
fused with a
part of the viral gag gene (Nishizawa et al, Proc. Natl. Acad. Sci.
USA 86,
7711-7715, 1989). Interestingly, some size variation was observed
among the
gag-maf fusion proteins found in individual clones of transformed
CEF.
Consistent with this observation, Southern blot analyses and
nucleotide
sequence determination of several independent isolates of proviral
DNA
indicated that this virus segregates multiple forms of deletion
mutants,
probably through homologous recombinations among the repetitive
sequences
present within the v-maf coding region.
107 NAL Call. No.: BJ52.5.J68
It is morally permissible to manipulate the genome of domestic
hogs.
Blatz, C.V.
Guelph, Ontario, Canada : University of Guelph; 1991.
Journal of agricultural & environmental ethics v. 4 (2): p.
166-176; 1991.
Includes references.
Language: English
Descriptors: Pigs; Genetic engineering; Animal welfare; Ethics;
Biotechnology;
Transgenics
108 NAL Call. No.: 421 B87
Keeping entomology on the map: Is molecular biology the solution?
A reply to
O'Brochta.
McGregor, R.
London : Commonwealth Agricultural Bureaux International; 1991 Sep.
Bulletin of entomological research v. 81 (3): p. 233; 1991 Sep.
Includes
references.
Language: English
Descriptors: Entomology; Biotechnology; Genetic transformation;
Molecular
biology; Problem analysis; Traditional technology
109 NAL Call. No.: 1.98 AG84
Life-saving drugs could be genetically produced.
Mazzola, V.
Washington, D.C. : The Service; 1991 Aug.
Agricultural research - U.S. Department of Agriculture,
Agricultural Research
Service v. 39 (8): p. 10-11; 1991 Aug.
Language: English
Descriptors: Drugs; Blood coagulation; Clotting; Gene transfer;
Whey protein;
Pigs; Mice
110 NAL Call. No.: SF140.B54A55
Liposome-mediated DNA transfer to chicken sperm cells.
Squires, E.J.; Drake, D.
New York, N.Y. : Marcel Dekker; 1993.
Animal biotechnology v. 4 (1): p. 71-88; 1993. Includes
references.
Language: English
Descriptors: Chickens; Gene transfer; Liposomes
111 NAL Call. No.: 47.8 AM33P
Liver-specific expression of a phosphoenolpyruvate
carboxykinase-neo gene in
genetically modified chickens.
Cook, R.F.; Cook, S.J.; Savon, S.; McGrane, M.; Hartitz, M.;
Hanson, R.W.;
Hodgson, C.P.
Champaign, Ill. : Poultry Science Association; 1993 Mar.
Poultry science v. 72 (3): p. 554-567; 1993 Mar. Includes
references.
Language: English
Descriptors: Chickens; Transgenics; Liver; Retroviral vectors; Gene expression; Genetic engineering; Genetic markers; Dna hybridization
Abstract: In order to investigate the potential of the avian liver
for the
expression of recombinant proteins in vivo, replication-competent
retroviral
vectors were used to introduce a recombinant rat
phosphoenolpyruvate
carboxykinase promoter-driven neomycin resistance gene (PEPCKneo)
into early
Line 11 Leghorn embryos. After hatching, these birds possessed
apparently
intact PEPCKneo sequences in most tissues examined, however, the
neo protein
was expressed preferentially in the liver (up to .45% of total
cellular
protein). Therefore, the tissue specificity of the PEPCK promoter
from the rat
was retained in the chicken, although hormone responsiveness was
not observed.
Retroviral vectors used to transmit the genes were more stable
during passage
in either fibroblast cells or in the animal if the inserted genes
were
oriented in the same (sense) direction as the viral genome. After
Geneticin
drug selection in cultured cells, PEPCKneo mRNA was the predominant
recombinant species observed on Northern blots, whereas embryos
expressed
mostly the RNA species originating in the retroviral long terminal
repeats.
The results demonstrate the potential usefulness of liver-specific
gene
expression in chickens, as well as the transcriptional effects
observed when a
foreign promoter is introduced into the replication-competent
vector.
112 NAL Call. No.: 44.8 J822
Manipulation of gastrointestinal nutrient delivery in livestock.
Croom, W.J. Jr; Bird, A.R.; Black, B.L.; McBride, B.W.
Champaign, Ill. : American Dairy Science Association; 1993 Jul.
Journal of dairy science v. 76 (7): p. 2112-2124; 1993 Jul.
Includes
references.
Language: English
Descriptors: Livestock; Digestive absorption; Nutrient
requirements; Limiting
factors; Glucose; Infusion; Pancreas; Starch digestion; Growth
factors; Active
transport
Abstract: Discussed herein are the constraints of nutrient
delivery from the
gastrointestinal tract that are placed on postabsorptive synthetic
processes
in highly selected strains of domestic livestock or livestock
treated with
growth promotants exogenously or via transgenic manipulation.
Emphasis is
placed on the discussion of recent advances in the knowledge of the
regulation
and manipulation of digestion and the absorption by the intestinal
epithelium.
Slaframine, a muscarinic exocrine secretagogue with a high affinity
for the
gastrointestinal tract, and epidermal growth factor may have
practical
potential for the manipulation of digestion and absorption,
respectively.
Special consideration is given to energetic considerations that
must accompany
any manipulation of gastrointestinal function. Down-regulation and
up-regulation of mechanisms must be equally considered as this area
is
explored further.
113 NAL Call. No.: QH442.B5
Manipulation of the repertoire of digestive enzymes secreted into
the
gastrointestinal tract of transgenic mice.
Hall, J.; Ali, S.; Surani, M.A.; Hazelwood, G.P.; Clark, A.J.;
Simons, J.P.;
Hirst, B.H.; Gilbert, H.J.
New York, N.Y. : Nature Publishing Company; 1993 Mar.
Bio/technology v. 11 (3): p. 376-379; 1993 Mar. Includes
references.
Language: English
Descriptors: Mice; Transgenic animals; Clostridium thermocellum;
Structural
genes; Cellulase; Genetic transformation; Gene expression;
Recombinant DNA;
Pancreas; Protein secretion; Small intestine; Enzyme activity;
Cellulose
digestion
114 NAL Call. No.: 448.8 V81
Mapping and molecular characterization of a funtional thymidine
kinase from
Amsacta moorei entomopoxvirus.
Gruidl, M.E.; Hall, R.L.; Moyer, R.W.
Orlando, Fla. : Academic Press; 1992 Feb.
Virology v. 186 (2): p. 507-516; 1992 Feb. Includes references.
Language: English
Descriptors: Amsacta moorei; Entomopoxvirus; Thymidine kinase;
Genes; Gene
mapping; Cloning; Nucleotide sequences; Amino acid sequences;
Genetic
transformation; Gene expression; Phenotypes
Abstract: A thymidine kinase (TK) gene from the entomopoxvirus of
Amsacta
moorei (AmEPV) has been identified, mapped, cloned, and sequenced.
The AmEPV
TK was shown to be biologically functional as cloning of the gene
into a TK
derivative of the orthopoxvirus vaccinia creates a TK+ virus. The
gene has
been localized to a 1.5-kb EcoRI-Q DNA fragment which maps to the
far left end
of the viral genome. Sequence analysis reveals an open reading
frame (ORF) of
182 amino acids potentially encoding a polypeptide of 21.2 kDa.
Amino acid
homology comparisons indicate that the gene is most closely related
to the TKs
of a variety of poxviruses (approximately 45%) and less so to the
TKs of
vertebrates (approximately 40%). The TK from African swine fever
virus (ASF)
showed the least homology (31.4%) to the AmEPV TK gene, suggesting
that these
two viruses are not closely related although ASF shares some
biological
features of poxviruses, and both ASF and AmEPV can replicate within
arthropod
hosts.
115 NAL Call. No.: QP251.A1T5
Methods for producing transgenic bovine embryos from in vitro
matured and
fertilized oocytes.
Thomas, W.K.; Schnieke, A.; Seidel, G.E. Jr
Stoneham, Mass. : Butterworth-Heinemann; 1993 Oct.
Theriogenology v. 40 (4): p. 679-658; 1993 Oct. Includes
references.
Language: English
Descriptors: Cattle; Embryo transfer; Genetic engineering; Transgenics
Abstract: Microinjection and in vitro culture procedures were
developed to
produce transgenic bovine embryos after in vitro fertilization of
in vitro
matured oocytes. In Experiment I, zygotes were subjected to
pronuclear
microinjection of DNA 18 or 24 h following addition of spermatozoa
to oocytes.
Microinjections were performed in either Hepes-buffered TCM-199 or
modified
Dulbecco's phosphate-buffered saline without glucose. Viability of
embryos was
similar at both injection times and for both media, as determined
by
morphological evaluation after culturing embryos in vitro for 10 d.
In
Experiment II, microinjected embryos were cultured 1) in rabbit
oviducts, 2)
in vitro in a 5% CO2 in air, or 3) in a 5% CO2/5% O2/90% N2
incubator. There
were no significant differences between the 2 in vitro culture
environments.
The in vitro culture systems supported development of embryos
significantly
better than the rabbit oviducts; 33% of cleaved ova developed to
blastocysts
in vitro vs 10% in vivo; 98% of transferred ova were recovered from
the rabbit
oviducts. From both experiments, 6 of 92 blastocysts were positive
for the
microinjected DNA as determined by a polymerase chain reaction
followed by gel
electrophoresis.
116 NAL Call. No.: Q320.B56
Methods for the introduction of recombinant DNA into chicken
embryos.
Kopchick, J.J.; Mills, E.; Rosenblum, C.; Taylor, J.; Macken, F.;
Leung, F.;
Smith, J.; Chen, H.
Stoneham, Mass. : Butterworth Publishers; 1991.
Biotechnology (16): p. 275-293; 1991. In the series analytic:
Transgenic
Animals / Edited by Neal L. First; Florence P. Haseltime. Includes
references.
Language: English
Descriptors: Chick embryos; Recombinant DNA; Introduction;
Techniques;
Transgenics
117 NAL Call. No.: 448.8 AD9
Molecular biology and genetics of neurodegenerative diseases caused
by prions.
Prusiner, S.B.
San Diego, Calif. : Academic Press; 1992.
Advances in virus research v. 41: p. 241-280; 1992. Literature
review.
Includes references.
Language: English
Descriptors: Sheep; Goats; Cattle; Mink; Mice; Man; Scrapie; Bovine
spongiform
encephalopathy; Mink diseases; Human diseases; Proteins; Genes;
Replication;
Transgenics; Etiology; Infectivity; Molecular biology; Molecular
genetics;
Literature reviews
118 NAL Call. No.: QD415.A1C75
Molecular biology and transgenetics of prion diseases.
Prusiner, S.B.
Boca Raton, Fla. : CRC Press; 1991.
Critical reviews in biochemistry and molecular biology v. 26 (5/6):
p.
397-438; 1991. Literature review. Includes references.
Language: English
Descriptors: Scrapie; Scrapie agent; Purification; Transgenics;
Gene
expression; Cloning; Mice; Sheep; Goats; Literature reviews
119 NAL Call. No.: SF600.C82
Molecular biology and transgenetics of prions causing CNS
degeneration in
humans and animals.
Prusiner, S.B.
Dordrecht : Kluwer Academic Publishers; 1991.
Current topics in veterinary medicine and animal science v. 55: p.
59-82;
1991. In the series analytic: Sub-acute spongiform
encephalopathies / edited
by R. Bradley, M. Savey, and B. Marchant. Proceedings of a Seminar
in the CEC
Agricultural Research Programme, November 12-14, 1990, Brussels.
Literature
review. Includes references.
Language: English
Descriptors: Animals; Man; Genes; Disease transmission; Prions;
Literature
reviews
120 NAL Call. No.: 470 SCI2
Molecular biology of prion diseases.
Prusiner, S.B.
Washington, D.C. : American Association for the Advancement of
Science; 1991
Jun14.
Science v. 252: p. 1515-1522; 1991 Jun14. Includes references.
Language: English
Descriptors: Scrapie agent; Bovine spongiform encephalopathy;
Prions;
Molecular genetics; Gene expression
Abstract: Prions cause transmissible and genetic neurodegenerative
diseases,
including scrapie and bovine spongiform encephalopathy of animals
and
Creutzfeldt-Jakob and Gerstmann-Straussler-Scheinker diseases of
humans.
Infectious prion particles are composed largely, if not entirely,
of an
abnormal isoform of the prion protein, which is encoded by a
chromosomal gene.
A posttranslational process, as yet unidentified, converts the
cellular prion
protein into an abnormal isoform. Scrapie incubation times,
neuropathology,
and prion synthesis in transgenic mice are controlled by the prion
protein
gene. Point mutations in the prion protein genes of animals and
humans are
genetically linked to development of neurodegeneration. Transgenic
mice
expressing mutant prion proteins spontaneously develop neurologic
dysfunction
and spongiform neuropathology. Understanding prion diseases may
advance
investigations of other neurodegenerative disorders and of the
processes by
which neurons differentiate, function for decades, and then grow
senescent.
121 NAL Call. No.: QH359.J6
Molecular characterization and evolution of a duck mitochondrial
genome.
Ramirez, V.; Savoie, P.; Morais, R.
New York, N.Y. : Springer-Verlag; 1993 Sep.
Journal of molecular evolution v. 37 (3): p. 296-310; 1993 Sep.
Includes
references.
Language: English
Descriptors: Anas platyrhynchos; Fowls; Mitochondrial genetics;
Molecular
biology; Amino acid sequences; Evolution; Gene transfer; Nucleotide
sequences;
Ribosomal RNA; Transcription; Literature reviews
Abstract: We sequenced 6,478 bp of mitochondrial DNA from Peking
duck (Anas
platyrhyncos). Eight protein genes, 11 tRNAs, part of the small and
large
ribosomal subunits, and the control region sequences were compared
to
homologous chicken sequences. The gene organization in duck and
chicken is
identical but differs from other vertebrates in the juxtaposition
of the tRNA
Glu-ND6 genes next to the control region and in the lack of a
hairpinlike
structure between the genes for tRNA(Asn) and tRNA(Cys) used for
light-strand
replication. Protein, tRNA, and rRNA genes evolved mainly through
base
substitutions and small insertions and deletions. Transitions
greatly
outnumber transversions in the tRNA and rRNA genes, but this bias
is not
evident in protein genes; the control region has a higher
proportion of
transversions. The duck and chicken control regions show a high
frequency of
length mutations. Large A-T-rich nucleotide stretches dispersed
across the
region between the bidirectional transcription promoter and the
heavy-strand
replication origin in the chicken are absent in the duck. Sequence
elements
for heavy-strand replication in mammals are conserved in the duck
and chicken
control regions. Estimates of divergence for ribosomal RNAs and
proteins based
on total substitutions, transversions, and amino acid replacements
show that
all the duck/chicken values are lower than the corresponding
mammal/mammal
(cow, human, mouse) values. If paleontological data suggesting that
avian and
eutherian ordinal radiation occurred at approximately the same time
are
correct, this suggests that at great evolutionary distance, rate of
mitochondrial DNA evolution in birds is somewhat decelerated
compared to
mammals.
122 NAL Call. No.: 443 D39
Molecular perspectives on the genetics of mosquitoes.
Besansky, N.J.; Finnerty, V.; Collins, F.H.
San Diego, Calif. : Academic Press; 1992.
Advances in genetics v. 30: p. 123-184; 1992. Literature review.
Includes
references.
Language: English
Descriptors: Anopheles; Culex; Aedes; Genetic variation; Evolution;
Genomes;
Genetic transformation; Molecular genetics; Disease vectors;
Pesticide
resistance; Defense mechanisms; Oogenesis; Salivation; Host
parasite
relationships; Literature reviews
123 NAL Call. No.: QH426.D32
Morphological abnormalities, neonatal mortality, and reproductive
abnormalities in mice transgenic for diphtheria toxin genes that
are driven by
the promoter for adipocyte lipid binding protein.
Homanics, G.E.
New York, N.Y. : Wiley-Liss, Inc; 1991.
Developmental genetics v. 12 (5): p. 371-379; 1991. Includes
references.
Language: English
Descriptors: Mice; Transgenics; Genetic transformation;
Corynebacterium;
Bacterial toxins; Structural genes; Lipids; Binding proteins;
Promoters; Gene
expression; Adipocytes; Inheritance; Syndactyly; Bone formation;
Infertility;
Mortality; Newborn animals; Genetic engineering; Fat percentage;
Meat animals
Abstract: Transgenic mice were used in an experiment that was
designed to
serve as a model of a possible approach to reducing the amount of
carcass fat
in meat animals. The objective was to reduce the number of
adipocytes in
transgenic mice thereby restricting the capacity to accumulate
lipid. Our
approach employed the technique of genetic ablation. The promoter
for the
adipocyte lipid binding protein gene was used in an attempt to
direct
expression of diphtheria toxin genes specifically to adipocytes.
Three
diphtheria toxin genes were used; they encode, respectively, an
extremely
cytotoxic wild type toxin, a less toxic attenuated toxin, and a
nonfunctional
toxin. While it was not possible to accurately assess effects of
the
transgenes on lipid accumulation, several informative observations
were noted.
A large percentage of transgenic founder mice that harbor either
wild type or
attenuated toxin genes are morphologically abnormal, die as
neonates, or
exhibit reproductive abnormalities including sterility or failure
to transmit
the transgene to offspring. In contrast, mice that harbor the
nonfunctional
toxin gene or are nontransgenic rarely have these same
abnormalities. These
results suggest that the transgenic mice are expressing the
transgenes in
cells other than adipocytes and that the aberrant production of
functional
toxin is responsible for the congenital abnormalities. The
production of
morphological and reproductive abnormalities in transgenic animals
should be
useful for investigating normal developmental processes.
124 NAL Call. No.: QL495.A1I57
The mosquito dihydrofolate reductase gene functions as a dominant
selectable
marker in transfected cells.
Shotkoski, F.A.; Fallon, A.M.
Exeter : Pergamon Press; 1993 Dec.
Insect biochemistry and molecular biology v. 23 (8): p. 883-893;
1993 Dec.
Includes references.
Language: English
Descriptors: Aedes albopictus; Genetic transformation; Genetic
markers; Cell
culture; Dna; Genetic vectors; Methotrexate; Dihydrofolate
reductase
Abstract: An Aedes albopictus dihydrofolate reductase gene was
used to
construct two chimeric DNA vectors that functioned as dominant
selectable
markers in transfected, wild type mosquito cells. Stably
transformed clones
were recovered after 10-15 days in the presence of selective medium
containing
1 micromolar methotrexate. The transformed clones contained an
estimated
100-500 copies of transfected DNA per nucleus. Combined data from
Southern
blots and in situ hybridization to metaphase chromosomes indicated
that
transfected DNA was likely integrated into chromosomes both as
repeated
structures and as randomly integrated single copy molecules, with
minimal
rearrangement of coding sequences. Transfected DNA was stably
maintained under
selective conditions, but in some cases was lost when cells were
maintained
for prolonged periods in the absence of methotrexate. These
observations
provide a general framework for further development of stable gene
transfer
systems for mosquito cells in culture.
125 NAL Call. No.: SF140.B54A55
Mouse mammary tumor virus promoter directs high-level expression of
bovine
alpha S1 casein in the milk of transgenic heterozygous and
homozygous mice.
Yom, H.C.; Bremel, R.D.; First, N.L.
New York, N.Y. : Marcel Dekker; 1993.
Animal biotechnology v. 4 (1): p. 89-107; 1993. Includes
references.
Language: English
Descriptors: Transgenic animals; Alphas1-casein; Mice
126 NAL Call. No.: QH511.G6
Multiphasic analysis of growth curves for progeny of a somatotropin
transgenic
male mouse.
Koops, W.J.; Grossman, M.
Bar Harbor, Me. : Growth Publishing Company; 1991.
Growth, development, and aging : GDA v. 55 (3): p. 193-202; 1991.
Includes
references.
Language: English
Descriptors: Mice; Transgenics; Somatotropin; Genes; Man; Growth
curve; Growth
analysis; Growth rate; Tail; Liveweight gain; Equations
127 NAL Call. No.: QH511.G6
Multiphasic growth and allometry.
Koops, W.J.; Grossman, M.
Bar Harbor, Me. : Growth Publishing Company; 1991.
Growth, development, and aging : GDA v. 55 (3): p. 203-212; 1991.
Includes
references.
Language: English
Descriptors: Mice; Allometry; Growth rate; Growth analysis;
Transgenics;
Somatotropin; Man; Growth curve; Tail; Length; Liveweight gain;
Equations
128 NAL Call. No.: QK725.P532
The N- and C-terminal regions regulate the transport of wheat
gamma-gliadin
through the endoplasmic reticulum in Xenopus oocytes.
Altschuler, Y.; Rosenberg, N.; Harel, R.; Galili, G.
Rockville, Md. : American Society of Plant Physiologists; 1993 Apr.
The Plant cell v. 5 (4): p. 443-450; 1993 Apr. Includes
references.
Language: English
Descriptors: Triticum aestivum; Gliadin; Amino acid sequences;
Regulation;
Protein transport; Endoplasmic reticulum; Oocytes; Xenopus; Genetic
transformation; Transgenic animals; Mutants; Induced mutations;
Structural
genes
Abstract: Following sequestration into the endoplasmic reticulum
(ER), wheat
storage proteins are naturally either retained and packaged into
protein
bodies within this organelle or exported to the Golgi apparatus. To
identify
protein domains that control the sorting of wheat storage proteins
within the
ER, a wild-type gamma-gliadin storage protein as well as two of its
deletion
mutants, each bearing either of the two autonomous N- and
C-terminal regions,
were expressed in Xenopus oocytes. Our results demonstrated that
the
N-terminal region of the gliadin, which is composed of several
tandem repeats
of the consensus sequence PQQPFPQ, was entirely retained within the
ER and
accumulated in dense protein bodies. In contrast, the C-terminal
autonomous
region was efficiently secreted to the medium. The wild-type
gamma-gliadin,
containing both regions, was secreted at a lower rate and less
efficiently
than its C-terminal region. These results suggest that sorting of
the wheat
gamma-gliadin within the ER may be determined by a balance between
two
opposing signals: one functions in the retention and packaging of
the storage
protein within the ER, while the second renders the protein
competent for
export from this organelle to the Golgi apparatus.
129 NAL Call. No.: S494.5.B563N33
The new creation: an update on animal gene engineering.
Fox, M.W.
Ithaca, N.Y. : National Agricultural Biotechnology Council; 1992.
NABC report / (4): p. 49-61; 1992. In the series analytic: Animal
biotechnology: opportunities and challenges. Proceedings of the
fourth annual
NABC meeting, May 1992, College Station, Texas. Includes
references.
Language: English
Descriptors: Transgenic animals; Genetic engineering; New species
130 NAL Call. No.: A00110 New livestock can produce rare proteins. San Francisco, Calif. : The Chronical Publishing Co; 1991 Aug27. San Francisco chronicle. p. A3; 1991 Aug27.
Language: English
Descriptors: Animal products; Proteins; Genetic engineering;
Biological
production; Transgenics
131 NAL Call. No.: QL55.A1L33
The newest machine in the Garden: some ethical perspectives on
transgenic
animals.
Balk, R.A.
New York, N.Y. : Nature Publishing Company; 1991 Jan.
Lab animal v. 20 (1): p. 36-37; 1991 Jan. Includes references.
Language: English
Descriptors: Animals; Transgenics; Bioethics
132 NAL Call. No.: QL55.A1I43
Nuclear transplantation and embryo cloning in mammals.
Prather, R.S.
Washington, D.C. : Institute of Laboratory Animal Resources,
National Research
Council; 1991.
I.L.A.R. news v. 33 (4): p. 62-68; 1991. Includes references.
Language: English
Descriptors: Mammals; Cloning; Gene transfer
133 NAL Call. No.: S494.5.B563C87
An ovine metallothinein-pig somatotropin fusion gene promotes
growth in
transgenic rabbits and pigs.
Chen, Y.F.; Dai, Y.F.; Lin, A.X.; Chen, D.; Wei, C.X.; Zhang, Z.C.;
An, M.
Dordrecht : Kluwer Academic Publishers; 1993.
Current plant science and biotechnology in agriculture v. 15: p.
479-482;
1993. In the series analytic: Biotechnology in Agriculture /
edited by C.
You, Z. Chen, Y. Ding. Proceedings of the First Asia-Pacific
Conference on
Agricultural Biotechnology held August 20-24, 1992, Beijing, China.
Includes
references.
Language: English
Descriptors: Rabbits; Pigs; Transgenic animals; Genetic
transformation; Gene
transfer; Somatotropin; Structural genes; Recombinant DNA; Sheep;
Metallothionein; Promoters; Gene expression; Growth rate;
Liveweight gain
134 NAL Call. No.: SB13.I52
Pharmaceuticals from agriculture: manufacture or discovery?.
Turner, M.K.
Amsterdem : Elsevier; 1992 Dec.
Industrial crops and products v. 1 (2/4): p. 125-131; 1992 Dec.
Proceedings
of the "First European Symposium on Industrial Crops and Products,"
November
25-27, 1991, Maastricht, The Netherlands. Includes references.
Language: English
Descriptors: Drugs; Agricultural products; Medicinal plants;
Transgenic
animals; Manufacture; Synthesis
135 NAL Call. No.: SB951.P49
Pharmacokinetic studies of the recombinant juvenile hormone
esterase in
Manduca sexta.
Ichinose, R.; Kamita, S.G.; Maeda, S.; Hammock, B.D.
Orlando, Fla. : Academic Press; 1992 Jan.
Pesticide biochemistry and physiology v. 42 (1): p. 13-23; 1992
Jan. Includes
references.
Language: English
Descriptors: Manduca sexta; Insect control; Larvae;
Pharmacokinetics; Juvenile
hormones; Esterases; Genes; Genetic transformation; Spodoptera
frugiperda;
Heliothis virescens; Autographa californica; Gene transfer; Gene
expression;
Enzyme activity; Hydrolysis; Inactivation; Genetic regulation;
Enzyme
inhibitors
Abstract: Catalytically active juvenile hormone esterase (JHE) was
expressed
at a high level by Spodoptera frugiperda cells infected with
recombinant
Autographa californica nuclear polyhedrosis virus carrying the JHE
gene cloned
from the tobacco budworm, Heliothis virescens. JHE was partially
purified from
the culture medium by DEAE ion-exchange chromatography to a
specific activity
of 3000-5200 nmol juvenile hormone III metabolized per minute per
milligram of
protein after viral particles were inactivated by Triton X-100
following
ultracentrifugation. Pharmacokinetic studies showed that catalytic
activity
was cleared with first-order kinetics after the purified enzyme was
injected
into larval hemolymph of the tobacco hornworm, Manduca sexta and H.
virescens.
The half-life of JHE was approximately 1.2 hr in both species.
Experiments
were undertaken to elucidate the mechanism of clearance from M.
sexta larvae.
Persistence of catalytic activity in hemolymph in vitro and Western
blot
analysis suggested an uptake process of JHE by tissue(s), rather
than
degradation in the plasma. injection of a high dose of JHE resulted
in an
increased half-life and showed that the clearance process was
saturable. The
clearance rate was decreased by coinjection of a high dose of JHE
inactivated
by an irreversible inhibitor, paraoxon. Coinjection of an equal
amount of
bovine serum albumin did not influence the clearance rate of JHE.
These
results suggest that a specific process is involved in JHE
clearance from
hemolymph. N-linked oligosaccharides of JHE apparently were not
important in
the clearance of JHE from hemolymph.
136 NAL Call. No.: 44.8 J822
The potential for genetic change in milk fat composition.
Gibson, J.P.
Champaign, Ill. : American Dairy Science Association; 1991 Sep.
Journal of dairy science v. 74 (9): p. 3256-3266; 1991 Sep.
Literature
review. Includes references.
Language: English
Descriptors: Milk fat; Fatty acids; Chemical composition; Breed
differences;
Genetic change; Heritability; Transgenics; Economic impact;
Literature reviews
Abstract: Effecting genetic improvement requires genetic
variation, a
mechanism of selection, and an economic incentive for the
improvement. Limited
data suggest that there is within-breed genetic variation in milk
fat
composition, but accurate estimates are lacking. There is some
evidence for
modest differences among breeds. Substantial differences exist
among Species,
indicating that substantial genetic change in fat composition is
biologically
possible. The economic incentives for genetic change are not clear.
Changes in
fat composition that would improve the quality of one milk product
would often
be detrimental to other products. Such changes would best work
where
subpopulations produced milk for specific end products. Such
division of the
industry would be difficult to organize and might impede existing
improvement
programs. Changes in fat composition that increased consumer
acceptance of
milk products, such as reduced saturated fat concentration, might
increase the
market for milk products. However, only large changes in
composition are
likely to affect consumer acceptance; thus, the gradual changes of
conventional genetic improvement would produce little or no return
to the
breeder. Genetic changes that reduced processing costs or increased
product
value might have low to moderate economic value, inducing slow
rates of
change. Production of transgenic animals might provide a route for
genetic
alteration of fat composition in the future. Such improvement would
most
likely be cost effective in a subdivided production industry in
which milk
from cows of a particular genotype can be directed to a particular
milk
product. It is concluded that although alteration of fat
composition could be
achieved, it is unlikely to be an important component of genetic
improvement
of dairy cattle.
137 NAL Call. No.: TP248.14.N35 1990
Potential role of CGIAR centres in animal biotechnology transfer.
Doyle, J.J.
Nairobi : Initiatives Publishers; 1991.
Biotechnology in Kenya : proceedings of the National Conference on
Plant and
Animal Biotechnology, held February 25-March 3, 1990 at Kenyatta
International
Conference Centre, Nairobi, Kenya / A.M. Mailu, J.O. Mugah. p.
267-270; 1991.
Includes references.
Language: English
Descriptors: U.S.A.; Animal breeding; Genetic engineering; Gene
transfer;
Biotechnology
138 NAL Call. No.: TP248.65.E59T47 1991
Poxvirus vectors: mammalian cytoplasmic-based expression systems.
Moss, B.
New York : Plenum Press; 1991.
Applications of enzyme biotechnology / edited by Jeffery W. Kelly
and Thomas
O. Baldwin. p. 293-300; 1991. (Industry-university cooperative
chemistry
program symposia). Paper presented at the Texas A&M University
IUCCP Ninth
Annual Symposium, March 18-21, 1991, College Station, Texas.
Includes
references.
Language: English
Descriptors: Vaccinia virus; Genetic vectors; Recombinant DNA;
Genetic
transformation; Gene transfer; Structural genes; Viral antigens;
Recombinant
vaccines
139 NAL Call. No.: 442.8 Z34
Preferential extrachromosomal localization of exogenous DNA in
transgenic
silkworm Bombyx mori L.
Nikolaev, A.I.; Tchkonia, T.T.; Kafiani-Eristavi, C.A.; Tarantul,
V.Z.
Berlin, W. Ger. : Springer International; 1993 Jan.
M G G : Molecular and general genetics v. 236 (2/3): p. 326-330;
1993 Jan.
Includes references.
Language: English
Descriptors: Bombyx mori; Genetic transformation; Transgenics; Gene
transfer;
Direct DNAuptake; Rous sarcoma virus; Dna; Plasmids; Cytoplasmic
inheritance;
Repetitive DNA
Abstract: Transgenic silkworms (Bombyx mori L.) were obtained by
microinjection of plasmid pPrC-LTR1.5, which carries 1.5 DNA copies
of Rous
sarcoma virus (RSV) long terminal repeats (LTRs) inserted in the
vector
pBR322. The transgene was transmitted over the three generations
obtained up
to now. Most of the exogenous DNA failed to integrate into the
genome and
persisted as an extrachromosomal element that is subject to
rearrangements.
Plasmids carrying only part of the input DNA together with
fragments of
silkworm DNA were rescued from the transgenic animals. One of the
rescued
plasmids contained a sequence which belongs to a family of
evolutionarily
conserved repeated sequences.
140 NAL Call. No.: MnSUThesis vet han
The primordial germ cell as a vehicle for transgenesis in the
chicken Gallus
domesticus.
Han, Jae Yong
1991; 1991.
x, 167 leaves : ill. ; 29 cm. Includes bibliographical references.
Language: English
141 NAL Call. No.: SF481.2.P68
Primordial germ cells and the scope for genetic manipulation using
embryos.
Simkiss, K.
Northants, UK : Butterworths-Heinnemann; 1991.
Poultry Science Symposium v. 22: p. 125-136; 1991. In the series
analytic:
Avian Incubation / edited by S.G. Tullet. Meeting held Sept. 12-15,
1989,
Auchincruive, Ayr, Scotland. Includes references.
Language: English
Descriptors: Chick embryos; Germ cells; Germ line; Transgenics;
Genetic
engineering
142 NAL Call. No.: QL55.A1L33
Problems that limit or complicate breeding transgenic mice.
Donnelly, T.M.; Walsh-Mullen, A.
New York, N.Y. : Nature Publishing Company; 1991 Mar.
Lab animal v. 20 (3): p. 34-35; 1991 Mar. Includes references.
Language: English
Descriptors: Mice; Transgenics; Animal breeding
143 NAL Call. No.: CoFSQP273.T46 1991
Production of in vitro fertilized transgenic bovine embryos.
Thomas, Wendell Keith
1991; 1991.
ii, 65 leaves ; 28 cm. Includes bibliographical references.
Language: English
Descriptors: Fertilization in vitro; Embryo transplantation; Cattle
144 NAL Call. No.: 475 EX7
Production of pharmaceutical proteins in milk.
Wilmut, I.; Archibald, A.L.; McClenaghan, M.; Simons, J.P.;
Whitelaw, C.B.A.;
Clark, A.J.
Basel : Birkhauser; 1991 Sep15.
Experientia v. 47 (9): p. 905-912; 1991 Sep15. Literature review.
Includes
references.
Language: English
Descriptors: Livestock; Pharmaceutical proteins; Milk products;
Gene transfer;
Gene expression; Transgenics; Milk proteins; Milk composition;
Literature
reviews
145 NAL Call. No.: TP248.2.B46
Production of recombinant proteins by baculovirus-infected gypsy
moth cells.
Betenbaugh, M.J.; Balog, L.; Lee, P.S.
New York, N.Y. : American Institute of Chemical Engineers; 1991
Sep.
Biotechnology progress v. 7 (5): p. 462-467; 1991 Sep. Includes
references.
Language: English
Descriptors: Lymantria dispar; Heliothis virescens; Spodoptera
frugiperda;
Nuclear polyhedrosis viruses; Genetic engineering; Recombinant
DNA; Genetic
transformation; Beta-galactosidase; Reporter genes; Cell lines;
Cell culture;
Cell suspensions; Gene expression; Protein synthesis; Vectors
146 NAL Call. No.: Q320.B56
Production of sheep transgenic for growth hormone genes.
Rexroad, C.E. Jr
Stoneham, Mass. : Butterworth Publishers; 1991.
Biotechnology (16): p. 259-263; 1991. In the series analytic:
Transgenic
Animals / Edited by Neal L. First; Florence P. Haseltime. Includes
references.
Language: English
Descriptors: Sheep; Transgenics; Somatotropin; Genes; Growth;
Improvement;
Gene transfer
147 NAL Call. No.: 49 J82
Production of the mouse whey acidic protein in transgenic pigs
during
lactation.
Shamay, A.; Solinas, S.; Pursel, V.G.; McKnight, R.A.; Alexander,
L.; Beattie,
C.; Hennighausen, L.; Wall, R.J.
Champaign, Ill. : American Society of Animal Science; 1991 Nov.
Journal of animal science v. 69 (11): p. 4552-4562; 1991 Nov.
Includes
references.
Language: English
Descriptors: Pigs; Transgenics; Genes; Whey protein; Sow lactation;
Sow milk;
Phenotypes; Chromosomes; Agalactia
Abstract: The mouse whey acidic protein (WAP) gene was introduced
into the
genome of pigs and its expression was analyzed in the mammary
gland. Mouse WAP
was detected in milk of lactating females from five lines at levels
between .5
and 1.5 g/liter, thereby representing as much as 2% of the total
milk
proteins. The corresponding mRNA was expressed in mammary tissue at
levels
similar to those of pig beta-lactoglobulin and beta-casein. The
pattern of WAP
secretion in three pigs over a period of 6 wk was quantitatively
similar to
that of pig beta-lactoglobulin. From the eight transgenic pigs
analyzed, three
successfully completed one lactational period, but five pigs
stopped lactating
a few days after parturition. Our results show that it is possible
to produce
large quantities of a foreign protein in milk of pigs over a full
lactational
period. However, expression of WAP can compromise the mammary gland
and render
it nonfunctional.
148 NAL Call. No.: 475 EX7
Production of transgenic birds.
Shuman, R.M.
Basel : Birkhauser; 1991 Sep15.
Experientia v. 47 (9): p. 897-905; 1991 Sep15. Literature review.
Includes
references.
Language: English
Descriptors: Fowls; Gene transfer; Transgenics; Genetic
engineering;
Retroviral vectors; Literature reviews
149 NAL Call. No.: Q320.B56
Production of transgenic cattle by pronuclear injection.
Bondioli, K.R.; Biery, K.A.; Hill, K.G.; Jones, K.B.; De Mayo, F.J.
Stoneham, Mass. : Butterworth Publishers; 1991.
Biotechnology (16): p. 265-273. ill; 1991. In the series analytic:
Transgenic
Animals / Edited by Neal L. First; Florence P. Haseltime. Includes
references.
Language: English
Descriptors: Cattle; Transgenics; Production; Pronucleus;
Injection; Dna;
Embryo culture; Embryo transfer; Animal tissues; Sampling; Analysis
150 NAL Call. No.: QP251.A1T5
Production of transgenic mice and rabbits that carry and express
the human
tissue plasminogen activator cDNA under the control of a bovine
alpha S1
casein promoter.
Riego, E.; Limonta, J.; Aguilar, A.; Perez, A.; Armas, R. de;
Solano, R.;
Ramos, B.; Castro, F.O.; Fuente, J. de la
Stoneham, Mass. : Butterworth-Heinemann; 1993 May.
Theriogenology v. 39 (5): p. 1173-1185; 1993 May. Includes
references.
Language: English
Descriptors: Rabbits; Mice; Transgenic animals; Plasminogen activator; Genes
Abstract: One-cell embryos from mice and rabbits were
microinjected with a
hybrid gene composed of 1.6 kilobases (kb) promoter/regulatory
sequences of
the bovine alpha S1 casein gene fused to the complementary DNA
(cDNA) encoding
for the human tissue plasminogen activator (htPA) and 3'
untranslated
sequences from rabbit beta-globin and SV 40 genes. Transgenic mice
and rabbits
that carry the htPA gene were obtained. In mice, 11 founder females
were
generated, and 6 of them expressed low levels (about 50
microgram/ml) of htPA
in their milk. Some of the transgenic mice showed rearrangements of
the
microinjected DNA sequences as judged by Southern blot analysis. A
position-dependent expression of the transgene is suspected to
occur. The only
live-born founder transgenic rabbit obtained was a male, and it
transmitted
the transgene in a Mendelian fashion to F1 females, which expressed
htPA at
very low levels (8 to 50 ng/l). Although the 1.6-kb bovine alpha S1
casein
promoter that was used directs the synthesis of htPA specifically
to the
mammary gland, it may not be sufficient for a high level of
expression.
151 NAL Call. No.: 500 N21P
Profound differences in potassium current properties of normal and
Rous
sarcoma virus-transformed chicken embryo fibroblasts.
Repp, H.; Draheim, H.; Ruland, J.; Seidel, G.; Beise, J.; Presek,
P.; Dreyer,
F.
Washington, D.C. : The Academy; 1993 Apr15.
Proceedings of the National Academy of Sciences of the United
States of
America v. 90 (8): p. 3403-3407; 1993 Apr15. Includes references.
Language: English
Descriptors: Chick embryos; Electrophysiology; Fibroblasts; Gene
expression;
Genetic transformation; Ions; Potassium; Rous sarcoma virus
Abstract: The membrane currents of chicken embryo fibroblasts
(CEFs)
transformed by Rous sarcoma virus (RSV) were compared with the
currents of
their nontransformed counterparts by using the whole-cell
patch-clamp
technique. In nontransformed CEFs, the main membrane current is a
delayed
outward K+ current that is sensitive to tetraethylammonium ion but
insensitive
to 4-aminopyridine. This K+ current is almost independent of the
intracellular
Ca2+ concentration and becomes completely inactivated at positive
membrane
potentials with a time constant of about 10 s at +30 mV. In
contrast,
transformed CEFs exhibit a noninactivating K+ current that
strongly, depends
on the intracellular Ca2+ concentration. This Ca2+-dependent K+
current is
blocked by the scorpion toxin charybdotoxin with an IC50 value of
19 nM,
whereas the K+ current of normal CEFs is insensitive to
charybdotoxin (up to
300 nM). The K+ current properties of transformed CEFs were also
found after
microinjection of purified, enzymatically active pp60v-src into
normal CEFs
but not after infection of CEFs with the Rous-associated virus
RAV5, which
lacks the v-src oncogene. Our results suggest that the oncogene
product
pp60v-src modulates existing K+ channel proteins, leading to
profound
electrophysiological and pharmacological alterations of the K+
current
properties in RSV-transformed CEFs. Furthermore, our experiments
identify for
the first time K+ channels as possible substrates of pp60v-src.
152 NAL Call. No.: TA166.T72
The proof of the cloning is in the eating.
Geisow, M.
Cambridge : Elsevier Publications; 1991 Jan.
Trends in biotechnology v. 9 (1): p. 5-7. ill; 1991 Jan. Includes
references.
Language: English
Descriptors: Livestock; Plants; Modification; Biotechnology;
Genetic
engineering; Transgenics; Food products; Risk; Assessment
153 NAL Call. No.: 448.8 V81
Properties of bovine papillomavirus E1 mutants.
Chiang, C.M.; Broker, T.R.; Chow, L.T.
Orlando, Fla. : Academic Press; 1992 Dec.
Virology v. 191 (2): p. 964-967; 1992 Dec. Includes references.
Language: English
Descriptors: Bovine papillomavirus; Mutants; Genetic
transformation; Dna; Dna
replication; Plasmids; Promoters; Phenotypes; Transfection; Mice;
Cell lines
Abstract: Ostensibly comparable mutants of bovine papillomavirus
type 1
(BPV-1) affecting the E1 open reading frame that were constructed
in several
laboratories have been reported to exhibit either reduced or
increased
transformation efficiencies in established mouse cell lines
relative to
wild-type BPV-1 DNA. To resolve these discrepancies, we have
reexamined many
of the mutants in mouse C127 cells by using focus formation assays.
Our
primary conclusions are that all E1 mutants tested consistently
generated
reduced numbers of transformants and that the reduced
transformation was not
due to cell toxicity associated with E1 mutations, as had been
proposed. Our
results can best be explained by the inability of the E1 mutants to
replicate
extrachromosomally, therefore leading to a rapid loss of the BPV-1
DNA and
consequently, reduced transformation. In support of this
hypothesis, we
demonstrated that the human papillomavirus type 11 E1 protein was
able to
suppress BPV-1 transformation, probably because of interference
with BPV-1
replication. Therefore, we attribute the phenotypic disparities
reported by
the various laboratories to still undefined differences in assay
conditions.
154 NAL Call. No.: TP248.13.B54
Puerto Rico selects Tufts to develop transgenic-swine breeding
stock.
New York : McGraw-Hill :.; 1991 Apr15.
Biotechnology newswatch v. 11 (8): p. 9; 1991 Apr15.
Language: English
Descriptors: Puerto Rico; Pig breeds; Genetic engineering;
Transgenics;
Research support; Fsh
155 NAL Call. No.: SF140.B54A55
Quantitative collection of milk and active recombinant proteins
from the
mammary glands of transgenic mice.
Stinnakre, M.G.; Devinoy, E.; Thepot, D.; Chene, N.; Bayat-Samardi,
M.;
Grabowski, H.; Houdebine, L.M.
New York, N.Y. : Marcel Dekker; 1992.
Animal biotechnology v. 3 (2): p. 245-255; 1992. Includes
references.
Language: English
Descriptors: Transgenic animals; Milk proteins
156 NAL Call. No.: QP251.M64
Recent advances in sperm cell mediated gene transfer.
Lauria, A.; Gandolfi, F.
New York, N.Y. : Wiley-Liss, Inc; 1993 Oct.
Molecular reproduction and development v. 36 (2): p. 255-257; 1993
Oct. Paper
presented at an "International Symposium on Animal Biotechnology",
Oct. 15-17,
1991, Kyoto, Japan. Includes references.
Language: English
Descriptors: Gene transfer; Spermatozoa
157 NAL Call. No.: QH442.G393
Recent developments in animal patenting.
Matthews, K.I.
Cambridge, Mass. : Council for Responsible Genetics; 1993 Mar.
Genewatch v. 8 (5/6): p. 5; 1993 Mar.
Language: English
Descriptors: U.S.A.; Livestock; Genetic engineering; Recombinant
DNA;
Laboratory animals; Mice; Transgenic animals; Patents; Legislation
158 NAL Call. No.: QP251.M64
Recent progress in the transgenic modification of swine and sheep.
Pursel, V.G.; Rexroad, C.E.
New York, N.Y. : Wiley-Liss, Inc; 1993 Oct.
Molecular reproduction and development v. 36 (2): p. 251-254; 1993
Oct. Paper
presented at an "International Symposium on Animal Biotechnology",
Oct. 15-17,
1991, Kyoto, Japan. Includes references.
Language: English
Descriptors: Pigs; Sheep; Transgenic animals
159 NAL Call. No.: QH442.B5
Recombinant baculovirus vectors expressing
glutathione-S-transferase fusion
proteins.
Davies, A.H.; Jowett, J.B.M.; Jones, I.M.
New York, N.Y. : Nature Publishing Company; 1993 Aug.
Bio/technology v. 11 (8): p. 933-936; 1993 Aug. Includes
references.
Language: English
Descriptors: Baculovirus; Genetic vectors; Gene transfer;
Structural genes;
Glutathione transferase; Recombinant DNA; Gene expression;
Spodoptera
frugiperda; Cell lines
160 NAL Call. No.: TP248.2.B46
Recombinant beta-galactosidase production in serum-free medium by
insect cells
in a 14-L airlift bioreactor.
King, G.A.; Daugulis, A.J.; Faulkner, P.; Goosen, M.F.A.
New York, N.Y. : American Institute of Chemical Engineers; 1992
Nov.
Biotechnology progress v. 8 (6): p. 567-571; 1992 Nov. Includes
references.
Language: English
Descriptors: Spodoptera frugiperda; Recombinant DNA; Gene
transfer; Gene
expression; Beta-galactosidase; Cell suspensions; Culture media;
Bioreactors
161 NAL Call. No.: QH442.6.C88 1992
Regulation and discussion on genetic modification of animals the
situation in
the European Community, the Netherlands, the United Kingdom,
Germany, Denmark,
France, and the United States.
Custers, Rene; Sterrenberg, Lydi
Nederlandse Organisatie voor Technologisch Aspectenonderzoek
The Hague : Netherlands Organization for Technology Assessment,;
1992.
vi, 86 p. : ill. ; 29 cm. (Werkdocument (Nederlandse Organisatie
voor
Technologisch Aspectenonderzoek) ; W38.). May 1992. Includes
bibliographical
references.
Language: English
Descriptors: Transgenic animals; Animal genetic engineering; Animal biotechnology
162 NAL Call. No.: QR360.J6
Replication-competent retrovirus vectors for the transfer and
expression of
gene cassettes in avian cells.
Petropoulos, C.J.; Hughes, S.H.
Washington, D.C. : American Society for Microbiology; 1991 Jul.
Journal of virology v. 65 (7): p. 3729-3737; 1991 Jul. Includes
references.
Language: English
Descriptors: Avian oncovirus; Rous sarcoma virus; Retroviral
vectors; Gene
transfer; Gene expression; Chloramphenicol acetyltransferase;
Reporter genes;
Promoters; Fowls; Actin; Mice; Metallothionein; Fibroblasts;
Quails; Reverse
transcriptase; Enzyme activity; Genomes
Abstract: We have constructed a series of replication-competent
retrovirus
vectors to introduce and express gene cassettes in avian cells. To
characterize these vectors, we inserted the coding sequences for
the bacterial
chloramphenicol acetyltransferase (CAT) gene linked to the chicken
beta-actin
gene promoter or the mouse metallothionein 1 gene promoter. In all
cases, we
found the structure of integrated proviruses to be stable during
serial cell
passage in vitro. Chloramphenicol acetyltransferase activity was
detected
biochemically and immunocytochemically in infected cells. Cassettes
were
inserted in the vectors in the same or in the opposite orientation
with
respect to viral transcription. Although both orientations were
functional,
the cassettes inserted in the forward orientation were usually
expressed at
higher levels than the corresponding backward constructions. The
level of
expression was strongly influenced by surrounding proviral
sequences,
particularly by the transcriptional enhancer elements within the
retrovirus
long terminal repeat sequences. Expression was higher with vectors
that
contained the polymerase (pol) region of the Bryan high-titer
strain of Rous
sarcoma virus. Inclusion of the Bryan pol region also improved
vector
replication in the chemically transformed quail fibroblast line
QT6.
163 NAL Call. No.: QH506.A1M622
Restriction endonuclease analysis of autonomously replicating
molecules
containing exogenous DNA in a transgenic silkworm line.
Chkoniya, T.T.; Nikolaev, A.I.; Kafiani-Eristavi, K.A.
New York, N.Y. : Consultants Bureau; 1992 Apr.
Molecular biology v. 25 (5,pt.2): p. 1121-1129; 1992 Apr.
Translated from:
Molekuliarnaia biologiia, v. 25 (5, pt. 2), 1991, p. 1427-1436.
(QH506.A1M62).
Includes references.
Language: English; Russian
Descriptors: Silkworms; Lines; Transgenics; Dna; Plasmids; Rous
sarcoma virus;
Nucleotide sequences; Restriction mapping; Genetic engineering
164 NAL Call. No.: TP368.T73
A role for transgenic animals in food production?.
McEvoy, T.G.; Robinson, J.J.; Sreenan, J.M.
Cambridge, U.K. : Elsevier Trends Journals; 1992 Nov.
Trends in food science & technology v. 3 (11): p. 294-302; 1992
Nov.
Literature review. Includes references.
Language: English
Descriptors: Animals; Transgenics; Food production; Food industry;
Literature
reviews
165 NAL Call. No.: 381 J824
Selective expression of trypsin fusion genes in acinar cells of the
pancreas
and stomach of transgenic mice.
Davis, B.P.; Hammer, R.E.; Messing, A.; MacDonald, R.J.
Baltimore, Md. : American Society for Biochemistry and Molecular
Biology; 1992
Dec25.
The Journal of biological chemistry v. 267 (36): p. 26070-26077;
1992 Dec25.
Includes references.
Language: English
Descriptors: Gene expression; Transgenics; Trypsin; Somatotropin;
Pancreas;
Stomach; Mice
Abstract: Fusion genes combining the 5'-transcriptional regulatory
region of
the rat trypsin I gene and the structural gene of human growth
hormone as a
reporter were expressed to the high levels characteristic of the
endogenous
trypsin I gene selectively in the acinar cells of the pancreas of
transgenic
mice. As little as 232 base pairs of trypsin gene sequences
containing the
transcriptional start site and upstream promoter elements were
sufficient to
direct pancreatic expression. The tissue-specific expression was
controlled
transcriptionally. Trypsin-human growth hormone fusion transgenes
also were
expressed, although at low levels, in the stomach, an unexpected
site for the
expression of pancreatic digestive enzymes. Expression in the
stomach of
endogenous trypsin, elastase, and amylase genes in both normal and
transgenic
mice verified that transgene expression was consistent with normal
expression
of pancreatic genes. Endogenous amylase colocalizes with pepsinogen
in the
acinar cell-like Chief cells of the glandular portion of the mouse
stomach.
The expression of pancreatic genes in stomach cells is probably the
consequence of similar developmental origins of pancreatic and
gastric acinar
cells from the primordial gut.
166 NAL Call. No.: 448.8 V81
Small deletion in v-src SH3 domain of a transformation defective
mutant of
Rous sarcoma virus restores wild type transforming properties.
Dezelee, P.; Barnier, J.V.; Hampe, A.; Laugier, D.; Marx, M.;
Galibert, F.;
Calothy, G.
Orlando, Fla. : Academic Press; 1992 Aug.
Virology v. 189 (2): p. 556-567; 1992 Aug. Includes references.
Language: English
Descriptors: Rous sarcoma virus; Mutants; Mutations; Deletions;
Genes; Genetic
transformation; Protein kinase; Enzyme activity; Nucleotide
sequences; Amino
acid sequences; Viral morphology; Plasmids; Transfection; Chimeras
Abstract: RSV mutant virus PA101T was obtained while assaying the
tumorigenicity of parental PA101 virus in chickens. PA101 is a
transformation
defective mutant of RSV which has a low src kinase activity.
However, PA101
retained a temperature-sensitive ability to induce sustained
proliferation of
neuroretina cells. PA101T appeared as a wild-type phenotype
revertant of
PA101. Molecular cloning and sequencing of PA101T showed that this
reversion
is due to additional mutations in PA101 src gene. These mutations
are a
deletion eliminating three amino acids in the N-terminal region of
SH3 domain
and mutation of Ala 426 to Val. Analysis of the properties of
chimeric src
genes associating either half of PA101T with the complementary
regions of
PA101 or wild-type virus showed that the N-terminal moiety of
PA101T src,
which contains the deletion, confers wild-type transforming
properties,
whereas its C-terminal moiety, which contains single amino acid
mutation,
confers a partially temperature-sensitive phenotype. These results
are
consistent with other reports showing that mutations or deletions
in this
region of SH3 activate the transforming potential of c-src. They
support the
hypothesis that the N-terminal region of SH3 interacts with a
cellular
negative regulator of src activity.
167 NAL Call. No.: QL55.A1I43
Standardized nomenclature for transgenic animals.
Washington, D.C. : Institute of Laboratory Animal Resources,
National Research
Council; 1992.
I.L.A.R. news v. 34 (4): p. 45-52; 1992. Includes references.
Language: English
Descriptors: Transgenic animals; Nomenclature
168 NAL Call. No.: 47.8 B77
Sterilising embryos for transgenic chimaeras.
Aige-Gil, V.; Simkiss, K.
Oxfordshire : Carfax Publishing Company; 1991 Jul.
British poultry science v. 32 (3): p. 427-438; 1991 Jul. Includes
references.
Language: English
Descriptors: Chick embryos; Chimeras; Transgenics; Ultraviolet
radiation;
Sterilization; Wavelengths; Abnormalities; Embryonic development
169 NAL Call. No.: QP251.A1T5
Strategies to express factor VIII gene constructs in the ovine
mammary gland.
Halter, R.; Carnwath, J.; Espanion, G.; Herrmann, D.; Lemme, E.;
Niemann, H.;
Paul, D.
Stoneham, Mass. : Butterworth-Heinemann; 1993 Jan.
Theriogenology v. 39 (1): p. 137-149; 1993 Jan. Paper presented at
the
"Annual Conference of the International Embryo Transfer Society,"
January
10-12, 1993, Baton Rouge, Louisiana. Includes references.
Language: English
Descriptors: Sheep; Mammary glands; Gene expression; Transgenics
Abstract: The transgenic technology focused on the production of
recombinant
proteins of therapeutic value in the milk of mammals has been
increasingly
successful in recent years. We have approached the problem of
expressing human
coagulation factor VIII in the lactating mammary gland of sheep by
employing
the whey acidic protein and the beta-lactoglobulin promoter
elements to drive
transcription of factor VIII cDNA in appropriate gene constructs.
To
understand and eventually optimize expression of the factor VIII
cDNA in
transgenic animals, several classes of constructs were produced, in
which
expression is controlled by either the well characterized murine
metallothionein I promoter or by one of the two mammary
gland-specific
promoter elements. In attempts to increase the efficiency of factor
VIII
production in transgenic animals, factors VIII cDNA-containing
constructs were
produced that include the introns of the metallothionein gene
and/or that have
had the sequences encoding the B-domain of factor VIII deleted.
Transgenic
mice and sheep have been obtained by microinjection of some of
these
constructs into zygotes and factor VIII gene expression in
lactating animals
is under investigation.
170 NAL Call. No.: QR360.J6
Structural analysis and transcriptional mapping of the Marek's
disease virus
gene encoding pp38, an antigen associated with transformed cells.
Cui, Z.; Lee, L.F.; Liu, J.L.; Kung, H.J.
Washington, D.C. : American Society for Microbiology; 1991 Dec.
Journal of virology v. 65 (12): p. 6509-6515; 1991 Dec. Includes
references.
Language: English
Descriptors: Marek's disease virus; Genes; Phosphoproteins;
Nucleotide
sequences; Genetic transformation
Abstract: The gene encoding a Marek's disease virus (MDV) pp38
phosphoprotein
has been identified, sequenced, and localized to the BamHI H
fragment to the
left of the putative MDV origin of replication. The open reading
frame was
defined by sequencing of a lacZ-pp38 fusion protein gene from a
lambdagt11
expression library. The entire open reading frame is 290 amino
acids long and
codes for a protein with a calculated molecular weight of 31,169,
compared
with the size of 38 kDa of the phosphorylated form estimated by
sodium dodecyl
sulfate-polyacrylamide gel electrophoresis. S1 nuclease protection
analysis
showed that the pp38 gene is transcribed leftward as an unspliced
mRNA. On the
basis of transcriptional mapping studies, the pp38 transcript is
predicted to
be about 1.8 kb in length without a poly(A) sequence. Its
promoter-enhancer
region overlaps that of the major rightward BamHI H 1.8-kb
transcript
implicated in tumor induction. This region contains Oct-1, Sp1, and
CCAAT
motifs as well as the putative origin of replication. The pp38
protein is the
only presently known antigen that is consistently associated with
the
transformation state. It may play a significant role in MDV
transformation.
171 NAL Call. No.: S1.S68
Study of expression of beta-galactosidase gene in transgenic early
embryos of
rabbits.
Gogolevskii, P.A.; Goldman, I.L.; Gusev, V.V.; Zhadanov, A.B.;
Kaurova, S.V.;
Kuznetsov, A.V.; Sobennikova, L.L.; Ernst, L.K.
New York, N.Y. : Allerton Press; 1991.
Soviet agricultural sciences (10): p. 37-40; 1991. Translated
from:
Vsesoiuznaia akademiia sel'skokhoziaistvennykh nauk. Includes
references.
Language: English; Russian
Descriptors: Rabbits; Embryos; Transgenics; Beta-galactosidase;
Gene
expression; Reporter genes; Dna; Synthesis; Zygotes; Genomes;
Transcription
172 NAL Call. No.: MnSUThesis stp yoon
Study on selection of transgenic goldfish.
Yoon, Sung-Joo
1991; 1991.
viii, 133 leaves : ill. ; 29 cm. Includes bibliographical
references.
Language: English
173 NAL Call. No.: QP1.C6
Surrogate eggs, chimaeric embryos and transgenic birds.
Simkiss, K.
Oxford: Pergamon Press Ltd; 1993 Mar.
Comparative biochemistry and physiology : A : Comparative
physiology v. 104
(3): p. 411-417; 1993 Mar. Includes references.
Language: English
Descriptors: Poultry; Transgenic animals; Embryos; Chimeras; Embryo
culture;
Germ line; Genetic engineering; Reviews
Abstract: The embryo of the domestic fowl is one of the best
studied examples
of vertebrate development. A mixture of commercial interests,
availability and
ease of study have produced a wealth of descriptive and
experimental data for
understanding its embryology (Lillie, 1919) but in the past decade
an entirely
different set of propositions have been posed. These range from
queries about
the possibility of raising the progeny of endangered species in
"surrogate
eggs" through to the use of the techniques of genetic engineering
in the
poultry industry. This article will briefly consider a number of
those
possibilities and indicate some of the surprising aspects of
comparative
physiology and biochemistry that are relevant to them. In the first
part
consideration is given to the conditions necessary to develop an
embryo in
culture while the second section is involved with genetic and
species
manipulations.
174 NAL Call. No.: 472 N21
Targeted misexpression of Hox-4.6 in the avian limb bud causes
apparent
homeotic transformations.
Morgan, B.A.; Izpisua-Belmonte, J.C.; Duboule, D.; Tabin, C.J.
London : Macmillan Magazines Ltd; 1992 Jul16.
Nature v. 358 (6383): p. 236-239; 1992 Jul16. Includes references.
Language: English
Descriptors: Chick embryos; Limbs; Embryonic development; Gene
expression;
Genetic transformation; Replication; Retroviral vectors
Abstract: In the limb bud the 5' members of the Hox-4 gene cluster
are
expressed in a nested set of overlapping domains which are
progressively
restricted in the posterior and distal directions. These domains
arise early
in limb bud development and come to approximate the primordia of
the major
structural elements of the limb along the anterior/posterior axis
(Fig. 1).
This pattern, and the fact that surgical manipulations which lead
to mirror
image duplications along the anterior/posterior axis give rise to
mirror image
duplications of the domains of expression of these genes, have led
to the
proposal that these transcription factors specify positional
identity along
the anterior/posterior axis. Here we test this hypothesis directly
using
replication-competent retroviral vectors to expand the domain of
expression of
the Hox-4.6 gene anteriorly during limb development in vivo. We
report that
alteration of the domain of expression of the Hox-4.6 gene in the
developing
limb leads to reproducible pattern alterations consistent with a
posterior
homeotic transformation.
175 NAL Call. No.: QD341.A2N8
Tissue-specific expression in the salivary glands of transgenic
mice.
Mikkelsen, T.R.; Brandt, J.; Larsen, H.J.; Larsen, B.B.; Poulsen,
K.;
Ingerslev, J.; Din, N.; Hjorth, J.P.
Oxford : IRL Press; 1992 May11.
Nucleic acids research v. 20 (9): p. 2249-2255; 1992 May11.
Includes
references.
Language: English
Descriptors: Salivary glands; Protein secretion; Animal proteins;
Genes; Gene
transfer; Gene expression; Transgenics; Mice
Abstract: Using a DNA construct, named Lama, derived from the
murine parotid
secretory protein (PSP) gene, we have obtained salivary gland
specific gene
expression in transgenic mice. Lama is a PSP minigene and allows
analysis of
the PSP gene 51 regulatory region by transgenesis. We show here
that the
regulatory region included in Lama with 4.6 kb of 5' flanking
sequence is
sufficient to direct expression specifically to the salivary
glands. The
expression level in the parotid gland is only about one percent of
the PSP
mRNA level, while that of the sublingual gland is near the PSP mRNA
level.
This suggests significant differences in the PSP gene regulation in
the two
glands. in addition, Lama is a secretory expression vector in which
cDNAs or
genomic fragments can be inserted. We demonstrate that the Lama
construct can
direct the expression of a heterologous cDNA encoding the
C-terminal peptide
of human factor VIII to salivary glands and that the corresponding
peptide is
secreted into saliva.
176 NAL Call. No.: 49 J82
Transferrin- and albumin-directed expression of growth-related
peptides in
transgenic sheep.
Rexroad, C.E. Jr; Mayo, K.; Bolt, D.J.; Elsasser, T.H.; Miller,
K.F.;
Behringer, R.R.; Palmiter, R.D.; Brinster, R.L.
Champaign, Ill. : American Society of Animal Science; 1991 Jul.
Journal of animal science v. 69 (7): p. 2995-3004; 1991 Jul.
Includes
references.
Language: English
Descriptors: Sheep; Transgenics; Structural genes; Controlling
elements;
Hormones; Growth; Feed conversion; Blood sugar; Insulin; Northern
blotting;
Animal tissues; Gene expression; Diabetes
Abstract: Chimeric genes containing either the mouse transferrin
(Trf)
enhancer/promoter fused to the structural sequences encoding bovine
growth
hormone (GH) or the mouse albumin (Alb) enhancer/promoter fused to
the gene
for human growth hormone-releasing factor (GRF) were microinjected
into sheep
zygotes. A low percentage of resulting transgenic sheep chronically
expressed
the respective genes, resulting in elevated plasma concentrations
of
circulating GH or GRF, respectively. Growth hormone-releasing
factor
expression induced elevated plasma levels of endogenous GH
production. In
addition, elevated levels of circulating insulin-like growth
factor-I were
observed in the bovine GH-expressing Trf transgenic sheep. Growth
of these
founder transgenic sheep relative to controls were not enhanced. In
part, this
may be due to the development of the diabetic condition exhibited
by both
transgenic groups. These results demonstrate that the mouse Trf and
Alb
enhancer/promoters are active in sheep and suggest that alternate
strategies
for expressing growth-related genes may be required to modulate
growth in
sheep.
177 NAL Call. No.: QH442.B5
Transformation of microbes, plants and animals by particle
bombardment.
Klein, T.M.; Arentzen, R.; Lewis, P.A.; Fitzpatrick-McElligott, S.
New York, N.Y. : Nature Publishing Company; 1992 Mar.
Bio/technology v. 10 (3): p. 286-291; 1992 Mar. Literature review.
Includes
references.
Language: English
Descriptors: Crops; Plants; Genetic transformation; Direct
DNAuptake; Gene
transfer; Literature reviews
178 NAL Call. No.: QR360.J6
Transformation-specific interaction of the bovine papillomavirus E5
oncoprotein with the platelet-derived growth factor receptor
transmembrane
domain and the epidermal growth factor receptor cytoplasmic domain.
Cohen, B.D.; Goldstein, D.J.; Rutledge, L.; Vass, W.C.; Lowly,
D.R.; Schlegel,
R.; Schiller, J.T.
Washington, D.C. : American Society for Microbiology; 1993 Sep.
Journal of virology v. 67(9): p. 5303-5311; 1993 Sep. Includes
references.
Language: English
Descriptors: Bovine papillomavirus; Viral proteins; Interactions;
Binding
site; Receptors; Epidermal growth factor; Growth factors;
Platelets;
Transformation; Transfection; Genetic transformation
Abstract: The bovine papillomavirus E5 transforming protein
appears to
activate both the epidermal growth factor receptor (EGF-R) and the
platelet-derived growth factor receptor (PDGF-R) by a
ligand-independent
mechanism. To further investigate the ability of E5 to activate
receptors of
different classes and to determine whether this stimulation occurs
through the
extracellular domain required for ligand activation, we constructed
chimeric
genes encoding PDGF-R and EGF-R by interchanging the extracellular,
membrane,
and cytoplasmic coding domains. Chimeras were transfected into NIH
3T3 and
CHO(LR73) cells. All chimeras expressed stable protein which, upon
addition of
the appropriate ligand, could be activated as assayed by tyrosine
autophosphorylation and biological transformation. Cotransfection
of E5 with
the wild-type and chimeric receptors resulted in the
ligand-independent
activation of receptors, provided that a receptor contained either
the
transmembrane domain of the PDGF-R or the cytoplasmic domain of the
EGF-R.
Chimeric receptors that contained both of these domains exhibited
the highest
level of E5-induced biochemical and biological stimulation. These
results
imply that E5 activates the PDGF-R and EGR-R by two distinct
mechanisms,
neither of which specifically involves the extracellular domain of
the
receptor. Consistent with the biochemical and biological activation
data,
coimmunoprecipitation studies demonstrated that E5 formed a complex
with any
chimera that contained a PDGF-R transmembrane domain or an EGF-R
cytoplasmic
domain, with those chimeras containing both domains demonstrating
the greatest
efficiency of complex formation. These results suggest that
although different
domains of the PDGF-R and EGF-R are required for E5 activation,
both receptors
are activated directly by formation of an E5-containing complex.
179 NAL Call. No.: 47.8 AM33P
A transgene alv6, that expresses the envelope of subgroup A avian
leukosis
virus reduces the rate of congenital transmission of a field strain
of avian
leukosis virus.
Crittenden, L.B.; Salter, D.W.
Champaign, Ill. : Poultry Science Association; 1992 May.
Poultry science v. 71 (5): p. 799-806; 1992 May. Includes
references.
Language: English
Descriptors: Fowls; Avian oncovirus; Vertical transmission;
Transgenics; Coat
proteins; Structural genes; Viral interference; Disease resistance;
Antibody
formation; Bursa fabricii
Abstract: A major mode of transmission of avian leukosis virus
(ALV) is from
a dam that is viremic with and imnmunologically tolerant to ALV,
through the
egg to the progeny. The authors have produced a line of chickens
transgenic
for a defective ALV provirus that expresses envelope glycoprotein,
but not
infectious virus, and is very resistant to infection with Subgroup
A ALV. In
the present experiment the authors sought to prevent or reduce
congenital
transmission by mating viremic tolerant hens to males carrying the
inserted
provirus, thus introducing a gene for resistance into the progeny.
Mature
viremic females were mated with males hemizygous for the transgene
to produce
over 80 progeny each with and without the transgene. The chicks
were hatched
and maintained for 36 wk and observed for viremia, antibody, and
the incidence
of bursal lymphomas. Over 90% of the transgene-negative controls
remained
viremic through 36 wk of age and 51% developed bursal lymphomas. In
contrast,
27% of the transgene-positive birds remained viremic and 18% died
with bursal
lymphomas. Thus, expression of Subgroup A envelope protein in the
developing
embryo reduced but did not eliminate congenital infection.
180 NAL Call. No.: 49 AN55
Transgene effects, introgression strategies and testing schemes in
pigs.
Gama, L.T.; Smith, C.; Gibson, J.P.
East Lothian, Scotland : Durrant; 1992 Jun.
Animal production v. 54 (pt.3): p. 427-440; 1992 Jun. Includes
references.
Language: English
Descriptors: Pigs; Transgenics; Genetic effects
181 NAL Call. No.: TP248.6.T73 1992
Transgenesis applications of gene transfer.
Murray, James A. H.
Chichester ; New York : Wiley,; 1992.
xviii, 331 p. : ill. ; 24 cm. Includes bibliographical references
and index.
Language: English
Descriptors: Microbial genetic engineering; Animal genetic
engineering;
Genetic transformation
182 NAL Call. No.: TP248.25.A96T68 1990
Transgenesis of animals.
Kondoh, H.; Agata, K.; Ozato, K.
Amsterdam : Elsevier; 1991.
Automation in biotechnology : a collection of contributions
presented at the
Fourth Toyota Conference, Aichi, Japan, 21-24 October 1990 / edited
by Isao
Karube. p. 203-216; 1991. Includes references.
Language: English
Descriptors: Mice; Fowls; Atheriniformes; Gene transfer;
Transgenics; Genetic
transformation; Blood cells; Reporter genes; Beta-galactosidase;
Ova; Gene
expression; Transcription
Abstract: We discuss the principles of transgenesis, describe a
model gene
suitable for analysis of the process of gene transfer, and compare
methodologies employed in the mouse, the chicken and the medaka
fish. We also
discuss embryonic stem cells which will be the major target of gene
manipulation in transgenic technology in the very near future.
183 NAL Call. No.: QH442.6.T73 1992
Transgenic animals.
Grosveld, F.G.; Kollias, G.
London ; San Diego : Academic Press,; 1992.
viii, 277 p. : ill. ; 24 cm. Includes bibliographical references
and index.
Language: English
Descriptors: Transgenic animals; Gene expression; Medicine
184 NAL Call. No.: A00034 Transgenic animals: contributions to animal breeding and therapy. London, England : IBC Technical Services :.; 1991 Mar. Biotechnology bulletin v. 10 (2): p. 5; 1991 Mar.
Language: English
Descriptors: Transgenics; Market research; Meat animals; Disease
resistance;
Leanness
185 NAL Call. No.: QD415.A1X4
Transgenic animals in the evaluation of compound efficacy and
toxicity: will
they be as useful as they are novel?.
Liggitt, H.D.; Reddington, G.M.
London : Taylor & Francis; 1992 Sep.
Xenobiotica v. 22 (9/10): p. 1043-1054; 1992 Sep. Includes
references.
Language: English
Descriptors: Toxicology; Models; Testing; Toxicity; Transgenics; Mice
Abstract: Construction of transgenic mice is predicated upon
inserting
foreign DNA into native host DNA and having this expressed in the
germline.
This may be accomplished by nuclear injection, retroviral vectors
or use of
embryonic stem (ES) cells. Expression of novel structural genes may
be
reasonably directed by the judicious use of an accompanying
promoter/enhancer
sequence. Insertion of foreign genes may be designed to result in
phenotypic
expression of a novel trait or ablation of a native gene or gene
product.
Resulting transgenic mice offer significant utility as models of
human
diseases and a unique opportunity for investigating immune and
metabolic
pathways as well as for exploring mechanisms of development,
mutagenesis and
teratogenesis. Use of transgenic animals in drug development has
considerable
potential although realization of this potential will take time.
Constructing
transgenics is only the first step in a complex series of events
culminating
in understanding the consequences of imposing novel genetic
material on an
intact, highly integrated living system. Practical use of
transgenic animals
will depend upon substantial effort being spent in investigating
and
validating the phenotypic consequences of gene transfer.
186 NAL Call. No.: TP248.14.N35 1990
Transgenic animals: potential for improved production efficiency.
Bolt, D.J.; Pursel, V.G.; Rexroad, C.E. Jr; Wall, R.J.
Nairobi : Initiatives Publishers; 1991.
Biotechnology in Kenya : proceedings of the National Conference on
Plant and
Animal Biotechnology, held February 25-March 3, 1990 at Kenyatta
International
Conference Centre, Nairobi, Kenya / A.M. Mailu, J.O. Mugah. p.
85-102; 1991.
Includes references.
Language: English
Descriptors: Transgenic animals; Genetic engineering
187 NAL Call. No.: Q320.B56 no.16
Transgenic animals proceedings of the Symposium on Transgenic
Technology in
Medicine and Agriculture.
First, Neal L.; Haseltine, Florence
Center for Population Research (National Institute of Child Health
and Human
Development)
Symposium on Transgenic Technology in Medicine and Agriculture 1988
: National
Institutes of Health.
Boston : Butterworth-Heinemann,; 1991.
xxv, 358 p. : ill. ; 25 cm. (Biotechnology ; 16). Includes
bibliographical
references and index.
Language: English
Descriptors: Transgenic animals; Gene expression; Medicine; Domestic animals
188 NAL Call. No.: QH442.B5
Transgenic expression of a variant of human tissue-type plasminogen
activator
in goat milk: purification and characterization of the recombinant
enzyme.
Denman, J.; Hayes, M.; O'Day, C.; Edmunds, T.; Bartlett, C.;
Hirani, S.;
Ebert, K.M.; Gordon, K.; McPherson, J.M.
New York, N.Y. : Nature Publishing Company; 1991 Sep.
Bio/technology v. 9 (9): p. 839-843; 1991 Sep. Includes
references.
Language: English
Descriptors: Goats; Transgenics; Proteins; Goat milk; Purification; Characterization
189 NAL Call. No.: QP251.A1T5
Transgenic farm animals: progress report.
Ebert, K.M.; Schindler, J.E.S.
Stoneham, Mass. : Butterworth-Heinemann; 1993 Jan.
Theriogenology v. 39 (1): p. 121-135; 1993 Jan. Paper presented at
the
"Annual Conference of the International Embryo Transfer Society,"
January
10-12, 1993, Baton Rouge, Louisiana. Literature review. Includes
references.
Language: English
Descriptors: Goats; Transgenics; Drugs; Gene transfer; Literature reviews
Abstract: The transfer of genetic material by recombinant DNA
technology is
an innovative method designed to produce animals with an altered
genotype.
Transgenic animals may demonstrate a variety of new phenotypes
through the
expression of the exogenous DNA molecule. Mice developed by these
methods have
shown that a wide range of promoter elements result in predictable
patterns of
tissue-specific and hormonally regulated fusion gene products.
However, only a
limited number of promoter elements have been introduced into
domestic farm
animals. Although several experiments were initially designed to
alter the
phenotype through increased rate of growth and improved carcass
composition,
the lack of specificity and regulation of fusion genes has
generally resulted
in negative side effects. The commercial sector, however, has
invested in this
new technology with the goal of producing large amounts of valuable
human
pharmaceutical drugs in a more efficient manner. If this is to be
successfully
accomplished transgenic animals must maintain their normal
physiological
characteristics. The challenge we face is to apply this novel
approach to the
large domestic species without altering their inherent genetic
competence.
This report updates the research on transgenic farm animals and
outlines a
strategy for the production of transgenic goats.
190 NAL Call. No.: QP251.A1T5
Transgenic farm animals--a critical analysis.
Wall, R.J.; Seidel, G.E. Jr
Stoneham, Mass. : Butterworth-Heinemann; 1992 Aug.
Theriogenology v. 38 (2): p. 337-357; 1992 Aug. Paper presented at
the
research symposium on "Reproduction in Farm Animals: Science,
Application and
Models," August 13, 1992, Ithaca, New York. Includes a list of his
publications. Literature review. Includes references.
Language: English
Descriptors: Livestock; Transgenics; Genetic engineering; Dna;
Species
differences; Research projects; Mice; Literature reviews
Abstract: The notion of directly introducing new genes or
otherwise
manipulating the genotype of an animal is conceptually
straightforward and
appealing from the standpoints of both speed and precision with
which
phenotypic changes can be made. Thus, it is little wonder that the
imagination
of many animal scientists has been captivated by the success others
have
achieved in introducing foreign genes into mice. Transgenic mice
not only
exhibit unique phenotypes, but they also pass those traits on to
their
progeny. However, before transgenic farm animals become a common
component of
the livestock industry, a number of formidable obstacles must be
overcome. In
this review we attempt to identify the critical issues that should
be
considered by both those currently working in the field and those
scientists
considering the feasibility of initiating a transgenic livestock
project. The
inefficiency of producing transgenic animals has been well
documented. This
does not constrain investigators using laboratory animal models,
but it has a
major impact of applying transgenic technology to farm animals. The
molecular
mechanisms of transgene integration have not been elucidated, and
as a
consequence it is difficult to design strategies to improve the
efficiency of
the process. In addition to the problems associated with
integration of new
genes, there are inefficiencies associated with collecting and
culturing
fertilized eggs as well as embryo transfer in farm animals.
Transgenic farm
animal studies are major logistical undertakings. Even in the face
of these
practical hindrances, some may be pressured by administrators to
embrace this
new technology. As powerful as the transgenic animal model system
is,
currently there are limits to the kinds of agricultural questions
that can be
addressed. Some uses are so appealing, however, that several
commercial
organizations have explored this technology. Within the next decade
or two, it
is likely that many of the technical hurdles will be overc
191 NAL Call. No.: aZ5076.A1U54 no.117
Transgenic fish research a bibliography : a selected bibliography
of research
in the field of molecular biology and genetic engineering using
fresh water
fish.
Warmbrodt, Robert D.; Stone, Virginia
National Agricultural Library (U.S.)
Beltsville, Md. : National Agricultural Library,; 1993; A
1.60/3:117.
viii, 48 p. ; 28 cm. (Bibliographies and literature of agriculture
; no. 117).
Shipping list no.: 93-0481-P. July 1993. Includes index.
Language: English
Descriptors: Transgenic fish
192 NAL Call. No.: QP251.M64
Transgenic mice carrying interferon genes.
Iwakura, Y.; Hayashi, M.; Asano, M.
New York, N.Y. : Wiley-Liss, Inc; 1993 Oct.
Molecular reproduction and development v. 36 (2): p. 245-247; 1993
Oct. Paper
presented at an "International Symposium on Animal Biotechnology",
Oct. 15-17,
1991, Kyoto, Japan. Includes references.
Language: English
Descriptors: Transgenic animals; Interferon; Mice
193 NAL Call. No.: QL55.A1L33
Transgenic mouse colony management.
Geistfeld, J.G.
New York, N.Y. : Nature Publishing Company; 1991 Jan.
Lab animal v. 20 (1): p. 21-25, 28-29; 1991 Jan. Includes
references.
Language: English
Descriptors: Mice; Transgenics; Breeding methods
194 NAL Call. No.: QL55.A1L33
A transgenic mouse model for genetic toxicology studies.
Myhr, B.; Brusick, D.
New York, N.Y. : Nature Publishing Company; 1991 Jan.
Lab animal v. 20 (1): p. 31-35. ill; 1991 Jan. Includes
references.
Language: English
Descriptors: Mice; Transgenics; Toxicology
195 NAL Call. No.: QH442.A1G4
Transgenic pigs carrying cDNA copies encoding the murine Mx1
protein which
confers resistance to influenza virus infection.
Muller, M.; Brenig, B.; Winnacker, E.L.; Brem, G.
Amsterdam : Elsevier Science Publishers; 1992.
Gene v. 121 (2): p. 263-270; 1992. Includes references.
Language: English
Descriptors: Pigs; Mice; Swine influenzavirus; Transgenics; Genetic
transformation; Gene transfer; Structural genes; Animal proteins;
Genetic
resistance; Dna; Gene expression
Abstract: An important aspect of gene transfer into farm animals
is the
improvement of disease resistance. The mouse Mx1 protein is known
to be
sufficient to confer resistance to influenza viruses. Gene
constructs
containing the mouse Mx1 cDNA controlled by the human
metallothionein II(A)
promoter (hMTII(A)::Mx), the SV40 early enhancer/promoter region
(SV40::Mx)
and the mouse Mx1 promoter (mMx::Mx) were transferred into pigs.
The results
of the gene transfer experiments with the hMTII(A)::Mx and the
SV40::Mx
constructs indicate that the permanent high-level synthesis of Mx1
might be
deleterious to the organism: the gene transfer efficiency was
surprisingly
low, and all transgenic piglets born had rearrangements in their
transgene
copies that abolished protein synthesis. The use of the interferon
(IFN)- and
virus-inducible mMx::Mx construct resulted in normal gene transfer
efficiency.
Two transgenic pig lines could be established which expressed
IFN-inducible
mouse Mx1 mRNA. Extensive protein analysis did not detect mouse Mx1
in
IFN-treated transgenic animals.
196 NAL Call. No.: QH442.B5
Transgenic production of a variant of human tissue-type plasminogen
activator
in goat milk: generation of transgenic goats and analysis of
expression.
Ebert, K.M.; Selgrath, J.P.; DiTullio, P.; Denman, J.; Smith, T.E.;
Memon,
M.A.; Schindler, J.E.; Monastersky, G.M.; Vitale, J.A.; Gordon, K.
New York, N.Y. : Nature Publishing Company; 1991 Sep.
Bio/technology v. 9 (9): p. 835-838; 1991 Sep. Includes
references.
Language: English
Descriptors: Goats; Transgenics; Proteins; Goat milk
197 NAL Call. No.: QP251.A1T5
Transgenic rabbits with antisense RNA gene targeted at adenovirus
H5.
Ernst, L.K.; Zakcharchenko, V.I.; Suraeva, N.M.; Ponomareva, T.I.;
Miroshnichenko, O.I.; Prokof'ev, M.I.; Tikchonenko, T.I.
Stoneham, Mass. : Butterworth-Heinemann; 1991 Jun.
Theriogenology v. 35 (6): p. 1257-1271; 1991 Jun. Includes
references.
Language: English
Descriptors: Rabbits; Adenoviridae; Transgenics; Antisense RNA;
Multiple
genes; Inheritance; Dna; Restriction mapping; Genetic resistance;
Kidneys;
Cell lines; Experimental infections; Deletions; Genetic variation
Abstract: Production of transgenic rabbits by pronuclear
microinjection of
antisense RNA (asRNA) genes targeted against adenovirus h5 (Ad5)
was
performed. Efficacy of transgenosis, calculated as the ratio of
transgenic to
total born offspring, was equal to 36% in the case of linear
plasmids. The
copy number of integrated transgenes varied from 1 to 25 per
genome. Only some
of the integrated transgene copies cut by the appropriate
restriction
endonucleases yielded the hybridization bands identical to those of
the
original pGMA delta plasmid during blotting-analysis. The asRNA
genes were
retained in the offspring of transgenic does mated with wild-type
bucks and
were inherited at least in some transgenic animals in accordance to
the normal
Mendelian pattern. Transgenosis and crosses were accompanied by
significant
deletions and rearrangements of asRNA genes, so that their copy
number varied
independently among the members of the same brood. Nevertheless, at
least two
of five transgenic rabbits studied retained the intact asRNA genes.
To
evaluate the resistance to adenovirus driven by the asRNA genes,
primary
kidney cell cultures were raised from transgenic and normal rabbits
and used
for titration of Ad5. Two of four cell lines possessing the asRNA
transgene
were estimated to be 90% to 98% more resistant to Ad5 than a normal
kidney
cell line. Among seven primary kidney cell lines devoid of asRNA
genes, only
one manifested enhanced resistance to adenoviral infection.
198 NAL Call. No.: Videocassette no.1143
Transgenic technologies BioConferences International, Inc.
BioConferences International, Inc
Potomac, MD : BioConferences International,; 1991.
1 videocassette (113 min.) : sd., col. ; 1/2 in. (BioEast'91 ;
9111).
Videorecording of session at BioEast'91 held in Washington, DC, Jan
6-9, 1991,
sponsored by BioConferences International, Inc., Genetic
Engineering News,
IBEX; co-sponsored by the Pennsylvania State University
Biotechnology and
Bioprocessing Resource Center.
Language: English
Descriptors: Biotechnology; Transgenic animals; Transgenic plants
Abstract: Panel discussion on transgenics and how they can be
applied to
biotechnoloyg, development studies on mice using transgenics;
immunological
developments using transgenics; transgenic pigs; and transgenics
and fish.
199 NAL Call. No.: SF492.M36 1993
The use of avian chimeras in developmental biology.
Dieterlen-Lievre, F.; Le Douarin, N.
Boca Raton : CRC Press; 1993.
Manipulation of the avian genome / edited by Robert J. Etches, Ann
M.
Verrinder Gibbins. p. 103-119; 1993. Includes references.
Language: English
Descriptors: Quails; Chicks; Chimeras; Gene transfer
200 NAL Call. No.: 49 AN55
Utilization of the sex-determining region Y gene in beef cattle
breeding
schemes.
Bishop, S.C.; Woolliams, J.A.
East Lothian, Scotland : Durrant; 1991 Oct.
Animal production v. 53 (pt.2): p. 157-164; 1991 Oct. Includes
references.
Language: English
Descriptors: Beef cattle; Chromosomes; Transgenics; Sires; Sex
ratio; Breeding
value; Selection responses; Genetic gain; Breeding programs
201 NAL Call. No.: aT223.V4A4
Vectors for gene insertion into avian germ line.
Hughes, S.H.; Salter, D.W.; Crittenden, L.B.
Washington, D.C.? : The Department; 1991 Mar05.
United States Department of Agriculture patents (4,997,763): 1 p.;
1991 Mar05.
Copies of USDA patents are available for a fee from the
Commissioner of
Patents and Trademarks, U.S. Patents and Trademarks Office,
Washington, D.C.
20231. Includes references.
Language: English
Descriptors: U.S.A.; Animal breeding; Birds; Gene transfer;
Vectors; Gene
expression; Usda; Patents
Abstract: A stable, substantially nononcogenic vector having a
cloning site
for the convenient insertion of a gene of interest has been
constructed by
recombinant technology from an avian retrovirus. The construct is
derived from
Rous sarcoma virus and the cloning site is a replacement for the
src oncogene.
This vector is useful for ferrying selected, expressible genes into
avian germ
cells for incorporation into the germ line. The vector is also
useful for
inserting and expressing foreign genes in somatic avian cells both
in vivo and
in vitro.
202 NAL Call. No.: HV4701.J6
Viewpoint: transgenic animals as 'alternatives' to animal use.
Gordon, J.
Baltimore, Md. : The Center; 1991.
The Johns Hopkins Center for Alternatives to Animal Testing :
[newsletter] v.
9 (2): p. 8-9; 1991.
Language: English
Descriptors: Animal testing alternatives; Transgenics
203 NAL Call. No.: 500 N21P
The v-src inducible gene 9E3/pCEF4 is regulated by both its
promoter upstream
sequence and its 3' untranslated region.
Blobel, G.A.; Hanafusa, H.
Washington, D.C. : The Academy; 1991 Feb15.
Proceedings of the National Academy of Sciences of the United
States of
America v. 88 (4): p. 1162-1166; 1991 Feb15. Includes references.
Language: English
Descriptors: Rous sarcoma virus; Chick embryos; Fibroblasts; Gene
mapping;
Genetic regulation; Genetic transformation; Nucleotide sequences;
Oncogenes;
Transcription; Transfer RNA
204 NAL Call. No.: 472 N42
White House changes rules for genetic engineering.
Charles, D.
London, Eng. : New Science Publications; 1991 May25.
New scientist v. 130 (1770): p. 14; 1991 May25.
Language: English
Descriptors: Genetic engineering; Legislation; Transgenics;
Environmental
impact
AB, G. 55
Agata, K. 182
Aguilar, A. 150
Aige-Gil, V. 168
Al-Thani, R. 50
Alexander, L. 147
Ali, S. 113
Altschuler, Y. 128
An, M. 133
Archibald, A.L. 144
Arentzen, R. 177
Armas, R. de 150
Asano, M. 192
Atchley, W.R. 54
Atkinson, P.W. 9
Aubert, D. 101
Balk, R.A. 131
Balog, L. 145
Barnier, J.V. 166
Bartlett, C. 188
Bates, P. 105
Bayat-Samardi, M. 155
Beaton, S. 9
Beattie, C. 147
Behringer, R.R. 176
Beise, J. 151
Belyaev, A.S. 40
Benchaibi, M. 101
Benkel, B. 10
Berkowitz, D. 70
Besansky, N.J. 122
Betenbaugh, M.J. 145
Biery, K.A. 149
BioConferences International, Inc 198
Biotechnology Working Group 98
Bird, A.R. 112
Bird, J.M. 16
Bishop, S.C. 200
Black, B.L. 112
Blatz, C.V. 107
Blobel, G.A. 203
Boggs, T. 92
Bolt, D.J. 47, 176, 186
Bondioli, K.R. 149
Booth, S.C. 38
Bosselman, R.A. 92
Bradac, J.A. 12
Bradley, M.P. 9
Brandt, J. 175
Brem, G. 43, 77, 88, 89, 100, 195
Bremel, R.D. 125
Brenig, B. 195
Brinster, R.L. 47, 96, 176
Briskin, M.J. 92
Broek, S. van den 82
Broker, T.R. 153
Brusick, D. 194
Bulfield, G. 23
Bumstead, N. 38
Burdon, T. 64
Burdon, T.G. 68
Butler-Wemken, I. von 88, 89
Calothy, G. 166
Cameron, N.D. 23
Canesco, R.S. 58
Canseco, R.S. 99
Cantwell, W.J. 10
Carnwath, J. 169
Carsience, R.S. 27, 67
Carter, J.K. 11
Carver, A. 94
Castro, F.O. 150
Center for Population Research (National Institute of Child Health
and Human
Development) 187
Charles, D. 204
Chebloune, Y. 97, 101
Chen, D. 133
Chen, H. 116
Chen, Y.F. 133
Chene, N. 155
Chiang, C.M. 153
Chkoniya, T.T. 66, 163
Chow, L.T. 153
Clark, A.J. 15, 103, 113, 144
Clark, M.E. 8, 27
Clarkson, J.L.R 63
Coghlan, A. 46
Cohen, B.D. 178
Coleman, J.R. 49
Collins, F.H. 122
Colman, A. 94
Cook, R.F. 111
Cook, S.J. 111
Cosset, F.L. 97
Cotelli, F. 60
Cottom, D. 94
Coulter, G.H. 21
Cowley, D.E. 54
Cremers, H.C. 57
Crenshaw, P. 54
Crittenden, L.B. 12, 62, 102, 179, 201
Croom, W.J. Jr 112
Cross, H.R. 71
Cui, Z. 170
Cullen, B.R.p 31
Cullen, J.M. 96
Custers, Rene 161
D'yakonov, L.P. 24
Dai, Y.F. 133
Darvsi, A. 28
Daugulis, A.J. 160
Davies, A.H. 159
Davis, B.P. 165
De Mayo, F.J. 149
Denman, J. 188, 196
Desnick, R.J. 69
Devinoy, E. 155
Dezelee, P. 166
Diaz-Martin, Clara, 33
Dieterlen-Lievre, F. 199
Din, N. 175
DiTullio, P. 29, 196
Donnelly, T.M. 142
Doyle, J.J. 137
Draheim, H. 151
Drake, D. 110
Dreyer, F. 151
Drohan, W.N. 58, 99
Duboule, D. 174
Dunham, Rex Alan, 75
Dyer, T.J. 53
Ebert, K.M. 188, 189, 196
Edmunds, T. 188
Eggleston, P. 32
Elias, V.D. 39
Elsasser, T.H. 176
Ernst, L.K. 24, 171, 197
Espanion, G. 169
Etches, R.J. 8, 27, 67
Eyestone, W. 82
Fainsod, A. 28
Fallon, A.M. 124
Farrand, S.K. 3
Faulkner, P. 160
Faure, C. 97
Federspiel, M.J. 12, 62
Filardo, E.J. 13
Finnerty, V. 122
First, N.L. 80, 125
First, Neal L. 187
Fiser, P. 10I
Fitzpatrick-McElligott, S. 177
Fox, M.W. 129
Francolini, M. 60
Fraser, P. 55
Fraser, R.A. 27
Frati, L. 60
French, D. 60
Frumkin, A. 28
Fuente, J. de la 150
Fukazawa, C. 91
Gagne, M.B. 52
Galibert, F. 166
Galili, G. 128
Gama, L.T. 180
Gandolfi, F. 156
Gannon, F. 16, 78
Gao, J. 61
Garcia, M. 101
Garver, I. 94
Gavora, J.S. 10
Geisow, M. 152
Geistfeld, J.G. 193
Gibbs, E.M. 85
Gibson, J.P. 136, 180
Gilbert, H.J. 113
Gogolevskii, P.A. 171
Gol'dman, I.L. 24
Goldman, I.L. 171
Goldstein, D.J. 178
Goosen, M.F.A. 160
Gordon, J. 202
Gordon, K. 29, 188, 196
Gordon, K.E. 103
Goto, N. 106
Grabowski, H. 155
Green, Margaret C. 90
Greunbaum, Y. 28
Griffin, H.D. 23
Grossman, M. 126, 127
Grosveld, F. 55
Grosveld, F.G. 183
Gruidl, M.E. 114
Gulve, E.A. 61
Gusev, V.V. 171
Guthrie, H.D. 47
Hajdu, Melissa Anne, 48
Hall, J. 113
Hall, R.L. 114
Halter, R. 169
Hammer, R.E. 165
Hammock, B.D. 44, 135
Hampe, A. 166
Han, Jae Yong 140
Hanafusa, H. 203
Haney, D.Q. 7
Hanson, R.W. 111
Harel, R. 128
Hartitz, M. 111
Hartmann, W. 59
Haseltine, Florence 187
Haskins, M.E. 69
Hayashi, M. 192
Hayashi, S. 41
Hayes, M. 188
Hazelwood, G.P. 113
Hehir, K. 29
Helferich, W.G. 39
Hennighausen, L. 64, 95, 147
Hermanns, W. 88, 89
Herrmann, D. 169
Hertzke, D. 18
Highkin, M.K. 26
Hill, K.G. 149
Hines, E.R. 9
Hippenmeyer, P.J. 26, 73
Hirani, S. 188
Hirst, B.H. 113
Hjorth, J.P. 175
Hodgson, C.P. 111
Holloszy, J.O. 61, 85
Homanics, G.E. 123
Horan, R. 16
Houdebine, L.M. 155
Houghton, J.A. 16
Howley, P.M. 20
Hoy, M.A. 17
Hsu, R.Y. 92
Huang, M.T.F. 74
Hughes, S. 12
Hughes, S.H. 62, 162, 201
Humphries, E.H. 13
Ichinose, R. 135
Ingerslev, J. 175
Iritani, A. 79
Iwakura, Y. 192
Izpisua-Belmonte, J.C. 174
Jackson Laboratory (Bar Harbor, Me.) 90
Jackson, C.E. 69
Johnson, D.W. 61, 85
Johnson, J.L. 58, 99
Jones, I.M. 159
Jones, K.B. 149
Jowett, J.B.M. 159
Kafiani-Eristavi, C.A. 139
Kafiani-Eristavi, K.A. 66, 163
Kajiwara, N. 41
Kamita, S.G. 135
Kataoka, K. 106
Katsuki, M. 91
Kaurova, S.V. 171
Kawai, S. 106
Khatib, H. 28
Kim, T. 80
Kimbrell, A. 22
King, G.A. 160
Klein, T.M. 177
Knight, J.W. 58, 99
Kollias, G. 183
Kolmer, M. 65
Kondoh, H. 182
Kooiman, P.O 82
Koops, W.J. 126, 127
Kootwijk, E. 82
Kooyman, D.L. 53
Kopchick, J.J. 116
Kornegay, E.T. 58
Kort, C.A.D. de 44
Krimpenfort, P. 82
Krivi, G.G. 26, 73
Kronnie, G. teO 45
Kung, H.J. 170
Kushner, D.J. 49
Kuznetsov, A.V. 171
Lamia, C.L. 60
Larsen, B.B. 175
Larsen, H.J. 175
Laugier, D. 166
Lauria, A. 156
Lavitrano, M. 60
Le Douarin, N. 199
Lee, L.F. 170
Lee, P.S. 145
Legras, C. 97
Leifried-Rutledge, M.L. 80
Lemme, E. 169
Leung, F. 116
Lewis, P.A. 177
Liggitt, H.D. 185
Lillquist, J.S. 85
Limonta, J. 150
Lin, A.X. 133
Liu, J.L. 170
Lowly, D.R. 178
MacDonald, R.J. 165
Macken, F. 116
MacKenzie, D. 57
Maeda, S. 135
Makarevich, A.V. 24
Malim, M.H. 31
Margalit, Y. 28
Maronpot, R.R. 96
Marshall, B.A. 61, 85
Marshall, J.T.A. 63
Marx, M. 166
Matthaei, K.I. 9
Matthews, K.I. 157
Matveev, V.A. 24
Maugh, T.H. II 86
Mayo, K. 176
Mazzola, V. 109
McBride, B.W. 112
McClenaghan, M. 144
McEvoy, T.G. 78, 164
McGrane, M. 111
McGregor, R. 108
McKnight, R.A. 95, 147
McPherson, J.M. 188
Meer, M.M.M. van 44
Mehigh, C.S. 39
Mehigh, R.J. 39
Memon, M.A. 196
Messing, A. 165
Meyers, N.L. 38
Mikkelsen, T.R. 175
Milan, D. 1
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Miller, K.F. 47, 176
Mills, E. 116
Miroshnichenko, O.I. 197
Molina, R.M. 97
Monastersky, G.M. 196
Morais, R. 121
Morgan, B.A. 174
Moss, B. 138
Moyer, R.W. 114
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Muller, M. 43, 195
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Myhr, B. 194
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Nakanishi, A. 79
Nancarrow, C.D. 63, 83
National Agricultural Biotechnology Council (U.S.),Texas A & M
University,
Center for Biotechnology Policy and Ethics 56
National Agricultural Library (U.S.) 191
Nederlandse Organisatie voor Technologisch Aspectenonderzoek 161
Newman, S. 34
Nicolas, J.F. 1
Niemann, H. 169
Nigon, V. 101
Nigon, V.M. 97
Nikolaev, A.I. 66, 139, 163
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O'Brien, S.J. 69
O'Day, C. 188
Ohsawa, N. 91
Ord, T. 65
Ozato, K. 182
Page, R.L. 58, 99
Palmiter, R.D. 47, 176
Paul, D. 169
Payne W.S. 12
Pearson, R.E. 58, 99
Perez, A. 150
Petitte, J.N. 8
Petropoulos, C.J. 12, 162
Philipsen, S. 55
Pieper, F. 82
Pinkert, C.A. 53
Pirchner, F. 88, 89
Pittius, C.W. 95
Platenburg, G. 82
Pomp, D. 54
Poncet, D. 101
Ponomareva, T.I. 197
Possee, R.D. 44
Pothier, F. 52
Poulsen, K. 175
Powell, R. 16
Prather, R.S. 132
Presek, P. 151
Prokof'ev, M.I. 197
Provencher, L.P. 62
Prusiner, S.B. 117, 118, 119, 120
Pruzina, S. 55
Purcel, V.G. 14
Pursel, V.G. 2, 47, 95, 147, 158, 186
Rademakers, A. 82
Ramirez, V. 121
Ramos, B. 150
Ramsey, U. 35
Rangini, Z. 28
Rapp, K. 89
Reddington, G.M. 185
Reed, K.C. 9
Reeves, D. 94
Ren, J.M. 61, 85
Repp, H. 151
Revel, E. 28
Rexroad, C.E. 158
Rexroad, C.E. Jr 4, 14, 42, 146, 176, 186
Riego, E. 150
Rishell, W. 92
Roberts, B. 29
Robertson, M. 103
Robinson, J.J. 164
Roelvink, P.W. 44
Roschlau, K. 81
Rosenberg, N. 128
Rosenblum, C. 116
Roy, P. 40
Ruland, J. 151
Rutledge, L. 178
Sabour, M.P. 10, 35
Saegusa, T. 106
Salter, D.W. 12, 102, 179, 201
Samallo, J. 45
Samarut, J. 101
Sandgren, E.P. 96
Sankaran, L. 64
Sasada, H. 10
Saveria Campo, M. 25
Savoie, P. 121
Savon, S. 111
Savva, D. 37
Schans, A. van der 82
Schiller, J.T. 178
Schindler, J.E. 196
Schindler, J.E.S. 189
Schlegel, R. 178
Schnieke, A. 115
Schuchman, E.H. 69
Schultz, J.A. 92
Scott, A. 94
Seidel, G. 151
Seidel, G.E. Jr 115, 190
Selgrath, J.P. 196
Semenova, V.A. 24
Shamay, A. �95, 147
Shanahan, C.M. 63
Shaw, D.L. 67
Shimada, M. 91
Shimano, H. 91
Shinno-Kohno, H. 106
Shotkoski, F.A. 124
Shuman, R.M. 148
Silva, R.F. 11
Simkiss, K. 37, 38, 50, 141, 168, 173
Simons, J.P. 113, 144
Simons, P. 94
Sirard, M.A. 52
Smirnov, O.K. 24
Smith, C. 180
Smith, J. 116
Smith, T.E. 196
Sobennikova, L.L. 171
Soeller, W.C. 85
Solano, R. 150
Solinas, S. 147
Solomon, M.B. 2
Soltes-Rak, E. 49
Spadafora, C. 60
Sparks, A.E.T. 58, 99
Sparks, Amy Elizabeth Thuemmel, 19
Spencer, M. 64
Squires, E.J. 110
Sreenan, J.M. 78, 164
Staeheli, P. 104
Stark, Margo D. 98
Sterrenberg, Lydi 161
Stijker, R. 82
Stinnakre, M.G. 155
Stipp, D. 6
Stone, V. 76
Stone, Virginia 191
Strel'chenko, N.S. 24
Sugiyama, F. 41
Sugiyama, Y. 41
Suraeva, N.M. 197
Surani, M.A. 113
Tabin, C.J. 174
Takaku, F. 91
Tarantul, V.Z. 139
Taylor, J. 116
Tchkonia, T.T. 139
Teather, R.M. 10
Thepot, D. 155
Thomas, J.L. 97
Thomas, W.K. 115
Thomas, Wendell Keith 143
Thompson, P.B. 36
Tikchonenko, T.I. 197
Tiley, L.S. 31
Toner, A. 27
Troyer, D. 18
Tucker, H.A. 39
Turner, M.K. 134
Ulmanen, I. 65
United States-Israel Binational Agricultural Research and
Development
Fund 75
Vande Pol, S.B. 20
Varmus, H.E. 105
Vass, W.C. 178
Velander, W.H. 58, 99
Verdier, G. 97, 101
Verhoog, H. 30
Verrinder Gibbins, A.M. 27, 67
Vick, L. 37, 38
Vitale, J. 29
Vitale, J.A. 196
Vlak, J.M. 44
Vogl, C. 54
Wall, R.J. 14, 64, 68, 95, 147, 186, 190
Walsh-Mullen, A. 142
Wanke, R. 88, 89
Ward, K.A. 63, 83
Warmbrodt, R. 76
Warmbrodt, Robert D. 191
Watson, C.J. 103
Webster, J. 5
Wei, C.X. 133
Wheeler, M.B. 3
Whitehead, T.R. 84
Whitelaw, C.B.A. 144
Widholm, J.M. 3
Wijnholds, J. 55
Wilker, N. 34
Williams, B.L. 58, 99
Williams, D.D.� 49
Wilmut, I. 15, 94, 144
Winnacker, E.L. 195
Witham, Barbara A. 90
Wolf, E. 88, 89
Woolliams, J.A. 200
Wright, G. 94
Wynn, P.C. 63
Yagami, K. 41
Yamada, N. 91
Yarus, S. 28
Yazaki, Y. 91
Yom, H.C. 125
Yoon, Sung-Joo 172
Young, J.A.T. 105
Young, J.M. 99
Yuhki, N. 69
Zakcharchenko, V.I. 197
Zhadanov, A.B. 171
Zhang, Z.C. 133
Abnormalities 168
Accuracy 59
Actin 162
Active transport 61, 85, 112
Adenoviridae 197
Adipocytes 123
Aedes 122
Aedes aegypti 32
Aedes albopictus 124
Agalactia 147
Age 41
Age differences 41
Agricultural products 134
Ai bulls 21
Allometry 127
Alphas1-casein 125
Amino acid sequences 29, 31, 69, 114, 121, 128, 166
Amsacta moorei 114
Analysis 149
Anas platyrhynchos 121
Animal biotchnology 56
Animal biotechnology 161
Animal breeding 11, 23, 30, 35, 50, 77, 137, 142, 201
Animal breeding methods 50
Animal genetic engineering 161, 181
Animal production 83
Animal products 6, 130
Animal proteins 61, 68, 175, 195
Animal testing alternatives 202
Animal tissues 24, 149, 176
Animal welfare 5, 30, 107
Animals 3, 14, 76, 119, 131, 164
Anopheles 122
Antibody formation 179
Antisense RNA 43, 197
Antitrypsin 94
Apis mellifera 9
Apolipoproteins 55, 91
Arthropod pests 17
Artificial insemination 10
Artificial selection 88, 89
Arylsulfatase 69
Assessment 152
Atheriniformes 182
Autographa californica 40, 44, 135
Autoradiography 60
Avian herpesvirus 11
Avian oncovirus 12, 13, 26, 62, 97, 101, 102, 105, 162, 179
Bacillus thuringiensis subsp. israelensis 49
Bacterial toxins 49, 123
Baculovirus 159
Beef cattle 200
Best linear unbiased prediction 59
Beta-casein 29
Beta-galactosidase 1, 145, 160, 171, 182
Beta-lactoglobulin 94, 103
Bibliographies 76
Binding 9
Binding proteins 82, 85, 123
Binding site 31, 103, 178
Bioethics 56, 131
Biological control 17
Biological production 6, 7, 86, 130
Bioreactors 14, 160
Biotechnology 4, 5, 14, 24, 71, 107, 108, 137, 152, 198
Birds 201
Bismuth 91
Blastomere 68
Blood cells 182
Blood coagulation 109
Blood plasma 47, 91
Blood sugar 85, 176
Bluetongue virus 40
Boars 47
Body weight 35, 89
Bombyx mori 66, 139
Bone formation 89, 123
Bones 89
Bovidae 24
Bovine oncovirus 1, 39
Bovine papillomavirus 20, 25, 153, 178
Bovine spongiform encephalopathy 117, 120
Breed differences 136
Breeding methods 59, 193
Breeding programs 200
Breeding value 59, 200
Broilers 59
Bursa fabricii 179
Butyrivibrio fibrisolvens 84
California 87
Calves 65, 93
Carbohydrate metabolism 61, 85
Carcass composition 2, 23
Carcinogenesis 96
Cartilage 54
Cats 69
Cattle 9, 16, 18, 19, 21, 25, 52, 57, 60, 80, 81, 87, 115, 117,
143,
149
Cell culture 24, 44, 124, 145
Cell cultures 39
Cell division 101
Cell lines 1, 18, 26, 38, 69, 73, 97, 145, 153, 159, 197
Cell membranes 50
Cell suspensions 145, 160
Cells 25
Cellulase 113
Cellulose digestion 113
Characterization 188
Chemical composition 136
Chick embryos 37, 50, 106, 116, 141, 151, 168, 174, 203
Chickens 12, 27, 28, 55, 67, 79, 105, 110, 111
Chicks 199
Chimeras 27, 31, 67, 166, 168, 173, 199
Chloramphenicol acetyltransferase 162
Chromosomes 67, 69, 147, 200
Chymosin 65
Cleavage 99
Clones 106
Cloning 29, 64, 65, 114, 118, 132
Clostridium thermocellum 113
Clotting 109
Coat proteins 179
Comparisons 69
Complementary DNA 85
Concanavalin a 50
Control 23
Controlling elements 176
Corynebacterium 123
Crops 34, 177
Crossbreds 59
Culex 122
Culex restuans 49
Culture media 160
Cysteine 83
Cytoplasmic inheritance 139
Dairy cattle 39, 82
Defense mechanisms 122
Deletions 166, 197
Detection 37
Diabetes 176
Digestive absorption 112
Dihydrofolate reductase 124
Dimensions 88, 89
Direct DNAuptake 60, 66, 68, 139, 177
Disease control 32
Disease resistance 43, 57, 102, 104, 179, 184
Disease transmission 119
Disease vectors 92, 122
Dna 1, 9, 37, 52, 58, 60, 68, 69, 99, 106, 124, 139, 149, 153,
163, 171,
190, 195, 197
Dna amplification 11
Dna binding proteins 18, 103
Dna conformation 68
Dna hybridization 111
Dna methylation 45, 68
Dna probes 45
Dna replication 20, 153
Domestic animals 83, 187
Drugs 109, 134, 189
Economic impact 136
Efficiency 26
Egg production 59
Eggs 66
Electrophysiology 151
Electroporation 52, 84
Embryo culture 41, 149, 173
Embryo transfer 41, 58, 82, 115, 149
Embryo transplantation 143
Embryology 48
Embryonic development 41, 168, 174
Embryos 8, 66, 68, 99, 171, 173
Endoplasmic reticulum 128
Endotoxins 49
Entomology 108
Entomopoxvirus 114
Environmental impact 204
Enzyme activity 1, 61, 65, 113, 135, 162, 166
Enzyme inhibitors 135
Enzyme precursors 65
Epidermal growth factor 178
Epigenetics 54
Epiphyses 54
Epstein-barr virus 65
Equations 126, 127
Esterases 135
Estradiol 55
Estrone 47
Estrus 58
Ethics 30, 36, 107
Etiology 117
Evolution 121, 122
Ewe milk 94
Exons 29
Experimental infections 197
Expressivity 73
Extracts 103
Fat percentage 123
Fatty acids 136
Feed conversion 176
Fertilization 10, 41, 52, 58
Fertilization in vitro 143�
Fibroblasts 13, 18, 101, 105, 106, 151, 162, 203
Fishes 75, 78
Food industry 164
Food processing 46
Food production 164
Food products 152
Food safety 70, 71, 72
Fowls 1, 8, 10, 13, 26, 38, 50, 62, 92, 97, 101, 102, 106, 121,
148, 162,
179, 182
Fsh 154
Gametes 8
Gene amplification 19
Gene expression 1, 11, 13, 15, 29, 31, 42, 44, 47, 49, 54, 55, 62,
63, 64,
65, 69, 75, 85, 91, 92, 94, 95, 97, 101, 102, 105, 111, 113, 114,
118, 120,
123, 133, 135, 144, 145, 151, 159, 160, 162, 165, 169, 171, 174,
175, 176,
182,
183, 187, 195, 201
Gene frequency 35
Gene location 69
Gene mapping 18, 114, 203
Gene transfer �1, 10, 11, 12, 15, 16, 29, 38, 39, 40, 44, 53, 65,
68, 73,
76,
77, 78, 79, 80, 81, 82, 83, 85, 88, 89, 97, 101, 102, 105, 109,
110, 121, 132,
133, 135, 137, 138, 139, 144, 146, 148, 156, 159, 160, 162, 175,
177, 182,
189,
195, 199, 201
Genes 11, 18, 35, 37, 43, 68, 73, 101, 103, 114, 117, 119, 126,
135, 146,
147, 150, 166, 170, 175
Genetic change 136
Genetic control 32
Genetic effects 180
Genetic engineering 2, 6, 17, 22, 24, 27, 28, 30, 32, 34, 35, 36,
46, 51,
70, 76, 83, 107, 111, 115, 123, 129, 130, 137, 141, 145, 148, 152,
154, 157,
163, 173, 186, 190, 204
Genetic gain 200
Genetic improvement 17
Genetic markers 111, 124
Genetic regulation 31, 49, 55, 64, 73, 103, 135, 203
Genetic resistance 195, 197
Genetic transformation 9, 10, 13, 18, 20, 25, 26, 29, 32, 33, 49,
54, 60,
66, 69, 76, 84, 85, 88, 89, 101, 106, 108, 113, 114, 122, 123, 124,
128, 133,
135, 138, 139, 145, 151, 153, 166, 170, 174, 177, 178, 181, 182,
195, 203
Genetic variation 43, 122, 197
Genetic vectors 80, 124, 138, 159
Genomes 32, 122, 162, 171
Genotypes 8
Germ cells 8, 38, 50, 141
Germ line 8, 12, 50, 141, 173
Gigantism 89
Gilts 47, 58, 95, 99
Gliadin 128
Glucose 61, 85, 112
Glutathione transferase 159
Glycogen 61
Goat milk 188, 196
Goats 29, 87, 117, 118, 188, 189, 196
Gonadotropins 47
Growth 53, 89, 146, 176
Growth analysis 126, 127
Growth curve 88, 126, 127
Growth factors 112, 178
Growth promoters 42
Growth rate 88, 101, 126, 127, 133
Hamsters 69
Hela cells 65
Heliothis virescens 44, 135, 145
Hemoglobin 14
Hens 59
Hereford cattle 33
Heritability 136
Hexokinase 61
Histones 101
Histopathology 106
Homeostasis 85
Hormonal control 85
Hormone secretion 47
Hormones 176
Host parasite relationships 122
Host range 1
Human diseases 117
Human immunodeficiency virus 31
Hybridization 67
Hybrids 31
Hydrolysis 135
Illinois 3
Immunization 104
Improvement 146
In vitro 21, 41, 82
In vitro culture 99
Inactivation 135
Inbreeding 90
Induced mutations 31, 128
Infection 97, 105
Infectivity 117
Infertility 123
Infusion 112
Inheritance 35, 66, 123, 197
Inhibitor genes 55
Injection 58, 149
Insect control 17, 135
Insecticidal properties 49
Insulin 85, 176
Interactions 103, 178
Interferon 192
Introduction 116
Introns 29
Ions 151
Juvenile hormones 135
Kidneys 91, 197
Kinetics 50
Laboratory animals 157
Lactation 64
Lactoferrin 82, 93
Larvae 49, 135
Leanness 184
Legislation 157, 204
Length 127
Lh 47
Limb bones 54
Limbs 174
Limiting factors 112
Line differences 35
Lines 92, 95, 163
Lipids 123
Lipoproteins 91
Liposomes 110
Literature reviews 2, 17, 21, 25, 43, 59, 83, 117, 118, 119, 121,
122, 136,
144, 148, 164, 177, 189, 190
Liver 55, 91, 96, 111
Livestock 34, 43, 77, 83, 104, 112, 144, 152, 157, 190
Liveweight gain 88, 126, 127, 133
Loci 105
Lucilia cuprina 9
Lungs 24
Lymantria dispar 145
Lymphocytes 74
Male fertility 21
Mammals 1, 132
Mammary glands 14, 29, 95, 103, 169
Man 61, 69, 85, 88, 89, 117, 119, 126, 127
Mandible 54
Manduca sexta 135
Manufacture 134
Marek's disease virus �11, 170
Marker genes 18
Market research 184
Markets 51
Massachusetts 87
Mastitis 57
Meat animals 23, 123, 184
Meat inspection 72
Medical research 14
Medicinal plants �134
Medicine 183, 187
Messenger RNA 39, 55, 91
Metallothionein 54, 88, 89, 91, 133, 162
Methotrexate 124
Methylation 73
Mice 10, 29, 35, 41, 54, 55, 61, 64, 68, 69, 74, 85, 88, 89, 91,
95, 96,
103, 105, 109, 113, 117, 118, 123, 125, 126, 127, 142, 150, 153,
157, 162,
165,
175, 182, 185, 190, 192, 193, 194, 195
Mice as laboratory animals 90
Mice, Inbred Strains 90
Microbial genetic engineering 181
Micromanipulation 93
Milk 65
Milk composition 144
Milk fat 136
Milk products 144
Milk proteins 83, 95, 144, 155
Mink 117
Mink diseases 117
Mitochondrial genetics 121
Models 185�
Modification 2, 152
Molecular biology 108, 117, 121
Molecular genetics 59, 117, 120, 122
Monkeys 25, 105
Monoclonal antibodies 43
Mortality 123
Mosquito-borne diseases 32
Mouse milk 64
Movement 50
Multiple genes 197
Mutants 104, 128, 153, 166
Mutations 166
Natural enemies 17
Neoplasms 106
Netherlands 46, 57, 93
New species 129
Newborn animals� 123
Nomenclature 167
Northern blotting 91, 176
Nuclear polyhedrosis viruses 40, 44, 145
Nuclei 60
Nucleotide sequences 29, 52, 69, 97, 106, 114, 121, 163, 166, 170,
203
Nutrient requirements 112
Obesity 23
Oncogenes 13, 106, 203
Oncogenic viruses 106
Oocytes 41, 52, 128
Oogenesis 122
Organizations 34
Ova 182
Ovulation rate 58
Pancreas 112, 113, 165
Patents 11, 34, 36, 157, 201
Performance 53
Pesticide resistance 122
Pharmaceutical proteins 144
Pharmacokinetics 135
Phenotypes 114, 147, 153
Phenotypic selection 59
Phosphoproteins 170
Phosphorylation 101
Phosphotransferases 18
Pig breeds 154
Pigs 2, 5, 45, 51, 53, 100, 107, 109, 133, 147, 158, 180, 195
Plants 3, 152, 177
Plasma membranes 61
Plasmid vectors 49
Plasmids 18, 26, 38, 52, 60, 66, 84, 139, 153, 163, 166
Plasminogen activator 150
Platelets 178
Polymerase chain reaction 37, 68, 69
Potassium 151
Poultry 173
Poultry diseases 11
Pregnancy 64
Pregnancy rate 58
Preimplantation period 68
Prions 119, 120
Problem analysis 108
Production 149
Promoters 49, 54, 123, 133, 153, 162
Pronucleus 149
Protein kinase 166
Protein secretion 113, 175
Protein synthesis 95, 145
Protein transport 128
Proteins 6, 7, 14, 86, 87, 117, 130, 188, 196
Puerto Rico 154
Purification 118, 188
Quails 13, 73, 101, 162, 199
Rabbit papillomavirus 25
Rabbits 24, 25, 100, 133, 150, 171, 197
Rats 35
Receptors 50, 85, 105, 178
Recombinant DNA 1, 32, 34, 49, 54, 64, 113, 116, 133, 138, 145,
157, 159,
160
Recombinant vaccines 138
Regulation 128
Regulations 71
Repetitive DNA 66, 139
Replication 38, 117, 174
Reporter genes 1, 18, 97, 145, 162, 171, 182
Research 17
Research projects 190
Research support 154
Restriction mapping 163, 197
Reticuloendotheliosis virus 92
Retroviral vectors 1, 26, 38, 73, 97, 101, 111, 148, 162, 174
Retroviridae 37, 38, 106
Reverse transcriptase 162
Reviews 173
Ribosomal RNA 121
Risk 17, 152
Rna 95, 97
Rna editing 55
Rous sarcoma virus 66, 97, 105, 139, 151, 162, 163, 166, 203
Salivary glands 175
Salivation 122
Sampling 149
Sarcoma 102
Scotland 87
Scrapie 117, 118
Scrapie agent 118, 120
Secretion 95
Segregation 35
Selection criteria 59
Selection responses 35, 200
Semen characters 21
Semen preservation 21
Sequences 73
Sex ratio 200
Sexual maturity 47
Sheep 1, 42, 54, 63, 87, 94, 103, 117, 118, 133, 146, 158, 169,
176
Silkworms 163
Simian polyomavirus 18
Sires 200
Skeletal development 54
Skeletal muscle 61, 85
Skeleton 89
Skull 54
Small intestine 113
Somatic hybridization 69
Somatoliberin 39
Somatotropin 24, 35, 47, 54, 83, 88, 89, 126, 127, 133, 146, 165
Sow lactation 147
Sow milk 147
Sows 58
Species differences 35, 190
Spermatozoa 9, 10, 16, 21, 52, 60, 79, 156
Spodoptera frugiperda 44, 135, 145, 159, 160
Starch digestion 112
Sterilization 50, 168
Stomach 165
Strain differences 41
Streptococcus bovis 84
Structural genes 29, 49, 54, 55, 69, 105, 113, 123, 128, 133, 138,
159,
176,
179, 195
Superovulation 41, 58
Susceptibility 105
Swine 48
Swine influenzavirus 195
Synchronization 58
Syndactyly 123
Synechococcus 49
Synthesis 134, 171
Tail 126, 127
Techniques 116
Technology 104
Testing 185
Testosterone 47
Thymidine kinase 114
Toxicity 185
Toxicology 185, 194
Traditional technology 108
Transcription 20, 103, 121, 171, 182, 203
Transduction 97
Transfection 1, 26, 39, 73, 101, 105, 153, 166, 178
Transfer 8, 24
Transfer RNA 203
Transformation 25, 178
Transgenic animals 4, 19, 22, 48, 54, 55, 56, 61, 70, 71, 74, 75,
85, 96,
100, 113, 125, 128, 129, 133, 134, 150, 155, 157, 158, 161, 167,
173, 183,
186,
187, 192, 198
Transgenic fish 191
Transgenic organisms 98
Transgenic plants 198
Transgenics 2, 3, 5, 6, 7, 8, 10, 14, 15, 17, 23, 24, 27, 28, 29,
30, 32,
34, 35, 36, 37, 38, 42, 43, 46, 47, 50, 51, 52, 53, 57, 58, 59, 62,
63, 66,
67,
68, 72, 82, 83, 86, 87, 88, 89, 91, 92, 93, 94, 95, 99, 102, 103,
104, 107,
111, 115, 116, 117, 118, 123, 126, 127, 130, 131, 136, 139, 141,
142, 144,
146,
147, 148, 149, 152, 154, 163, 164, 165, 168, 169, 171, 175, 176,
179, 180,
182,
184, 185, 188, 189, 190, 193, 194, 195, 196, 197, 200, 202, 204
Transposable elements 32
Triticum aestivum 128
Trypsin 165
U.S.A. 11, 14, 72, 137, 157, 201
Ultraviolet radiation 168
Uptake 9, 85
Usda 11, 51, 72, 201
Vaccinia virus 138
Vectors 9, 11, 39, 52, 65, 145, 201
Vertical transmission 179
Very low density lipoprotein 55
Viability 41�
Viral antigens 138
Viral interference 179
Viral morphology 166
Viral proteins 31, 104, 106, 178
Visna maedi virus 31
Wavelengths 168
Whey protein 64, 95, 109, 147
Xenopus 128
Zinc 91
Zygotes 58, 99, 171
BULLET 15
ELECTRONIC MAIL ACCESS FOR INTERLIBRARY LOAN (ILL) REQUESTS
June 1993
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| AG University/NAL ILLRQ 231 4/1/93 NEED BY: 6/1/93 | | | | Interlibrary Loan Department | | Agriculture University | | Heartland, IA 56789 | | | | Dr. Smith Faculty Ag School | | | | Canadian Journal of Soil Science 1988 v 68(1): 17-27 | | DeJong, R. Comparison of two soil-water models under | | semi-arid growing conditions | | Ver: AGRICOLA | | Remarks: Not available at IU or in region. | | NAL CA: 56.8 C162 | | | | Auth: C. Johnson CCL Maxcost: $15.00 | | | | MORE | | |
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The following information is provided to assist your librarian in obtaining the required materials.
LOAN SERVICE -- Materials in NAL's collection are loaned only to other U.S. libraries. Requests for loans are made through local public, academic, or special libraries.
The following materials are not available for loan: serials (except USDA serials); rare, reference, and reserve books; microforms; and proceedings of conferences or symposia. Photocopy or microform of non-circulating publications may be purchased as described below.
DOCUMENT DELIVERY SERVICE -- Photocopies of articles are available for a fee. Make requests through local public, academic, or special libraries. The library will submit a separate interlibrary loan form for each article or item requested. If the citation is from an NAL database (CAIN/AGRICOLA, "Bibliography of Agriculture," or the NAL Catalog) and the call number is given, put that call number in the proper block on the request form. Willingness to pay charges must be indicated on the form. Include compliance with copyright law or a statement that the article is for "research purposes only" on the interlibrary loan form or letter. Requests cannot be processed without these statements.
CHARGES:
the first 10 pages or fraction copied from a single article or publication. $3.00 for each additional 10 pages or fraction.
fiche and $ .50 for each additional fiche per title.
BILLING -- Charges include postage and handling, and are subject to change. Invoices are issued quarterly by the National Technical Information Service (NTIS), 5285 Port Royal Road, Springfield, VA 22161. Establishing a deposit account with NTIS is encouraged. DO NOT SEND PREPAYMENT.
SEND REQUESTS TO:
USDA, National Agricultural Library
Document Delivery Services Branch, PhotoLab
10301 Baltimore Blvd., NAL Bldg.
Beltsville, Maryland 20705-2351
Contact the Head, Document Delivery Services Branch in writing or by calling (301) 504-5755 with questions or comments about this policy.
2) DOCUMENT DELIVERY SERVICES AVAILABLE TO LIBRARIES, OTHER
INFORMATION CENTERS AND COMMERCIAL ORGANIZATIONS.
The National Agricultural Library (NAL) accepts requests from libraries and other organizations in accordance with the national and international interlibrary loan code and guidelines. In its national role, NAL supplies copies of agricultural materials not found elsewhere. Filling requests for materials readily available from other sources diverts NAL's resources and diminishes its ability to serve as a national source for agricultural and agriculturally related materials. Therefore, NAL is viewed as a library of last resort.
Submit requests to state/region/network sources prior to sending to NAL. Within the United States, possible sources are public libraries, land-grant university libraries or other large research libraries within a state. In other countries submit requests to major university, national or provincial institutions. If the needed publications are not available from these sources, submit requests to NAL with a statement indicating their non-availability.
REQUESTS -- Submit on the American Library Association (ALA) or the International Federation of Library Associations and Institutions (IFLA) interlibrary loan form or via electronic mail or telefacsimile (see over for more details). Include the complete name of the person authorizing the request on each form; the standard bibliographic source which lists the title as owned by NAL; and the call number if the citation is from an NAL database (CAIN/AGRICOLA, "Bibliography of Agriculture," or the NAL catalog).
LOAN SERVICE -- Materials in the NAL collection are loaned only to U.S. libraries. The loan period is one month.
The following materials are not available for loan: serials (except for USDA serials); rare, reference, and reserve books; microforms; and proceedings of conferences or symposia. Photocopy or microform of the non-circulating publications is supplied automatically (as described below) when the requesting organization indicates that photocopy is acceptable on the loan form.
AUDIOVISUALS (AVs) -- Order at least 3-4 weeks before the intended show date. Give show date and alternate show date when requesting specific titles. Request specific format needed if more than one format is given in the citation.
DOCUMENT DELIVERY SERVICE -- Submit a separate completed interlibrary loan form for each article required. Indicate willingness to pay charges on the form and compliance with copyright law or include a statement that the article is for "research purposes only." Requests are not processed without these statements.
CHARGES:
the first 10 pages or fraction copied from a single article or publication. $3.00 for each additional 10 pages or fraction.
fiche and $ .50 for each additional fiche per title.
BILLING - Charges include postage and handling, and are subject to change. Invoices are issued quarterly by the National Technical Information Service (NTIS), 5285 Port Royal Road, Springfield, VA 22161. Establishing a deposit account with NTIS is encouraged. DO NOT SEND PREPAYMENT.
Send Requests to:
USDA, National Agricultural Library
Document Delivery Services Branch, ILL, PhotoLab
10301 Baltimore Blvd., NAL Bldg.
Beltsville, Maryland 20705-2351
Contact the Head, Document Delivery Services Branch in writing or by calling (301) 504-5755 with questions or comments about this policy.
3) DOCUMENT DELIVERY SERVICES AVAILABLE TO FOREIGN LIBRARIES,
INFORMATION CENTERS AND COMMERCIAL ORGANIZATIONS.
The National Agricultural Library (NAL) accepts requests from libraries and other organizations in accordance with the national and international interlibrary loan code and guidelines.
In its national role, NAL supplies copies of agricultural materials not found elsewhere. Filling requests for materials readily available from other sources diverts NAL's resources and diminishes its ability to serve as a national source for agricultural and agriculturally related materials. Therefore, NAL is viewed as a library of last resort.
Submit requests to major university libraries, national or provincial institutions or network sources prior to sending requests to NAL. If the needed publications are not available from these sources, submit requests to NAL with a statement indicating their non-availability.
AGLINET -- Requesters in countries with an AGLINET library are encouraged to make full use of that library and its networking capabilities. As an AGLINET participant, NAL provides free document delivery service for materials published in the United States to other AGLINET participants.
REQUESTS -- Submit requests on the American Library Association (ALA) or the International Federation of Library Associations and Institutions (IFLA) interlibrary loan form or via electronic mail or telefacsimile (see over for more details). Include the complete name of the person authorizing the request on each form; the standard bibliographic source which lists the title as owned by NAL; and the call number if the citation is from an NAL database (CAIN/AGRICOLA, "Bibliography of Agriculture", or the NAL catalog).
DOCUMENT DELIVERY SERVICE -- Submit a separate completed interlibrary loan form for each article requested. Indicate willingness to pay charges on the form, and compliance with copyright law or include a statement that the article is for "research purposes only". Requests cannot be processed without these statements.
CHARGES:
the first 10 pages or fraction copied from a single article or publication. $3.00 for each additional 10 pages or fraction.
fiche and $ .50 for each additional fiche per title.
BILLING - Charges include postage and handling, and are subject to change. Invoices are issued quarterly by the National Technical Information Service (NTIS), 5285 Port Royal Road, Springfield, VA 22161. Establishing deposit account with NTIS is encouraged. Annual billing is available to foreign institutions on request by contacting NAL at the address below. DO NOT SEND PREPAYMENT.
Send Requests to:
USDA, National Agricultural Library
Document Delivery Services Branch, ILL, PhotoLab
10301 Baltimore Blvd., NAL Bldg.
Beltsville, Maryland 20705-2351
Contact the Head, Document Delivery Services Branch at (301) 504-5755 with questions or comments about this policy.