Compositions and methods for increasing animal size growth rate

Details Compositions and methods for increasing animal size growth rate Compositions and methods for increasing animal size growth rate

2003-01-27

2008-10-14

Bertoglio, Valarie (Department: 1632)

Chemistry: molecular biology and microbiology

Animal cell, per se ; composition thereof; process of...

Rodent cell, per se

C435S375000, C435S455000, C435S320100, C435S463000

Reexamination Certificate

active

07435591

ABSTRACT:
The present invention relates to germ line and somatic cells comprising a mutant p27kip1protein lacking a Cdk2 phosphorylation site. Also provided are transgenic animals and methods of making such transgenic animals which have increased size and/or growth rate.

REFERENCES:
patent: 5958769 (1999-09-01), Roberts et al.
patent: 6242575 (2001-06-01), Massague et al.
Campbell and Wilmut, 1997, Totipotency or multipotency of cultured cells: applications and progress, Theriogenology, vol. 47, pp. 63-72.
Wheeler, M.B. 2001, Transgenic technology and applications in swine. Theriogenology, vol. 56, pp. 1345-1369.
Prelle, K. 1999, Establishment of pluripotent cell lines from verterbrate species-present status and future prosopects, Cells Tissues Organs, vol. 165, pp. 220-236.
Thomson AJ et al., 2003, Gene targeting in livestock, Reprod. Supp., 61:495-508.
Poljaeva, I.A., 2000, Clone pigs produced by nuclear transfer from adult somatic cells. Nature, 407:86-90.
Williams, SH et al., 2003, Evaluation of gene targeting by homologous recombination in ovine somatic cells, Molecular Reproduction and Development, 66:115-125.
Harrison, SJ et al., 2002, Efficient generation of a(1,3) galactosyltransferase knockout porcine fetal fibroblasts for nuclear transfer, Transgenic Research, 11:143-150.
Denning, C et al., 2001, Gene targeting in primary fetal fibroblasts from sheep and pig, Cloning and Stem cells, 3:221-231.
McCreath, 2000, Production of gene-targeted sheep by nuclear transfer from cultured somatic cells, Nature, vol. 405, pp. 1066-1069.
Mir, B and Piedrahita, JA, 2004, Nuclear localization signal and cell synchrony enhance gene targeting efficiency in primary fetal fibroblasts, Nucl. Acids, Res., 32:e25.
MSN Encarta dictionary definition of murine, printout dated Aug. 9, 2007, http://encarta.msn.com/encnet/features/dictionary/DictionaryResults.aspx?refid=1861631945.
Agrawal, D. et al., “Repression of p27kip1synthesis by platelet-derived growth factor in BALB/c 3T3 cells,”Mol. Cell. Biol., 16(8):4327-4336 (Aug. 1996).
Bai, C. et al., “SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box,”Cell, 86(2):263-274 (Jul. 26, 1996).
Carrano, A. et al., “SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27,”Nat. Cell. Biol., 1(4):193-199 (Aug. 1999).
Feldman, R.M. et al., “A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p,”Cell, 91(2):221-230 (Oct. 17, 1997).
Fero, M. et al., “A syndrome of multiorgan hyperplasia with features of gigantism, tumorigenesis, and female sterility in p27Kip1-deficient mice,”Cell, 85(5):733-744 (May 31, 1996).
Friedrich, G. and Soriano, P., “Promoter traps in embryonic stem cells: genetic screen to identify and mutate development genes in mice,”Genes Dev., 5(9):1513-1523 (Sep. 1991).
Gould, K. et al., “Phosphorylation at Thr167 is required forSchizosaccharomyces pombep34cdc2function,”EMBO J., 10(11):3297-3309 (Nov. 1991).
Hannon, G.and Beach, D., “p15INK4Bis a potential effector of TGF-β-induced cell cycle arrest,”Nature, 371(6494):257-261 (Sep. 15, 1994).
Hatakeyama, M. et al., “The cancer cell and the cycle clock,”Cold Spring Harb. Symp. Quant. Biol., 59:1-10 (1994).
Hengst, L., and Reed, S., “Translational control of p27Kip1accumulation during the cell cycle,”Science, 271(5257):1861-1864 (Mar. 29, 1996).
Holmes, J. and Solomon, M., “A predictive scale for evaluating cyclin-dependent kinase substrates. A comparison of p34cdc2and p33cdk2,”J. Biol. Chem., 271(41):25240-25246 (Oct. 11, 1996).
Jeffrey, P., et al., “Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex,”Nature, 376(6538):313-320 (Jul. 27, 1995).
Kato, J. et al., “Cyclic AMP-induced G1 phase arrest mediated by an inhibitor (p27Kip1) of cyclin-dependent kinase 4 activation,”Cell, 79(3):487-496 (Nov. 4, 1994).
Koff, A. et al., “Negative regulation of G1 in mammalian cells: inhibition of cyclin E-dependent kinase by TGF-β,”Science, 260(5107):536-539 (Apr. 23, 1993).
Lee, MH et al., “Cloning of p57KIP2, a cyclin-dependent kinase inhibitor with unique domain structure and tissue distribution,”Genes Dev., 9(6):639-649 (Mar. 15, 1995).
Leone, G. et al., “Myc and Ras collaborate in incducing accumulation of active cyclin E/Cdk2 and E2F,”Nature, 387(6631):422-426 (May 22, 1997).
Malek, N. et al., “A mouse knock-in model exposes sequential proteolytic pathways that regulate p27Kip1in G1 and S phase,”Nature, 413(6853):323-327 (Sep. 20, 2001).
Millard, S.S. et al., “A U-rich element in the 5′ untranslated region is necessary for the translation of p27 mRNA,”Mol. Cell. Biol., 20(16):5947-5959 (Aug. 2000).
Millard, S.S. et al., “Enhanced ribosomal association of p27Kip1mRNA is a mechanism contributing to accumulation during growth arrest,”J. Biol. Chem., 272(11):7093-7098 (Mar. 14, 1997).
Montagnoli, A. et al., “Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation,”Genes Dev., 13(9):1181-1189 (May 1, 1999).
Morgan, D., “Principles of CDK regulation,”Nature, 374(6518):131-134 (Mar. 9, 1995).
Morimoto, M. et al., “Modification of cullin-1 by ubiquitin-like protein Nedd8 enhances the activity of SCFskp2toward p27Kip1,”Biochem. Biophys. Res. Commun., 270(3):1093-1096 (Apr. 21, 2000).
Müller, D. et al., “Cdk2-dependent phosphorylation of p27 facilitates its Myc-induced release from cyclin E/cdk2 complexes,”Oncogene, 15(21):2561-2576 (Nov. 20, 1997).
Nagy, A. et al., “Dissecting the role ofN-mycin development using a single targeting vector to generate a series of alleles,”Curr. Biol., 8(11):661-664 (May 21, 1998).
Nourse, J. et al., “Interleukin-2-mediated elimination of the p27Kip1cyclin-dependent kinase inhibitor prevented by rapamycin,”Nature, 372(6506):570-573 (Dec. 8, 1994).
O'Hagan, R. et al., “Myc-enhanced expression of Cul1 promotes ubiquitin-dependent proteolysis and cell cycle progression,”Genes Dev., 14(17):2185-2191 (Sep. 1, 2000).
Pardee, A., “A restriction point for control of normal animal cell proliferation,”Proc. Natl. Acad. Sci. USA., 71(4):1286-1290 (Apr. 1974).
Polyak, K. et al., “Cloning of p27Kip1, a cyclin-dependent kinase inhibitor and a potential mediator of extracellular antimitogenic signals,”Cell, 78(1):59-66 (Jul. 15, 1994).
Rolfe, M. et al., “The ubiquitin-mediated proteolytic pathway as a therapeutic area,”J. Mol. Med., 75(1):5-17 (Jan. 1997).
Serrano, M. et al., “A new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4,”Nature, 366(6456):704-707 (Dec. 16, 1993).
Sheaff, R. et al., “Cyclin E-CDK2 is a regulator of p27Kip1,”Genes Dev., 11(11):1464-1478 (Jun. 1, 1997).
Sherr, C. and Roberts, J. “CD inhibitors: positive and negative regulators of G1-phase progression,”Genes Dev., 13(12):1501-1512 (Jun. 15, 1999).
Shilo, B.Z. and Weinberg, R., “DNA sequences homologous to vertebrate oncogenes are conserved inDrosophilia melanogaster,” Proc. Natl. Acad. Sci. USA., 78(11):6789-6792 (Nov. 1981).
Skowyra, D. et al., “F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex,”Cell, 91(2):209-219 (Oct. 17, 1997).
Solomon, M. et al., “CAK, the p34cdc2activating kinase, contains a protein identical or closely related to p40MO15,”EMBO J., 12(8):3133-3142 (Aug. 1993).
Solomon, M. et al., “Role of phosphorylation in p34cdc2activation: Identification of an activating kinase,”Mol. Biol. Cell, 3(1):13-27 (Jan. 1992).
Sutterlüty, H. et al., “p45SKP2promotes p27Kip1degradation and induces S phase in q

Affiliated with

Also associated with

Rating

Compositions and methods for increasing animal size growth rate does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Compositions and methods for increasing animal size growth rate, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Compositions and methods for increasing animal size growth rate will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-4018571