pDJA1, a cardiac specific gene, corresponding proteins, and...

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues

Reexamination Certificate

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C514S012200

Reexamination Certificate

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07009038

ABSTRACT:
The present invention provides novel nucleic acid and protein sequences for methods and compositions for treating, screening, and diagnosing cardiovascular disease and methods for using these genes and gene products for prevention of cardiac cell death and prevention of cardiac tissue damage resulting from ischemic events in cardiac tissue, as well as other tissue that is subject to damage resulting from an ischemic event. The genes, gene products and agents of the invention are also useful for treating other related clinical or coronary events such as angina, myocardial infarct (MI), and stroke, for monitoring the effectiveness of their treatment, and for drug development. The genes, gene products and agents of the present invention are also provided as pharmaceutical compositions for treatment of cardiovascular disease, ischemic heart disease, myocardial infarct and related conditions. Kits are also provided for the diagnosis, treatment and prognosis of cardiac diseases and related conditions.

REFERENCES:
patent: WO 01/53312 (2001-08-01), None
Hata et al., Murine cDNA enoding a novel type I HSP40/DNAJ homolog, mmDjA4, Biochim. Biophys. Acta (2000), 1493, 1493, p. 208-210.
Terada et al., Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperons of hsc70, J. Biol. Chem., (2000), 275, p. 24728-24734.
Ohtsuka, Kenzo et al. (2000) “Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature” Cell Stress & Chaperones. vol.: 5, No. 2, pp. 98-112.
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Minami, Yasufumi et al. (1996) “Regulation of the Heat-shock Protein 70 Reaction Cycle by the Mammalian DnaJ Homolog, Hsp40” J. of Biological Chem. vol.: 271, No. 32, pp. 19617-19624.
Depre, Christophe et al. (2001) “Gene program for cardiac cell survival induced by transient ischemia in conscious pigs” Proc Natl Acad Sci USA vol.: 98 No. 16, pp. 9336-9341.
Shu, Won-Chul et al. (1998) “Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ” Proc Natl Acad Sci USA vol.: 95, pp. 15223-15228.
Diefenbach, Jorg et al. (2000) “The membrane-bound DnaJ protein located at athe cytosolic site of glyoxysomes specifically binds the cytosolic isoform 1 of Hsp70 but not other Hsp70 species” Eur J. Biochem vol.: 267, pp. 746-754.
Laufen, Thomas et al. (1999) “Mechanism of regulation of Hsp70 chaperones by DnaJ cocaperones” Proc Natl Acad Sci USA vol.: 96, pp. 5452-5457.
Hunter, Patricia J. et al (1999) “Mrj encodes a DnaJ-related co-chaperone that is essential for murine placental development” Development vol.: 126, pp. 1247-1258.
Kobayashi, Yasushi et al. (2000) “Chaperones Hsp70 and Hsp40 Suppress Aggregate Formation and Apoptosis in Cultured Neuronal Cells Expressing Truncated Androgen Receptor Protein with Expanded Polyglutamine Tract” J of Biological Chemistry vol.: 275, No. 12 pp. 8772-8778.
Greene, Michael K. et al. (1998) “Role of the J-domain in the cooperation of Hsp40 with Hsp70” Proc Natl Acad Sci USA vol.: 95, pp. 6108-6113.

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