HspBP polypeptides and peptide fragments that bind Hsp 70

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

Reexamination Certificate

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C424S185100, C530S412000, C530S417000, C530S418000

Reexamination Certificate

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06908985

ABSTRACT:
Human heat-shock protein-binding proteins (HspBP-1 and HspBP-2) and fragments thereof are disclosed with the polynucleotides which identify and encode them. Genetically engineered expression vectors and host cells comprising the nucleic acid sequences encoding heat-shock protein-binding proteins (HspBP) are also disclosed and a method for producing HspBP polypeptides.

REFERENCES:
patent: 5955312 (1999-09-01), Hillman et al.
Sandström et al. Antiviral Therapy in AIDS: Clinical and pharmacological properties and therapeutic experience to date. Drugs (1987) vol. 34, pp. 372-390.
Kerr et al. The relationship between cytotoxic drup exposure and tumor cell kill in vitro and in vivo, In Vivo (1991) vol. 5, pp. 385-388.
Chornienne et al., Discrepancy between in vitro and in vivo passaged U-937 human leukemic Cells: Tumerorigenicity and sensitivity to differentiating drugs. In Vivo, 1988.
Washington Times Article by Joyce Howard Price, Nov. 16, 2001, p. 3.
Mitsuya et al. Suramin protection of T Cells in vitro against infectivity and cytopathic effect of HTLV-III. Science, (1984) vol. 22 pp. 172-174.
Paul Fundamental Immunology, Rave Press, New York, NY; 1993, 3rd Edition, p. 251, col. 1, lines 11-12.
Klein Self-nonself discrimination, histoincompatibility, and the concept of immunology, Immunogenetics, 1999, vol. 50, No. 3-4 pp. 116-123.
Ristori et al. Compositional bias and mimicry toward the nonself proteome in immunodominant T cell epitopes of self and nons antigens. FASEB, 2000, vol. 14, No. 3, pp. 431-438.
Planchon et al. Differential effect of butyrate derivatives on human breast cancer cells grown as organotypic nodules in vitro an as xenografts in vivo, In Vivo (1992) vol. 6, pp. 605-610.
S. Lindquist and B.A. Craig, “The Heat Shock Proteins,” Annual Revue of Genetics, 22:631-77, 1988.
Hohfeld, Jorg, et al., “Hip, a Novel Cochaperone Involved in the Eukaryotic Hsc70/Hsp40 Reaction Cycle,” Cell vol. 83, 589-598 (Nov. 17, 1995).
Cyr, D. M. et al., “DnaJ-like Proteins: Molecular Chaperones and Specific Regulators of Hsp70,” TIBS 19 (Apr., 1994).
Johnson, B.D., et al., “Hop Modulates Hsp70/Hsp90 Interactions in Protein Folding,” JBS 273:6, pp. 3679-3686 (Feb. 6, 1998).
Leung, S.N. and L.E. Hightower, “A 16-kDa Protein Functions as a New Regulatory Protein for Hsc70 Molecular Chaperone and Is Identified as a Member of the Nm23/Nucleoside Diphosphate Kinase Family,” JBC 272:5, pp. 2607-2614 (Jan. 31, 1997).
Chamberlain, L.H. and R.D. Burgoyne, “Activation of the ATPase Activity of Heat-Shock Proteins Hsc70/Hsp70 by Cysteine-String Protein,” Biochem. J. 322, pp. 853-858 (1997).
Braun, J.E.A., et al., “The Cysteine String Secretory Vesicle Protein Activates Hsc70 ATPase,” JBC 271:42, pp. 25989-25993 (Oct. 18, 1996).
Jiang, R.F. et al., “Interaction of Auxilin with the Molecular Chaperone, Hsc70,” JBC 272:10, pp. 6141-6145 (Mar. 7, 1997).
Zeiner, N. et al., “Mammalian protein RAP46: an interaction partner and modulator of 70 dDA heat shock proteins,” EMBO J. 16:18, pp. 5483-5490 (1997).
Takayama, S. et al., “BAG-1 modulates the chaperone activity of Hsp70/Hsc70,” EMBO J. 16:16, pp. 4887-4896 (1997).
V.L. et al., “Hsp70 Prevents Activation of Stress Kinase,” JBC 272:29, pp. 18033-18037 (Jul. 18, 1997).
Mosser, D.D. et al., “Role of the Human Heat Shock Protein Hsp70 in Protection Against Stress-Induced Apoptosis,” Mol. and Cell. Biol., 17:9, pp. 5317-5327 (Sep., 1997).
Bartel, P.L. et al., “Using the two-hybrid system to detect protein—protein interactions,” from “Cellular Interactions in Development: A Practical Approach” (Ed. David Hartley) Oxford University Press (1993).
Berger and Kimmel (1987, “Guide to Molecular Cloning Techniques, Methods in Enzymology,” v. 152, Academic Press, San Diego, CA).
Sambrook, J. et al., “Molecular Cloning, A Laboratory Manual,” Cold Spring Harbor Press, Plainview, N.Y. (1989).
“Remington's Pharmaceutical Sciences” (Maack Publishing Co., Easton, PA).
Raynes et al., “Inhibition of Hsp70 ATPase Activity and Protein Renaturation by a Novel Hsp70-binding Protein,” The Journal of Biological Chemistry, vol. 273, pp. 32883-32888, Dec. 4, 1998.
Hillier et al. Generation and Analysis of 280,000 Human Expressed Sequence Tags. Genome Research. Sep. 1996, see pp. 807-827.
Pharmacia Biotech Overview of Molecular Biology Products. 1996, pp. 107, 110-117, 139, 163-165.
Stratagene Cloning Systems. 1997, see pp. 42-43.
Fix, J.A. Oral Controlled Release Technology for Peptides: Status and Future Prospects. Pharmaceutical Research, 1996, vol. 13, No. 12, see pp. 1760-1764.
Takakura et al. Macromolecular Carrier Systems for Targeted Drug Delivery: Pharmacokinetic Considerations on Biodistribution. Pharmaceutical Research, 1996, vol. 13, No. 6, pp. 820-831.
Riffkin et al. A Single Amino Acid Change Between the Antigenically Different Extracellular Serine Proteases V2 and B2 from Dichelobacter Nodosus. Gene (1995) vol. 167, pp 279-283.
Raynes, Deborah A. and Vince Guerriero, “Isolation and Characterization of Isoforms of HspBP1, Inhibitors of Hsp70”, Biochimica et Biophysica Acta 1490 (2000) pp. 203-207.

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