Hsp90: The vulnerable chaperone

Drug Discovery Today

Volumn 9, Issue 20, 2004, Pages 881-888

  Chiosis, Gabriela ^a   Vilenchik, Maria ^a   Kim, Joungnam ^a   Solit, David ^a  

^a MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

Author keywords

17AAG; anti cancer therapy; CCT018159; Drug Discovery; Hsp90 chaperone; Hsp90 posttranslational modifications; PU24FCl

Indexed keywords

ALKYLATING AGENT; ANSAMYCIN DERIVATIVE; ANTIINFECTIVE AGENT; CHAPERONE; CISPLATIN; FR 901228; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; HERBIMYCIN; HYPERICIN; MELPHALAN; OXALIPLATIN; PROTEIN INHIBITOR; PURINE DERIVATIVE; PYRAZOLE; RADICICOL; STEROID RECEPTOR;

ACETYLATION; APOPTOSIS; CANCER THERAPY; CARBOXY TERMINAL SEQUENCE; CELL GROWTH; CELL SURVIVAL; CLINICAL TRIAL; COMPLEX FORMATION; DRUG BINDING; HUMAN; LIVER TOXICITY; NAUSEA; ODOR; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN PROCESSING; REVIEW; STRUCTURE ANALYSIS;

ANIMALS; ANTINEOPLASTIC AGENTS; APOPTOSIS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; NEOPLASMS;

EID: 4744350064     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-6446(04)03245-3     Document Type: Review

References (59)

1. Wegele H., et al. Hsp70 and Hsp90-a relay team for protein folding. Rev. Physiol. Biochem. Pharmacol. 151:2004;1-44
2. Mosser D.D., et al. Molecular chaperones and the stress of oncogenesis. Oncogene. 23:2004;2907-2918
3. Kamal A., et al. Therapeutic and diagnostic implications of Hsp90 activation. Trends Mol. Med. 10:2004;283-290
4. Kamal A., et al. A high affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature. 425:2003;407-410
5. Vilenchik M., et al. Targeting wide-range oncogenic transformation via PU24FCl, a specific inhibitor of tumor Hsp90. Chem. Biol. 11:2004;787-797
6. Fortugno P., et al. Regulation of survivin function by Hsp90. Proc. Natl. Acad. Sci. U. S. A. 100:2003;13791-13796
7. Sato S., et al. Modulation of Akt kinase activity by binding to Hsp90. Proc. Natl. Acad. Sci. U. S. A. 97:2000;10832-10837
8. Schulte T.W., et al. Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association. J. Biol. Chem. 270:1995;24585-24588
9. Lewis J., et al. Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation. J. Biol. Chem. 275:2000;10519-10526
10. Zhao C., Wang E. Heat shock protein 90 suppresses tumor necrosis factor alpha induced apoptosis by preventing the cleavage of Bid in NIH3T3 fibroblasts. Cell Signal. 16:2004;313-321
11. Pandley P., et al. Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procasapse-9 by heat shock. EMBO J. 19:2000;4310-4322
12. Neckers L., et al. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol. Med. 8:2002;S55-S61
13. Workman P., Maloney A., et al. HSP90 as a new therapeutic target for cancer therapy: the story unfolds. Expert Opin. Biol. Ther. 2:2002;3-24
14. Sreedhar A.S., et al. Inhibition of Hsp90: a new strategy for inhibiting protein kinases. Biochim. Biophys. Acta. 1697:2004;233-242
15. Prodromou C., et al. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell. 90:1997;65-75
16. Chene P., et al. ATPases as drug targets: learning from their structure. Nat. Rev. Drug Discov. 1:2002;665-673
17. Stebbins C.E., et al. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell. 89:1997;239-250
18. Neckers L., et al. Geldanamycin as a potential anti-cancer agent: its molecular target and biochemical activity. Invest. New Drugs. 17:1999;361-373
19. Schulte T.W., et al. GA-induced destabilization of Raf-1 involves the proteasome. Biochem. Biophys. Res. Commun. 239:1997;655-659
20. Munster P.N., et al. Inhibition of Hsp90 Function by Ansamycins Causes Morphological and Functional Differentiation of Breast Cancer Cells. Cancer Res. 61:2001;2945-2952
21. Hostein I., et al. Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in cytostasis and apoptosis. Cancer Res. 61:2001;4003-4009
22. Schulte T.W., Neckers L.M., et al. The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to Hsp90 and shares important biologic activities with geldanamycin. Cancer Chemother. Pharmacol. 42:1998;273-279
23. Zhang H. Characterization of a novel HSP90 inhibitor with an extended duration of action. In Proceedings of the AACR, 44, 2nd ed., July 2003, Washington, DC, USA
24. Solit D.B., et al. 17-Allylamino-17-demethoxygeldanamycin induces the degradation of androgen receptor and HER-2/neu and inhibits the growth of prostate cancer xenografts. Clin. Cancer Res. 8:2002;986-993
25. Kelland L.R., et al. DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90. J. Natl. Cancer Inst. 91:1999;1940-1949
26. Banerji U., et al. Preclinical and clinical activity of the molecular chaperone inhibitor 17-allylamino, 17-demethoxygeldanamycin (17AAG) in malignant melanoma. Proc. Am. Assoc. Cancer Res. 44:2003;677
27. Sausville E.A., et al. Clinical development of 17-allylamino, 17-demethoxygeldanamycin. Curr. Cancer Drug Targets. 3:2003;377-383
28. Solit D.Phase 1 pharmacokinetic and pharmacodynamic trial of docetaxel and 17AAG (17-allylamino-17-demethoxygeldanamycin), Annual Meeting of ASCO 3-8 June 2004, New Orleans, LA, USA
29. Egorin M.J., et al. Pharmacokinetics, tissue distribution, and metabolism of 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (NSC 707545) in CD2F1 mice and Fischer 344 rats. Cancer Chemother. Pharmacol. 49:2002;7-19
30. Kaur G., et al. Antiangiogenic properties of 17-(dimethylaminoethylamino) -17-demethoxygeldanamycin: an orally bioavailable heat shock protein 90 modulator. Clin. Cancer Res. 10:2004;4813-4821
31. Burger A.M., et al. 17-(Allylamino)-17-demethoxygeldanamycin activity in human melanoma models. Anticancer Drugs. 15:2004;377-387
32. th Annual Meeting of AACR, 27-31 March 2004, Orlando, FL, USA
33. th In Annual Meeting of AACR, 11-14 July 2003, Washington, DC, USA
34. th Annual Meeting of AACR, 11-14 July 2003, Washington, DC, USA
35. Schulte T.W., et al. Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin. Cell Stress Chaperones. 3:1998;100-108
36. Roe S.M., et al. Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J. Med. Chem. 42:1999;260-266
37. Soga S., et al. Development of radicicol analogues. Curr. Cancer Drug Targets. 3:2003;359-369
38. Yamamoto K., et al. Oriented total synthesis as a resource in the discovery of potentially valuable agents in oncology: Cycloproparadicicol. Angew. Chem. 42:2003;1280-1284
39. Chiosis G., et al. A Small Molecule Designed to Bind to the Adenine Nucleotide Pocket of Hsp90 Causes Her2 Degradation and the Growth Arrest and Differentiation of Breast Cancer Cells. Chem. Biol. 8:2001;289-299
40. Chiosis G., et al. Development of a Purine-based Novel Class of Hsp90 Binders That Inhibit the Proliferation of Cancer Cells and Induce the Degradation of Her2 Tyrosine Kinase. Bioorg. Med. Chem. 10:2002;3555-3564
41. Chiosis G., et al. Development of purine-scaffold small molecule inhibitors of Hsp90. Curr. Cancer Drug Targets. 3:2003;371-376
42. Wright L., et al. Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms. Chem. Biol. 11:2004;775-785
43. Rowlands M.G., et al. High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity. Anal. Biochem. 327:2004;176-183
44. th Annual Meeting of AACR, 11-14 July 2003, Washington, DC, USA
45. th Annual Meeting of AACR, 27-31 March 2004, Orlando, FL, USA
46. Marcu M.G., Neckers L.M., et al. The C-terminal half of heat shock protein 90 represents a second site for pharmacologic intervention in chaperone function. Curr Cancer Drug Targets. 3:2003;343-347
47. Marcu M.G., et al. The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone. J. Biol. Chem. 275:2000;37181-37186
48. Marcu M.G., et al. Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins. J. Natl. Cancer Inst. 92:2000;242-248
49. Soti C., et al. Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket. J. Biol. Chem. 277:2002;7066-7075
50. Itoh H., et al. A novel chaperone-activity-reducing mechanism of the 90-kDa molecular chaperone HSP90. Biochem. J. 343:1999;697-703
51. Rosenhagen M.C., et al. The heat shock protein 90-targeting drug cisplatin selectively inhibits steroid receptor activation. Mol. Endocrinol. 17:2003;1991-2001
52. th Annual Meeting of AACR, 27-31 March 2004, Orlando, FL, USA
53. Nardai G., et al. Reactive cysteines of the 90-kDa heat shock protein, Hsp90. Arch. Biochem. Biophys. 384:2000;59-67
54. Zhao Y.G., et al. Hsp90 phosphorylation is linked to its chaperoning function. Assembly of the reovirus cell attachment protein. J. Biol. Chem. 276:2001;32822-32827
55. Yu X., et al. Modulation of p53, ErbB1, ErbB2, and Raf-1 expression in lung cancer cells by depsipeptide FR901228. J. Natl. Cancer Inst. 94:2002;504-513
56. Atadja P., et al. Molecular and cellular basis for the anti-proliferative effects of the HDAC inhibitor LAQ824. Novartis Found. Symp. 259:2004;249-266
57. Blank M., et al. Enhanced ubiquitinylation of heat shock protein 90 as a potential mechanism for mitotic cell death in cancer cells induced with hypericin. Cancer Res. 63:2003;8241-8247
58. Barbosa J.A., et al. Discovery of novel small molecule hsp90 complex inhibitors using a forward chemical genetics approach. Supplement to Clinical Cancer Research. 9:2003;. (Abstract B161)
59. Rutherford S.L., Lindquist S., et al. Hsp90 as a capacitor for morphological evolution. Nature. 396:1998;336-342