Heat shock protein 90 as a molecular target for cancer therapeutics

Cancer Cell

Volumn 3, Issue 3, 2003, Pages 213-217

  Isaacs, Jennifer S ^a   Xu, Wanping ^a   Neckers, Len ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

17 ALLYLAMINO 17 DESMETHOXYGELDANAMYCIN; ANSAMYCIN DERIVATIVE; ANTIINFECTIVE AGENT; BENZOQUINONE; CHAPERONE; DOXORUBICIN; GELDANAMYCIN; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HERBIMYCIN A; IMATINIB; PACLITAXEL; PROTEIN INHIBITOR; RADICICOL; UNCLASSIFIED DRUG;

ACUTE LYMPHOCYTIC LEUKEMIA; AMINO TERMINAL SEQUENCE; BREAST CARCINOMA; CANCER CELL; CANCER GROWTH; CANCER THERAPY; CELL GROWTH; CELL STRAIN 3T3; CHRONIC MYELOID LEUKEMIA; DRUG BINDING; HUMAN; KIDNEY CARCINOMA; MOLECULAR BIOLOGY; NONHUMAN; PRIORITY JOURNAL; PROSTATE CARCINOMA; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DEGRADATION; REDUCTION; REVIEW; ANIMAL; BIOLOGICAL MODEL; BREAST TUMOR; FEMALE; GENE EXPRESSION REGULATION; GENETICS; MALE; METABOLISM; NEOPLASM; PROSTATE TUMOR;

ANIMALS; BREAST NEOPLASMS; CARCINOMA, RENAL CELL; FEMALE; GENE EXPRESSION REGULATION, NEOPLASTIC; HSP90 HEAT-SHOCK PROTEINS; HUMANS; LEUKEMIA, MYELOID, CHRONIC; MALE; MODELS, BIOLOGICAL; NEOPLASMS; PROSTATIC NEOPLASMS;

EID: 0043288724     PISSN: 15356108     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1535-6108(03)00029-1     Document Type: Review

References (41)

1. Baselga J., Norton L., Albanell J., Kim Y.M., Mendelsohn J. Recombinant humanized anti-HER2 antibody (Herceptin) enhances the antitumor activity of paclitaxel and doxorubicin against HER2/neu overexpressing human breast cancer xenografts. Cancer Res. 58:1998;2825-2831.
2. Basso A.D., Solit D.B., Munster P.N., Rosen N. Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2. Oncogene. 21:2002;1159-1166.
3. Blagosklonny M.V., Fojo T., Bhalla K.N., Kim J.S., Trepel J.B., Figg W.D., Rivera Y., Neckers L.M. The Hsp90 inhibitor geldanamycin selectively sensitizes Bcr-Abl-expressing leukemia cells to cytotoxic chemotherapy. Leukemia. 15:2001;1537-1543.
4. Connell P., Ballinger C.A., Jiang J., Wu Y., Thompson L.J., Hohfeld J., Patterson C. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat. Cell Biol. 3:2001;93-96.
5. Csermely P., Kajtar J., Hollosi M., Jalsovszky G., Holly S., Kahn C.R., Gergely P. Jr., Soti C., Mihaly K., Somogyi J. ATP induces a conformational change of the 90-kDa heat shock protein (hsp90). J. Biol. Chem. 268:1993;1901-1907.
6. Gnarra J.R., Tory K., Weng Y., Schmidt L., Wei M.H., Li H., Latif F., Liu S., Chen F., Duh F.M., et al. Mutations of the VHL tumour suppressor gene in renal carcinoma. Nat. Genet. 7:1994;85-90.
7. Gorre M.E., Ellwood-Yen K., Chiosis G., Rosen N., Sawyers C.L. BCR-ABL point mutants isolated from patients with STI571-resistant chronic myeloid leukemia remain sensitive to inhibitors of the BCR-ABL chaperone heat shock protein 90. Blood. 100:2002;3041-3044.
8. Gradin K., McGuire J., Wenger R.H., Kvietikova I., Whitelaw M.L., Toftgard R., Tora L., Gassmann M., Poellinger L. Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor. Mol. Cell. Biol. 16:1996;5221-5231.
9. Grenert J.P., Sullivan W.P., Fadden P., Haystead T., Clark J., Mimnaugh E., Krutzsch H., Ochel H.J., Schulte T.W., Sausville E., et al. The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation. J. Biol. Chem. 272:1997;23843-23850.
10. Grenert J.P., Johnson B.D., Toft D.O. The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes. J. Biol. Chem. 274:1999;17525-17533.
11. Harris A.L. Hypoxia - a key regulatory factor in tumor growth. Nat. Rev. Cancer. 2:2002;38-47.
12. Hernandez M.P., Sullivan W.P., Toft D.O. The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex. J. Biol. Chem. 277:2002;38294-38304.
13. Hur E., Kim H.H., Choi S.M., Kim J.H., Yim S., Kwon H.J., Choi Y., Kim D.K., Lee M.O., Park H. Reduction of hypoxia-induced transcription through the repression of hypoxia-inducible factor-1alpha/aryl hydrocarbon receptor nuclear translocator DNA binding by the 90-kDa heat-shock protein inhibitor radicicol. Mol. Pharmacol. 62:2002;975-982.
14. Isaacs J.S., Jung Y.J., Mimnaugh E.G., Martinez A., Cuttitta F., Neckers L.M. Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 alpha-degradative pathway. J. Biol. Chem. 277:2002;29936-29944.
15. Kelland L.R., Sharp S.Y., Rogers P.M., Myers T.G., Workman P. 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.
16. Kondo K., Klco J., Nakamura E., Lechpammer M., Kaelin W.G. Jr. Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein. Cancer Cell. 1:2002;237-246.
17. Maloney A., Workman P. HSP90 as a new therapeutic target for cancer therapy: the story unfolds. Expert Opin. Biol. Ther. 2:2002;3-24.
18. Maxwell P.H., Wiesener M.S., Chang G.-W., Clifford S.C., Vaux E.C., Cockman M.E., Wykoff C.C., Pugh C.W., Maher E.R., Ratcliffe P.J. The tumor suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis. Nature. 399:1999;271-275.
19. McLaughlin S.H., Smith H.W., Jackson S.E. Stimulation of the weak ATPase activity of human hsp90 by a client protein. J. Mol. Biol. 315:2002;787-798.
20. Minet E., Mottet D., Michel G., Roland I., Raes M., Remacle J., Michiels C. Hypoxia-induced activation of HIF-1: role of HIF-1alpha-Hsp90 interaction. FEBS Lett. 460:1999;251-256.
21. Neckers L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol. Med. 8:2002;S55-S61.
22. Nimmanapalli R., O'Bryan E., Bhalla K. Geldanamycin and its analogue 17-allylamino-17-demethoxygeldanamycin lowers Bcr-Abl levels and induces apoptosis and differentiation of Bcr- Abl-positive human leukemic blasts. Cancer Res. 61:2001;1799-1804.
23. Ohh M., Park C.W., Ivan M., Hoffman M.A., Kin T.-Y., Huang L.E., Pavletich N., Chau V., Kaelin W.G. Ubiquitination of hypoxia-inducible factor requires direct binding to the B-domain of the von Hippel-Lindau protein. Nat. Cell Biol. 2:2000;423-427.
24. Oppermann H., Levinson A.D., Levintow L., Varmus H.E., Bishop J.M., Kawai S. Two cellular proteins that immunoprecipitate with the transforming protein of Rous sarcoma virus. Virology. 113:1981;736-751.
25. Panaretou B., Prodromou C., Roe S.M., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J. 17:1998;4829-4836.
26. Panaretou B., Siligardi G., Meyer P., Maloney A., Sullivan J.K., Singh S., Millson S.H., Clarke P.A., Naaby-Hansen S., Stein R., et al. Activation of the ATPase activity of Hsp90 by the stress-regulated cochaperone Aha1. Mol. Cell. 10:2002;1307-1318.
27. Pegram M.D., Lipton A., Hayes D.F., Weber B.L., Baselga J.M., Tripathy D., Baly D., Baughman S.A., Twaddell T., Glaspy J.A., Slamon D.J. Phase II study of receptor-enhanced chemosensitivity using recombinant humanized anti-p185HER2/neu monoclonal antibody plus cisplatin in patients with HER2/neu-overexpressing metastatic breast cancer refractory to chemotherapy treatment. J. Clin. Oncol. 16:1998;2659-2671.
28. Prodromou C., Roe S.M., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell. 90:1997;65-75.
29. Scheibel T., Buchner J. The Hsp90 complex-a super-chaperone machine as a novel drug target. Biochem. Pharmacol. 56:1998;675-682.
30. Schneider C., Sepp-Lorenzino L., Nimmesgern E., Ouerfelli O., Danishefsky S., Rosen N., Hartl F.U. Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90. Proc. Natl. Acad. Sci. USA. 93:1996;14536-14541.
31. Seizinger B.R., Rouleau G.A., Ozelius L.J., Lane A.H., Farmer G.E., Lamiell J.M., Haines J., Yuen J.W., Collins D., Majoor-Krakauer D., et al. Von Hippel-Lindau disease maps to the region of chromosome 3 associated with renal cell carcinoma. Nature. 332:1988;268-269.
32. Sharma S.V., Agatsuma T., Nakano H. Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol. Oncogene. 16:1998;2639-2645.
33. Shiotsu Y., Neckers L.M., Wortman I., An W.G., Schulte T.W., Soga S., Murakata C., Tamaoki T., Akinaga S. Novel oxime derivatives of radicicol induce erythroid differentiation associated with preferential G(1) phase accumulation against chronic myelogenous leukemia cells through destabilization of Bcr-Abl with Hsp90 complex. Blood. 96:2000;2284-2291.
34. Siligardi G., Panaretou B., Meyer P., Singh S., Woolfson D.N., Piper P.W., Pearl L.H., Prodromou C. Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37. J. Biol. Chem. 277:2002;20151-20159.
35. Solit D., Zheng F., Drobnjak M., Munster P., Higgins B., Verbel D., Heller G., Tong W., Cordon-Cardo C., Agus D., et al. 17-allylamino-17- demthoxygeldanamycin 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.
36. Stebbins C.E., Russo A.A., Schneider C., Rosen N., Hartl F.U., Pavletich N.P. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell. 89:1997;239-250.
37. Whitesell L., Mimnaugh E.G., De Costa B., Myers C.E., Neckers L.M. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc. Natl. Acad. Sci. USA. 91:1994;8324-8328.
38. Wiesener M.S., Munchenhagen P.M., Berger I., Morgan N.V., Roigas J., Schwiertz A., Jurgensen J.S., Gruber G., Maxwell P.H., Loning S.A., et al. Constitutive activation of hypoxia-inducible genes related to overexpression of hypoxia-inducible factor-1alpha in clear cell renal carcinomas. Cancer Res. 61:2001;5215-5222.
39. Xu W., Mimnaugh E., Rosser M.F., Nicchitta C., Marcu M., Yarden Y., Neckers L. Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90. J. Biol. Chem. 276:2001;3702-3708.
40. Xu W., Marcu M., Yuan X., Mimnaugh E., Patterson C., Neckers L. The chaperone-dependent E3 ubiquitin ligase CHIP mediates a novel degradative pathway for c-ErbB2/Neu. Proc. Natl. Acad. Sci. USA. 99:2002;12847-12852.
41. Young J.C., Hartl F.U. Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23. EMBO J. 19:2000;5930-5940.