A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors

Nature

Volumn 425, Issue 6956, 2003, Pages 407-410

  Kamal, Adeela ^a   Thao, Lia ^a   Sensintaffar, John ^a   Zhang, Lin ^a   Boehm, Marcus F ^a   Fritz, Lawrence C ^a   Burrows, Francis J ^a  

^a BIOGEN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEXATION; CONFORMATIONS; DEGRADATION; TUMORS;

TUMOR SELECTIVITY;

PROTEINS;

17 ALLYLAMINOGELDANAMYCIN; ADENOSINE TRIPHOSPHATASE; BCR ABL PROTEIN; CHAPERONE; EPIDERMAL GROWTH FACTOR RECEPTOR 2; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; NEU DIFFERENTIATION FACTOR; ONCOPROTEIN; PROTEIN INHIBITOR; PROTEIN KINASE B; PROTEIN P53; UNCLASSIFIED DRUG;

CANCER; MEDICINE;

ANTINEOPLASTIC ACTIVITY; ARTICLE; BINDING AFFINITY; CANCER INHIBITION; CANCER THERAPY; CELL MATURATION; CLINICAL TRIAL; COMPLEX FORMATION; CONTROLLED CLINICAL TRIAL; CONTROLLED STUDY; DISEASE COURSE; DRUG SELECTIVITY; GENE MUTATION; HEAT STRESS; HUMAN; HUMAN CELL; IN VITRO STUDY; INHIBITION KINETICS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN INDUCTION; SIGNAL TRANSDUCTION;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; ANTINEOPLASTIC AGENTS; BENZOQUINONES; CELL LINE; CYSTEINE ENDOPEPTIDASES; HSP90 HEAT-SHOCK PROTEINS; HUMANS; INHIBITORY CONCENTRATION 50; LACTAMS, MACROCYCLIC; MULTIENZYME COMPLEXES; NEOPLASMS; PRECIPITIN TESTS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN BINDING; PROTEIN CONFORMATION; RIFABUTIN; SUBSTRATE SPECIFICITY; TUMOR CELLS, CULTURED;

EID: 0141484615     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01913     Document Type: Article

References (30)

1. Schulte, T W. & Neckers, L. M. The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin. Cancer Chemother. Pharmacol. 42, 273-279 (1998).
2. Xu, W. et al. Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90. J. Biol. Chem. 276, 3702-3708 (2001).
3. Sato, S., Fujita, N. & Tsuruo, T. Modulation of Akt kinase activity by binding to Hsp90. Proc. Natl Acad. Sci. USA 97, 10832-10837 (2000).
4. 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, 1159-1166 (2002).
5. Schulte, T. W., Blagosklonny, M. V., Ingui, C. & Neckers, L. 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, 24585-24588 (1995).
6. An, W. G., Schulte, T. W. & Neckers, L. M. The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation b), the proteasome. Cell Growth Differ. 11, 355-360 (2000).
7. Blagosldonny, M. V., Toretsky, J. & Neckers, L. Geldanamycin selectively destabilizes and conformationally alters mutated p53. Oncogene 11, 933-939 (1995).
8. 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, 8324-8328 (1994).
9. Miller, P. et al. Depletion of the erbB-2 gene product p185 by benzoquinoid ansamycins. Cancer Res. 54, 2724-2730 (1994).
10. Mimnaugh, E. G., Chavany, C. & Neckers, L. Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin. J. Biol. Chem. 271, 22796-22801 (1996).
11. Schulte, T. W., An, W. G. & Neckers, L. M. Geldanamycin-induced destabilization of Raf-1 involves the proteasome. Biochem. Biophys. Res. Commun. 239, 655-659 (1997).
12. Workman, P. Auditing the pharmacological accounts for hsp90 molecular chaperone inhibitors: Unfolding the relationship between pharmacokinetics and pharmacodynamics. Mol. Cancer Ther. 2, 131-138 (2003).
13. Isaacs, J. S., Xu, W. & Neckers, L. Heal shock protein 90 as a molecular target for cancer therapeutics. Cancer Cell 3, 213-217 (2003).
14. Prodromou, C. et al. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90, 65-75 (1997).
15. Stebbins, C. E. et al. Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent. Cell 89, 239-250 (1997).
16. Obermann, W. M., Sondermann, H., Russo, A. A., Pavletich, N. P. & Hartl, F. U. In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. J. Cell Biol. 143, 901-910 (1998).
17. Panaretou, B. et al. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J. 17, 4829-4836 (1998).
18. 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, 17525-17533 (1999).
19. 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, 986-993 (2002).
20. Blagosklonny, M. V. Hsp-90-associated oncoproteins: Multiple targets of geldanamycin and its analogs. Leukemia 16, 455-462 (2002).
21. 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, 289-299 (2001).
22. Egorin, M. J. et al. PC3 human prostate xenograft retention of, and oncoprotein modulation by 17-(allylamino)-17-demothoxygeldanamycin(17AAG) in vivo. Proc. Am. Assoc. Cancer Res. 40, 3409 (1999).
23. Chiosis, G. et al. 17AAG: Low target binding affinity and potent cell activity-finding an explanation. Mol Cancer Ther. 2, 123-129 (2003).
24. Richter, K. & Buchner, J. Hsp90: Chaperoning signal transduction. J. Cell. Physiol. 188, 281-290 (2001).
25. Schuh, S. et al. A 90,000-dalton binding protein common to both steroid receptors and the Rous sarcoma virus transforming protein, pp60v-src. J. Biol. Chem. 260, 14292-14296 (1985).
26. Kosano, H., Stensgard, B., Charlesworth, M. C., McMahon, N. & Toft, D. The assembly of progesterone receptor-hsp90 complexes using purified proteins. J. Biol. Chem. 273, 32973-32979 (1998).
27. Gress, T. M. et al. Differential expression of heat shock proteins in pancreatic carcinoma. Cancer Res. 54, 547-551 (1994).
28. Yano, M., Naito, Z., Tanaka, S. & Asano, G. Expression and roles of heat shock proteins in human breast cancer. Jpn. J. Cancer Res. 87, 908-915 (1996).
29. Rutherford, S. L. & Lindquist, S. Hsp90 as a capacitor for morphological evolution. Nature 396, 336-342 (1998).
30. Queitsch,C., Sangster, T. A. & Lindquist, S. Hsp90 as a capacitor of phenotypic variation. Nature 417, 618-624 (2002).