Advanced search
Publication Cover
Expert Opinion on Therapeutic Targets Volume 10, 2006 - Issue 1
Submit an article Journal homepage
177
Views
65
CrossRef citations to date
0
Altmetric
Review

Targeting chaperones in transformed systems – a focus on Hsp90 and cancer

Gabriela Chiosis Assistant Member and Laboratory Head, Memorial Sloan-Kettering Cancer Center, Programme in Molecular Pharmacology and Chemistry, Department of Medicine, 1275 York Ave., Box 482, New York, NY 10021, USA. [email protected]
Pages 37-50 | Published online: 27 Jan 2006

Bibliography

  • DRUKER BJ: Imatinib as a paradigm of targeted therapies. Adv. Cancer Res. (2004) 91:1-30.
  • WILLEMS A, GAUGER K, HENRICHS C, HARBECK N: Antibody therapy for breast cancer. Anti-Cancer Res. (2005) 25:1483-1489.
  • BYRNE BJ, GARST J: Epidermal growth factor receptor inhibitors and their role in non-small-cell lung cancer. Curr. Oncol. Rep. (2005) 7:241-247.
  • REN R: Mechanisms of BCR-ABL in the pathogenesis of chronic myelogenous leukaemia. Nat. Rev. Cancer (2005) 5:172-183.
  • WORKMAN P: Combinatorial attack on multistep oncogenesis by inhibiting the Hsp90 molecular chaperone. Cancer Lett. (2004) 206:149-157.
  • ZHANG H, BURROWS F: Targeting multiple signal transduction pathways through inhibition of Hsp90. J. Mol. Med. (2004) 82:488-499.
  • CHIOSIS G, VILENCHIK M, KIM J, SOLIT D: Hsp90: the vulnerable chaperone. Drug Discov. Today (2004) 9:881-888.
  • WHITESELL L, LINDQUIST SL: HSP90 and the chaperoning of cancer. Nat. Rev. Cancer (2005) 5:761-772.
  • NECKERS L, NECKERS K: Heat-shock protein 90 inhibitors as novel cancer chemotherapeutics – an update. Expert Opin. Emerg. Drugs (2005) 10:137-149.
  • WEGELE H, MULLER L, BUCHNER J: Hsp70 and Hsp90-a relay team for protein folding. Rev. Physiol. Biochem. Pharmacol. (2004) 151:1-44.
  • PRODROMOU C, PEARL LH: Structure and functional relationships of Hsp90. Curr. Cancer Drug Targets (2003) 3:301-323.
  • PRATT WB, GALIGNIANA MD, MORISHIMA Y, MURPHY PJ: Role of molecular chaperones in steroid receptor action. Essays Biochem. (2004) 40:41-58.
  • CHENE P: ATPases as drug targets: learning from their structure. Nat. Rev. Drug Discov. (2002) 1:665-673.
  • DUTTA R, INOUYE M: GHKL, an emergent ATPase/kinase superfamily. Trends Biochem. Sci. (2000) 25:24-28.
  • NECKERS L, SCHULTE TW, MIMNAUGH E: Geldanamycin as a potential anti-cancer agent: its molecular target and biochemical activity. Invest. New Drugs (1999) 17:361-373.
  • SCHULTE TW, NECKERS LM: The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to Hsp90 and shares important biologic activities with geldanamycin. Cancer Chemother. Pharmacol. (1998) 42:273-279.
  • SMITH V, SAUSVILLE EA, CAMALIER RF, FIEBIG HH, BURGER AM: Comparison of 17-dimethylaminoethylamino-17-demethoxy-geldanamycin (17DMAG) and 17-allylamino-17-demethoxygeldanamycin (17AAG) in vitro: effects on Hsp90 and client proteins in melanoma models. Cancer Chemother. Pharmacol. (2005) 56:126-137.
  • SOGA S, SHIOTSU Y, AKINAGA S, SHARMA SV: Development of radicicol analogues. Curr. Cancer Drug Targets (2003) 3:359-369.
  • YAMAMOTO K, GARBACCIO RM, STACHEL SJ et al.: Target oriented total synthesis as a resource in the discovery of potentially valuable agents in oncology: Cycloproparadicicol. Angew. Chemie (2003) 42:1280-1284.
  • MOULIN E, ZOETE V, BARLUENGA S, KARPLUS M, WINSSINGER N: Design, synthesis, and biological evaluation of HSP90 inhibitors based on conformational analysis of radicicol and its analogues. J. Am. Chem. Soc. (2005) 127:6999-7004.
  • CHIOSIS G, LUCAS B, HUEZO H, SOLIT D, BASSO A, ROSEN N: Development of purine-scaffold small molecule inhibitors of Hsp90. Curr. Cancer Drug Targets (2003) 3:363-368.
  • DYMOCK B, BARRIL X, BESWICK M et al.: Adenine derived inhibitors of the molecular chaperone HSP90-SAR explained through multiple X-ray structures. Bioorg. Med. Chem. Lett. (2004) 14:325-328.
  • CHEUNG KM, MATTHEWS TP, JAMES K et al.: The identification, synthesis, protein crystal structure and in vitro biochemical evaluation of a new 3,4-diarylpyrazole class of Hsp90 inhibitors. Bioorg. Med. Chem. Lett. (2005) 15:3338-3343.
  • DYMOCK BW, BARRIL X, BROUGH PA et al.: Novel, potent small-molecule inhibitors of the molecular chaperone Hsp90 discovered through structure-based design. J. Med. Chem. (2005) 48:4212-4215.
  • KREUSCH A, HAN S, BRINKER A et al.: Crystal structures of human HSP90alpha-complexed with dihydroxyphenylpyrazoles. Bioorg. Med. Chem. Lett. (2005) 15:1475-1478.
  • STEBBINS CE, RUSSO AA, SCHNEIDER C, ROSEN N, HARTL U, PAVLETICH NP: Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent. Cell (1997) 89:239-250.
  • ROE SM, PRODROMOU C, O’BRIEN R, LADBURY JE, PIPER PW, PEARL LH: Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J. Med. Chem. (1999) 42:260-266.
  • JEZ JM, CHEN JC, RASTELLI G, STROUD RM, SANTI DV: Crystal structure and molecular modeling of 17-DMAG in complex with human Hsp90. Chem. Biol. (2003) 10:361-368.
  • WRIGHT L, BARRIL X, DYMOCK B et al.: Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms. Chem. Biol. (2004) 11:775-785.
  • MARCU MG, SCHULTE TW, NECKERS L: Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins. J. Natl. Cancer Inst. (2000) 92:242-248.
  • YU XM, SHEN G, NECKERS L et al.: Hsp90 inhibitors identified from a library of novobiocin analogues. J. Am. Chem. Soc. (2005) 127:12778-12779.
  • MARCU MG, CHADLI A, BOUHOUCHE I, CATELLI M, NECKERS LM: 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. (2000) 275:37181-37186.
  • SOTI C, RACZ A, CSERMELY P: A 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. (2002) 277:7066-7075.
  • ITOH H, OGURA M, KOMATSUDA A, WAKUI H, MIURA AB, TASHIMA Y: A novel chaperone-activity-reducing mechanism of the 90-kDa molecular chaperone HSP90. Biochem. J. (1999) 343:697-703.
  • ROSENHAGEN MC, SOTI C, SCHMIDT U et al.: The heat shock protein 90-targeting drug cisplatin selectively inhibits steroid receptor activation. Mol. Endocrinol. (2003) 17:1991-2001.
  • MARCU MG, NECKERS LM: The C-terminal half of heat shock protein 90 represents a second site for pharmacologic intervention in chaperone function. Curr. Cancer Drug Targets (2003) 3:343-347.
  • ZHAO YG, GILMORE R, LEONE G, COFFEY MC, WEBER B, LEE PW: Hsp90 phosphorylation is linked to its chaperoning function. Assembly of the reovirus cell attachment protein. J. Biol. Chem. (2001) 276:32822-32827.
  • MIMNAUGH EG, WORLAND PJ, WHITESELL L, NECKERS LM: Possible role for serine/threonine phosphorylation in the regulation of the heteroprotein complex between the hsp90 stress protein and the pp60v-src tyrosine kinase. J. Biol. Chem. (1995) 270:28654-28659.
  • MURPHY PJ, MORISHIMA Y, KOVACS JJ, YAO TP, PRATT WB: Regulation of the dynamics of hsp90 action on the glucocorticoid receptor by acetylation/deacetylation of the chaperone. J. Biol. Chem. (2005) 280:33792-33799.
  • BLANK M, MANDEL M, KEISARI Y, MERUELO D, LAVIE G: Enhanced ubiquitinylation of heat shock protein 90 as a potential mechanism for mitotic cell death in cancer cells induced with hypericin. Cancer Res. (2003) 63:8241-8247.
  • MARTINEZ-RUIZ A, VILLANUEVA L, GONZALEZ DE ORDUNA C et al.: S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities. Proc. Natl. Acad. Sci. USA (2005) 102:8525-8530.
  • AOYAGI S, ARCHER TK: Modulating molecular chaperone Hsp90 functions through reversible acetylation. Trends Cell Biol. (2005) 15:565-567.
  • YU X, GUO ZS, MARCU MG et al.: Modulation of p53, ErbB1, ErbB2, and Raf-1 expression in lung cancer cells by depsipeptide FR901228. J. Natl. Cancer Inst. (2002) 94:504-513.
  • NIMMANAPALLI R, FUINO L, BALI P et al.: Histone deacetylase inhibitor LAQ824 both lowers expression and promotes proteasomal degradation of Bcr-Abl and induces apoptosis of imatinib mesylate-sensitive or -refractory chronic myelogenous leukemia-blast crisis cells. Cancer Res. (2003) 63:5126-5135.
  • GEORGE P, BALI P, ANNAVARAPU S et al.: Combination of the histone deacetylase inhibitor LBH589 and the hsp90 inhibitor 17-AAG is highly active against human CML-BC cells and AML cells with activating mutation of FLT-3. Blood (2005) 105:1768-1776.
  • RAHMANI M, REESE E, DAI Y et al.: Cotreatment with suberanoylanilide hydroxamic acid and 17-allylamino 17-demethoxygeldanamycin synergistically induces apoptosis in Bcr-Abl+ Cells sensitive and resistant to STI571 (imatinib mesylate) in association with down-regulation of Bcr-Abl, abrogation of signal transducer and activator of transcription 5 activity, and Bax conformational change. Mol. Pharmacol. (2005) 67:1166-1176.
  • BALI P, PRANPAT M, SWABY R et al.: Activity of suberoylanilide hydroxamic acid against human breast cancer cells with amplification of her-2. Clin. Cancer Res. (2005) 11:6382-6309.
  • BALI P, PRANPAT M, BRADNER J et al.: Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors. J. Biol. Chem. (2005) 280:26729-26734.
  • PLESCIA J, SALZ W, XIA F et al.: Rational design of shepherdin, a novel anticancer agent. Cancer Cell (2005) 7:457-468.
  • KAMAL A, THAO L, SENSINTAFFAR J et al.: A high affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature (2003) 425:407-410.
  • PANARETOU B, SILIGARDI G, MAYER P et al.: Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Mol. Cell (2002) 10:1307-1318.
  • RIGGS D, COX M, CHEUNG-FLYNN J, PRAPAPANICH V, CARRIGAN P, SMITH D: Functional specificity of co-chaperone interactions with Hsp90 client proteins. Crit. Rev. Biochem. Mol. Biol. (2004) 39:279-295.
  • XU Y, LINDQUIST S: Heat-shock protein hsp90 governs the activity of pp60v-src kinase. Proc. Natl. Acad. Sci. USA (1993) 90:7074-7078.
  • WHITESELL L, MIMNAUGH EG, DE COSTA B, MYERS CE, NECKERS LM: 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 (1994) 91:8324-8328.
  • UEHARA Y: Natural product origins of Hsp90 inhibitors. Curr. Cancer Drug Targets (2003) 3:325-330.
  • XU W, YUAN X, JUNG YJ et al.: The heat shock protein 90 inhibitor geldanamycin and the ErbB inhibitor ZD1839 promote rapid PP1 phosphatase-dependent inactivation of AKT in ErbB2 overexpressing breast cancer cells. Cancer Res. (2003) 63:7777-7784.
  • MIMNAUGH EG, CHAVANY C, NECKERS L: Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin. J. Biol. Chem. (1996) 271:22796-22801.
  • SALESSE S, VERFAILLIE CM: BCR/ABL-mediated increased expression of multiple known and novel genes that may contribute to the pathogenesis of chronic myelogenous leukemia. Mol. Cancer Ther. (2003) 2:173-182
  • SHIOTSU Y, NECKERS LM, WORTMAN I et al.: 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 (2000) 96:2284-2291.
  • BONVINI P, DALLA ROSA H, VIGNES N, ROSOLEN A: Ubiquitination and proteasomal degradation of nucleophosmin-anaplastic lymphoma kinase induced by 17-allylamino-demethoxygeldanamycin: role of the co-chaperone carboxyl heat shock protein 70-interacting protein. Cancer Res. (2004) 64:3256-3264.
  • GEORGE P, BALI P, COHEN P et al.: Cotreatment with 17-allylamino-demethoxygeldanamycin and FLT-3 kinase inhibitor PKC412 is highly effective against human acute myelogenous leukemia cells with mutant FLT-3. Cancer Res. (2004) 64:3645-3652.
  • BELIAKOFF J, BAGATELL R, PAINE-MURRIETA G et al.: Hormone-refractory breast cancer remains sensitive to the antitumor activity of heat shock protein 90 inhibitors. Clin. Cancer Res. (2003) 9:4961-4971.
  • SOLIT DB, ZHENG FF, DROBNJAK M 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. (2002) 8:986-993.
  • SHIMAMURA T, LOWELL AM, ENGELMAN JA, SHAPIRO GI: Epidermal growth factor receptors harboring kinase domain mutations associate with the heat shock protein 90 chaperone and are destabilized following exposure to geldanamycins. Cancer Res. (2005) 65:6401-6408.
  • CASTRO JE, PRADA CE, LORIA O et al.: ZAP-70 is a novel conditional heat shock protein 90 (Hsp90) client: inhibition of Hsp90 leads to ZAP-70 degradation, apoptosis, and impaired signaling in chronic lymphocytic leukemia. Blood (2005) 106:2506-2512.
  • VILENCHIK M, SOLIT D, BASSO A et al.: Targeting wide-range oncogenic transformation via PU24FCl, a specific inhibitor of tumor Hsp90. Chem. Biol. (2004) 11:787-797.
  • RUTHERFORD SL, LINDQUIST S: Hsp90 as a capacitor for morphological evolution. Nature (1998) 396:336-342.
  • QUEITSCH C, SANGSTER TA, LINDQUIST S: Hsp90 as a capacitor of phenotypic variation. Nature (2002) 417:618-624.
  • SATO S, FUJITA N, TSURUO T: Modulation of Akt kinase activity by binding to Hsp90. Proc. Natl. Acad. Sci. USA (2000) 97:10832-10837.
  • BASSO AD, SOLIT DB, CHIOSIS G, GIRI B, TSICHLIS P, ROSEN N: Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. J. Biol. Chem. (2002) 277:39858-39866.
  • SCHULTE TW, BLAGOSKLONNY MV, 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. (1995) 270:24585-24588.
  • FORTUGNO P, BELTRAMI E, PLESCIA J et al.: Regulation of survivin function by Hsp90. Proc. Natl. Acad. Sci. USA (2003) 100:13791-13796.
  • EUSTACE BK, SAKURAI T, STEWART JK et al.: Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasiveness. Nat. Cell Biol. (2004) 6:507-514.
  • STEWART SA: Telomere maintenance and tumorigenesis: an ‘ALT’ernative road. Curr. Mol. Med. (2005) 5:253-257.
  • FORSYTHE HL, JARVIS JL, TURNER JW, ELMORE LW, HOLT SE: Stable association of hsp90 and p23, but not hsp70, with active human telomerase. J. Biol. Chem. (2001) 276:15571-15574.
  • AKALIN A, ELMORE LW, FORSYTHE HL et al.: A novel mechanism for chaperone-mediated telomerase regulation during prostate cancer progression. Cancer Res. (2001) 61:4791-4796.
  • BELOZEROV VE, VAN MEIR EG: Hypoxia inducible factor-1: a novel target for cancer therapy. Anti-Cancer Drugs (2005) 16:901-909.
  • ISAACS JS, JUNG YJ, MIMNAUGH EG, MARTINEZ A, CUTTITTA F, NECKERS LM: Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 alpha-degradative pathway. J. Biol. Chem. (2002) 277:29936-29944.
  • LEWIS J, DEVIN A, MILLER A 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. (2000) 275:10519-10526.
  • 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. (2004) 16:313-321.
  • PANDEY P, SALEH A, NAKAZAWA A et al.: Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procasapse-9 by heat shock. EMBO J. (2000) 19:4310-4322.
  • LLAUGER L, HE H, KIM J et al.: 8-Arylsulfanyl and 8-arylsulfoxyl adenine derivatives as inhibitors of the heat shock protein 90. J. Med. Chem. (2005) 48:2892-2905.
  • LE BRAZIDEC JY, KAMAL A, BUSCH D et al.: Synthesis and biological evaluation of a new class of geldanamycin derivatives as potent inhibitors of Hsp90. J. Med. Chem. (2004) 47:3865-73.
  • SOGA S, NECKERS LM, SCHULTE TW et al.: KF25706, a novel oxime derivative of radicicol, exhibits in vivo antitumor activity via selective depletion of Hsp90 binding signaling molecules. Cancer Res. (1999) 59:2931-2938.
  • EISEMAN JL, LAN J, LAGATTUTA TF et al.: Pharmacokinetics and pharmacodynamics of 17-demethoxy 17-[[(2-dimethylamino) ethyl]amino]geldanamycin (17DMAG, NSC 707545) in C.B-17 SCID mice bearing MDA-MB-231 human breast cancer xenografts. Cancer Chemother. Pharmacol. (2005) 55:21-32.
  • BANERJI U, WALTON M, RAYNAUD F et al.: Pharmacokinetic-pharmacodynamic relationships for the heat shock protein 90 molecular chaperone inhibitor 17-allylamino, 17-demethoxygeldanamycin in human ovarian cancer xenograft models. Clin. Cancer Res. (2005) 11:7023-7032.
  • SYDOR JR, PIEN CS, ZHANG Y et al.: Anti-tumor activity of a novel, water soluble Hsp90 inhibitor IPI-504 in multiple myeloma. Proc. Amer. Assoc. Cancer Res. (2005) 46:Abstract 6160.
  • BANERJI U, O’DONNELL A, SCURR M et al.: Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies. J. Clin. Oncol. (2005) 23:4152-4161.
  • RAMANATHAN RK, TRUMP DL, EISEMAN JL et al.: Phase I pharmacokinetic-pharmacodynamic study of 17-(allylamino)-17-demethoxygeldanamycin (17AAG, NSC 330507), a novel inhibitor of heat shock protein 90, in patients with refractory advanced cancers. Clin. Cancer Res. (2005) 11:3385-3391.
  • GOETZ MP, , et al.: Phase I trial of 17-allylamino-17-demethoxygeldanamycin in patients with advanced cancer. J. Clin. Oncol. (2005) 23:1078-1087.
  • KOVACS JJ, MURPHY PJM, GAILLARD S et al.: HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor. Mol. Cell (2005) 18:601-607.
  • XU Y, SINGER MA, LINDQUIST S: Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90. Proc. Natl. Acad. Sci. USA (1999) 96:109-114.
  • MALONEY A, CLARKE PA, WORKMAN P: Genes and proteins governing the cellular sensitivity to HSP90 inhibitors: a mechanistic perspective. Curr. Cancer Drug Targets (2003) 3:331-341.
  • ZOU J, GUO Y, GUETTOUCHE T, SMITH DF, VOELLMY R: Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell (1998) 94:471-480.
  • BHARADWAJ S, ALI A, OVSENEK N: Multiple components of the HSP90 chaperone complex function in regulation of heat shock factor 1 In vivo. Mol. Cell Biol. (1999) 19:8033-8041.
  • SAMALI A, COTTER TG: Heat shock proteins increase resistance to apoptosis. Exp. Cell. Res. (1996) 223:163-170.
  • JÄÄTTELÄ M: Escaping cell death: survival proteins in cancer. Exp. Cell Res. (1999) 248:30-43.
  • REED JC: Mechanisms of apoptosis avoidance in cancer. Curr. Opin. Oncol. (1999) 11:68-75.
  • MOSSER DD, MORIMOTO RI: Molecular chaperones and the stress of oncogenesis. Oncogene (2004) 23:2907-2918.
  • LI CY, LEE JS, KO YG, KIM JI, SEO JS: Heat shock protein 70 inhibits apoptosis downstream of cytochrome c release and upstream of caspase-3 activation. J. Biol. Chem. (2000) 275:25665-25671.
  • SALEH A, SRINIVASULA SM, BALKIR L, ROBBINS PD, ALNEMRI ES: Negative regulation of the Apaf-1 apoptosome by Hsp70. Nat. Cell Biol. (2000) 2:476-483.
  • BEERE HM, WOLF BB, CAIN K et al.: Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome. Nat. Cell Biol. (2000) 8:469-475.
  • JAATTELA M, WISSING D, KOKHOLM K, KALLUNKI T, EGEBLAD M: Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. EMBO J. (1998) 17:6124-6134.
  • KOMAROVA EY, AFANASYEVA EA, BULATOVA MM et al.: Downstream caspases are novel targets for the antiapoptotic activity of the molecular chaperone hsp70. Cell Stress Chaperones (2004) 9:265-275.
  • STANKIEWICZ AR, LACHAPELLE G, FOO CP, RADICIONI SM, MOSSER DD: Hsp70 inhibits heat-induced apoptosis upstream of mitochondria by preventing Bax translocation. J. Biol. Chem. (2005) 280:38729-38739.
  • RAVAGNAN L, GURBUXANI S, SUSIN SA et al.: Heat-shock protein 70 antagonizes apoptosis-inducing factor. Nat. Cell Biol. (2001) 9:839-843.
  • GABAI VL, MERIIN AB, YAGLOM JA, MOSSER DD, SHERMAN MY: Heat shock protein 70 protects from caspase-independent programmed cell death via suppression of stress kinase jnk. Scientific WorldJournal (2001) 1:36.
  • BAGATELL R, PAINE-MURRIETA GD, TAYLOR CW et al.: Induction of a heat shock factor 1-dependent stress response alters the cytotoxic activity of hsp90-binding agents. Clin. Cancer Res. (2000) 6:3312-3318.
  • GABAI VL, BUDAGOVA KR, SHERMAN MY: Increased expression of the major heat shock protein Hsp72 in human prostate carcinoma cells is dispensable for their viability but confers resistance to a variety of anticancer agents. Oncogene (2005) 24:3328-3338.
  • BURGER AM, FIEBIG HH, STINSON SF, SAUSVILLE EA: 17-(Allylamino)-17-demethoxygeldanamycin activity in human melanoma models. Anti-Cancer Drugs (2004) 15:377-387.
  • MALONEY A, CLARKE PA, WORKMAN P: Genes and proteins governing the cellular sensitivity to HSP90 inhibitors: a mechanistic perspective. Curr. Cancer Drug Targets (2003) 3:331-341.
  • GUO F, SIGUA C, BALI P et al.: Abrogation of hsp70 induction: A strategy to enhance the antileukemia effects of hsp90 inhibitor 17-allylamino-demethoxy geldanamycin (17-AAG). Proc. Amer. Assoc. Cancer Res. (2005):Abstract 3275.
  • ZHANG H, YANG Y-C, LE D et al.: The two faces of Hsp90: Dissecting the cytotoxic and cytoprotective responses with selective Hsp90 modulators. Proc. Amer. Assoc. Cancer Res. (2005):Abstract 1527.
  • BAGATELL R, BELIAKOFF J, DAVID CL, MARRON MT, WHITESELL L: Hsp90 inhibitors deplete key anti-apoptotic proteins in pediatric solid tumor cells and demonstrate synergistic anticancer activity with cisplatin. Int. J. Cancer (2005) 113:179-188.
  • MCCOLLUM A, TOFT D, ERLICHMAN C: . Proc. Amer. Assoc. Cancer Res. (2004):Abstract 3748.
  • NARDAI G, SASS B, EBER J, OROSZ G, CSERMELY P: Reactive cysteines of the 90-kDa heat shock protein, Hsp90. Arch. Biochem. Biophys. (2000) 384(1):59-67.
  • MADDEN T-A, PUMFORD S, BARROW D et al.: Development of acquired resistance to 17(Allylamino)-17-demethoxygeldanamycin (17-AAG) in hormone refractory breast cancers in vitro. Proc. Amer. Assoc. Cancer Res. (2005):Abstract LB-267.
  • MIMNAUGH EG, XU W, VOS M et al.: Simultaneous inhibition of hsp90 and the proteasome promotes protein ubiquitination, causes endoplasmic reticulum-derived cytosolic vacuolization, and enhances antitumor activity. Mol. Cancer Ther. (2004) 3(5):551-566.
  • ENMON R, YANG WH, BALLANGRUD AM et al.: Combination treatment with 17-N-allylamino-17-demethoxy geldanamycin and acute irradiation produces supra-additive growth suppression in human prostate carcinoma spheroids. Cancer Res. (2003) 63:8393-8399.
  • BISHT KS, BRADBURY CM, MATTSON D et al.: Geldanamycin and 17-allylamino-17-demethoxygeldanamycin potentiate the in vitro and in vivo radiation response of cervical tumor cells via the heat shock protein 90-mediated intracellular signaling and cytotoxicity. Cancer Res. (2003) 63:8984-8995.
  • MCCOLLUM A, TOFT DO, ERLICHMAN C: Geldanamycin enhances cisplatin cytotoxicity through loss of Akt activation in A549 cells. Clin. Cancer Res. (2003) 9:6178.
  • MUNSTER PN, BASSO A, SOLIT D, NORTON L, ROSEN N: Modulation of Hsp90 function by ansamycins sensitizes breast cancer cells to chemotherapy-induced apoptosis in an RB- and schedule-dependent manner. Clin. Cancer Res. (2001) 7:2228-2236.
  • SMITH-JONES PM, SOLIT DB, AKHURST T, AFROZE F, ROSEN N, LARSON M: The pharmacodynamics of HER2 degradation in response to Hsp90 inhibitors can be imaged in animals with 68Ga labeled F(ab’)2 fragments of Herceptin. Nature Biotech. (2004) 22:701-706.
  • COWEN LE, LINDQUIST S: Hsp90 potentiates the rapid evolution of new traits: drug resistance in diverse fungi. Science (2005) 309:2185-2189.
  • DEVANEY E, O’NEILL K, HARNETT W, WHITESELL L, KINNAIRD JH: Hsp90 is essential in the filarial nematode Brugia pahangi. Int. J. Parasitol. (2005) 35:627-636.

Patents

Website

  • http://www.neutecpharma.com Neutech Pharma website. Mycograb® (2005).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.