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Volumn 120, Issue 4, 2007, Pages 918-926

Dimeric ansamycins - A new class of antitumor Hsp90 modulators with prolonged inhibitory activity

Author keywords

17 AAG; Cancer therapy; Dimeric inhibitor; Hsp90

Indexed keywords

17 ALLYLAMINO 17 DEMETHOXYGELDANAMYCIN; ANSAMYCIN DERIVATIVE; BIOTIN; CF 237; CF 483; DIMER; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; MONOMER; STEROID; UNCLASSIFIED DRUG;

EID: 33846629429     PISSN: 00207136     EISSN: 10970215     Source Type: Journal    
DOI: 10.1002/ijc.22392     Document Type: Article
Times cited : (10)

References (39)
  • 2
    • 0035989680 scopus 로고    scopus 로고
    • HSP90 as a new therapeutic target for cancer therapy: The story unfolds
    • Maloney A, Workman P. HSP90 as a new therapeutic target for cancer therapy: the story unfolds. Expert Opin Biol Ther 2002;2:3-24.
    • (2002) Expert Opin Biol Ther , vol.2 , pp. 3-24
    • Maloney, A.1    Workman, P.2
  • 3
    • 4344674482 scopus 로고    scopus 로고
    • Targeting multiple signal transduction pathways through inhibition of Hsp90
    • Zhang H, Burrows F. Targeting multiple signal transduction pathways through inhibition of Hsp90. J Mol Med 2004;82:488-99.
    • (2004) J Mol Med , vol.82 , pp. 488-499
    • Zhang, H.1    Burrows, F.2
  • 4
    • 0141596939 scopus 로고    scopus 로고
    • Structure and functional relationships of Hsp90
    • Prodromou C, Pearl LH. Structure and functional relationships of Hsp90. Curr Cancer Drug Targets 2003;3:301-23.
    • (2003) Curr Cancer Drug Targets , vol.3 , pp. 301-323
    • Prodromou, C.1    Pearl, L.H.2
  • 5
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • 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;91:8324-8.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 6
    • 0028786332 scopus 로고
    • Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association
    • 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;270:24585-8.
    • (1995) J Biol Chem , vol.270 , pp. 24585-24588
    • Schulte, T.W.1    Blagosklonny, M.V.2    Ingui, C.3    Neckers, L.4
  • 7
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 1997;90:65-75.
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 8
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU, Pavletich NP. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 1997;89:239-50.
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 9
    • 0037265586 scopus 로고    scopus 로고
    • Development of small molecule Hsp90 inhibitors: Utilizing both forward and reverse chemical genomics for drug identification
    • Neckers LM. Development of small molecule Hsp90 inhibitors: utilizing both forward and reverse chemical genomics for drug identification. Curr Med Chem 2003;10:733-9.
    • (2003) Curr Med Chem , vol.10 , pp. 733-739
    • Neckers, L.M.1
  • 11
    • 0000076189 scopus 로고    scopus 로고
    • Comparison of geldanamycin (NSC-122750) and 17-allylaminogeldanamycin (NSC-330507D) toxicity in rats
    • Page J, Heath J, Fulton R. Comparison of geldanamycin (NSC-122750) and 17-allylaminogeldanamycin (NSC-330507D) toxicity in rats. Proc Am Assoc Cancer Res 1997;38:308.
    • (1997) Proc Am Assoc Cancer Res , vol.38 , pp. 308
    • Page, J.1    Heath, J.2    Fulton, R.3
  • 12
    • 0031875042 scopus 로고    scopus 로고
    • The benzoquinone ansamycin 17-allylamino-17- demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin
    • 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;42:273-9.
    • (1998) Cancer Chemother Pharmacol , vol.42 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 13
    • 0037075232 scopus 로고    scopus 로고
    • Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2
    • Basso AD, Solit DB, Munster PN, Rosen N. Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2. Oncogene 2002;21:1159-66.
    • (2002) Oncogene , vol.21 , pp. 1159-1166
    • Basso, A.D.1    Solit, D.B.2    Munster, P.N.3    Rosen, N.4
  • 18
    • 33846564261 scopus 로고    scopus 로고
    • Lin Z, Boehm MF, Zegar S. Process for preparing 17-allyl amino geldanamycin (17-AAG) and other ansamycins. US Patent WO03026571, 2003
    • Lin Z, Boehm MF, Zegar S. Process for preparing 17-allyl amino geldanamycin (17-AAG) and other ansamycins. US Patent WO03026571, 2003.
  • 19
    • 33846599145 scopus 로고    scopus 로고
    • Ansamycins having improved pharmacological and biological properties
    • US Patent Application number: WO03066005
    • Lin Z, Le Brazidec J-Y, Boehm MF, McHugh SK, Fan J, Fritz LC, Burrows FJ. Ansamycins having improved pharmacological and biological properties. US Patent Application number: WO03066005, 2003.
    • (2003)
    • Lin, Z.1    Le Brazidec, J.-Y.2    Boehm, M.F.3    McHugh, S.K.4    Fan, J.5    Fritz, L.C.6    Burrows, F.J.7
  • 21
    • 0141729370 scopus 로고    scopus 로고
    • Physiologically-based pharmacokinetics and molecular pharmacodynamics of 17-(allyl-amino)-17- demethoxygeldanamycin and its active metabolite in tumor-bearing mice
    • Xu L, Eiseman JL, Egorin MJ, D'Argenio DZ. Physiologically-based pharmacokinetics and molecular pharmacodynamics of 17-(allyl-amino)-17- demethoxygeldanamycin and its active metabolite in tumor-bearing mice. J Pharmacokinet Pharmacodyn 2003;30:185-219.
    • (2003) J Pharmacokinet Pharmacodyn , vol.30 , pp. 185-219
    • Xu, L.1    Eiseman, J.L.2    Egorin, M.J.3    D'Argenio, D.Z.4
  • 24
    • 2342625412 scopus 로고    scopus 로고
    • 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
    • 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;64:3256-64.
    • (2004) Cancer Res , vol.64 , pp. 3256-3264
    • Bonvini, P.1    Dalla Rosa, H.2    Vignes, N.3    Rosolen, A.4
  • 25
    • 2442695516 scopus 로고    scopus 로고
    • Cotreatment with 17-allylamino-demethoxygeldanamycin and FLT-3 kinase inhibitor PKC412 is highly effective against human acute myelogenous leukemia cells with mutant FLT-3
    • George P, Bali P, Cohen P, Tao J, Guo F, Sigua C, Vishvanath A, Fiskus W, Scuto A, Annavarapu S, Moscinski L, Bhalla K. 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;64:3645-52.
    • (2004) Cancer Res , vol.64 , pp. 3645-3652
    • George, P.1    Bali, P.2    Cohen, P.3    Tao, J.4    Guo, F.5    Sigua, C.6    Vishvanath, A.7    Fiskus, W.8    Scuto, A.9    Annavarapu, S.10    Moscinski, L.11    Bhalla, K.12
  • 26
    • 0037352446 scopus 로고    scopus 로고
    • Structural and functional analysis of the middle segment of hsp90: Implications for ATP hydrolysis and client protein and cochaperone interactions
    • Meyer P, Prodromou C, Hu B, Vaughan C, Roe SM, Panaretou B, Piper PW, Pearl LH. Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions. Mol Cell 2003;11:647-58.
    • (2003) Mol Cell , vol.11 , pp. 647-658
    • Meyer, P.1    Prodromou, C.2    Hu, B.3    Vaughan, C.4    Roe, S.M.5    Panaretou, B.6    Piper, P.W.7    Pearl, L.H.8
  • 27
    • 0141645488 scopus 로고    scopus 로고
    • Mechanism of action of anti-HER2 monoclonal antibodies: Scientific update on trastuzumab and 2C4
    • Albanell J, Codony J, Rovira A, Mellado B, Gascon P. Mechanism of action of anti-HER2 monoclonal antibodies: scientific update on trastuzumab and 2C4. Adv Exp Med Biol 2003;532:253-68.
    • (2003) Adv Exp Med Biol , vol.532 , pp. 253-268
    • Albanell, J.1    Codony, J.2    Rovira, A.3    Mellado, B.4    Gascon, P.5
  • 28
    • 1542751704 scopus 로고    scopus 로고
    • Inhibiting tyrosine kinases: Successes and limitations
    • Arteaga CL. Inhibiting tyrosine kinases: successes and limitations. Cancer Biol Ther 2003;2:S79-S83.
    • (2003) Cancer Biol Ther , vol.2
    • Arteaga, C.L.1
  • 30
    • 0141819944 scopus 로고    scopus 로고
    • The clinical applications of heat shock protein inhibitors in cancer-present and future
    • Banerji U, Judson I, Workman P. The clinical applications of heat shock protein inhibitors in cancer-present and future. Curr Cancer Drug Targets 2003;3:385-90.
    • (2003) Curr Cancer Drug Targets , vol.3 , pp. 385-390
    • Banerji, U.1    Judson, I.2    Workman, P.3
  • 31
    • 33846593126 scopus 로고    scopus 로고
    • 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. See: Sausville EA. Combining cytotoxics and 17-allylamino, 17-demethoxygeldanamycin: sequence and tumor biology matters, Clin Cancer Res 2001;7:2155-8. CHlin Cancer Res 2001;7:2228-36.
    • 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. See: Sausville EA. Combining cytotoxics and 17-allylamino, 17-demethoxygeldanamycin: sequence and tumor biology matters, Clin Cancer Res 2001;7:2155-8. CHlin Cancer Res 2001;7:2228-36.
  • 32
    • 33846632623 scopus 로고    scopus 로고
    • Sausville EA. Combining cytotoxics and 17-allylamino, 17-demethoxygeldanamycin: sequence and tumor biology matters. Commentary re: Munster P, et al. 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;7:2228-36. Clin Cancer Res 2001;7:2155-8.
    • Sausville EA. Combining cytotoxics and 17-allylamino, 17-demethoxygeldanamycin: sequence and tumor biology matters. Commentary re: Munster P, et al. 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;7:2228-36. Clin Cancer Res 2001;7:2155-8.
  • 33
    • 0037564865 scopus 로고    scopus 로고
    • Regulation of 17-AAG-induced apoptosis: Role of Bcl-2, Bc1-XL, and Bax downstream of 17-AAG-mediated down-regulation of Akt, Raf-1, and Src kinases
    • Nimmanapalli R, O'Bryan E, Kuhn D, Yamaguchi H, Wang HG, Bhalla KN. Regulation of 17-AAG-induced apoptosis: role of Bcl-2, Bc1-XL, and Bax downstream of 17-AAG-mediated down-regulation of Akt, Raf-1, and Src kinases. Blood 2003;102:269-75.
    • (2003) Blood , vol.102 , pp. 269-275
    • Nimmanapalli, R.1    O'Bryan, E.2    Kuhn, D.3    Yamaguchi, H.4    Wang, H.G.5    Bhalla, K.N.6
  • 34
    • 27544446054 scopus 로고    scopus 로고
    • Formation of 17-AAG hydroquinone by NAD(P)H: Quinone oxidoreductase 1: role of 17-AAG hydroquinone in heat shock protein 90 inhibition
    • Guo W, Reigan P, Siegel D, Zirrolli J, Gustafson D, Ross D. Formation of 17-AAG hydroquinone by NAD(P)H: quinone oxidoreductase 1: role of 17-AAG hydroquinone in heat shock protein 90 inhibition. Cancer Res 2005;65:10006-15.
    • (2005) Cancer Res , vol.65 , pp. 10006-10015
    • Guo, W.1    Reigan, P.2    Siegel, D.3    Zirrolli, J.4    Gustafson, D.5    Ross, D.6
  • 35
    • 0036307898 scopus 로고    scopus 로고
    • Limited penetration of anticancer drugs through tumor tissue: A potential cause of resistance of solid tumors to chemotherapy
    • Tannock IF, Lee CM, Tunggal JK, Cowan DS, Egorin MJ. Limited penetration of anticancer drugs through tumor tissue: a potential cause of resistance of solid tumors to chemotherapy. Clin Cancer Res 2002;8:878-84.
    • (2002) Clin Cancer Res , vol.8 , pp. 878-884
    • Tannock, I.F.1    Lee, C.M.2    Tunggal, J.K.3    Cowan, D.S.4    Egorin, M.J.5
  • 36
    • 18844396087 scopus 로고    scopus 로고
    • Potent activity of a novel dimeric heat shock protein 90 inhibitor against head and neck squamous cell carcinoma in vitro and in vivo
    • Yin X, Zhang H, Burrows F, Zhang L, Shores CG. Potent activity of a novel dimeric heat shock protein 90 inhibitor against head and neck squamous cell carcinoma in vitro and in vivo. Clin Cancer Res 2005;11:3889-96.
    • (2005) Clin Cancer Res , vol.11 , pp. 3889-3896
    • Yin, X.1    Zhang, H.2    Burrows, F.3    Zhang, L.4    Shores, C.G.5
  • 38
    • 0037492417 scopus 로고    scopus 로고
    • Medicines that make a difference
    • McCarthy AA. Theravance. Medicines that make a difference. Chem Biol 2003;10:473-1.
    • (2003) Chem Biol , vol.10 , pp. 473-471
    • Theravance, M.A.A.1
  • 39
    • 3843113481 scopus 로고    scopus 로고
    • 2-(1-adamantyl)-4-(thio) chromenone-6-carboxylic acids: Potent reversible inhibitors of human steroid sulfatase
    • Horvath A, Nussbaumer P, Wolff B, Billich A. 2-(1-adamantyl)-4-(thio) chromenone-6-carboxylic acids: potent reversible inhibitors of human steroid sulfatase. J Med Chem 2004;47:4268-76.
    • (2004) J Med Chem , vol.47 , pp. 4268-4276
    • Horvath, A.1    Nussbaumer, P.2    Wolff, B.3    Billich, A.4


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