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Volumn 14, Issue 12, 2005, Pages 1471-1474

17-AAG: Mechanisms of antitumour activity

Author keywords

17 AAG; Apoptosis; Cell cycle; Chaperones; Hsp90; Hsp90 inhibitor

Indexed keywords

17 ALLYLAMINO 17 DEMETHOXYGELDANAMYCIN; ANSAMYCIN DERIVATIVE; CHAPERONE; FR 901228; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; HISTONE DEACETYLASE INHIBITOR; PROTEIN INHIBITOR;

EID: 28644432986     PISSN: 13543784     EISSN: None     Source Type: Journal    
DOI: 10.1517/13543784.14.12.1471     Document Type: Editorial
Times cited : (16)

References (30)
  • 1
    • 15544385359 scopus 로고    scopus 로고
    • Hsp90 inhibitor geldanamycin its derivatives as novel cancer chemotherapeutic agents
    • MIYATA Y: Hsp90 inhibitor geldanamycin and its derivatives as novel cancer chemotherapeutic agents. Curr. Pharm. Des. (2005) 11(9):1131-1138.
    • (2005) Curr. Pharm. Des. , vol.11 , Issue.9 , pp. 1131-1138
    • Miyata, Y.1
  • 3
    • 0033579175 scopus 로고    scopus 로고
    • DT-diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90
    • KELLAND LR, SHARP SY, ROGERS PM, MYERS TG, 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. (1999) 91(22):1940-1949.
    • (1999) J. Natl. Cancer Inst. , vol.91 , Issue.22 , pp. 1940-1949
    • Kelland, L.R.1    Sharp, S.Y.2    Rogers, P.M.3    Myers, T.G.4    Workman, P.5
  • 4
    • 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(18):8324-8328.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , Issue.18 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 5
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: A specialized but essential protein-folding tool
    • YOUNG JC, MOAREFI I, HARTL FU: Hsp90: a specialized but essential protein-folding tool. J. Cell Biol. (2001) 154(2):267-273.
    • (2001) J. Cell Biol. , vol.154 , Issue.2 , pp. 267-273
    • Young, J.C.1    Moarefi, I.2    Hartl, F.U.3
  • 6
    • 4143095430 scopus 로고    scopus 로고
    • Altered Hsp90 function in cancer: A unique therapeutic opportunity
    • BAGATELL R, WHITESELL L: Altered Hsp90 function in cancer: a unique therapeutic opportunity. Mol. Cancer Ther. (2004) 3(8):1021-1030.
    • (2004) Mol. Cancer Ther. , vol.3 , Issue.8 , pp. 1021-1030
    • Bagatell, R.1    Whitesell, L.2
  • 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(1):65-75.
    • (1997) Cell , vol.90 , Issue.1 , 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
    • 0029008487 scopus 로고
    • Herbimycin A induces the 20S proteasome- and ubiquitin-dependent degradation of receptor tyrosine kinases
    • SEPP-LORENZINO L, MA Z, LEBWOHL DE, VINITSKY A, ROSEN N: Herbimycin A induces the 20S proteasome- and ubiquitin-dependent degradation of receptor tyrosine kinases. J. Biol. Chem. (1995) 270(28):16580-16587.
    • (1995) J. Biol. Chem. , vol.270 , Issue.28 , pp. 16580-16587
    • Sepp-Lorenzino, L.1    Ma, Z.2    Lebwohl, D.E.3    Vinitsky, A.4    Rosen, N.5
  • 9
    • 0035872442 scopus 로고    scopus 로고
    • Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in cytostasis and apoptosis
    • HOSTEIN I, ROBERTSON D, DISTEFANO F, WORKMAN P, CLARKE PA: Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17-demethoxygeldanamycin results in cytostasis and apoptosis. Cancer Res. (2001) 61(10):4003-4009.
    • (2001) Cancer Res. , vol.61 , Issue.10 , pp. 4003-4009
    • Hostein, I.1    Robertson, D.2    Distefano, F.3    Workman, P.4    Clarke, P.A.5
  • 10
    • 0034660856 scopus 로고    scopus 로고
    • Inhibition of Hsp90 function by ansamycins causes retinoblastoma gene product-dependent G1 arrest
    • SRETHAPAKDI M, LIU F, TAVORATH R, ROSEN N: Inhibition of Hsp90 function by ansamycins causes retinoblastoma gene product-dependent G1 arrest. Cancer Res. (2000) 60(14):3940-3946.
    • (2000) Cancer Res. , vol.60 , Issue.14 , pp. 3940-3946
    • Srethapakdi, M.1    Liu, F.2    Tavorath, R.3    Rosen, N.4
  • 11
    • 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(8):1159-1166.
    • (2002) Oncogene , vol.21 , Issue.8 , pp. 1159-1166
    • Basso, A.D.1    Solit, D.B.2    Munster, P.N.3    Rosen, N.4
  • 15
    • 0033809941 scopus 로고    scopus 로고
    • p53 from complexity to simplicity: Mutant p53 stabilization, gain-of-function, and dominant-negative effect
    • BLAGOSKLONNY MV: p53 from complexity to simplicity: mutant p53 stabilization, gain-of-function, and dominant-negative effect. FASEB J. (2000) 14(13):1901-1907.
    • (2000) FASEB J. , vol.14 , Issue.13 , pp. 1901-1907
    • Blagosklonny, M.V.1
  • 16
    • 0029737509 scopus 로고    scopus 로고
    • Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90
    • BLAGOSKLONNY MV, TORETSKY J, BOHEN S, NECKERS L: Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90. Proc. Natl. Acad. Sci. USA (1996) 93(16):8379-8383.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , Issue.16 , pp. 8379-8383
    • Blagosklonny, M.V.1    Toretsky, J.2    Bohen, S.3    Neckers, L.4
  • 17
    • 0037564865 scopus 로고    scopus 로고
    • Regulation of 17-AAG-induced apoptosis: Role of Bcl-2, Bcl-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, Bcl-XL, and Bax downstream of 17-AAG-mediated down-regulation of Akt, Raf-1, and Src kinases. Blood (2003) 102(1):269-275.
    • (2003) Blood , vol.102 , Issue.1 , pp. 269-275
    • Nimmanapalli, R.1    O'Bryan, E.2    Kuhn, D.3    Yamaguchi, H.4    Wang, H.G.5    Bhalla, K.N.6
  • 18
    • 0034532066 scopus 로고    scopus 로고
    • Modulation of metastasis phenotypes of non-small cell lung cancer cells by 17-allylamino 17-demethoxy geldanamycin
    • NGUYEN DM, DESAI S, CHEN A, WEISER TS, SCHRUMP DS: Modulation of metastasis phenotypes of non-small cell lung cancer cells by 17-allylamino 17-demethoxy geldanamycin. Ann. Thorac. Surg. (2000) 70(6):1853-1860.
    • (2000) Ann. Thorac. Surg. , vol.70 , Issue.6 , pp. 1853-1860
    • Nguyen, D.M.1    Desai, S.2    Chen, A.3    Weiser, T.S.4    Schrump, D.S.5
  • 19
    • 0037119415 scopus 로고    scopus 로고
    • Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 alpha-degradative pathway
    • 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(33):29936-29944.
    • (2002) J. Biol. Chem. , vol.277 , Issue.33 , pp. 29936-29944
    • Isaacs, J.S.1    Jung, Y.J.2    Mimnaugh, E.G.3    Martinez, A.4    Cuttitta, F.5    Neckers, L.M.6
  • 20
    • 0038309566 scopus 로고    scopus 로고
    • Inhibition of telomerase activity by geldanamycin and 17-allylamino, 17-demethoxygeldanamycin in human melanoma cells
    • VILLA R, FOLINI M, PORTA CD et al.: Inhibition of telomerase activity by geldanamycin and 17-allylamino, 17-demethoxygeldanamycin in human melanoma cells. Carcinogenesis (2003) 24(5):851-859.
    • (2003) Carcinogenesis , vol.24 , Issue.5 , pp. 851-859
    • Villa, R.1    Folini, M.2    Porta, C.D.3
  • 21
    • 0035266132 scopus 로고    scopus 로고
    • Geldanamycin and its analogue 17-allylamino-17-demethoxygeldanamycin lowers Bcr-Abl levels and induces apoptosis and differentiation of Bcr-Abl-positive human leukemic blasts
    • 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. (2001) 61(5):1799-1804.
    • (2001) Cancer Res. , vol.61 , Issue.5 , pp. 1799-1804
    • Nimmanapalli, R.1    O'Bryan, E.2    Bhalla, K.3
  • 22
    • 0037307095 scopus 로고    scopus 로고
    • The influence of the src-family kinases, Lck and Fyn, on T cell differentiation, survival and activation
    • ZAMOYSKA R, BASSON A, FILBY A, LEGNAME G, LOVATT M, SEDDON B: The influence of the src-family kinases, Lck and Fyn, on T cell differentiation, survival and activation. Immunol. Rev. (2003) 191:107-118.
    • (2003) Immunol. Rev. , vol.191 , pp. 107-118
    • Zamoyska, R.1    Basson, A.2    Filby, A.3    Legname, G.4    Lovatt, M.5    Seddon, B.6
  • 23
    • 0036098002 scopus 로고    scopus 로고
    • Heat shock protein 90 inhibition by 17-allylamino-17-demethoxygeldanamycin: A novel therapeutic approach for treating hormone-refractory prostate cancer
    • NECKERS L: Heat shock protein 90 inhibition by 17-allylamino-17-demethoxygeldanamycin: a novel therapeutic approach for treating hormone-refractory prostate cancer. Clin. Cancer Res. (2002) 8(5):962-966.
    • (2002) Clin. Cancer Res. , vol.8 , Issue.5 , pp. 962-966
    • Neckers, L.1
  • 24
    • 4143153881 scopus 로고    scopus 로고
    • Hsp90: An emerging target for breast cancer therapy
    • BELIAKOFF J, WHITESELL L: Hsp90: an emerging target for breast cancer therapy. Anti-Cancer Drugs (2004) 15(7):651-662.
    • (2004) Anti-Cancer Drugs , vol.15 , Issue.7 , pp. 651-662
    • Beliakoff, J.1    Whitesell, L.2
  • 25
    • 23044441106 scopus 로고    scopus 로고
    • Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies
    • 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(18):4152-4161.
    • (2005) J. Clin. Oncol. , vol.23 , Issue.18 , pp. 4152-4161
    • Banerji, U.1    O'Donnell, A.2    Scurr, M.3
  • 26
    • 0142124533 scopus 로고    scopus 로고
    • Phase I trial of 17-AAG (17-allylamino-17-demethoxygeldanamycin) in patients (pts) with advanced cancer
    • SOLIT DB, ANANA M, VALENTIN G et al.: Phase I trial of 17-AAG (17-allylamino-17-demethoxygeldanamycin) in patients (pts) with advanced cancer. Am. Soc. Clin. Oncol. (2003)
    • (2003) Am. Soc. Clin. Oncol.
    • Solit, D.B.1    Anana, M.2    Valentin, G.3
  • 27
    • 0346995281 scopus 로고    scopus 로고
    • Combination treatment with 17-N-allylamino- 17-demethoxy geldanamycin and acute irradiation produces supra-additive growth suppression in human prostate carcinoma spheroids
    • 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(23):8393-8399.
    • (2003) Cancer Res. , vol.63 , Issue.23 , pp. 8393-8399
    • Enmon, R.1    Yang, W.H.2    Ballangrud, A.M.3
  • 28
    • 0034890377 scopus 로고    scopus 로고
    • Modulation of Hsp90 function by ansamycins sensitizes breast cancer cells to chemotherapy-induced apoptosis in an RB- and schedule-dependent manner
    • [See: E. A. Sausville, Combining cytotoxics and 17-allylamino, 17-demethoxygeldanamycin: sequence and tumor biology matters. Clin. Cancer Res. (2001) 7:2155-2158]
    • 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) 8:2228-2236. [See: E. A. Sausville, Combining cytotoxics and 17-allylamino, 17-demethoxygeldanamycin: sequence and tumor biology matters. Clin. Cancer Res. (2001) 7:2155-2158].
    • (2001) Clin. Cancer Res. , vol.8 , pp. 2228-2236
    • Munster, P.N.1    Basso, A.2    Solit, D.3    Norton, L.4    Rosen, N.5
  • 29
    • 0037012344 scopus 로고    scopus 로고
    • Modulation of p53, ErbB1, ErbB2, and Raf-1 expression in lung cancer cells by depsipeptide FR901228
    • 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(7):504-513.
    • (2002) J. Natl. Cancer Inst. , vol.94 , Issue.7 , pp. 504-513
    • Yu, X.1    Guo, Z.S.2    Marcu, M.G.3
  • 30
    • 0345734267 scopus 로고    scopus 로고
    • Coadministration of the heat shock protein 90 antagonist 17-allylamino-17-demethoxygeldanamycin with suberoylanilide hydroxamic acid or sodium butyrate synergistically induces apoptosis in human leukemia cells
    • RAHMANI M, YU C, DAI Y et al.: Coadministration of the heat shock protein 90 antagonist 17-allylamino-17-demethoxygeldanamycin with suberoylanilide hydroxamic acid or sodium butyrate synergistically induces apoptosis in human leukemia cells. Cancer Res. (2003) 63(23):8420-8427.
    • (2003) Cancer Res. , vol.63 , Issue.23 , pp. 8420-8427
    • Rahmani, M.1    Yu, C.2    Dai, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.