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Volumn 56, Issue 2, 2005, Pages 126-137

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

Author keywords

17AAG; 17DMAG; Hsp90 modulation; Melanoma

Indexed keywords

17 ALLYLAMINO 17 DEMETHOXYGELDANAMYCIN; 17 DIMETHYLAMINOETHYLAMINO 17 DEMETHOXYGELDANAMYCIN; 4 HYDROXYCYCLOPHOSPHAMIDE; 4 HYDROXYIFOSFAMIDE; B RAF KINASE; BLEOMYCIN; CISPLATIN; CYCLIN D1; CYCLIN DEPENDENT KINASE 4; DACARBAZINE; DOXORUBICIN; ELMUSTINE; EPIDERMAL GROWTH FACTOR RECEPTOR 2; EPIDERMAL GROWTH FACTOR RECEPTOR 3; ETOPOSIDE; FLUOROURACIL; GELDANAMYCIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; IFOSFAMIDE; MITOXANTRONE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NSC 707545; PROTEIN KINASE B; UNCLASSIFIED DRUG; VINBLASTINE; VINCRISTINE; VINDESINE;

EID: 21244466289     PISSN: 03445704     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00280-004-0947-2     Document Type: Article
Times cited : (136)

References (34)
  • 1
    • 0035989680 scopus 로고    scopus 로고
    • HSP90 as a new therapeutic target for cancer therapy: The story unfolds
    • Maloney A, Workman P (2002) HSP90 as a new therapeutic target for cancer therapy: the story unfolds. Expert Opin Biol Ther 2:3
    • (2002) Expert Opin Biol Ther , vol.2 , pp. 3
    • Maloney, A.1    Workman, P.2
  • 2
    • 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 (2001) Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17- demethoxygeldanamycin results in cytostasis and apoptosis. Cancer Res 61:4003
    • (2001) Cancer Res , vol.61 , pp. 4003
    • Hostein, I.1    Robertson, D.2    DiStefano, F.3    Workman, P.4    Clarke, P.A.5
  • 3
    • 0037131187 scopus 로고    scopus 로고
    • Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and cdc37 and is destabilised by inhibitors of Hsp90 function
    • Basso A, Solit D, Chiosis G, Giri B, Tsichlis P, Rosen N (2002) Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and cdc37 and is destabilised by inhibitors of Hsp90 function. J Biol Chem 277:39858
    • (2002) J Biol Chem , vol.277 , pp. 39858
    • Basso, A.1    Solit, D.2    Chiosis, G.3    Giri, B.4    Tsichlis, P.5    Rosen, N.6
  • 4
    • 0037155901 scopus 로고    scopus 로고
    • Involvement of Hsp90 in signaling and stability of 3-phosphoinositide- dependent kinase
    • Fujita N, Sato S, Ishida A, Tsuruo T (2002) Involvement of Hsp90 in signaling and stability of 3-phosphoinositide-dependent kinase. J Biol Chem 277:10346
    • (2002) J Biol Chem , vol.277 , pp. 10346
    • Fujita, N.1    Sato, S.2    Ishida, A.3    Tsuruo, T.4
  • 5
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins C, Russo A, Schnieder C, Rosen N, Hartl F, Pavletich N (1997) Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 89:239
    • (1997) Cell , vol.89 , pp. 239
    • Stebbins, C.1    Russo, A.2    Schnieder, C.3    Rosen, N.4    Hartl, F.5    Pavletich, N.6
  • 6
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou C, Roe S, O'Brien R, Ladbury J, Piper P, Pearl L (1997) Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90:65
    • (1997) Cell , vol.90 , pp. 65
    • Prodromou, C.1    Roe, S.2    O'Brien, R.3    Ladbury, J.4    Piper, P.5    Pearl, L.6
  • 8
    • 0029123128 scopus 로고
    • erbB-2 oncogene inhibition by geldanamycin derivatives: Synthesis, mechanism of action, and structure-activity relationships
    • Schnur R, Corman M, Cooper B, Dee M, Coty J (1995) erbB-2 oncogene inhibition by geldanamycin derivatives: synthesis, mechanism of action, and structure-activity relationships. J Med Chem 38:3813
    • (1995) J Med Chem , vol.38 , pp. 3813
    • Schnur, R.1    Corman, M.2    Cooper, B.3    Dee, M.4    Coty, J.5
  • 9
    • 11244305093 scopus 로고    scopus 로고
    • Pharmacokinetics of 17-allylamino(17-demethoxy)geldanamycin in SCID mice bearing MDA.MB-453 xenografts and alterations in the expression of p185erb-B2 in the xenografts following treatment
    • Eiseman JL, Grimm A, Sentz DL, Lesser T, Gessner R, Zuhowski E, Nimieboka M, Egorin MJ (1999) Pharmacokinetics of 17-allylamino(17-demethoxy)geldanamycin in SCID mice bearing MDA.MB-453 xenografts and alterations in the expression of p185erb-B2 in the xenografts following treatment. Clin Cancer Res 5:3837s
    • (1999) Clin Cancer Res , vol.5
    • Eiseman, J.L.1    Grimm, A.2    Sentz, D.L.3    Lesser, T.4    Gessner, R.5    Zuhowski, E.6    Nimieboka, M.7    Egorin, M.J.8
  • 10
    • 0036139023 scopus 로고    scopus 로고
    • Pharmacokinetics, tissue distribution, and metabolism of 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (NSC 707545) in CD2F1 mice and Fischer 344 rats
    • Egorin MJ, Lagattuta TF, Hambruger DR, Covey JM, White KD, Musser SM, Eiseman JL (2002) Pharmacokinetics, tissue distribution, and metabolism of 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (NSC 707545) in CD2F1 mice and Fischer 344 rats. Cancer Chemother Pharmacol 49:7
    • (2002) Cancer Chemother Pharmacol , vol.49 , pp. 7
    • Egorin, M.J.1    Lagattuta, T.F.2    Hambruger, D.R.3    Covey, J.M.4    White, K.D.5    Musser, S.M.6    Eiseman, J.L.7
  • 11
    • 0000378255 scopus 로고
    • Combined in vitro/in vivo test procedure with human tumor xenografts
    • Fiebig HH, Berger D (eds) Karger Verlag, Basel
    • Fiebig H, Berger D, Dengler W, Wallbrecher E, Winterhalter B (1992) Combined in vitro/in vivo test procedure with human tumor xenografts. In: Fiebig HH, Berger D (eds) Immunodeficient mice in oncology. Karger Verlag, Basel, pp 321
    • (1992) Immunodeficient Mice in Oncology , pp. 321
    • Fiebig, H.1    Berger, D.2    Dengler, W.3    Wallbrecher, E.4    Winterhalter, B.5
  • 12
    • 1942518912 scopus 로고    scopus 로고
    • Clonogenic assay with established human tumor xenografts: Correlation of in vitro to in vivo activity as a basis for anticancer drug discovery
    • Fiebig HH, Maier A, Burger AM (2004) Clonogenic assay with established human tumor xenografts: correlation of in vitro to in vivo activity as a basis for anticancer drug discovery. Eur J Cancer 40:802
    • (2004) Eur J Cancer , vol.40 , pp. 802
    • Fiebig, H.H.1    Maier, A.2    Burger, A.M.3
  • 13
    • 0000397439 scopus 로고    scopus 로고
    • Human tumor cell lines demonstrating the characteristics of patient tumors as useful models for anticancer drug development
    • Fiebig HH, Burger AM (eds) Karger Verlag, Basel
    • Roth T, Burger AM, Dengler W, Fiebig HH (1999) Human tumor cell lines demonstrating the characteristics of patient tumors as useful models for anticancer drug development. In: Fiebig HH, Burger AM (eds) Relevance of tumor models for anticancer drug development. Karger Verlag, Basel, p 145
    • (1999) Relevance of Tumor Models for Anticancer Drug Development , pp. 145
    • Roth, T.1    Burger, A.M.2    Dengler, W.3    Fiebig, H.H.4
  • 14
    • 0017785769 scopus 로고
    • Primary bioassay of human tumor stem cells
    • Hamburger A, Salmon S (1977) Primary bioassay of human tumor stem cells. Science 197:461
    • (1977) Science , vol.197 , pp. 461
    • Hamburger, A.1    Salmon, S.2
  • 15
    • 0020416136 scopus 로고
    • Improved detection of drug cytotoxicity in the soft agar colony formation assay through use of a metabolizable tetrazolium salt
    • Alley M, Uhl C, Lieber, M (1982) Improved detection of drug cytotoxicity in the soft agar colony formation assay through use of a metabolizable tetrazolium salt. Life Sci 27:3071
    • (1982) Life Sci , vol.27 , pp. 3071
    • Alley, M.1    Uhl, C.2    Lieber, M.3
  • 16
    • 0033709414 scopus 로고    scopus 로고
    • Predicting tumour responses to mitomycin C on the basis of DT-diaphorase activity or drug metabolism by tumour homogenates: Implications for enzyme directed bioreductive drug development
    • Phillips RM, Burger AM, Loadman PM, Jarrett CM, Swaine DJ, Fiebig HH (2000) Predicting tumour responses to mitomycin C on the basis of DT-diaphorase activity or drug metabolism by tumour homogenates: implications for enzyme directed bioreductive drug development. Cancer Res 60:6384
    • (2000) Cancer Res , vol.60 , pp. 6384
    • Phillips, R.M.1    Burger, A.M.2    Loadman, P.M.3    Jarrett, C.M.4    Swaine, D.J.5    Fiebig, H.H.6
  • 19
  • 20
    • 0024312538 scopus 로고
    • Display and analysis of patterns of differential activity of drugs against human tumor cell lines: Development of mean graph and COMPARE algorithm
    • Paull, KD, Shoemaker RH, Hodes L, Monks A, Scudiero DA, Rubinstein L, Plowman J, Boyd MR (1989) Display and analysis of patterns of differential activity of drugs against human tumor cell lines: development of mean graph and COMPARE algorithm. J Natl Cancer Inst 81:1088
    • (1989) J Natl Cancer Inst , vol.81 , pp. 1088
    • Paull, K.D.1    Shoemaker, R.H.2    Hodes, L.3    Monks, A.4    Scudiero, D.A.5    Rubinstein, L.6    Plowman, J.7    Boyd, M.R.8
  • 21
    • 0036606332 scopus 로고    scopus 로고
    • Degradation of HER2 by ansamycins induces growth arrest and apoptosis in cells with HER2 overexpression via a HER3, phosphatidylinositol 3′-kinase-AKT-dependent pathway
    • Münster P, Marchion D, Basso A, Rosen N (2002) Degradation of HER2 by ansamycins induces growth arrest and apoptosis in cells with HER2 overexpression via a HER3, phosphatidylinositol 3′-kinase-AKT-dependent pathway. Cancer Res 62:3132
    • (2002) Cancer Res , vol.62 , pp. 3132
    • Münster, P.1    Marchion, D.2    Basso, A.3    Rosen, N.4
  • 22
    • 0043092165 scopus 로고    scopus 로고
    • Medulloblastoma sensitivity to 17-allylamino-17-demethoxygeldanamycin requires MEK/ERK
    • Calabrese C, Frank A, Maclean K, Gilbertson R (2003) Medulloblastoma sensitivity to 17-allylamino-17-demethoxygeldanamycin requires MEK/ERK. J Biol Chem 278:24951
    • (2003) J Biol Chem , vol.278 , pp. 24951
    • Calabrese, C.1    Frank, A.2    Maclean, K.3    Gilbertson, R.4
  • 23
    • 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 (2002) Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2. Oncogene 21:1159
    • (2002) Oncogene , vol.21 , pp. 1159
    • Basso, A.D.1    Solit, D.B.2    Munster, P.N.3    Rosen, N.4
  • 24
    • 0034710542 scopus 로고    scopus 로고
    • Gene expression profiling of human colon cancer cells following inhibition of signal transduction by 17-allylamino-17-demethoxygeldanamycin, an inhibitor of the Hsp90 molecular chaperone
    • Clarke PA, Hostein I, Banerji U, Di Stefano F, Maloney A, Walton M, Judson I, Workman P (2000) Gene expression profiling of human colon cancer cells following inhibition of signal transduction by 17-allylamino-17- demethoxygeldanamycin, an inhibitor of the Hsp90 molecular chaperone. Oncogene 19:4125
    • (2000) Oncogene , vol.19 , pp. 4125
    • Clarke, P.A.1    Hostein, I.2    Banerji, U.3    Di Stefano, F.4    Maloney, A.5    Walton, M.6    Judson, I.7    Workman, P.8
  • 25
    • 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 (2001) 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 61:1799
    • (2001) Cancer Res , vol.61 , pp. 1799
    • Nimmanapalli, R.1    O'Bryan, E.2    Bhalla, K.3
  • 28
    • 0141819944 scopus 로고    scopus 로고
    • The clinical applications of heat shock protein inhibitors in cancer - Present and future
    • Banerji U, Judson I, Workman P (2003) The clinical applications of heat shock protein inhibitors in cancer - present and future. Curr Cancer Drug Targets 3:385
    • (2003) Curr Cancer Drug Targets , vol.3 , pp. 385
    • Banerji, U.1    Judson, I.2    Workman, P.3
  • 30
  • 31
    • 0345734276 scopus 로고    scopus 로고
    • Enhanced ubiquitinylation of heat shock protein 90 as a potential mechanism for mitotic cell death in cancer cells induced with hypericin
    • Blank M, Mandel M, Keisari Y, Meruelo D, Lavie G (2003) Enhanced ubiquitinylation of heat shock protein 90 as a potential mechanism for mitotic cell death in cancer cells induced with hypericin. Cancer Res 63:8241
    • (2003) Cancer Res , vol.63 , pp. 8241
    • Blank, M.1    Mandel, M.2    Keisari, Y.3    Meruelo, D.4    Lavie, G.5
  • 32
    • 0036339108 scopus 로고    scopus 로고
    • ErbB2 overexpression in an ovarian cancer cell line confers sensitivity to the Hsp90 inhibitor geldanamycin
    • Smith V, Hobbs S, Court W, Eccles S, Workman P, Kelland LR (2002) ErbB2 overexpression in an ovarian cancer cell line confers sensitivity to the Hsp90 inhibitor geldanamycin. Anticancer Res 22:1993
    • (2002) Anticancer Res , vol.22 , pp. 1993
    • Smith, V.1    Hobbs, S.2    Court, W.3    Eccles, S.4    Workman, P.5    Kelland, L.R.6
  • 34
    • 85069410301 scopus 로고    scopus 로고
    • Activate, mutated B-raf protein kinase requires the Hsp90 chaperone for folding and stability and is degraded in response to Hsp90 inhibitors
    • abstract 100
    • Grbovic OM, Basso AD, Friedlander P, Houghton A, Solit DB, Rosen N (2004) Activate, mutated B-raf protein kinase requires the Hsp90 chaperone for folding and stability and is degraded in response to Hsp90 inhibitors (abstract 100). Proc Am Assoc Cancer Res 45
    • (2004) Proc Am Assoc Cancer Res , vol.45
    • Grbovic, O.M.1    Basso, A.D.2    Friedlander, P.3    Houghton, A.4    Solit, D.B.5    Rosen, N.6


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