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Volumn 15, Issue 4, 2004, Pages 377-387

17-(Allylamino)-17-demethoxygeldanamycin activity in human melanoma models

Author keywords

Ansamycin; c Raf 1; Cancer treatment; Hsp90; Melanoma

Indexed keywords

17 ALLYLAMINO 17 DEMETHOXYGELDANAMYCIN; ANTINEOPLASTIC AGENT; GELDANAMYCIN; HEAT SHOCK PROTEIN 72; HEAT SHOCK PROTEIN 90; UNCLASSIFIED DRUG;

EID: 1942485334     PISSN: 09594973     EISSN: None     Source Type: Journal    
DOI: 10.1097/00001813-200404000-00011     Document Type: Article
Times cited : (91)

References (33)
  • 1
    • 0033502429 scopus 로고    scopus 로고
    • Geldanamycin as a potential anticancer agent: Its molecular target and biochemical activity
    • Neckers L, Schulte TW, Mimnaugh E. Geldanamycin as a potential anticancer agent: its molecular target and biochemical activity. Invest New Drugs 1999; 17:361-373.
    • (1999) Invest New Drugs , vol.17 , pp. 361-373
    • Neckers, L.1    Schulte, T.W.2    Mimnaugh, E.3
  • 3
    • 0000076189 scopus 로고    scopus 로고
    • Comparison of geldanamycin (NSC-122750) and 17-allylaminogeldanamycin (NSC-330507D) toxicity in rats
    • Page J, Heath J, Fulton R, Yalkowsky E, Tabibi E, Tomaszewski J, et al. Comparison of geldanamycin (NSC-122750) and 17-allylaminogeldanamycin (NSC-330507D) toxicity in rats. Proc Am Ass Cancer Res 1997; 38:308.
    • (1997) Proc Am Ass Cancer Res , vol.38 , pp. 308
    • Page, J.1    Heath, J.2    Fulton, R.3    Yalkowsky, E.4    Tabibi, E.5    Tomaszewski, J.6
  • 4
    • 0029123128 scopus 로고
    • erbB-2 oncogene inhibition by geldanamycin derivatives: Synthesis, mechanism of action, and structure-activity relationships
    • Schnur RC, Corman ML, Gallachun RJ, Cooper BA, Dee MF, Coty JL, et al. erbB-2 oncogene inhibition by geldanamycin derivatives: synthesis, mechanism of action, and structure-activity relationships. J Med Chem 1995; 38:3813-3820.
    • (1995) J Med Chem , vol.38 , pp. 3813-3820
    • Schnur, R.C.1    Corman, M.L.2    Gallachun, R.J.3    Cooper, B.A.4    Dee, M.F.5    Coty, J.L.6
  • 6
    • 0000318466 scopus 로고    scopus 로고
    • Plasma pharmacokinetics and tissue distribution of 17- allylaminogeldanamycin (NSC 330507), a prodrug for geldanamycin, in CD2F1 mice and Fischer 344 rats
    • Eiseman JL, Sentz DL, Zuhowski EG, Ramsland TS, Rosen DM, Reyna SP, et al. Plasma pharmacokinetics and tissue distribution of 17-allylaminogeldanamycin (NSC 330507), a prodrug for geldanamycin, in CD2F1 mice and Fischer 344 rats. Proc Am Ass Cancer Res 1997; 38:308.
    • (1997) Proc Am Ass Cancer Res , vol.38 , pp. 308
    • Eiseman, J.L.1    Sentz, D.L.2    Zuhowski, E.G.3    Ramsland, T.S.4    Rosen, D.M.5    Reyna, S.P.6
  • 7
    • 11244305093 scopus 로고    scopus 로고
    • A. 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 J, Grimm A, Sentz D, Lessor T, Gessner R, Zuhowski E, et al. A. 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 1999; 5:3837s.
    • (1999) Clin Cancer Res , vol.5
    • Eiseman, J.1    Grimm, A.2    Sentz, D.3    Lessor, T.4    Gessner, R.5    Zuhowski, E.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; 89:239-250.
    • (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
    • 0031025859 scopus 로고    scopus 로고
    • Effects of the tyrosine-kinase inhibitor geldanamycin on ligand-induced her-2/neu activation, receptor expression and proliferation of her-2-positive malignant cells
    • Hartmann F, Horak EM, Cho C, Lupu R, Bolen JB, Stetler-Stevenson MA, et al. Effects of the tyrosine-kinase inhibitor geldanamycin on ligand-induced her-2/neu activation, receptor expression and proliferation of her-2-positive malignant cells. Int J Cancer 1997; 70:221-229.
    • (1997) Int J Cancer , vol.70 , pp. 221-229
    • Hartmann, F.1    Horak, E.M.2    Cho, C.3    Lupu, R.4    Bolen, J.B.5    Stetler-Stevenson, M.A.6
  • 10
    • 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; 270:24585-24588.
    • (1995) J Biol Chem , vol.270 , pp. 24585-24588
    • Schulte, T.W.1    Blagosklonny, M.V.2    Ingui, C.3    Neckers, L.4
  • 11
    • 0028064940 scopus 로고
    • vsrc heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • vsrc heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci USA 1994; 91:8324-8328.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    DeCosta, B.3    Myers, C.4    Neckers, L.M.5
  • 12
    • 0031909866 scopus 로고    scopus 로고
    • The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent
    • Whitesell L, Sutphin PD, Pulcini EJ, Martinex JD, Cook PH. The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent. Mol Cell Biol 1998; 18:1517-1524.
    • (1998) Mol Cell Biol , vol.18 , pp. 1517-1524
    • Whitesell, L.1    Sutphin, P.D.2    Pulcini, E.J.3    Martinex, J.D.4    Cook, P.H.5
  • 15
    • 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 (editors): Basel: Karger
    • Roth T, Burger AM, Dengler W, Fiebig HH, Monks A, McMahon J, et al. Human tumor cell lines demonstrating the characteristics of patient tumors as useful models for anticancer drug development. In: Fiebig HH, Burger AM (editors): Relevance of Tumor Models for Anticancer Drug Development. Basel: Karger; 1999, pp. 145-156.
    • (1999) Relevance of Tumor Models for Anticancer Drug Development , pp. 145-156
    • Roth, T.1    Burger, A.M.2    Dengler, W.3    Fiebig, H.H.4    Monks, A.5    McMahon, J.6
  • 17
    • 0017785769 scopus 로고
    • Primary bioassay of human tumor stem cells
    • Hamburger AW, Salmon SE. Primary bioassay of human tumor stem cells. Science 1977; 197:461-463.
    • (1977) Science , vol.197 , pp. 461-463
    • Hamburger, A.W.1    Salmon, S.E.2
  • 18
    • 0033709414 scopus 로고    scopus 로고
    • Predicting tumor responses to mitomycin C on the basis of DT-diaphorase activity or drug metabolism by tumor homogenates: Implications for enzyme directed bioreductive drug development
    • Phillips RM, Burger AW, Jarrett C, Loadman PM, Fiebig HH. Predicting tumor responses to mitomycin C on the basis of DT-diaphorase activity or drug metabolism by tumor homogenates: implications for enzyme directed bioreductive drug development. Cancer Res 2000; 60:6384-6390.
    • (2000) Cancer Res , vol.60 , pp. 6384-6390
    • Phillips, R.M.1    Burger, A.W.2    Jarrett, C.3    Loadman, P.M.4    Fiebig, H.H.5
  • 19
    • 0035371902 scopus 로고    scopus 로고
    • Preclinical evaluation of a methotrexate-albumine-conjugate (MTX-HSA) in human tumor xenografts in vivo
    • Burger AM, Hartung G, Stehle G, Sinn H, Fiebig HH. Preclinical evaluation of a methotrexate-albumine-conjugate (MTX-HSA) in human tumor xenografts in vivo. Int J Cancer 2001; 92:718-24.
    • (2001) Int J Cancer , vol.92 , pp. 718-724
    • Burger, A.M.1    Hartung, G.2    Stehle, G.3    Sinn, H.4    Fiebig, H.H.5
  • 20
    • 0036260242 scopus 로고    scopus 로고
    • Plasma pharmacokinetics of a liver-selective nitric oxide-donating diazeniumdiolate in the male C57BL/6 mouse
    • Stinson SF, House T, Bramhall C, Saavedra JE, Keefer LK, Nims RW. Plasma pharmacokinetics of a liver-selective nitric oxide-donating diazeniumdiolate in the male C57BL/6 mouse. Xenobiotica 2002; 32:339-347
    • (2002) Xenobiotica , vol.32 , pp. 339-347
    • Stinson, S.F.1    House, T.2    Bramhall, C.3    Saavedra, J.E.4    Keefer, L.K.5    Nims, R.W.6
  • 22
    • 0033577233 scopus 로고    scopus 로고
    • Energy intake and prostate tumor growth, angiogenesis, and vascular endothelial growth factor expression
    • Mukherjee P, Sotnikov V, Mangian HJ, Zhou J-R, Visek WJ, Clinton SK. Energy intake and prostate tumor growth, angiogenesis, and vascular endothelial growth factor expression. J Natl Cancer Inst, 1999; 91: 512-523.
    • (1999) J Natl Cancer Inst , vol.91 , pp. 512-523
    • Mukherjee, P.1    Sotnikov, V.2    Mangian, H.J.3    Zhou, J.-R.4    Visek, W.J.5    Clinton, S.K.6
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72:248-234.
    • (1976) Anal Biochem , vol.72 , pp. 248-1234
    • Bradford, M.M.1
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0036494113 scopus 로고    scopus 로고
    • + lymphoma cells by the Hsp90 antagonist 17-allylamino,17-demethoxygeldanamycin
    • + lymphoma cells by the Hsp90 antagonist 17-allylamino,17- demethoxygeldanamycin. Cancer Res 2002; 62:1559-1566.
    • (2002) Cancer Res , vol.62 , pp. 1559-1566
    • Bonvini, P.1    Gastaldi, T.2    Falini, B.3    Rosolen, A.4
  • 26
    • 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; 61:1799-1804.
    • (2001) Cancer Res , vol.61 , pp. 1799-1804
    • Nimmanapalli, R.1    O'Bryan, E.2    Bhalla, K.3
  • 27
    • 0038404927 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 90 function down-regulates Akt kinase and sensitizes tumors to Taxol
    • Solit DB, Basso AD, Olshen AB, Scher HI, Rosen N. Inhibition of heat shock protein 90 function down-regulates Akt kinase and sensitizes tumors to Taxol. Cancer Res 2003; 63:2139-2144.
    • (2003) Cancer Res , vol.63 , pp. 2139-2144
    • Solit, D.B.1    Basso, A.D.2    Olshen, A.B.3    Scher, H.I.4    Rosen, N.5
  • 28
    • 0034777916 scopus 로고    scopus 로고
    • Destabilization of steroid receptors by heat shock protein 90-binding drugs: A ligand-independent approach to hormonal therapy of breast cancer
    • Bagatell R, Khan O, Paine-Marrieta G, Taylor CW, Akinaga S, Whitesell L. Destabilization of steroid receptors by heat shock protein 90-binding drugs: a ligand-independent approach to hormonal therapy of breast cancer. Clin Cancer Res 2001; 7:2076-2084.
    • (2001) Clin Cancer Res , vol.7 , pp. 2076-2084
    • Bagatell, R.1    Khan, O.2    Paine-Marrieta, G.3    Taylor, C.W.4    Akinaga, S.5    Whitesell, L.6
  • 29
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal A, Thao L, Sensintaffar J, Zhang L, Boehm MF, Fritz LC, et al. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 2003; 425:407-410.
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1    Thao, L.2    Sensintaffar, J.3    Zhang, L.4    Boehm, M.F.5    Fritz, L.C.6
  • 30
    • 0001148460 scopus 로고    scopus 로고
    • Phase I trial of the heat shock protein 90 (Hsp90) inhibitor 17-allylamino-17-demethoxygeldanamycin (17aag). Pharmacokinetic (PK) profile and pharmacodynamic (PD) endpoints
    • Banjeri U, O'Donnell A, Scurr M, Benson C, Hanwell J, Clark S, et al. Phase I trial of the heat shock protein 90 (Hsp90) inhibitor 17-allylamino-17-demethoxygeldanamycin (17aag). Pharmacokinetic (PK) profile and pharmacodynamic (PD) endpoints. Proc Am Soc Clin Oncol 2001; 20:82a.
    • (2001) Proc Am Soc Clin Oncol , vol.20
    • Banjeri, U.1    O'Donnell, A.2    Scurr, M.3    Benson, C.4    Hanwell, J.5    Clark, S.6
  • 31
    • 0000165431 scopus 로고    scopus 로고
    • Phase I pharmacological study of 17-(allylamino)-17-demethoxygeldanamycin (AAG) in adult patients with advanced solid tumors
    • Wilson RH, Takimoto CH, Agnew EB, Morrison G, Grollman F, Thomas RR, et al. Phase I pharmacological study of 17-(allylamino)-17-demethoxygeldanamycin (AAG) in adult patients with advanced solid tumors. Proc Am Soc Clin Oncol 2001; 20:82a.
    • (2001) Proc Am Soc Clin Oncol , vol.20
    • Wilson, R.H.1    Takimoto, C.H.2    Agnew, E.B.3    Morrison, G.4    Grollman, F.5    Thomas, R.R.6
  • 32
    • 0000235617 scopus 로고    scopus 로고
    • Phase I trial of 17-(allylamino)-17-demethoxygeldanamycin (17-AAG) in patients (pts) with advanced solid malignancies
    • Münster PN, Tong W, Schwartz L, Larson S, Keneson K, De La Cruz A, et al. Phase I trial of 17-(allylamino)-17-demethoxygeldanamycin (17-AAG) in patients (pts) with advanced solid malignancies. Proc Am Soc Clin Oncol 2001; 20:83a.
    • (2001) Proc Am Soc Clin Oncol , vol.20
    • Münster, P.N.1    Tong, W.2    Schwartz, L.3    Larson, S.4    Keneson, K.5    De La Cruz, A.6
  • 33
    • 1142267027 scopus 로고    scopus 로고
    • Preclinical an clinical activity of the molecular chaperone inhibitor 17-allylamino, 17-demethoxygeldanamycin(17AAG) in malignant melanoma
    • abstr 2966
    • Banerji U, Clake P, Walton M, O'Donnel A, Raynaud F, Turner A, et al. Preclinical an clinical activity of the molecular chaperone inhibitor 17-allylamino, 17-demethoxygeldanamycin(17AAG) in malignant melanoma. Proc Am Ass Cancer Res 2003; 44:677 (abstr 2966).
    • (2003) Proc Am Ass Cancer Res , vol.44 , pp. 677
    • Banerji, U.1    Clake, P.2    Walton, M.3    O'Donnel, A.4    Raynaud, F.5    Turner, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.