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Volumn 69, Issue 9, 2009, Pages 3947-3954

Transcription inhibition of heat shock proteins: A strategy for combination of 17-allylamino-17-demethoxygeldanamycin andactinomycin d

Author keywords

[No Author keywords available]

Indexed keywords

DACTINOMYCIN; MESSENGER RNA; TANESPIMYCIN;

EID: 65949096108     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-08-4406     Document Type: Article
Times cited : (20)

References (47)
  • 1
    • 0030154255 scopus 로고    scopus 로고
    • Discovery of the heat shock response
    • Ritossa F. Discovery of the heat shock response. Cell Stress Chaperones 1996; 1: 97-8.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 97-98
    • Ritossa, F.1
  • 2
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU. Molecular chaperones in cellular protein folding. Nature 1996; 381: 571-9.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 4
    • 85047695528 scopus 로고    scopus 로고
    • Blagosklonny MV. Hsp-90-associated oncoproteins:multiple targets of geldanamycin and its analogs. Leukemia 2002; 16: 455-62.
    • Blagosklonny MV. Hsp-90-associated oncoproteins:multiple targets of geldanamycin and its analogs. Leukemia 2002; 16: 455-62.
  • 5
    • 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
  • 7
    • 36849056135 scopus 로고    scopus 로고
    • Drug-mediated targeted disruption of multiple protein activities through functional inhibition of the Hsp90 chaperone complex
    • Stravopodis DJ, Margaritis LH, Voutsinas GE. Drug-mediated targeted disruption of multiple protein activities through functional inhibition of the Hsp90 chaperone complex. Curr Med Chem 2007; 14: 3122-38.
    • (2007) Curr Med Chem , vol.14 , pp. 3122-3138
    • Stravopodis, D.J.1    Margaritis, L.H.2    Voutsinas, G.E.3
  • 8
    • 33746191768 scopus 로고    scopus 로고
    • Inhibitors of the HSP90 molecular chaperone:current status
    • Sharp S, Workman P. Inhibitors of the HSP90 molecular chaperone:current status. Adv Cancer Res 2006; 95: 323-48.
    • (2006) Adv Cancer Res , vol.95 , pp. 323-348
    • Sharp, S.1    Workman, P.2
  • 9
    • 34447507818 scopus 로고    scopus 로고
    • Inhibitors of the heat shock response:biology and pharmacology
    • Powers MV, Workman P. Inhibitors of the heat shock response:biology and pharmacology. FEBS Lett 2007; 581: 3758-69.
    • (2007) FEBS Lett , vol.581 , pp. 3758-3769
    • Powers, M.V.1    Workman, P.2
  • 10
    • 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: 1021-30.
    • (2004) Mol Cancer Ther , vol.3 , pp. 1021-1030
    • Bagatell, R.1    Whitesell, L.2
  • 11
    • 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
  • 12
    • 0036842742 scopus 로고    scopus 로고
    • Heat-shock protein 90 inhibitors as novel cancer chemotherapeutic agents
    • Neckers L, Neckers K. Heat-shock protein 90 inhibitors as novel cancer chemotherapeutic agents. Expert Opin Emerg Drugs 2002; 7: 277-88.
    • (2002) Expert Opin Emerg Drugs , vol.7 , pp. 277-288
    • Neckers, L.1    Neckers, K.2
  • 13
    • 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: 4152-61.
    • (2005) J Clin Oncol , vol.23 , pp. 4152-4161
    • Banerji, U.1    O'Donnell, A.2    Scurr, M.3
  • 14
    • 33846861747 scopus 로고    scopus 로고
    • Targeting of multiple signalling pathways by heat shock protein 90 molecular chaperone inhibitors
    • Powers MV, Workman P. Targeting of multiple signalling pathways by heat shock protein 90 molecular chaperone inhibitors. Endocr Relat Cancer 2006; 13 Suppl 1: S125-35.
    • (2006) Endocr Relat Cancer , vol.13 , Issue.SUPPL. 1
    • Powers, M.V.1    Workman, P.2
  • 15
    • 34250162501 scopus 로고    scopus 로고
    • Phase I pharmacokinetic and pharmacodynamic study of 17- N-allylamino-17-demethoxygeldanamycin in pediatric patients with recurrent or refractory solid tumors:a pediatric oncology experimental therapeutics investigators consortium study
    • Bagatell R, Gore L, Egorin MJ, et al. Phase I pharmacokinetic and pharmacodynamic study of 17- N-allylamino-17-demethoxygeldanamycin in pediatric patients with recurrent or refractory solid tumors:a pediatric oncology experimental therapeutics investigators consortium study. Clin Cancer Res 2007; 13: 1783-8.
    • (2007) Clin Cancer Res , vol.13 , pp. 1783-1788
    • Bagatell, R.1    Gore, L.2    Egorin, M.J.3
  • 16
    • 0027474909 scopus 로고
    • Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1
    • Baler R, Dahl G, Voellmy R. Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1. Mol Cell Biol 1993; 13: 2486-96.
    • (1993) Mol Cell Biol , vol.13 , pp. 2486-2496
    • Baler, R.1    Dahl, G.2    Voellmy, R.3
  • 17
    • 0027475243 scopus 로고
    • Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases
    • Nadeau K, Das A, Walsh CT. Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases. J Biol Chem 1993; 268: 1479-87.
    • (1993) J Biol Chem , vol.268 , pp. 1479-1487
    • Nadeau, K.1    Das, A.2    Walsh, C.T.3
  • 18
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • 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: 471-80.
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5
  • 19
    • 0030043401 scopus 로고    scopus 로고
    • Activation of heat shock factor 1 DNA binding precedes stress-induced serine phosphorylation. Evidence for a multistep pathway of regulation
    • Cotto JJ, Kline M, Morimoto RI. Activation of heat shock factor 1 DNA binding precedes stress-induced serine phosphorylation. Evidence for a multistep pathway of regulation. J Biol Chem 1996; 271: 3355-8.
    • (1996) J Biol Chem , vol.271 , pp. 3355-3358
    • Cotto, J.J.1    Kline, M.2    Morimoto, R.I.3
  • 20
    • 0029564954 scopus 로고
    • Heat shock transcription factors:structure and regulation
    • Wu C. Heat shock transcription factors:structure and regulation. Annu Rev Cell Dev Biol 1995; 11: 441-69.
    • (1995) Annu Rev Cell Dev Biol , vol.11 , pp. 441-469
    • Wu, C.1
  • 21
    • 0034664030 scopus 로고    scopus 로고
    • Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90
    • Pandey P, Saleh A, Nakazawa A, et al. Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90. EMBO J 2000; 19: 4310-22.
    • (2000) EMBO J , vol.19 , pp. 4310-4322
    • Pandey, P.1    Saleh, A.2    Nakazawa, A.3
  • 22
    • 0034605446 scopus 로고    scopus 로고
    • Role of the heat shock response and molecular chaperones in oncogenesis and cell death
    • Jolly C, Morimoto RI. Role of the heat shock response and molecular chaperones in oncogenesis and cell death. J Natl Cancer Inst 2000; 92: 1564-72.
    • (2000) J Natl Cancer Inst , vol.92 , pp. 1564-1572
    • Jolly, C.1    Morimoto, R.I.2
  • 23
    • 0038668000 scopus 로고    scopus 로고
    • Escaping cell death:survival proteins in cancer
    • Jaattela M. Escaping cell death:survival proteins in cancer. Exp Cell Res 1999; 248: 30-43.
    • (1999) Exp Cell Res , vol.248 , pp. 30-43
    • Jaattela, M.1
  • 24
    • 3242879188 scopus 로고    scopus 로고
    • The stress of dying:the role of heat shock proteins in the regulation of apoptosis
    • Beere HM. "The stress of dying":the role of heat shock proteins in the regulation of apoptosis. J Cell Sci 2004; 117: 2641-51.
    • (2004) J Cell Sci , vol.117 , pp. 2641-2651
    • Beere, H.M.1
  • 25
    • 33751203833 scopus 로고    scopus 로고
    • Heat shock proteins 27 and 70:antiapoptotic proteins with tumorigenic properties
    • Garrido C, Brunet M, Didelot C, Zermati Y, Schmitt E, Kroemer G. Heat shock proteins 27 and 70:antiapoptotic proteins with tumorigenic properties. Cell Cycle 2006; 5: 2592-601.
    • (2006) Cell Cycle , vol.5 , pp. 2592-2601
    • Garrido, C.1    Brunet, M.2    Didelot, C.3    Zermati, Y.4    Schmitt, E.5    Kroemer, G.6
  • 26
    • 33747041690 scopus 로고    scopus 로고
    • Pharmacological induction of Hsp70 protects apoptosis-prone cells from doxorubicin:comparison with caspaseinhibitor- and cycle-arrest-mediated cytoprotection
    • Demidenko ZN, Vivo C, Halicka HD, et al. Pharmacological induction of Hsp70 protects apoptosis-prone cells from doxorubicin:comparison with caspaseinhibitor- and cycle-arrest-mediated cytoprotection. Cell Death Differ 2006; 13: 1434-41.
    • (2006) Cell Death Differ , vol.13 , pp. 1434-1441
    • Demidenko, Z.N.1    Vivo, C.2    Halicka, H.D.3
  • 27
    • 51049098720 scopus 로고    scopus 로고
    • A pivotal role for heat shock protein 90 in Ewing sarcoma resistance to anti-insulin-like growth factor 1 receptor treatment:in vitro and in vivo study
    • Martins AS, Ordonez JL, Garcia-Sanchez A, et al. A pivotal role for heat shock protein 90 in Ewing sarcoma resistance to anti-insulin-like growth factor 1 receptor treatment:in vitro and in vivo study. Cancer Res 2008; 68: 6260-70.
    • (2008) Cancer Res , vol.68 , pp. 6260-6270
    • Martins, A.S.1    Ordonez, J.L.2    Garcia-Sanchez, A.3
  • 28
    • 33846208233 scopus 로고    scopus 로고
    • STAT3 and MAPK signaling maintain overexpression of heat shock proteins 90 αand βin multiple myeloma cells, which critically contribute to tumor-cell survival
    • Chatterjee M, Jain S, Stuhmer T, et al. STAT3 and MAPK signaling maintain overexpression of heat shock proteins 90 αand βin multiple myeloma cells, which critically contribute to tumor-cell survival. Blood 2007; 109: 720-8.
    • (2007) Blood , vol.109 , pp. 720-728
    • Chatterjee, M.1    Jain, S.2    Stuhmer, T.3
  • 29
    • 28544433004 scopus 로고    scopus 로고
    • Abrogation of heat shock protein 70 induction as a strategy to increase antileukemia activity of heat shock protein 90 inhibitor 17- allylamino-demethoxy geldanamycin
    • Guo F, Rocha K, Bali P, et al. Abrogation of heat shock protein 70 induction as a strategy to increase antileukemia activity of heat shock protein 90 inhibitor 17- allylamino-demethoxy geldanamycin. Cancer Res 2005; 65: 10536-44.
    • (2005) Cancer Res , vol.65 , pp. 10536-10544
    • Guo, F.1    Rocha, K.2    Bali, P.3
  • 30
    • 33749554554 scopus 로고    scopus 로고
    • Small interference RNA targeting heat-shock protein 27 inhibits the growth of prostatic cell lines and induces apoptosis via caspase-3 activation in vitro
    • Rocchi P, Jugpal P, So A, et al. Small interference RNA targeting heat-shock protein 27 inhibits the growth of prostatic cell lines and induces apoptosis via caspase-3 activation in vitro. BJU Int 2006; 98: 1082-9.
    • (2006) BJU Int , vol.98 , pp. 1082-1089
    • Rocchi, P.1    Jugpal, P.2    So, A.3
  • 31
    • 50349096803 scopus 로고    scopus 로고
    • Dual targeting of HSC70 and HSP72 inhibits HSP90 function and induces tumor-specific apoptosis
    • Powers MV, Clarke PA, Workman P. Dual targeting of HSC70 and HSP72 inhibits HSP90 function and induces tumor-specific apoptosis. Cancer Cell 2008; 14: 250-62.
    • (2008) Cancer Cell , vol.14 , pp. 250-262
    • Powers, M.V.1    Clarke, P.A.2    Workman, P.3
  • 32
    • 0042912912 scopus 로고    scopus 로고
    • Clinical and cellular pharmacology in relation to solid tumours of childhood
    • Estlin EJ, Veal GJ. Clinical and cellular pharmacology in relation to solid tumours of childhood. Cancer Treat Rev 2003; 29: 253-73.
    • (2003) Cancer Treat Rev , vol.29 , pp. 253-273
    • Estlin, E.J.1    Veal, G.J.2
  • 33
    • 0004820949 scopus 로고
    • Actinomycin and DNA transcription
    • Sobell HM. Actinomycin and DNA transcription. Proc Natl Acad Sci U S A 1985; 82: 5328-31.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 5328-5331
    • Sobell, H.M.1
  • 34
    • 0037383192 scopus 로고    scopus 로고
    • Characterization of the MM.1 human multiple myeloma (MM) cell lines:a model system to elucidate the characteristics, behavior, and signaling of steroid-sensitive and -resistant MM cells
    • Greenstein S, Krett NL, Kurosawa Y, et al. Characterization of the MM.1 human multiple myeloma (MM) cell lines:a model system to elucidate the characteristics, behavior, and signaling of steroid-sensitive and -resistant MM cells. Exp Hematol 2003; 31: 271-82.
    • (2003) Exp Hematol , vol.31 , pp. 271-282
    • Greenstein, S.1    Krett, N.L.2    Kurosawa, Y.3
  • 35
    • 0022485356 scopus 로고
    • Characterization of a new drug-resistant human myeloma cell line that expresses P-glycoprotein
    • Dalton WS, Durie BG, Alberts DS, Gerlach JH, Cress AE. Characterization of a new drug-resistant human myeloma cell line that expresses P-glycoprotein. Cancer Res 1986; 46: 5125-30.
    • (1986) Cancer Res , vol.46 , pp. 5125-5130
    • Dalton, W.S.1    Durie, B.G.2    Alberts, D.S.3    Gerlach, J.H.4    Cress, A.E.5
  • 36
    • 23844488773 scopus 로고    scopus 로고
    • Pharmacokinetics of dactinomycin in a pediatric patient population:a United Kingdom Children's Cancer Study Group Study
    • Veal GJ, Cole M, Errington J, et al. Pharmacokinetics of dactinomycin in a pediatric patient population:a United Kingdom Children's Cancer Study Group Study. Clin Cancer Res 2005; 11: 5893-9.
    • (2005) Clin Cancer Res , vol.11 , pp. 5893-5899
    • Veal, G.J.1    Cole, M.2    Errington, J.3
  • 37
    • 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. Anticancer Drugs 2004; 15: 651-62.
    • (2004) Anticancer Drugs , vol.15 , pp. 651-662
    • Beliakoff, J.1    Whitesell, L.2
  • 38
    • 0033944777 scopus 로고    scopus 로고
    • Heat shock proteins-modulators of apoptosis in tumour cells
    • Creagh EM, Sheehan D, Cotter TG. Heat shock proteins-modulators of apoptosis in tumour cells. Leukemia 2000; 14: 1161-73.
    • (2000) Leukemia , vol.14 , pp. 1161-1173
    • Creagh, E.M.1    Sheehan, D.2    Cotter, T.G.3
  • 39
    • 0142245588 scopus 로고    scopus 로고
    • Hsp27 inhibits release of mitochondrial protein Smac in multiple myeloma cells and confers dexamethasone resistance
    • Chauhan D, Li G, Hideshima T, et al. Hsp27 inhibits release of mitochondrial protein Smac in multiple myeloma cells and confers dexamethasone resistance. Blood 2003; 102: 3379-86.
    • (2003) Blood , vol.102 , pp. 3379-3386
    • Chauhan, D.1    Li, G.2    Hideshima, T.3
  • 40
    • 33750711384 scopus 로고    scopus 로고
    • A phase I trial of twice-weekly 17-allylamino-demethoxygeldanamycin in patients with advanced cancer
    • Nowakowski GS, McCollum AK, Ames MM, et al. A phase I trial of twice-weekly 17-allylamino-demethoxygeldanamycin in patients with advanced cancer. Clin Cancer Res 2006; 12: 6087-93.
    • (2006) Clin Cancer Res , vol.12 , pp. 6087-6093
    • Nowakowski, G.S.1    McCollum, A.K.2    Ames, M.M.3
  • 41
    • 0023889668 scopus 로고
    • Tumor response and toxicity after single high-dose versus standard five-day divided-dose dactinomycin in childhood rhabdomyosarcoma
    • Carli M, Pastore G, Perilongo G, et al. Tumor response and toxicity after single high-dose versus standard five-day divided-dose dactinomycin in childhood rhabdomyosarcoma. J Clin Oncol 1988; 6: 654-8.
    • (1988) J Clin Oncol , vol.6 , pp. 654-658
    • Carli, M.1    Pastore, G.2    Perilongo, G.3
  • 43
    • 33644787084 scopus 로고    scopus 로고
    • Gene-specific requirement for P-TEFb activity and RNA polymerase II phosphorylation within the p53 transcriptional program
    • Gomes NP, Bjerke G, Llorente B, Szostek SA, Emerson BM, Espinosa JM. Gene-specific requirement for P-TEFb activity and RNA polymerase II phosphorylation within the p53 transcriptional program. Genes Dev 2006; 20: 601-12.
    • (2006) Genes Dev , vol.20 , pp. 601-612
    • Gomes, N.P.1    Bjerke, G.2    Llorente, B.3    Szostek, S.A.4    Emerson, B.M.5    Espinosa, J.M.6
  • 44
    • 21444432928 scopus 로고    scopus 로고
    • Transcriptional blockade induces p53-dependent apoptosis associated with translocation of p53 to mitochondria
    • Arima Y, Nitta M, Kuninaka S, et al. Transcriptional blockade induces p53-dependent apoptosis associated with translocation of p53 to mitochondria. J Biol Chem 2005; 280: 19166-76.
    • (2005) J Biol Chem , vol.280 , pp. 19166-19176
    • Arima, Y.1    Nitta, M.2    Kuninaka, S.3
  • 45
    • 0033590624 scopus 로고    scopus 로고
    • Inhibition of RNA polymerase II as a trigger for the p53 response
    • Ljungman M, Zhang F, Chen F, Rainbow AJ, McKay BC. Inhibition of RNA polymerase II as a trigger for the p53 response. Oncogene 1999; 18: 583-92.
    • (1999) Oncogene , vol.18 , pp. 583-592
    • Ljungman, M.1    Zhang, F.2    Chen, F.3    Rainbow, A.J.4    McKay, B.C.5
  • 46
    • 38149082690 scopus 로고    scopus 로고
    • R-Roscovitine simultaneously targets both the p53 and NF-nB pathways and causes potentiation of apoptosis:implications in cancer therapy
    • Dey A, Wong ET, Cheok CF, Tergaonkar V, Lane DP. R-Roscovitine simultaneously targets both the p53 and NF-nB pathways and causes potentiation of apoptosis:implications in cancer therapy. Cell Death Differ 2008; 15: 263-73.
    • (2008) Cell Death Differ , vol.15 , pp. 263-273
    • Dey, A.1    Wong, E.T.2    Cheok, C.F.3    Tergaonkar, V.4    Lane, D.P.5
  • 47
    • 0000097632 scopus 로고
    • Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70
    • Hunt C, Morimoto RI. Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70. Proc Natl Acad Sci U S A 1985; 82: 6455-9.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 6455-6459
    • Hunt, C.1    Morimoto, R.I.2


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