메뉴 건너뛰기




Volumn 31, Issue 6, 2014, Pages 2482-2492

Dual targeting of heat shock proteins 90 and 70 promotes cell death and enhances the anticancer effect of chemotherapeutic agents in bladder cancer

Author keywords

Akt; Bladder cancer; Chemotherapy; HSP70; HSP90

Indexed keywords

ANTINEOPLASTIC AGENT; CASPASE 3; CASPASE 7; CISPLATIN; DOCETAXEL; GEMCITABINE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; PIFITHRIN MU; PROTEIN BAD; PROTEIN KINASE B; TANESPIMYCIN; UNCLASSIFIED DRUG; BENZOQUINONE DERIVATIVE; MACROCYCLIC LACTAM;

EID: 84902169156     PISSN: 1021335X     EISSN: 17912431     Source Type: Journal    
DOI: 10.3892/or.2014.3132     Document Type: Article
Times cited : (48)

References (46)
  • 3
    • 21744435151 scopus 로고    scopus 로고
    • Molecular staging of bladder cancer
    • DOI 10.1111/j.1464-410X.2005.05557.x
    • Mitra AP, Datar RH and Cote RJ: Molecular staging of bladder cancer. BJU Int 96: 7-12, 2005. (Pubitemid 40942859)
    • (2005) BJU International , vol.96 , Issue.1 , pp. 7-12
    • Mitra, A.P.1    Datar, R.H.2    Cote, R.J.3
  • 4
    • 84881522229 scopus 로고    scopus 로고
    • Advanced urothelial carcinoma: Overcoming treatment resistance through novel treatment approaches
    • Bambury RM and Rosenberg JE: Advanced urothelial carcinoma: overcoming treatment resistance through novel treatment approaches. Front Pharmacol 4: 3, 2013.
    • (2013) Front Pharmacol , vol.4 , pp. 3
    • Bambury, R.M.1    Rosenberg, J.E.2
  • 5
    • 84862983611 scopus 로고    scopus 로고
    • Electron transfer-based combination therapy of cisplatin with tetramethyl-p-phenylenediamine for ovarian, cervical, and lung cancers
    • Luo T, Yu J, Nguyen J, et al: Electron transfer-based combination therapy of cisplatin with tetramethyl-p-phenylenediamine for ovarian, cervical, and lung cancers. Proc Natl Acad Sci USA 109: 10175-10180, 2012.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 10175-10180
    • Luo, T.1    Yu, J.2    Nguyen, J.3
  • 6
    • 84856897209 scopus 로고    scopus 로고
    • Molecular mechanisms of cisplatin resistance in bladder cancer
    • Drayton RM and Catto JW: Molecular mechanisms of cisplatin resistance in bladder cancer. Expert Rev Anticancer Ther 12: 271-281, 2012.
    • (2012) Expert Rev Anticancer Ther , vol.12 , pp. 271-281
    • Drayton, R.M.1    Catto, J.W.2
  • 10
    • 33746000407 scopus 로고    scopus 로고
    • Phase I trial of intravesical docetaxel in the management of superficial bladder cancer refractory to standard intravesical therapy
    • McKiernan JM, Masson P, Murphy AM, et al: Phase I trial of intravesical docetaxel in the management of superficial bladder cancer refractory to standard intravesical therapy. J Clin Oncol 24: 3075-3080, 2006.
    • (2006) J Clin Oncol , vol.24 , pp. 3075-3080
    • McKiernan, J.M.1    Masson, P.2    Murphy, A.M.3
  • 11
    • 0031786379 scopus 로고    scopus 로고
    • Docetaxel (Taxotere): An active agent in metastatic urothelial cancer; results of a phase II study in non-chemotherapy-pretreated patients
    • de Wit R, Kruit WH, Stoter G, de Boer M, Kerger J and Verweij J: Docetaxel (Taxotere): an active agent in metastatic urothelial cancer; results of a phase II study in non-chemotherapy-pretreated patients. Br J Cancer 78: 1342-1345, 1998.
    • (1998) Br J Cancer , vol.78 , pp. 1342-1345
    • De Wit, R.1    Kruit, W.H.2    Stoter, G.3    De Boer, M.4    Kerger, J.5    Verweij, J.6
  • 14
    • 33745616821 scopus 로고    scopus 로고
    • Gemcitabine in the treatment of advanced transitional cell carcinoma of the urothelium
    • DOI 10.1093/annonc/mdj964
    • Bellmunt J, Albiol S, de Olano AR, Pujadas J, Maroto P; Spanish Oncology Genitourinary Group (SOGUG): Gemcitabine in the treatment of advanced transitional cell carcinoma of the urothelium. Ann Oncol 17 (Suppl 5): v113-v117, 2006. (Pubitemid 43985219)
    • (2006) Annals of Oncology , vol.17 , Issue.SUPPL. 5
    • Bellmunt, J.1    Albiol, S.2    De Olano, A.R.3    Pujadas, J.4    Maroto, P.5
  • 15
    • 84857509409 scopus 로고    scopus 로고
    • Adjuvant chemotherapy with cisplatin and gemcitabine versus chemotherapy at relapse in patients with muscle-invasive bladder cancer submitted to radical cystectomy: An Italian, multicenter, randomized phase III trial
    • Cognetti F, Ruggeri EM, Felici A, et al: Adjuvant chemotherapy with cisplatin and gemcitabine versus chemotherapy at relapse in patients with muscle-invasive bladder cancer submitted to radical cystectomy: an Italian, multicenter, randomized phase III trial. Ann Oncol 23: 695-700, 2012.
    • (2012) Ann Oncol , vol.23 , pp. 695-700
    • Cognetti, F.1    Ruggeri, E.M.2    Felici, A.3
  • 16
    • 84862787781 scopus 로고    scopus 로고
    • Recent advances in treatment of advanced urothelial carcinoma
    • Kim JJ: Recent advances in treatment of advanced urothelial carcinoma. Curr Urol Rep 13: 147-152, 2012.
    • (2012) Curr Urol Rep , vol.13 , pp. 147-152
    • Kim, J.J.1
  • 17
    • 34748837817 scopus 로고    scopus 로고
    • Gemcitabine plus docetaxel as first-line biweekly therapy in locally advanced and/or metastatic urothelial carcinoma: A phase II study
    • DOI 10.1097/CAD.0b013e3282be8d5a, PII 0000181320071100000012
    • Neri B, Vannini L, Giordano C, et al: Gemcitabine plus docetaxel as first-line biweekly therapy in locally advanced and/or metastatic urothelial carcinoma: a phase II study. Anticancer Drugs 18: 1207-1211, 2007. (Pubitemid 47480746)
    • (2007) Anti-Cancer Drugs , vol.18 , Issue.10 , pp. 1207-1211
    • Neri, B.1    Vannini, L.2    Giordano, C.3    Grifoni, R.4    Pantaleo, P.5    Baldazzi, V.6    Crisci, A.7    Lapini, A.8    Raugei, A.9    Carini, M.10
  • 19
    • 0035989680 scopus 로고    scopus 로고
    • HSP90 as a new therapeutic target for cancer therapy: The story unfolds
    • DOI 10.1517/14712598.2.1.3
    • Maloney A and Workman P: HSP90 as a new therapeutic target for cancer therapy: the story unfolds. Expert Opin Biol Ther 2: 3-24, 2002. (Pubitemid 34462457)
    • (2002) Expert Opinion on Biological Therapy , vol.2 , Issue.1 , pp. 3-24
    • Maloney, A.1    Workman, P.2
  • 20
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • DOI 10.1038/nature01913
    • Kamal A, Thao L, Sensintaffar J, Zhang L, Boehm MF, Fritz LC and Burrows FJ: A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 425: 407-410, 2003. (Pubitemid 37187270)
    • (2003) Nature , vol.425 , Issue.6956 , pp. 407-410
    • Kamal, A.1    Thao, L.2    Sensintaffar, J.3    Zhang, L.4    Boehm, M.F.5    Fritz, L.C.6    Burrows, F.J.7
  • 21
    • 0031875042 scopus 로고    scopus 로고
    • The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin
    • DOI 10.1007/s002800050817
    • Schulte TW and Neckers LM: The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin. Cancer Chemother Pharmacol 42: 273-279, 1998. (Pubitemid 28393843)
    • (1998) Cancer Chemotherapy and Pharmacology , vol.42 , Issue.4 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 22
    • 77956476510 scopus 로고    scopus 로고
    • 17-Allylamino-17-demethoxygeldanamycin induces downregulation of critical Hsp90 protein clients and results in cell cycle arrest and apoptosis of human urinary bladder cancer cells
    • Karkoulis PK, Stravopodis DJ, Margaritis LH and Voutsinas GE: 17-Allylamino-17-demethoxygeldanamycin induces downregulation of critical Hsp90 protein clients and results in cell cycle arrest and apoptosis of human urinary bladder cancer cells. BMC Cancer 10: 481, 2010.
    • (2010) BMC Cancer , vol.10 , pp. 481
    • Karkoulis, P.K.1    Stravopodis, D.J.2    Margaritis, L.H.3    Voutsinas, G.E.4
  • 23
    • 73149098975 scopus 로고    scopus 로고
    • Inhibition of HSP90 with pochoximes: SAR and structure-based insights
    • Barluenga S, Fontaine JG, Wang C, et al: Inhibition of HSP90 with pochoximes: SAR and structure-based insights. Chembiochem 10: 2753-2759, 2009.
    • (2009) Chembiochem , vol.10 , pp. 2753-2759
    • Barluenga, S.1    Fontaine, J.G.2    Wang, C.3
  • 24
    • 46749131522 scopus 로고    scopus 로고
    • Divergent synthesis of a pochonin library targeting HSP90 and in vivo efficacy of an identified inhibitor
    • Barluenga S, Wang C, Fontaine JG, et al: Divergent synthesis of a pochonin library targeting HSP90 and in vivo efficacy of an identified inhibitor. Angew Chem Int Ed Engl 47: 4432-4435, 2008.
    • (2008) Angew Chem Int Ed Engl , vol.47 , pp. 4432-4435
    • Barluenga, S.1    Wang, C.2    Fontaine, J.G.3
  • 25
    • 58149340657 scopus 로고    scopus 로고
    • Phase II trial of 17-allylamino-17-demethoxygeldanamycin in patients with metastatic melanoma
    • Solit DB, Osman I, Polsky D, et al: Phase II trial of 17-allylamino-17-demethoxygeldanamycin in patients with metastatic melanoma. Clin Cancer Res 14: 8302-8307, 2008.
    • (2008) Clin Cancer Res , vol.14 , pp. 8302-8307
    • Solit, D.B.1    Osman, I.2    Polsky, D.3
  • 26
    • 84860668954 scopus 로고    scopus 로고
    • Inhibition of thymidine phosphorylase expression by using an HSP90 inhibitor potentiates the cytotoxic effect of cisplatin in non-small-cell lung cancer cells
    • Weng SH, Tseng SC, Huang YC, Chen HJ and Lin YW: Inhibition of thymidine phosphorylase expression by using an HSP90 inhibitor potentiates the cytotoxic effect of cisplatin in non-small-cell lung cancer cells. Biochem Pharmacol 84: 126-136, 2012.
    • (2012) Biochem Pharmacol , vol.84 , pp. 126-136
    • Weng, S.H.1    Tseng, S.C.2    Huang, Y.C.3    Chen, H.J.4    Lin, Y.W.5
  • 27
    • 1642576969 scopus 로고    scopus 로고
    • Quantitative Effects on c-Jun N-Terminal Protein Kinase Signaling Determine Synergistic Interaction of Cisplatin and 17-Allylamino-17- Demethoxygeldanamycin in Colon Cancer Cell Lines
    • DOI 10.1124/mol.65.1.235
    • Vasilevskaya IA, Rakitina TV and O'Dwyer PJ: Quantitative effects on c-Jun N-terminal protein kinase signaling determine synergistic interaction of cisplatin and 17-allylamino-17-demethoxygeldanamycin in colon cancer cell lines. Mol Pharmacol 65: 235-243, 2004. (Pubitemid 38113905)
    • (2004) Molecular Pharmacology , vol.65 , Issue.1 , pp. 235-243
    • Vasilevskaya, I.A.1    Rakitina, T.V.2    O'Dwyer, P.J.3
  • 28
    • 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 and Rosen N: Inhibition of heat shock protein 90 function down-regulates Akt kinase and sensitizes tumors to Taxol. Cancer Res 63: 2139-2144, 2003. (Pubitemid 36538618)
    • (2003) Cancer Research , vol.63 , Issue.9 , pp. 2139-2144
    • Solit, D.B.1    Basso, A.D.2    Olshen, A.B.3    Scher, H.I.4    Rosen, N.5
  • 30
    • 77955908479 scopus 로고    scopus 로고
    • Down-regulation of heat shock protein 70 improves arsenic trioxide and 17-DMAG effects on constitutive signal transducer and activator of transcription 3 activity
    • Ghoshal S, Rao I, Earp JC, Jusko WJ and Wetzler M: Down-regulation of heat shock protein 70 improves arsenic trioxide and 17-DMAG effects on constitutive signal transducer and activator of transcription 3 activity. Cancer Chemother Pharmacol 66: 681-689, 2010.
    • (2010) Cancer Chemother Pharmacol , vol.66 , pp. 681-689
    • Ghoshal, S.1    Rao, I.2    Earp, J.C.3    Jusko, W.J.4    Wetzler, M.5
  • 31
    • 80052188068 scopus 로고    scopus 로고
    • Targeting heat shock proteins 70/90 and proteasome for cancer therapy
    • Wang RE: Targeting heat shock proteins 70/90 and proteasome for cancer therapy. Curr Med Chem 18: 4250-4264, 2011.
    • (2011) Curr Med Chem , vol.18 , pp. 4250-4264
    • Wang, R.E.1
  • 32
    • 70349768075 scopus 로고    scopus 로고
    • A small molecule inhibitor of inducible heat shock protein 70
    • Leu JI, Pimkina J, Frank A, Murphy ME and George DL: A small molecule inhibitor of inducible heat shock protein 70. Mol Cell 36: 15-27, 2009.
    • (2009) Mol Cell , vol.36 , pp. 15-27
    • Leu, J.I.1    Pimkina, J.2    Frank, A.3    Murphy, M.E.4    George, D.L.5
  • 33
    • 84865785716 scopus 로고    scopus 로고
    • HSP90 inhibitor 17-AAG selectively eradicates lymphoma stem cells
    • Newman B, Liu Y, Lee HF, Sun D and Wang Y: HSP90 inhibitor 17-AAG selectively eradicates lymphoma stem cells. Cancer Res 72: 4551-4561, 2012.
    • (2012) Cancer Res , vol.72 , pp. 4551-4561
    • Newman, B.1    Liu, Y.2    Lee, H.F.3    Sun, D.4    Wang, Y.5
  • 34
    • 4344674482 scopus 로고    scopus 로고
    • Targeting multiple signal transduction pathways through inhibition of Hsp90
    • DOI 10.1007/s00109-004-0549-9
    • Zhang H and Burrows F: Targeting multiple signal transduction pathways through inhibition of Hsp90. J Mol Med 82: 488-499, 2004. (Pubitemid 39149859)
    • (2004) Journal of Molecular Medicine , vol.82 , Issue.8 , pp. 488-499
    • Zhang, H.1    Burrows, F.2
  • 35
    • 84055190677 scopus 로고    scopus 로고
    • Low-dose Hsp90 inhibitors tumor-selectively sensitize bladder cancer cells to chemoradiotherapy
    • Yoshida S, Koga F, Tatokoro M, et al: Low-dose Hsp90 inhibitors tumor-selectively sensitize bladder cancer cells to chemoradiotherapy. Cell Cycle 10: 4291-4299, 2011.
    • (2011) Cell Cycle , vol.10 , pp. 4291-4299
    • Yoshida, S.1    Koga, F.2    Tatokoro, M.3
  • 36
    • 84856934940 scopus 로고    scopus 로고
    • Potential role of Hsp90 inhibitors in overcoming cisplatin resistance of bladder cancer-initiating cells
    • Tatokoro M, Koga F, Yoshida S, Kawakami S, Fujii Y, Neckers L and Kihara K: Potential role of Hsp90 inhibitors in overcoming cisplatin resistance of bladder cancer-initiating cells. Int J Cancer 131: 987-996, 2012.
    • (2012) Int J Cancer , vol.131 , pp. 987-996
    • Tatokoro, M.1    Koga, F.2    Yoshida, S.3    Kawakami, S.4    Fujii, Y.5    Neckers, L.6    Kihara, K.7
  • 38
    • 84873946023 scopus 로고    scopus 로고
    • The role of the Hsp90/Akt pathway in myocardial calpain-induced caspase-3 activation and apoptosis during sepsis
    • Li X, Luo R, Jiang R, Meng X, Wu X, Zhang S and Hua W: The role of the Hsp90/Akt pathway in myocardial calpain-induced caspase-3 activation and apoptosis during sepsis. BMC Cardiovasc Disord 13: 8, 2013.
    • (2013) BMC Cardiovasc Disord , vol.13 , pp. 8
    • Li, X.1    Luo, R.2    Jiang, R.3    Meng, X.4    Wu, X.5    Zhang, S.6    Hua, W.7
  • 39
    • 77953734857 scopus 로고    scopus 로고
    • Heat shock protein 70 (Hsp70) as an emerging drug target
    • Evans CG, Chang L and Gestwicki JE: Heat shock protein 70 (Hsp70) as an emerging drug target. J Med Chem 53: 4585-4602, 2010.
    • (2010) J Med Chem , vol.53 , pp. 4585-4602
    • Evans, C.G.1    Chang, L.2    Gestwicki, J.E.3
  • 41
    • 18844378888 scopus 로고    scopus 로고
    • Increased expression of the major heat shock protein Hsp72 in human prostate carcinoma cells is dispensable for their viability but confers resistance to a variety of anticancer agents
    • DOI 10.1038/sj.onc.1208495
    • Gabai VL, Budagova KR and Sherman MY: Increased expression of the major heat shock protein Hsp72 in human prostate carcinoma cells is dispensable for their viability but confers resistance to a variety of anticancer agents. Oncogene 24: 3328-3338, 2005. (Pubitemid 40695114)
    • (2005) Oncogene , vol.24 , Issue.20 , pp. 3328-3338
    • Gabai, V.L.1    Budagova, K.R.2    Sherman, M.Y.3
  • 43
    • 34548030229 scopus 로고    scopus 로고
    • Additive viability-loss following hsp70/hsc70 double interference and Hsp90 inhibition in two breast cancer cell lines
    • Håvik B and Bramham CR: Additive viability-loss following hsp70/hsc70 double interference and Hsp90 inhibition in two breast cancer cell lines. Oncol Rep 17: 1501-1510, 2007.
    • (2007) Oncol Rep , vol.17 , pp. 1501-1510
    • Håvik, B.1    Bramham, C.R.2
  • 44
    • 0037200043 scopus 로고    scopus 로고
    • The turn motif is a phosphorylation switch that regulates the binding of Hsp70 to protein kinase C
    • DOI 10.1074/jbc.M204335200
    • Gao T and Newton AC: The turn motif is a phosphorylation switch that regulates the binding of Hsp70 to protein kinase C. J Biol Chem 277: 31585-31592, 2002. (Pubitemid 34968961)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.35 , pp. 31585-31592
    • Gao, T.1    Newton, A.C.2
  • 45
    • 84862001413 scopus 로고    scopus 로고
    • Multiple kinase pathways involved in the different de novo sensitivity of pancreatic cancer cell lines to 17-AAG
    • Liu H, Zhang T, Chen R, McConkey DJ, Ward JF and Curley SA: Multiple kinase pathways involved in the different de novo sensitivity of pancreatic cancer cell lines to 17-AAG. J Surg Res 176: 147-153, 2012.
    • (2012) J Surg Res , vol.176 , pp. 147-153
    • Liu, H.1    Zhang, T.2    Chen, R.3    McConkey, D.J.4    Ward, J.F.5    Curley, S.A.6
  • 46
    • 2442464889 scopus 로고    scopus 로고
    • Apoptosis defects and chemotherapy resistance: Molecular interaction maps and networks
    • DOI 10.1038/sj.onc.1207515
    • Pommier Y, Sordet O, Antony S, Hayward RL and Kohn KW: Apoptosis defects and chemotherapy resistance: molecular interaction maps and networks. Oncogene 23: 2934-2949, 2004. (Pubitemid 38638854)
    • (2004) Oncogene , vol.23 , Issue.16 REV. ISS. 2 , pp. 2934-2949
    • Pommier, Y.1    Sordet, O.2    Antony, S.3    Hayward, R.L.4    Kohn, K.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.