메뉴 건너뛰기




Volumn 13, Issue 1, 2014, Pages

FW-04-806 inhibits proliferation and induces apoptosis in human breast cancer cells by binding to N-terminus of Hsp90 and disrupting Hsp90-Cdc37 complex formation

Author keywords

Breast cancer; Cdc37; FW 04 806; HER2; Hsp90

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ANTINEOPLASTIC AGENT; CASPASE 9; CELL CYCLE PROTEIN 37; CHAPERONE; DOXORUBICIN; EPIDERMAL GROWTH FACTOR RECEPTOR 2; FW 04 806; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; PROTEIN KINASE B; RAF PROTEIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; CDC37 PROTEIN, HUMAN; CELL CYCLE PROTEIN; CHAPERONIN; CONGLOBATIN; ERBB2 PROTEIN, HUMAN; MACROLIDE; MULTIPROTEIN COMPLEX; OXAZOLE DERIVATIVE; PROTEIN BINDING;

EID: 84902044721     PISSN: None     EISSN: 14764598     Source Type: Journal    
DOI: 10.1186/1476-4598-13-150     Document Type: Article
Times cited : (69)

References (39)
  • 1
    • 5044239107 scopus 로고    scopus 로고
    • Pathways of chaperone-mediated protein folding in the cytosol
    • 10.1038/nrm1492, 15459659
    • Young JC, Agashe VR, Siegers K, Hartl FU. Pathways of chaperone-mediated protein folding in the cytosol. Nat Rev Mol Cell Biol 2004, 5:781-791. 10.1038/nrm1492, 15459659.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 781-791
    • Young, J.C.1    Agashe, V.R.2    Siegers, K.3    Hartl, F.U.4
  • 2
    • 0027925653 scopus 로고
    • Heat shock proteins functioning as molecular chaperones: their roles in normal and stressed cells
    • Welch WJ. Heat shock proteins functioning as molecular chaperones: their roles in normal and stressed cells. Phil Trans Roy Soc Lond B Biol Sci 1993, 339:327-333.
    • (1993) Phil Trans Roy Soc Lond B Biol Sci , vol.339 , pp. 327-333
    • Welch, W.J.1
  • 3
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • 10.1038/381571a0, 8637592
    • Hartl FU. Molecular chaperones in cellular protein folding. Nature 1996, 381:571-579. 10.1038/381571a0, 8637592.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 4
    • 79955432735 scopus 로고    scopus 로고
    • Advances in the discovery and development of heat-shock protein 90 inhibitors for cancer treatment
    • Patel HJ, Modi S, Chiosis G, Taldone T. Advances in the discovery and development of heat-shock protein 90 inhibitors for cancer treatment. Expet Opin Drug Discov 2011, 6:559-587.
    • (2011) Expet Opin Drug Discov , vol.6 , pp. 559-587
    • Patel, H.J.1    Modi, S.2    Chiosis, G.3    Taldone, T.4
  • 5
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • 10.1038/nature01913, 14508491
    • Kamal A, Thao L, Sensintaffar J, Zhang L, Boehm MF, Fritz LC, Burrows FJ. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 2003, 425:407-410. 10.1038/nature01913, 14508491.
    • (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    Burrows, F.J.7
  • 6
    • 2642521990 scopus 로고    scopus 로고
    • Therapeutic and diagnostic implications of Hsp90 activation
    • 10.1016/j.molmed.2004.04.006, 15177193
    • Kamal A, Boehm MF, Burrows FJ. Therapeutic and diagnostic implications of Hsp90 activation. Trends Mol Med 2004, 10:283-290. 10.1016/j.molmed.2004.04.006, 15177193.
    • (2004) Trends Mol Med , vol.10 , pp. 283-290
    • Kamal, A.1    Boehm, M.F.2    Burrows, F.J.3
  • 7
    • 27744485422 scopus 로고    scopus 로고
    • A proteomic snapshot of the human heat shock protein 90 interactome
    • 10.1016/j.febslet.2005.10.020, 16263121
    • Falsone SF, Gesslbauer B, Tirk F, Piccinini AM, Kungl AJ. A proteomic snapshot of the human heat shock protein 90 interactome. FEBS Lett 2005, 579:6350-6354. 10.1016/j.febslet.2005.10.020, 16263121.
    • (2005) FEBS Lett , vol.579 , pp. 6350-6354
    • Falsone, S.F.1    Gesslbauer, B.2    Tirk, F.3    Piccinini, A.M.4    Kungl, A.J.5
  • 9
    • 37649024109 scopus 로고    scopus 로고
    • Development and application of Hsp90 inhibitors
    • 10.1016/j.drudis.2007.10.007, 18190862
    • Solit DB, Chiosis G. Development and application of Hsp90 inhibitors. Drug Discov Today 2008, 13:38-43. 10.1016/j.drudis.2007.10.007, 18190862.
    • (2008) Drug Discov Today , vol.13 , pp. 38-43
    • Solit, D.B.1    Chiosis, G.2
  • 10
    • 77953916528 scopus 로고    scopus 로고
    • HSP90 at the hub of protein homeostasis: emerging mechanistic insights
    • 10.1038/nrm2918, 20531426
    • Taipale M, Jarosz DF, Lindquist S. HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat Rev Mol Cell Biol 2010, 11:515-528. 10.1038/nrm2918, 20531426.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 515-528
    • Taipale, M.1    Jarosz, D.F.2    Lindquist, S.3
  • 11
    • 77955506092 scopus 로고    scopus 로고
    • Gymnastics of molecular chaperones
    • 10.1016/j.molcel.2010.07.012, 20705236
    • Mayer MP. Gymnastics of molecular chaperones. Mol Cell 2010, 39:321-331. 10.1016/j.molcel.2010.07.012, 20705236.
    • (2010) Mol Cell , vol.39 , pp. 321-331
    • Mayer, M.P.1
  • 14
    • 84865150187 scopus 로고    scopus 로고
    • Optimization of fermentation conditions for FW-04-806, a macrolide dilactone compound with two oxazole ring
    • Hong C, Wei J, Wei H, Hui-ling F, Hong J, Wei Z. Optimization of fermentation conditions for FW-04-806, a macrolide dilactone compound with two oxazole ring. Chin J Antibiot 2012, 37:45-49.
    • (2012) Chin J Antibiot , vol.37 , pp. 45-49
    • Hong, C.1    Wei, J.2    Wei, H.3    Hui-ling, F.4    Hong, J.5    Wei, Z.6
  • 15
    • 0018620143 scopus 로고
    • Conglobatin, a novel macrolide dilactone from Streptomyces conglobatus ATCC 31005
    • 10.7164/antibiotics.32.874, 511778
    • Westley JW, Liu CM, Evans RH, Blount JF. Conglobatin, a novel macrolide dilactone from Streptomyces conglobatus ATCC 31005. J Antibiot 1979, 32:874-877. 10.7164/antibiotics.32.874, 511778.
    • (1979) J Antibiot , vol.32 , pp. 874-877
    • Westley, J.W.1    Liu, C.M.2    Evans, R.H.3    Blount, J.F.4
  • 18
    • 35648998466 scopus 로고    scopus 로고
    • Proteomics evaluation of chemically cleavable activity-based probes
    • 10.1074/mcp.M700124-MCP200, 17615255
    • Fonovic M, Verhelst SH, Sorum MT, Bogyo M. Proteomics evaluation of chemically cleavable activity-based probes. Mol Cell Proteomics 2007, 6:1761-1770. 10.1074/mcp.M700124-MCP200, 17615255.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1761-1770
    • Fonovic, M.1    Verhelst, S.H.2    Sorum, M.T.3    Bogyo, M.4
  • 19
    • 84869090566 scopus 로고    scopus 로고
    • Sulforaphane inhibits pancreatic cancer through disrupting Hsp90-p50(Cdc37) complex and direct interactions with amino acids residues of Hsp90
    • 10.1016/j.jnutbio.2011.11.004, 3386376, 22444872
    • Li Y, Karagoz GE, Seo YH, Zhang T, Jiang Y, Yu Y, Duarte AM, Schwartz SJ, Boelens R, Carroll K, Rüdiger SG, Sun D. Sulforaphane inhibits pancreatic cancer through disrupting Hsp90-p50(Cdc37) complex and direct interactions with amino acids residues of Hsp90. J Nutr Biochem 2012, 23:1617-1626. 10.1016/j.jnutbio.2011.11.004, 3386376, 22444872.
    • (2012) J Nutr Biochem , vol.23 , pp. 1617-1626
    • Li, Y.1    Karagoz, G.E.2    Seo, Y.H.3    Zhang, T.4    Jiang, Y.5    Yu, Y.6    Duarte, A.M.7    Schwartz, S.J.8    Boelens, R.9    Carroll, K.10    Rüdiger, S.G.11    Sun, D.12
  • 20
    • 1642503079 scopus 로고    scopus 로고
    • High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity
    • 10.1016/j.ab.2003.10.038, 15051534
    • Rowlands MG, Newbatt YM, Prodromou C, Pearl LH, Workman P, Aherne W. High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity. Anal Biochem 2004, 327:176-183. 10.1016/j.ab.2003.10.038, 15051534.
    • (2004) Anal Biochem , vol.327 , pp. 176-183
    • Rowlands, M.G.1    Newbatt, Y.M.2    Prodromou, C.3    Pearl, L.H.4    Workman, P.5    Aherne, W.6
  • 21
    • 36148989163 scopus 로고    scopus 로고
    • High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK
    • 10.1016/j.ab.2007.08.020, 17904512
    • Chang L, Bertelsen EB, Wisen S, Larsen EM, Zuiderweg ER, Gestwicki JE. High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK. Anal Biochem 2008, 372:167-176. 10.1016/j.ab.2007.08.020, 17904512.
    • (2008) Anal Biochem , vol.372 , pp. 167-176
    • Chang, L.1    Bertelsen, E.B.2    Wisen, S.3    Larsen, E.M.4    Zuiderweg, E.R.5    Gestwicki, J.E.6
  • 22
    • 0037265586 scopus 로고    scopus 로고
    • Development of small molecule Hsp90 inhibitors: utilizing both forward and reverse chemical genomics for drug identification
    • 10.2174/0929867033457818, 12678776
    • Neckers L. Development of small molecule Hsp90 inhibitors: utilizing both forward and reverse chemical genomics for drug identification. Curr Med Chem 2003, 10:733-739. 10.2174/0929867033457818, 12678776.
    • (2003) Curr Med Chem , vol.10 , pp. 733-739
    • Neckers, L.1
  • 23
    • 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
    • 10.1073/pnas.91.18.8324, 44598, 8078881
    • 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 U S A 1994, 91:8324-8328. 10.1073/pnas.91.18.8324, 44598, 8078881.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 24
    • 0029812759 scopus 로고    scopus 로고
    • Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin
    • 10.1074/jbc.271.37.22796, 8798456
    • Mimnaugh EG, Chavany C, Neckers L. Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin. J Biol Chem 1996, 271:22796-22801. 10.1074/jbc.271.37.22796, 8798456.
    • (1996) J Biol Chem , vol.271 , pp. 22796-22801
    • Mimnaugh, E.G.1    Chavany, C.2    Neckers, L.3
  • 25
    • 33646114761 scopus 로고    scopus 로고
    • Hsp90 inhibitors: small molecules that transform the Hsp90 protein folding machinery into a catalyst for protein degradation
    • 10.1002/med.20052, 16385472
    • Blagg BS, Kerr TD. Hsp90 inhibitors: small molecules that transform the Hsp90 protein folding machinery into a catalyst for protein degradation. Med Res Rev 2006, 26:310-338. 10.1002/med.20052, 16385472.
    • (2006) Med Res Rev , vol.26 , pp. 310-338
    • Blagg, B.S.1    Kerr, T.D.2
  • 26
    • 33645975518 scopus 로고    scopus 로고
    • Chaperoning oncogenes: Hsp90 as a target of geldanamycin
    • 10.1007/3-540-29717-0_11, 16610363
    • Neckers L. Chaperoning oncogenes: Hsp90 as a target of geldanamycin. Handb Exp Pharmacol 2006, 172:259-277. 10.1007/3-540-29717-0_11, 16610363.
    • (2006) Handb Exp Pharmacol , vol.172 , pp. 259-277
    • Neckers, L.1
  • 27
    • 0029056501 scopus 로고
    • Preclinical pharmacologic evaluation of geldanamycin as an antitumor agent
    • 10.1007/BF00689048, 7628050
    • Supko JG, Hickman RL, Grever MR, Malspeis L. Preclinical pharmacologic evaluation of geldanamycin as an antitumor agent. Cancer Chemother Pharmacol 1995, 36:305-315. 10.1007/BF00689048, 7628050.
    • (1995) Cancer Chemother Pharmacol , vol.36 , pp. 305-315
    • Supko, J.G.1    Hickman, R.L.2    Grever, M.R.3    Malspeis, L.4
  • 28
    • 38349153572 scopus 로고    scopus 로고
    • A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells
    • 10.1158/1535-7163.MCT-07-0484, 18202019
    • Zhang T, Hamza A, Cao X, Wang B, Yu S, Zhan CG, Sun D. A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells. Mol Cancer Ther 2008, 7:162-170. 10.1158/1535-7163.MCT-07-0484, 18202019.
    • (2008) Mol Cancer Ther , vol.7 , pp. 162-170
    • Zhang, T.1    Hamza, A.2    Cao, X.3    Wang, B.4    Yu, S.5    Zhan, C.G.6    Sun, D.7
  • 29
    • 37549060720 scopus 로고    scopus 로고
    • Targeting Cdc37 inhibits multiple signaling pathways and induces growth arrest in prostate cancer cells
    • 10.1158/0008-5472.CAN-07-3162, 18089825
    • Gray PJ, Stevenson MA, Calderwood SK. Targeting Cdc37 inhibits multiple signaling pathways and induces growth arrest in prostate cancer cells. Cancer Res 2007, 67:11942-11950. 10.1158/0008-5472.CAN-07-3162, 18089825.
    • (2007) Cancer Res , vol.67 , pp. 11942-11950
    • Gray, P.J.1    Stevenson, M.A.2    Calderwood, S.K.3
  • 30
    • 45849131623 scopus 로고    scopus 로고
    • Targeting the oncogene and kinome chaperone CDC37
    • 10.1038/nrc2420, 2779120, 18511936
    • Gray PJ, Prince T, Cheng J, Stevenson MA, Calderwood SK. Targeting the oncogene and kinome chaperone CDC37. Nat Rev Cancer 2008, 8:491-495. 10.1038/nrc2420, 2779120, 18511936.
    • (2008) Nat Rev Cancer , vol.8 , pp. 491-495
    • Gray, P.J.1    Prince, T.2    Cheng, J.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 31
    • 12344291243 scopus 로고    scopus 로고
    • Hsp90 and Cdc37 - a chaperone cancer conspiracy
    • 10.1016/j.gde.2004.12.011, 15661534
    • Pearl LH. Hsp90 and Cdc37 - a chaperone cancer conspiracy. Curr Opin Genet Dev 2005, 15:55-61. 10.1016/j.gde.2004.12.011, 15661534.
    • (2005) Curr Opin Genet Dev , vol.15 , pp. 55-61
    • Pearl, L.H.1
  • 33
    • 0032493624 scopus 로고    scopus 로고
    • P50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site
    • 10.1074/jbc.273.32.20090, 9685350
    • Silverstein AM, Grammatikakis N, Cochran BH, Chinkers M, Pratt WB. p50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site. J Biol Chem 1998, 273:20090-20095. 10.1074/jbc.273.32.20090, 9685350.
    • (1998) J Biol Chem , vol.273 , pp. 20090-20095
    • Silverstein, A.M.1    Grammatikakis, N.2    Cochran, B.H.3    Chinkers, M.4    Pratt, W.B.5
  • 34
    • 84865695733 scopus 로고    scopus 로고
    • Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition
    • 10.1016/j.cell.2012.06.047, 3894786, 22939624
    • Taipale M, Krykbaeva I, Koeva M, Kayatekin C, Westover KD, Karras GI, Lindquist S. Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition. Cell 2012, 150:987-1001. 10.1016/j.cell.2012.06.047, 3894786, 22939624.
    • (2012) Cell , vol.150 , pp. 987-1001
    • Taipale, M.1    Krykbaeva, I.2    Koeva, M.3    Kayatekin, C.4    Westover, K.D.5    Karras, G.I.6    Lindquist, S.7
  • 35
    • 70349921403 scopus 로고    scopus 로고
    • Molecular mechanism of inhibition of the human protein complex Hsp90-Cdc37, a kinome chaperone-cochaperone, by triterpene celastrol
    • 10.1002/anie.200900929, 19585625
    • Sreeramulu S, Gande SL, Gobel M, Schwalbe H. Molecular mechanism of inhibition of the human protein complex Hsp90-Cdc37, a kinome chaperone-cochaperone, by triterpene celastrol. Angew Chem Int Ed Engl 2009, 48:5853-5855. 10.1002/anie.200900929, 19585625.
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 5853-5855
    • Sreeramulu, S.1    Gande, S.L.2    Gobel, M.3    Schwalbe, H.4
  • 36
    • 33646406554 scopus 로고    scopus 로고
    • Celastrol, a triterpene extracted from the Chinese " Thunder of God Vine," is a potent proteasome inhibitor and suppresses human prostate cancer growth in nude mice
    • 10.1158/0008-5472.CAN-05-4529, 16651429
    • Yang H, Chen D, Cui QC, Yuan X, Dou QP. Celastrol, a triterpene extracted from the Chinese " Thunder of God Vine," is a potent proteasome inhibitor and suppresses human prostate cancer growth in nude mice. Cancer Res 2006, 66:4758-4765. 10.1158/0008-5472.CAN-05-4529, 16651429.
    • (2006) Cancer Res , vol.66 , pp. 4758-4765
    • Yang, H.1    Chen, D.2    Cui, Q.C.3    Yuan, X.4    Dou, Q.P.5
  • 38
    • 84864067111 scopus 로고    scopus 로고
    • Non-nucleosidic inhibition of Herpes simplex virus DNA polymerase: mechanistic insights into the anti-herpetic mode of action of herbal drug withaferin A
    • Grover A, Agrawal V, Shandilya A, Bisaria VS, Sundar D. Non-nucleosidic inhibition of Herpes simplex virus DNA polymerase: mechanistic insights into the anti-herpetic mode of action of herbal drug withaferin A. BMC Bioinformatics 2011, 12(Suppl 13):S22.
    • (2011) BMC Bioinformatics , vol.12 , Issue.SUPPL. 13
    • Grover, A.1    Agrawal, V.2    Shandilya, A.3    Bisaria, V.S.4    Sundar, D.5
  • 39
    • 0035793546 scopus 로고    scopus 로고
    • Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90
    • 10.1074/jbc.M006864200, 11071886
    • Xu W, Mimnaugh E, Rosser MF, Nicchitta C, Marcu M, Yarden Y, Neckers L. Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90. J Biol Chem 2001, 276:3702-3708. 10.1074/jbc.M006864200, 11071886.
    • (2001) J Biol Chem , vol.276 , pp. 3702-3708
    • Xu, W.1    Mimnaugh, E.2    Rosser, M.F.3    Nicchitta, C.4    Marcu, M.5    Yarden, Y.6    Neckers, L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.