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Volumn 79, Issue 5, 2011, Pages 823-832

A mechanistic and structural analysis of the inhibition of the 90-kDa heat shock protein by the benzoquinone and hydroquinone ansamycins

Author keywords

[No Author keywords available]

Indexed keywords

ANSAMYCIN DERIVATIVE; BENZOQUINONE; FLAVINE MONONUCLEOTIDE REDUCTASE; HEAT SHOCK PROTEIN 90; HYDROQUINONE;

EID: 79955042825     PISSN: 0026895X     EISSN: 15210111     Source Type: Journal    
DOI: 10.1124/mol.110.070086     Document Type: Article
Times cited : (14)

References (40)
  • 1
    • 0028243181 scopus 로고
    • Metabolism of bioreductive antitumor compounds by purified rat and human DT-diaphorases
    • Beall HD, Mulcahy RT, Siegel D, Traver RD, Gibson NW, and Ross D (1994) Metabolism of bioreductive antitumor compounds by purified rat and human DT-diaphorases. Cancer Res 54:3196-3201. (Pubitemid 24208928)
    • (1994) Cancer Research , vol.54 , Issue.12 , pp. 3196-3201
    • Beall, H.D.1    Mulcahy, R.T.2    Siegel, D.3    Traver, R.D.4    Gibson, N.W.5    Ross, D.6
  • 2
    • 0034733506 scopus 로고    scopus 로고
    • The structural features of concanavalin A governing non-proline peptide isomerization
    • DOI 10.1074/jbc.M001251200
    • Bouckaert J, Dewallef Y, Poortmans F, Wyns L, and Loris R (2000) The structural features of concanavalin A governing non-proline peptide isomerization. J Biol Chem 275:19778-19787. (Pubitemid 30441578)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.26 , pp. 19778-19787
    • Bouckaert, J.1    Dewallef, Y.2    Poortmans, F.3    Wyns, L.4    Loris, R.5
  • 4
    • 0342902311 scopus 로고    scopus 로고
    • Mechanism of NAD(P)H:quinone reductase: Ab initio studies of reduced flavin
    • DOI 10.1002/prot.1055
    • Cavelier G and Amzel LM (2001) Mechanism of NAD (P) H:quinone reductase: Ab initio studies of reduced flavin. Proteins 43:420-432. (Pubitemid 32476438)
    • (2001) Proteins: Structure, Function and Genetics , vol.43 , Issue.4 , pp. 420-432
    • Cavelier, G.1    Mario Amzel, L.2
  • 6
    • 33845302853 scopus 로고    scopus 로고
    • Tumor selectivity of Hsp90 inhibitors: The explanation remains elusive
    • Chiosis G and Neckers L (2006) Tumor selectivity of Hsp90 inhibitors: the explanation remains elusive. ACS Chem Biol 1:279-284.
    • (2006) ACS Chem. Biol. , vol.1 , pp. 279-284
    • Chiosis, G.1    Neckers, L.2
  • 7
    • 0021326093 scopus 로고
    • Cis-trans isomerization of the
    • 5-nitro-2-furyl acrylamide, AF-2, initiated by ascorbate, glutathione, F II and OH-
    • Clarke ED, Wardman P, and Wilson I (1984) Cis-trans isomerization of the (5-nitro-2-furyl) acrylamide, AF-2, initiated by ascorbate, glutathione, F (II) and OH-. Biochem Pharmacol 33:83-87.
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 83-87
    • Clarke, E.D.1    Wardman, P.2    Wilson, I.3
  • 8
    • 33645471864 scopus 로고    scopus 로고
    • Reaction of geldanamycin and C17-substituted analogues with glutathione: Product identifications and pharmacological implications
    • Cysyk RL, Parker RJ, Barchi JJ, Jr., Steeg PS, Hartman NR, and Strong JM (2006) Reaction of geldanamycin and C17-substituted analogues with glutathione: product identifications and pharmacological implications. Chem Res v19:376-381.
    • (2006) Chem. Res. , vol.19 , pp. 376-381
    • Cysyk, R.L.1    Parker, R.J.2    Barchi Jr., J.J.3    Steeg, P.S.4    Hartman, N.R.5    Strong, J.M.6
  • 9
    • 66149188136 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of conformationally constrained cis-amide Hsp90 inhibitors
    • Duerfeldt AS, Brandt GE, and Blagg BS (2009) Design, synthesis, and biological evaluation of conformationally constrained cis-amide Hsp90 inhibitors. Org Lett 11:2353-2356.
    • (2009) Org. Lett. , vol.11 , pp. 2353-2356
    • Duerfeldt, A.S.1    Brandt, G.E.2    Blagg, B.S.3
  • 10
    • 0032101569 scopus 로고    scopus 로고
    • Metabolism of 17-(allylamino)-17-demethoxygeldanamycin
    • NSC 330507 by murine and human hepatic preparations
    • Egorin MJ, Rosen DM, Wolff JH, Callery PS, Musser SM, and Eiseman JL (1998) Metabolism of 17-(allylamino)-17-demethoxygeldanamycin (NSC 330507) by murine and human hepatic preparations. Cancer Res 58:2385-2396.
    • (1998) Cancer Res. , vol.58 , pp. 2385-2396
    • Egorin, M.J.1    Rosen, D.M.2    Wolff, J.H.3    Callery, P.S.4    Musser, S.M.5    Eiseman, J.L.6
  • 11
    • 0346971105 scopus 로고    scopus 로고
    • Performance comparison of generalized born and Poisson methods in the calculation of electrostatic solvation energies for protein structures
    • Feig M, Onufriev A, Lee MS, Im W, Case DA, and Brooks CL 3rd (2004) Performance comparison of generalized born and Poisson methods in the calculation of electrostatic solvation energies for protein structures. J Comput Chem 25:265-284.
    • (2004) J. Comput. Chem. , vol.25 , pp. 265-284
    • Feig, M.1    Onufriev, A.2    Lee, M.S.3    Im, W.4    Case, D.A.5    Brooks III, C.L.6
  • 13
    • 52949096836 scopus 로고    scopus 로고
    • Enzymatic reduction and glutathione conjugation of benzoquinone ansamycin heat shock protein 90 inhibitors: Relevance for toxicity and mechanism of action
    • Guo W, Reigan P, Siegel D, and Ross D (2008) Enzymatic reduction and glutathione conjugation of benzoquinone ansamycin heat shock protein 90 inhibitors: relevance for toxicity and mechanism of action. Drug Metab Dispos 36:2050-2057.
    • (2008) Drug Metab. Dispos , vol.36 , pp. 2050-2057
    • Guo, W.1    Reigan, P.2    Siegel, D.3    Ross, D.4
  • 14
    • 27544446054 scopus 로고    scopus 로고
    • Formation of 17-allylamino-demethoxygeldanamycin (17-AAG) hydroquinone by NAD(P)H:quinone oxidoreductase 1: Role of 17-AAG hydroquinone in heat shock protein 90 inhibition
    • DOI 10.1158/0008-5472.CAN-05-2029
    • Guo W, Reigan P, Siegel D, Zirrolli J, Gustafson D, and Ross D (2005) Formation of 17-allylamino-demethoxygeldanamycin (17-AAG) hydroquinone by NAD (P) H: quinone oxidoreductase 1: role of 17-AAG hydroquinone in heat shock protein 90 inhibition. Cancer Res 65:10006-10015. (Pubitemid 41541482)
    • (2005) Cancer Research , vol.65 , Issue.21 , pp. 10006-10015
    • Guo, W.1    Reigan, P.2    Siegel, D.3    Zirrolli, J.4    Gustafson, D.5    Ross, D.6
  • 15
    • 33748923662 scopus 로고    scopus 로고
    • The bioreduction of a series of benzoquinone ansamycins by NAD(P)H:quinone oxidoreductase 1 to more potent heat shock protein 90 inhibitors, the hydroquinone ansamycinss
    • DOI 10.1124/mol.106.025643
    • Guo W, Reigan P, Siegel D, Zirrolli J, Gustafson D, and Ross D (2006) The bioreduction of a series of benzoquinone ansamycins by NAD (P) H:quinone oxidoreductase 1 to more potent heat shock protein 90 inhibitors, the hydroquinone ansamycins. Mol Pharmacol 70:1194-1203. (Pubitemid 44435970)
    • (2006) Molecular Pharmacology , vol.70 , Issue.4 , pp. 1194-1203
    • Guo, W.1    Reigan, P.2    Siegel, D.3    Zirrolli, J.4    Gustafson, D.5    Ross, D.6
  • 16
    • 0037178118 scopus 로고    scopus 로고
    • The mechanism of Cis-trans isomerization of prolyl peptides by cyclophilin
    • DOI 10.1021/ja020222s
    • Hur S and Bruice TC (2002) The mechanism of cis-trans isomerization of prolyl peptides by cyclophilin. J Am Chem Soc 124:7303-7313. (Pubitemid 34670439)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.25 , pp. 7303-7313
    • Hur, S.1    Bruice, T.C.2
  • 17
    • 0344511727 scopus 로고    scopus 로고
    • Crystal structure and molecular modeling of 17-DMAG in complex with human Hsp90
    • DOI 10.1016/S1074-5521(03)00075-9
    • Jez JM, Chen JC, Rastelli G, Stroud RM, and Santi DV (2003) Crystal structure and molecular modeling of 17-DMAG in complex with human Hsp90. Chem Biol 10:361-368. (Pubitemid 36516654)
    • (2003) Chemistry and Biology , vol.10 , Issue.4 , pp. 361-368
    • Jez, J.M.1    Chen, J.C.-H.2    Rastelli, G.3    Stroud, R.M.4    Santi, D.V.5
  • 18
    • 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 (2003) A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 425:407-410. (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
  • 19
    • 0033579175 scopus 로고    scopus 로고
    • DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90
    • Kelland LR, Sharp SY, Rogers PM, Myers TG, and Workman P (1999) DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90. J Natl Cancer Inst 91:1940-1949.
    • (1999) J. Natl. Cancer Inst. , vol.91 , pp. 1940-1949
    • Kelland, L.R.1    Sharp, S.Y.2    Rogers, P.M.3    Myers, T.G.4    Workman, P.5
  • 21
    • 33845956606 scopus 로고    scopus 로고
    • Biotransformation of geldanamycin and 17-allylamino-17- demethoxygeldanamycin by human liver microsomes: Reductive versus oxidative metabolism and implications
    • DOI 10.1124/dmd.106.009639
    • Lang W, Caldwell GW, Li J, Leo GC, Jones WJ, and Masucci JA (2007) Biotransformation of geldanamycin and 17-allylamino-17-demethoxygeldanamycin by human liver microsomes: reductive versus oxidative metabolism and implications. Drug Metab Dispos 35:21-29. (Pubitemid 46036472)
    • (2007) Drug Metabolism and Disposition , vol.35 , Issue.1 , pp. 21-29
    • Lang, W.1    Caldwell, G.W.2    Li, J.3    Leo, G.C.4    Jones, W.J.5    Masucci, J.A.6
  • 22
    • 3242893125 scopus 로고    scopus 로고
    • Quantum chemical calculations and mutational analysis suggest heat shock protein 90 catalyzes trans-cis isomerization of geldanamycin
    • DOI 10.1016/j.chembiol.2004.05.010, PII S1074552104001693
    • Lee YS, Marcu MG, and Neckers L (2004) Quantum chemical calculations and mutational analysis suggest heat shock protein 90 catalyzes trans-cis isomerization of geldanamycin. Chem Biol 11:991-998. (Pubitemid 38991793)
    • (2004) Chemistry and Biology , vol.11 , Issue.7 , pp. 991-998
    • Lee, Y.-S.1    Marcu, M.G.2    Neckers, L.3
  • 23
    • 0029068515 scopus 로고
    • The three-dimensional structure of NAD (P) H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: Mechanism of the two-electron reduction
    • Li R, Bianchet MA, Talalay P, and Amzel LM (1995) The three-dimensional structure of NAD (P) H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction. Proc Natl Acad Sci USA 92:8846-8850.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8846-8850
    • Li, R.1    Bianchet, M.A.2    Talalay, P.3    Amzel, L.M.4
  • 24
    • 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 (2002) HSP90 as a new therapeutic target for cancer therapy: the story unfolds. Expert Opin Biol Ther 2:3-24. (Pubitemid 34462457)
    • (2002) Expert Opinion on Biological Therapy , vol.2 , Issue.1 , pp. 3-24
    • Maloney, A.1    Workman, P.2
  • 27
    • 0033951278 scopus 로고    scopus 로고
    • Structure and in vivo function of Hsp90
    • DOI 10.1016/S0959-440X(99)00047-0
    • Pearl LH and Prodromou C (2000) Structure and in vivo function of Hsp90. Curr Opin Struct Biol 10:46-51. (Pubitemid 30099326)
    • (2000) Current Opinion in Structural Biology , vol.10 , Issue.1 , pp. 46-51
    • Pearl, L.H.1    Prodromou, C.2
  • 28
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • DOI 10.1146/annurev.biochem.75.103004.142738
    • Pearl LH and Prodromou C (2006) Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu Rev Biochem 75:271-294. (Pubitemid 44118034)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 29
    • 34249089217 scopus 로고    scopus 로고
    • Development of indolequinone mechanism-based inhibitors of NAD(P)H:quinone oxidoreductase 1 (NQO1): NQO1 inhibition and growth inhibitory activity in human pancreatic MIA PaCa-2 cancer cells
    • DOI 10.1021/bi700008y
    • Reigan P, Colucci MA, Siegel D, Chilloux A, Moody CJ, and Ross D (2007) Development of indolequinone mechanism-based inhibitors of NAD (P) H:quinone oxidoreductase 1 (NQO1): NQO1 inhibition and growth inhibitory activity in human pancreatic MIA PaCa-2 cancer cells. Biochemistry 46:5941-5950. (Pubitemid 46799156)
    • (2007) Biochemistry , vol.46 , Issue.20 , pp. 5941-5950
    • Reigan, P.1    Colucci, M.A.2    Siegel, D.3    Chilloux, A.4    Moody, C.J.5    Ross, D.6
  • 30
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • DOI 10.1021/jm980403y
    • Roe SM, Prodromou C, O'Brien R, Ladbury JE, Piper PW, and Pearl LH (1999) Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J Med Chem 42:260-266. (Pubitemid 29069861)
    • (1999) Journal of Medicinal Chemistry , vol.42 , Issue.2 , pp. 260-266
    • Roe, S.M.1    Prodromou, C.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 32
    • 7544236965 scopus 로고    scopus 로고
    • Quinone reductases multitasking in the metabolic world
    • DOI 10.1081/DMR-200033465
    • Ross D (2004) Quinone reductases multitasking in the metabolic world. Drug Metab Rev 36:639-654. (Pubitemid 39453067)
    • (2004) Drug Metabolism Reviews , vol.36 , Issue.3-4 , pp. 639-654
    • Ross, D.1
  • 33
    • 1642503079 scopus 로고    scopus 로고
    • High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity
    • DOI 10.1016/j.ab.2003.10.038, PII S0003269703007541
    • Rowlands MG, Newbatt YM, Prodromou C, Pearl LH, Workman P, and Aherne W (2004) High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity. Anal Biochem 327:176-183. (Pubitemid 38402186)
    • (2004) Analytical Biochemistry , vol.327 , Issue.2 , pp. 176-183
    • Rowlands, M.G.1    Newbatt, Y.M.2    Prodromou, C.3    Pearl, L.H.4    Workman, P.5    Aherne, W.6
  • 34
    • 0036263966 scopus 로고    scopus 로고
    • The hsp70 chaperone DnaK is a secondary amide peptide bond cis-trans isomerase
    • DOI 10.1038/nsb804
    • Schiene-Fischer C, Habazettl J, Schmid FX, and Fischer G (2002) The hsp70 chaperone DnaK is a secondary amide peptide bond cis-trans isomerase. Nat Struct Biol 9:419-424. (Pubitemid 34568785)
    • (2002) Nature Structural Biology , vol.9 , Issue.6 , pp. 419-424
    • Schiene-Fischer, C.1    Habazettl, J.2    Schmid, F.X.3    Fischer, G.4
  • 35
    • 0027256737 scopus 로고
    • Prolyl isomerase: Enzymatic catalysis of slow protein-folding reactions
    • Schmid FX (1993) Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions. Annu Rev Biophys Biomol Struct 22:123-142.
    • (1993) Annu. Rev. Biophys. Biomol. Struct , vol.22 , pp. 123-142
    • Schmid, F.X.1
  • 36
    • 0001402694 scopus 로고
    • Tandem [3,3]-sigmatropic rearrangements in an ansamycin-stereospecific conversion of an (S)-allylic alcohol to an (S)-allylic amine derivative
    • Schnur R and Corman ML (1994) Tandem [3,3]-sigmatropic rearrangements in an ansamycin-stereospecific conversion of an (S)-allylic alcohol to an (S)-allylic amine derivative. J Org Chem 59:2581-2584.
    • (1994) J. Org. Chem. , vol.59 , pp. 2581-2584
    • Schnur, R.1    Corman, M.L.2
  • 37
    • 0033801337 scopus 로고    scopus 로고
    • Immunodetection of NAD (P) H:quinone oxidoreductase 1 (NQO1) in human tissues
    • Siegel D and Ross D (2000) Immunodetection of NAD (P) H:quinone oxidoreductase 1 (NQO1) in human tissues. Free Radic Biol 29:246-253.
    • (2000) Free Radic Biol. , vol.29 , pp. 246-253
    • Siegel, D.1    Ross, D.2
  • 38
    • 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, and Pavletich NP (1997) Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 89:239-250. (Pubitemid 27199896)
    • (1997) Cell , vol.89 , Issue.2 , 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
  • 39
    • 33947427870 scopus 로고    scopus 로고
    • Relationship among ligand conformations in solution, in the solid state, and at the Hsp90 binding site: Geldanamycin and radicicol
    • DOI 10.1021/ja064863p
    • Thepchatri P, Eliseo T, Cicero DO, Myles D, and Snyder JP (2007) Relationship among ligand conformations in solution, in the solid state, and at the Hsp90 binding site: geldanamycin and radicicol. J Am Chem Soc 129:3127-3134. (Pubitemid 46449344)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.11 , pp. 3127-3134
    • Thepchatri, P.1    Eliseo, T.2    Cicero, D.O.3    Myles, D.4    Snyder, J.P.5
  • 40
    • 0035909827 scopus 로고    scopus 로고
    • Characterization of a mechanism-based inhibitor of NAD(P)H:Quinone oxidoreductase 1 by biochemical, x-ray crystallographic, and mass spectrometric approaches
    • DOI 10.1021/bi011324i
    • Winski SL, Faig M, Bianchet MA, Siegel D, Swann E, Fung K, Duncan MW, Moody CJ, Amzel LM, and Ross D (2001) Characterization of a mechanism-based inhibitor of NAD (P) H:quinone oxidoreductase 1 by biochemical, X-ray crystallographic, and mass approaches. Biochemistry 40:15135-15142. (Pubitemid 33151928)
    • (2001) Biochemistry , vol.40 , Issue.50 , pp. 15135-15142
    • Winski, S.L.1    Faig, M.2    Bianchet, M.A.3    Siegel, D.4    Swann, E.5    Fung, K.6    Duncan, M.W.7    Moody, C.J.8    Amzel, L.M.9    Ross, D.10


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