메뉴 건너뛰기




Volumn 7, Issue 7, 2012, Pages

Hsp90 is cleaved by reactive oxygen species at a highly conserved N-terminal amino acid motif

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BCR ABL PROTEIN; GLYCINE; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90BETA; I KAPPA B KINASE GAMMA; IRON; NUCLEOTIDE; PROTEIN; PROTEIN C RAF; PROTEIN RIP; RAF PROTEIN; REACTIVE OXYGEN METABOLITE; TELOMERASE REVERSE TRANSCRIPTASE; UNCLASSIFIED DRUG;

EID: 84864414686     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0040795     Document Type: Article
Times cited : (61)

References (36)
  • 1
    • 0024421221 scopus 로고
    • hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures
    • Borkovich KA, Farrelly FW, Finkelstein DB, Taulien J, Lindquist S, (1989) hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol Cell Biol 9: 3919-3930.
    • (1989) Mol Cell Biol , vol.9 , pp. 3919-3930
    • Borkovich, K.A.1    Farrelly, F.W.2    Finkelstein, D.B.3    Taulien, J.4    Lindquist, S.5
  • 2
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl LH, Prodromou C, (2006) Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu Rev Biochem 75: 271-294.
    • (2006) Annu Rev Biochem , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 3
    • 7944225978 scopus 로고    scopus 로고
    • Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform
    • McLaughlin SH, Ventouras LA, Lobbezoo B, Jackson SE, (2004) Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform. J Mol Biol 344: 813-826.
    • (2004) J Mol Biol , vol.344 , pp. 813-826
    • McLaughlin, S.H.1    Ventouras, L.A.2    Lobbezoo, B.3    Jackson, S.E.4
  • 4
    • 0036219609 scopus 로고    scopus 로고
    • Hsp90 inhibitors as novel cancer chemotherapeutic agents
    • Neckers L, (2002) Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol Med 8: S55-61.
    • (2002) Trends Mol Med , vol.8
    • Neckers, L.1
  • 6
    • 0026749295 scopus 로고
    • Unusual expression and localization of heat-shock proteins in human tumor cells
    • Ferrarini M, Heltai S, Zocchi MR, Rugarli C, (1992) Unusual expression and localization of heat-shock proteins in human tumor cells. Int J Cancer 51: 613-619.
    • (1992) Int J Cancer , vol.51 , pp. 613-619
    • Ferrarini, M.1    Heltai, S.2    Zocchi, M.R.3    Rugarli, C.4
  • 8
    • 0037067712 scopus 로고    scopus 로고
    • Geldanamycin leads to superoxide formation by enzymatic and non-enzymatic redox cycling. Implications for studies of Hsp90 and endothelial cell nitric-oxide synthase
    • Dikalov S, Landmesser U, Harrison DG, (2002) Geldanamycin leads to superoxide formation by enzymatic and non-enzymatic redox cycling. Implications for studies of Hsp90 and endothelial cell nitric-oxide synthase. J Biol Chem 277: 25480-25485.
    • (2002) J Biol Chem , vol.277 , pp. 25480-25485
    • Dikalov, S.1    Landmesser, U.2    Harrison, D.G.3
  • 9
    • 70350227307 scopus 로고    scopus 로고
    • Role of oxidative stress in geldanamycin-induced cytotoxicity and disruption of Hsp90 signaling complex
    • Clark CB, Rane MJ, El Mehdi D, Miller CJ, Sachleben LR Jr, et al. (2009) Role of oxidative stress in geldanamycin-induced cytotoxicity and disruption of Hsp90 signaling complex. Free Radic Biol Med 47: 1440-1449.
    • (2009) Free Radic Biol Med , vol.47 , pp. 1440-1449
    • Clark, C.B.1    Rane, M.J.2    El Mehdi, D.3    Miller, C.J.4    Sachleben Jr., L.R.5
  • 10
    • 33750710080 scopus 로고    scopus 로고
    • Protein oxidation and aging
    • Stadtman ER, (2006) Protein oxidation and aging. Free Radic Res 40: 1250-1258.
    • (2006) Free Radic Res , vol.40 , pp. 1250-1258
    • Stadtman, E.R.1
  • 11
    • 58649121962 scopus 로고    scopus 로고
    • Hsp90 cleavage by an oxidative stress leads to its client proteins degradation and cancer cell death
    • Beck R, Verrax J, Gonze T, Zappone M, Pedrosa RC, et al. (2009) Hsp90 cleavage by an oxidative stress leads to its client proteins degradation and cancer cell death. Biochem Pharmacol 77: 375-383.
    • (2009) Biochem Pharmacol , vol.77 , pp. 375-383
    • Beck, R.1    Verrax, J.2    Gonze, T.3    Zappone, M.4    Pedrosa, R.C.5
  • 12
    • 68449092620 scopus 로고    scopus 로고
    • In situ modulation of oxidative stress: a novel and efficient strategy to kill cancer cells
    • Verrax J, Pedrosa RC, Beck R, Dejeans N, Taper H, et al. (2009) In situ modulation of oxidative stress: a novel and efficient strategy to kill cancer cells. Curr Med Chem 16: 1821-1830.
    • (2009) Curr Med Chem , vol.16 , pp. 1821-1830
    • Verrax, J.1    Pedrosa, R.C.2    Beck, R.3    Dejeans, N.4    Taper, H.5
  • 13
    • 20544466104 scopus 로고    scopus 로고
    • Enhancement of quinone redox cycling by ascorbate induces a caspase-3 independent cell death in human leukaemia cells. An in vitro comparative study
    • Verrax J, Delvaux M, Beghein N, Taper H, Gallez B, et al. (2005) Enhancement of quinone redox cycling by ascorbate induces a caspase-3 independent cell death in human leukaemia cells. An in vitro comparative study. Free Radic Res 39: 649-657.
    • (2005) Free Radic Res , vol.39 , pp. 649-657
    • Verrax, J.1    Delvaux, M.2    Beghein, N.3    Taper, H.4    Gallez, B.5
  • 14
    • 80555137586 scopus 로고    scopus 로고
    • Ascorbate/menadione-induced oxidative stress kills cancer cells that express normal or mutated forms of the oncogenic protein Bcr-Abl. An in vitro and in vivo mechanistic study
    • Beck R, Pedrosa RC, Dejeans N, Glorieux C, Leveque P, et al. (2011) Ascorbate/menadione-induced oxidative stress kills cancer cells that express normal or mutated forms of the oncogenic protein Bcr-Abl. An in vitro and in vivo mechanistic study. Invest New Drugs 29: 891-900.
    • (2011) Invest New Drugs , vol.29 , pp. 891-900
    • Beck, R.1    Pedrosa, R.C.2    Dejeans, N.3    Glorieux, C.4    Leveque, P.5
  • 15
    • 0022460610 scopus 로고
    • The effects of basic substances and acidic ionophores on the digestion of exogenous and endogenous proteins in mouse peritoneal macrophages
    • Ohkuma S, Chudzik J, Poole B, (1986) The effects of basic substances and acidic ionophores on the digestion of exogenous and endogenous proteins in mouse peritoneal macrophages. J Cell Biol 102: 959-966.
    • (1986) J Cell Biol , vol.102 , pp. 959-966
    • Ohkuma, S.1    Chudzik, J.2    Poole, B.3
  • 16
    • 0020365443 scopus 로고
    • Separation and characterization of the aldehydic products of lipid peroxidation stimulated by ADP-Fe2+ in rat liver microsomes
    • Esterbauer H, Cheeseman KH, Dianzani MU, Poli G, Slater TF, (1982) Separation and characterization of the aldehydic products of lipid peroxidation stimulated by ADP-Fe2+ in rat liver microsomes. Biochem J 208: 129-140.
    • (1982) Biochem J , vol.208 , pp. 129-140
    • Esterbauer, H.1    Cheeseman, K.H.2    Dianzani, M.U.3    Poli, G.4    Slater, T.F.5
  • 17
    • 61449183461 scopus 로고    scopus 로고
    • Immuno-spin trapping of protein and DNA radicals: "tagging" free radicals to locate and understand the redox process
    • Gomez-Mejiba SE, Zhai Z, Akram H, Deterding LJ, Hensley K, et al. (2009) Immuno-spin trapping of protein and DNA radicals: "tagging" free radicals to locate and understand the redox process. Free Radic Biol Med 46: 853-865.
    • (2009) Free Radic Biol Med , vol.46 , pp. 853-865
    • Gomez-Mejiba, S.E.1    Zhai, Z.2    Akram, H.3    Deterding, L.J.4    Hensley, K.5
  • 18
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett BS, Stadtman ER, (1997) Protein oxidation in aging, disease, and oxidative stress. J Biol Chem 272: 20313-20316.
    • (1997) J Biol Chem , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 19
    • 0346100345 scopus 로고    scopus 로고
    • Free radical-mediated oxidation of free amino acids and amino acid residues in proteins
    • Stadtman ER, Levine RL, (2003) Free radical-mediated oxidation of free amino acids and amino acid residues in proteins. Amino Acids 25: 207-218.
    • (2003) Amino Acids , vol.25 , pp. 207-218
    • Stadtman, E.R.1    Levine, R.L.2
  • 20
    • 0024548919 scopus 로고
    • Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II
    • Lees-Miller SP, Anderson CW, (1989) Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II. J Biol Chem 264: 2431-2437.
    • (1989) J Biol Chem , vol.264 , pp. 2431-2437
    • Lees-Miller, S.P.1    Anderson, C.W.2
  • 21
    • 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, et al. (1997) Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 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
  • 22
    • 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, et al. (1997) Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 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
  • 23
    • 0242582865 scopus 로고    scopus 로고
    • Hydrogen peroxide signaling through tumor necrosis factor receptor 1 leads to selective activation of c-Jun N-terminal kinase
    • Pantano C, Shrivastava P, McElhinney B, Janssen-Heininger Y, (2003) Hydrogen peroxide signaling through tumor necrosis factor receptor 1 leads to selective activation of c-Jun N-terminal kinase. J Biol Chem 278: 44091-44096.
    • (2003) J Biol Chem , vol.278 , pp. 44091-44096
    • Pantano, C.1    Shrivastava, P.2    McElhinney, B.3    Janssen-Heininger, Y.4
  • 24
    • 13244249801 scopus 로고    scopus 로고
    • Iron-mediated H2O2 production as a mechanism for cell type-specific inhibition of tumor necrosis factor alpha-induced but not interleukin-1beta-induced IkappaB kinase complex/nuclear factor-kappaB activation
    • Panopoulos A, Harraz M, Engelhardt JF, Zandi E, (2005) Iron-mediated H2O2 production as a mechanism for cell type-specific inhibition of tumor necrosis factor alpha-induced but not interleukin-1beta-induced IkappaB kinase complex/nuclear factor-kappaB activation. J Biol Chem 280: 2912-2923.
    • (2005) J Biol Chem , vol.280 , pp. 2912-2923
    • Panopoulos, A.1    Harraz, M.2    Engelhardt, J.F.3    Zandi, E.4
  • 25
    • 43449105876 scopus 로고    scopus 로고
    • Reactive oxygen species-dependent HSP90 protein cleavage participates in arsenical As(+3)- and MMA(+3)-induced apoptosis through inhibition of telomerase activity via JNK activation
    • Shen SC, Yang LY, Lin HY, Wu CY, Su TH, et al. (2008) Reactive oxygen species-dependent HSP90 protein cleavage participates in arsenical As(+3)- and MMA(+3)-induced apoptosis through inhibition of telomerase activity via JNK activation. Toxicol Appl Pharmacol 229: 239-251.
    • (2008) Toxicol Appl Pharmacol , vol.229 , pp. 239-251
    • Shen, S.C.1    Yang, L.Y.2    Lin, H.Y.3    Wu, C.Y.4    Su, T.H.5
  • 26
    • 0026740508 scopus 로고
    • Biologically relevant metal ion-dependent hydroxyl radical generation. An update
    • Halliwell B, Gutteridge JM, (1992) Biologically relevant metal ion-generation. An update. FEBS Lett 307: 108-112.
    • (1992) FEBS Lett , vol.307 , pp. 108-112
    • Halliwell, B.1    Gutteridge, J.M.2
  • 27
    • 0036510547 scopus 로고    scopus 로고
    • A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket
    • Soti C, Racz A, Csermely P, (2002) A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket. J Biol Chem 277: 7066-7075.
    • (2002) J Biol Chem , vol.277 , pp. 7066-7075
    • Soti, C.1    Racz, A.2    Csermely, P.3
  • 28
    • 0038730655 scopus 로고    scopus 로고
    • Comparative analysis of the ATP-binding sites of Hsp90 by nucleotide affinity cleavage: a distinct nucleotide specificity of the C-terminal ATP-binding site
    • Soti C, Vermes A, Haystead TA, Csermely P, (2003) Comparative analysis of the ATP-binding sites of Hsp90 by nucleotide affinity cleavage: a distinct nucleotide specificity of the C-terminal ATP-binding site. Eur J Biochem 270: 2421-2428.
    • (2003) Eur J Biochem , vol.270 , pp. 2421-2428
    • Soti, C.1    Vermes, A.2    Haystead, T.A.3    Csermely, P.4
  • 29
    • 0001608033 scopus 로고
    • Formation constants for the complexes of adenosine di- or tri-phosphate with magnesium or calcium ions
    • Burton K, (1959) Formation constants for the complexes of adenosine di- or tri-phosphate with magnesium or calcium ions. Biochem J 71: 388-395.
    • (1959) Biochem J , vol.71 , pp. 388-395
    • Burton, K.1
  • 30
    • 0141560781 scopus 로고
    • Compounds of Ferric Iron with Adenosine Triphosphate and Other Nucleoside Phosphates
    • Goucher CR, Taylor JF, (1964) Compounds of Ferric Iron with Adenosine Triphosphate and Other Nucleoside Phosphates. J Biol Chem 239: 2251-2255.
    • (1964) J Biol Chem , vol.239 , pp. 2251-2255
    • Goucher, C.R.1    Taylor, J.F.2
  • 31
    • 0021045327 scopus 로고
    • On the cytotoxicity of vitamin C and metal ions. A site-specific Fenton mechanism
    • Samuni A, Aronovitch J, Godinger D, Chevion M, Czapski G, (1983) On the cytotoxicity of vitamin C and metal ions. A site-specific Fenton mechanism. Eur J Biochem 137: 119-124.
    • (1983) Eur J Biochem , vol.137 , pp. 119-124
    • Samuni, A.1    Aronovitch, J.2    Godinger, D.3    Chevion, M.4    Czapski, G.5
  • 32
    • 0030987132 scopus 로고    scopus 로고
    • An atypical topoisomerase II from Archaea with implications for meiotic recombination
    • Bergerat A, de Massy B, Gadelle D, Varoutas PC, Nicolas A, et al. (1997) An atypical topoisomerase II from Archaea with implications for meiotic recombination. Nature 386: 414-417.
    • (1997) Nature , vol.386 , pp. 414-417
    • Bergerat, A.1    de Massy, B.2    Gadelle, D.3    Varoutas, P.C.4    Nicolas, A.5
  • 33
    • 0023338482 scopus 로고
    • Ferrous-salt-promoted damage to deoxyribose and benzoate. The increased effectiveness of hydroxyl-radical scavengers in the presence of EDTA
    • Gutteridge JM, (1987) Ferrous-salt-promoted damage to deoxyribose and benzoate. The increased effectiveness of hydroxyl-radical scavengers in the presence of EDTA. Biochem J 243: 709-714.
    • (1987) Biochem J , vol.243 , pp. 709-714
    • Gutteridge, J.M.1
  • 34
    • 67650071137 scopus 로고    scopus 로고
    • Targeting cancer cells by ROS-mediated mechanisms: a radical therapeutic approach?
    • Trachootham D, Alexandre J, Huang P, (2009) Targeting cancer cells by ROS-mediated mechanisms: a radical therapeutic approach? Nat Rev Drug Discov 8: 579-591.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 579-591
    • Trachootham, D.1    Alexandre, J.2    Huang, P.3
  • 35
    • 70449107252 scopus 로고    scopus 로고
    • Redox-directed cancer therapeutics: molecular mechanisms and opportunities
    • Wondrak GT, (2009) Redox-directed cancer therapeutics: molecular mechanisms and opportunities. Antioxid Redox Signal 11: 3013-3069.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 3013-3069
    • Wondrak, G.T.1
  • 36
    • 80555144320 scopus 로고    scopus 로고
    • Cytotoxic effects of Mn(III) N-alkylpyridylporphyrins in the presence of cellular reductant, ascorbate
    • Ye X, Fels D, Tovmasyan A, Aird KM, Dedeugd C, et al. (2011) Cytotoxic effects of Mn(III) N-alkylpyridylporphyrins in the presence of cellular reductant, ascorbate. Free Radic Res 45: 1289-1306.
    • (2011) Free Radic Res , vol.45 , pp. 1289-1306
    • Ye, X.1    Fels, D.2    Tovmasyan, A.3    Aird, K.M.4    Dedeugd, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.