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Volumn 52, Issue 4, 2008, Pages 221-228

Upon oxidative stress, the antiapoptotic Hsp60/procaspase-3 complex persists in mucoepidermoid carcinoma cells

Author keywords

Apoptosis; Chaperonin; Cpn60; DNA damage; Hsp60; P53; Procaspase 3 caspase 3

Indexed keywords

DNA; HEAT SHOCK PROTEIN 60; HYDROGEN PEROXIDE; PROCASPASE 3; PROTEIN P21; PROTEIN P53; TRYPTOPHAN; CASPASE 3; CHAPERONIN; FORMAZAN; MTT FORMAZAN; TETRAZOLIUM; TRYPAN BLUE; UNCLASSIFIED DRUG;

EID: 59849125903     PISSN: 1121760X     EISSN: None     Source Type: Journal    
DOI: 10.4081/1220     Document Type: Article
Times cited : (50)

References (46)
  • 1
    • 38449100535 scopus 로고    scopus 로고
    • Extracellular heat shock proteins in cell signaling and immunity
    • Calderwood SK, Mambula SS, Gray PJ Jr. Extracellular heat shock proteins in cell signaling and immunity. Ann N Y Acad Sci 2007;1113:28-39.
    • (2007) Ann N Y Acad Sci , vol.1113 , pp. 28-39
    • Calderwood, S.K.1    Mambula, S.S.2    Gray Jr., P.J.3
  • 4
    • 0037900829 scopus 로고    scopus 로고
    • Immunohistochemical evaluation of PCNA, p53, HSP60, HSP10 and MUC-2 presence and expression in prostate carcinogenesis
    • Cappello F, Rappa F, David S, Anzalone R, Zummo G. Immunohistochemical evaluation of PCNA, p53, HSP60, HSP10 and MUC-2 presence and expression in prostate carcinogenesis. Anticancer Res 2003(b);23:1325-1331
    • (2003) Anticancer Res , vol.23 , pp. 1325-1331
    • Cappello, F.1    Rappa, F.2    David, S.3    Anzalone, R.4    Zummo, G.5
  • 7
    • 56149106877 scopus 로고    scopus 로고
    • Hsp60 expression, new locations, functions and perspectives for cancer diagnosis and therapy
    • Cappello F, Conway de Macario E, Marasà L, Zummo G, Macario AJL. Hsp60 expression, new locations, functions, and perspectives for cancer diagnosis and therapy. Cancer Biol Ther 2008;7:801-809 (Pubitemid 351948804)
    • (2008) Cancer Biology and Therapy , vol.7 , Issue.6 , pp. 619-627
    • Cappello, F.1    De Macario, E.C.2    Marasa, L.3    Zummo, G.4    Macario, A.J.L.5
  • 8
    • 35748929414 scopus 로고    scopus 로고
    • Cytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release: Evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase-3
    • DOI 10.1074/jbc.M702777200
    • Chandra D, Choy G, Tang DG. Cytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release: evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase-3. J Biol Chem 2007;282:31289-31301 (Pubitemid 350044883)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.43 , pp. 31289-31301
    • Chandra, D.1    Choy, G.2    Tang, D.G.3
  • 9
    • 33751170698 scopus 로고    scopus 로고
    • Mitochondrial chaperones in cancer: From molecular biology to clinical diagnostics
    • Czarnecka AM, Campanella C, Zummo G, Cappello F. Mitochondrial chaperones in cancer: from molecular biology to clinical diagnostics. Cancer Biol Ther 2006;5:714-720 (Pubitemid 44775122)
    • (2006) Cancer Biology and Therapy , vol.5 , Issue.7 , pp. 714-720
    • Czarnecka, A.M.1    Campanella, C.2    Zummo, G.3    Cappello, F.4
  • 10
    • 0025382818 scopus 로고
    • The molecular chaperone concept
    • Ellis RJ. The molecular chaperone concept. Semin Cell Biol 1990;1:1-9.
    • (1990) Semin Cell Biol , vol.1 , pp. 1-9
    • Ellis, R.J.1
  • 11
    • 30844452690 scopus 로고    scopus 로고
    • Immunohistochemical analysis of P57(kip2), p53 and hsp60 expressions in premalignant and malignant oral tissues
    • DOI 10.1016/j.oraloncology.2005.06.017, PII S1368837505002010
    • Fan GK, Chen J, Ping F, Geng Y. Immunohistochemical analysis of P57(kip2), p53 and hsp60 expressions in premalignant and malignant oral tissues. Oral Oncol 2006;42:147-153 (Pubitemid 43106879)
    • (2006) Oral Oncology , vol.42 , Issue.2 , pp. 147-153
    • Fan, G.-K.1    Chen, J.2    Ping, F.3    Geng, Y.4
  • 12
    • 0037154980 scopus 로고    scopus 로고
    • Protein folding and unfolding at atomic resolution
    • DOI 10.1016/S0092-8674(02)00620-7
    • Fersht AR, Daggett V. Protein folding and unfolding at atomic resolution. Cell 2002;108:573-582 (Pubitemid 34260881)
    • (2002) Cell , vol.108 , Issue.4 , pp. 573-582
    • Fersht, A.R.1    Daggett, V.2
  • 13
    • 2942569101 scopus 로고    scopus 로고
    • Oxidative and osmotic stress signaling in tumor cells is mediated by ADAM proteases and heparin-binding epidermal growth factor
    • DOI 10.1128/MCB.24.12.5172-5183.2004
    • Fischer OM, Hart S, Gschwind A, Prenzel N, Ullrich A. Oxidative and osmotic stress signaling in tumor cells is mediated by ADAM pro teases and heparin-binding epidermal growth factor. Mol Cel Biol 2004;24:5172-5183 (Pubitemid 38738154)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.12 , pp. 5172-5183
    • Fischer, O.M.1    Hart, S.2    Gschwind, A.3    Prenzel, N.4    Ullrich, A.5
  • 15
    • 0141569311 scopus 로고    scopus 로고
    • Adaptive responses to the stress induced by hyperthermia or hydrogen peroxide in human fibroblasts
    • Grasso S, Scifo C, Cardile V, Gulino R, Renis M. Adaptive responses to the stress induced by hyperthermia or hydrogen peroxide in human fibroblasts. Exp Biol Med 2003;228:491-498 (Pubitemid 37203666)
    • (2003) Experimental Biology and Medicine , vol.228 , Issue.5 , pp. 491-498
    • Grasso, S.1    Scifo, C.2    Cardile, V.3    Gulino, R.4    Renis, M.5
  • 16
    • 17144421593 scopus 로고    scopus 로고
    • HSP60, Bax, apoptosis and the heart
    • Gupta S, Knowlton AA. HSP60, Bax, apoptosis and the heart. J Cell Mol Med 2005;9:51-58
    • (2005) J Cell Mol Med , vol.9 , pp. 51-58
    • Gupta, S.1    Knowlton, A.A.2
  • 18
    • 0242719924 scopus 로고    scopus 로고
    • Appraisal of the MTT-based assay as a useful tool for predicting drug chemosensitivity in leukemia
    • DOI 10.1080/1042819031000116607
    • Hayon T, Dvilansky A, Shpilberg O, Nathan I. Appraisal of the MTT-based assay as a useful tool for predicting drug chemosensitivity in leukemia. Leuk Lymphoma 2003;44:1957-1962 (Pubitemid 37369631)
    • (2003) Leukemia and Lymphoma , vol.44 , Issue.11 , pp. 1957-1962
    • Hayon, T.1    Dvilansky, A.2    Shpilberg, O.3    Nathan, I.4
  • 20
    • 0029062216 scopus 로고
    • The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol
    • Kubota H, Hynes G, Willison K. The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol. Eur J Biochem 1995;230:3-16.
    • (1995) Eur J Biochem , vol.230 , pp. 3-16
    • Kubota, H.1    Hynes, G.2    Willison, K.3
  • 21
    • 0018348655 scopus 로고
    • T antigen is bound to a host protein in SV40-transformed cells
    • Lane DP, Crawford LV. T antigen is bound to a host protein in SV40-transformed cells. Nature 1979; 278:261-263
    • (1979) Nature , vol.278 , pp. 261-263
    • Lane, D.P.1    Crawford, L.V.2
  • 22
    • 0037010181 scopus 로고    scopus 로고
    • Type I chaperonins: Not all are created equal
    • DOI 10.1016/S0014-5793(02)03178-2, PII S0014579302031782
    • Levy-Rimler G, Bell RE, Ben-Tal N, Azem A. Type I chaperonins: not all are created equal. FEBS Lett 2002;529:1-5. (Pubitemid 35283902)
    • (2002) FEBS Letters , vol.529 , Issue.1 , pp. 1-5
    • Levy-Rimler, G.1    Bell, R.E.2    Ben-Tal, N.3    Azem, A.4
  • 24
    • 2442718034 scopus 로고    scopus 로고
    • Evolution of assisted protein folding: The distribution of the main chaperoning systems within the phylogenetic domain Archaea
    • d1000-1499
    • Macario AJL, Malz M, Conway de Macario E. Evolution of assisted protein folding: the distribution of the main chaperoning systems within the phylogenetic domain archaea. Front Biosci 2004;9:1318-1332 (Pubitemid 39060845)
    • (2004) Frontiers in Bioscience , vol.9 , pp. 1318-1332
    • Macario, A.J.L.1    Malz, M.2    Conway De Macario, E.3
  • 25
    • 0034717014 scopus 로고    scopus 로고
    • Death signal-induced localization of p53 protein to mitochondria
    • Marchenko ND, Zaika A, Moll UM. Death signal-induced localization of p53 protein to mitochondria. J Biol Chem 2000;275:16202-16212
    • (2000) J Biol Chem , vol.275 , pp. 16202-16212
    • Marchenko, N.D.1    Zaika, A.2    Moll, U.M.3
  • 27
    • 0032884582 scopus 로고    scopus 로고
    • A single-ring mitochondrial chaperonin (Hsp60-Hsp10) can substitute for GroEL-GroES in vivo
    • Nielsen KL, McLennan N, Masters M, Cowan NJ. A single-ring mitochondrial chaperonin (Hsp60-Hsp10) can substitute for GroEL-GroES in vivo. J Bacteriol 1999; 181:5871-5875 (Pubitemid 29437165)
    • (1999) Journal of Bacteriology , vol.181 , Issue.18 , pp. 5871-5875
    • Nielsen, K.L.1    McLennan, N.2    Masters, M.3    Cowan, N.J.4
  • 29
    • 0030597971 scopus 로고    scopus 로고
    • Nuclear DNA strand breaks during ethanol-induced oxidative stress in rat brain
    • DOI 10.1016/0014-5793(96)00647-3
    • Renis M, Calabrese V, Russo A, Calderone A, Barcellona ML, Rizza V. Nuclear DNA strand breaks during ethanol-induced oxidative stress in rat brain. FEBS Lett 1996;390:153-156 (Pubitemid 26281190)
    • (1996) FEBS Letters , vol.390 , Issue.2 , pp. 153-156
    • Renis, M.1    Calabrese, V.2    Russo, A.3    Calderone, A.4    Barcellona, M.L.5    Rizza, V.6
  • 30
    • 0030154255 scopus 로고    scopus 로고
    • Discovery of the heat shock response
    • Ritossa F. Discovery of the heat shock response. Cell Stress Chaperones 1996;1:97-98
    • (1996) Cell Stress Chaperones , vol.1 , pp. 97-98
    • Ritossa, F.1
  • 31
    • 0035370483 scopus 로고    scopus 로고
    • Regulation and function of the p53 tumor suppressor protein
    • DOI 10.1016/S0955-0674(00)00216-7
    • Ryan KK, Philips AC, Vousden KH. Regulation and function of the p53 tumor supressor protein. Current Opin Cell Biol 2001;13:332-337 (Pubitemid 32429498)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.3 , pp. 332-337
    • Ryan, K.M.1    Phillips, A.C.2    Vousden, K.H.3
  • 32
    • 0033561295 scopus 로고    scopus 로고
    • Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of Jurkat cells
    • Samali A, Cai J, Zhivotovsky B, Jones DP, Orrenius S. Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of Jurkat cells. EMBO J 1999;18:2040-2048
    • (1999) EMBO J , vol.18 , pp. 2040-2048
    • Samali, A.1    Cai, J.2    Zhivotovsky, B.3    Jones, D.P.4    Orrenius, S.5
  • 33
    • 0035910385 scopus 로고    scopus 로고
    • Hypoxia death stimulus induces translocation of p53 protein to mitochondria. Detection by immunofluorescence on whole cells
    • Sansome C, Zaika A, Marchenko ND, Moll UM. Hypoxia death stimulus induces translocation of p53 protein to mitochondria. Detection by immunofluorescence on whole cells. FEBS Lett 2001;488:110-115
    • (2001) FEBS Lett , vol.488 , pp. 110-115
    • Sansome, C.1    Zaika, A.2    Marchenko, N.D.3    Moll, U.M.4
  • 34
    • 0344631749 scopus 로고    scopus 로고
    • Immunohistochemical detection of HSP60-expression in human ovarian cancer. Correlation with survival in a series of 247 patients
    • Schneider J, Jiménez E, Marenbach K, Romero H, Marx D, Meden H. Immunohistochemical detection of HSP60-expression in human ovarian cancer. Correlation with survival in a series of 247 patients. Anticancer Res 1999;19:2141-2146
    • (1999) Anticancer Res , vol.19 , pp. 2141-2146
    • Schneider, J.1    Jiménez, E.2    Marenbach, K.3    Romero, H.4    Marx, D.5    Meden, H.6
  • 35
    • 0023919963 scopus 로고
    • A simple technique for quantitation of low levels of DNA damage in individual cells
    • Singh NP, McCoy MT, Tice RR, Schneider EL. A simple technique for quantitation of low levels of DNA damage in individual cells. Exp Cell Res 1988;175:184-191
    • (1988) Exp Cell Res , vol.175 , pp. 184-191
    • Singh, N.P.1    McCoy, M.T.2    Tice, R.R.3    Schneider, E.L.4
  • 36
    • 0030023858 scopus 로고    scopus 로고
    • Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (HSP60) in mammalian cells
    • Soltys BJ, Gupta RS. Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (HSP60) in mammalian cells. Exp Cell Res 1996;222:16-27.
    • (1996) Exp Cell Res , vol.222 , pp. 16-27
    • Soltys, B.J.1    Gupta, R.S.2
  • 37
    • 0031147756 scopus 로고    scopus 로고
    • Cell surface localization of the 60 kDa heat shock chaperonin protein (HSP60) in mammalian cells
    • Soltys BJ, Gupta RS. Cell surface localization of the 60 kDa heat shock chaperonin protein (HSP60) in mammalian cells. Cell Biol Int 1997;21:315-320
    • (1997) Cell Biol Int , vol.21 , pp. 315-320
    • Soltys, B.J.1    Gupta, R.S.2
  • 38
    • 0033133729 scopus 로고    scopus 로고
    • Mitochondrial-matrix proteins at unexpected locations: Are they exported?
    • Soltys BJ, Gupta RS. Mitochondrial-matrix proteins at unexpected locations: are they exported? Trends Biochem Sci 1999;24:174-177
    • (1999) Trends Biochem Sci , vol.24 , pp. 174-177
    • Soltys, B.J.1    Gupta, R.S.2
  • 39
    • 51149102710 scopus 로고    scopus 로고
    • Trypan blue exclusion test of cell viability
    • Appendix 3:Appendix 3B
    • Strober W. Trypan blue exclusion test of cell viability. Curr Protoc Immunol 2001; Appendix 3:Appendix 3B.
    • (2001) Curr Protoc Immunol
    • Strober, W.1
  • 41
    • 0029043888 scopus 로고
    • A novel assay for apoptosis: Flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V
    • Vermes I, Haanen C, Steffens-Nakken H, Reutelingsperger C. A novel assay for apoptosis: flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V. J Immunol Methods 1995;184:39-51.
    • (1995) J Immunol Methods , vol.184 , pp. 39-51
    • Vermes, I.1    Haanen, C.2    Steffens-Nakken, H.3    Reutelingsperger, C.4
  • 42
    • 33749543406 scopus 로고    scopus 로고
    • Differential effects of mitochondrial heat shock protein 60 and related molecular chaperones to prevent intracellular beta-amyloid-induced inhibition of complex IV and limit apoptosis
    • DOI 10.1074/jbc.M602533200
    • Veereshwarayya V, Kumar P, Rosen KM, Mestril R, Querfurth HW. Differential effects of mitochondrial heat shock protein 60 and related molecular chaperones to prevent intracellular beta-amyloid-induced inhibition of complex IV and limit apoptosis. J Biol Chem 2006;281:29468-29478 (Pubitemid 44536955)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.40 , pp. 29468-29478
    • Veereshwarayya, V.1    Kumar, P.2    Rosen, K.M.3    Mestril, R.4    Querfurth, H.W.5
  • 43
    • 0037007283 scopus 로고    scopus 로고
    • Molecular chaperones - Cellular machines for protein folding
    • Walter S, Buchner J. Molecular chaperones-cellular machines for protein folding. Angew Chem Int Ed Engl 2002;241:1098-1113 (Pubitemid 34406944)
    • (2002) Angewandte Chemie - International Edition , vol.41 , Issue.7 , pp. 1099-1113
    • Walter, S.1    Buchner, J.2
  • 44
    • 0030049032 scopus 로고    scopus 로고
    • Damage to DNA by reactive oxygen and nitrogen species: Role in inflammatory disease and progression to cancer
    • Wiseman H, Halliwell B. Damage to DNA by reactive oxygen and nitrogen species: role in inflammatory disease and progression to cancer. Biochem J 1996;313:17-29. (Pubitemid 26013419)
    • (1996) Biochemical Journal , vol.313 , Issue.1 , pp. 17-29
    • Wiseman, H.1    Halliwell, B.2


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