메뉴 건너뛰기




Volumn 313, Issue 1, 2003, Pages 147-157

Bcl-2 and Bcl-xL overexpression inhibits cytochrome c release, activation of multiple caspases, and virus release following coxsackievirus B3 infection

Author keywords

Apoptosis; Bcl 2; Bcl xL; Caspase; Coxsackievirus B3; Cytochrome c; Myocarditis

Indexed keywords

BENZYLOXYCARBONYLVALYLALANYLASPARTYL FLUOROMETHYL KETONE; CASPASE; CASPASE 2; CASPASE 3; CASPASE 6; CASPASE 7; CASPASE 8; CASPASE 9; CYTOCHROME C; EPITOPE; PROTEIN BCL 2; PROTEIN BCL XL; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; VIRUS ENZYME; VIRUS PROTEIN;

EID: 0041887188     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0042-6822(03)00242-3     Document Type: Article
Times cited : (107)

References (60)
  • 1
    • 0029890234 scopus 로고    scopus 로고
    • Direct interactions of coxsackievirus B3 with immune cells in the splenic compartment of mice susceptible or resistant to myocarditis
    • Anderson D.R., Wilson J.E., Carthy C.M., Yang D., Kandolf R., McManus B.M. Direct interactions of coxsackievirus B3 with immune cells in the splenic compartment of mice susceptible or resistant to myocarditis. J. Virol. 70:1996;4632-4645.
    • (1996) J. Virol. , vol.70 , pp. 4632-4645
    • Anderson, D.R.1    Wilson, J.E.2    Carthy, C.M.3    Yang, D.4    Kandolf, R.5    McManus, B.M.6
  • 2
    • 0034646690 scopus 로고    scopus 로고
    • Enteroviral protease 2A directly cleaves dystrophin and is inhibited by a dystrophin-based substrate analogue
    • Badorff C., Berkely N., Mehrotra S., Talhouk J.W., Rhoads R.E., Knowlton K.U. Enteroviral protease 2A directly cleaves dystrophin and is inhibited by a dystrophin-based substrate analogue. J. Biol. Chem. 275:2000;11191-11197.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11191-11197
    • Badorff, C.1    Berkely, N.2    Mehrotra, S.3    Talhouk, J.W.4    Rhoads, R.E.5    Knowlton, K.U.6
  • 3
    • 0033918245 scopus 로고    scopus 로고
    • Enteroviral cardiomyopathy: Bad news for the dystrophin-glycoprotein complex
    • Badorff C., Lee G.H., Knowlton K.U. Enteroviral cardiomyopathy bad news for the dystrophin-glycoprotein complex . Herz. 25:2000;227-232.
    • (2000) Herz , vol.25 , pp. 227-232
    • Badorff, C.1    Lee, G.H.2    Knowlton, K.U.3
  • 4
    • 0033017374 scopus 로고    scopus 로고
    • Enteroviral protease 2A cleaves dystrophin: Evidence of cytoskeletal disruption in an acquired cardiomyopathy
    • Badorff C., Lee G.H., Lamphear B.J., Martone M.E., Campbell K.P., Rhoads R.E., Knowlton K.U. Enteroviral protease 2A cleaves dystrophin evidence of cytoskeletal disruption in an acquired cardiomyopathy . Nat. Med. 5:1999;320-326.
    • (1999) Nat. Med. , vol.5 , pp. 320-326
    • Badorff, C.1    Lee, G.H.2    Lamphear, B.J.3    Martone, M.E.4    Campbell, K.P.5    Rhoads, R.E.6    Knowlton, K.U.7
  • 5
    • 0033580901 scopus 로고    scopus 로고
    • Caspases induce cytochrome c release from mitochondria by activating cytosolic factors
    • Bossy-Wetzel E., Green D.R. Caspases induce cytochrome c release from mitochondria by activating cytosolic factors. J. Biol. Chem. 274:1999;17484-17490.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17484-17490
    • Bossy-Wetzel, E.1    Green, D.R.2
  • 7
    • 0027535652 scopus 로고
    • Direct cleavage of human TATA-binding protein by poliovirus protease 3C in vivo and in vitro
    • Clark M.E., Lieberman P.M., Berk A.J., Dasgupta A. Direct cleavage of human TATA-binding protein by poliovirus protease 3C in vivo and in vitro. Mol. Cell. Biol. 13:1993;1232-1237.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1232-1237
    • Clark, M.E.1    Lieberman, P.M.2    Berk, A.J.3    Dasgupta, A.4
  • 9
    • 0033936787 scopus 로고    scopus 로고
    • Bax, Bid and the permeabilization of the mitochondrial outer membrane in apoptosis
    • Crompton M. Bax, Bid and the permeabilization of the mitochondrial outer membrane in apoptosis. Curr. Opin. Cell. Biol. 12:2000;414-419.
    • (2000) Curr. Opin. Cell. Biol. , vol.12 , pp. 414-419
    • Crompton, M.1
  • 11
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C., Fang M., Li Y., Li L., Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell. 102:2000;33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 12
    • 0008899802 scopus 로고
    • Cytopathology of virus infections
    • Enders J.F. Cytopathology of virus infections. Ann. Rev. Microbiol. 8:1954;473-502.
    • (1954) Ann. Rev. Microbiol. , vol.8 , pp. 473-502
    • Enders, J.F.1
  • 13
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
    • Eskes R., Desagher S., Antonsson B., Martinou J.C. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol. Cell Biol. 20:2000;929-935.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 929-935
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.C.4
  • 14
    • 0020356106 scopus 로고
    • Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220,000-dalton polypeptide associated with eucaryotic initiation factor 3 and a cap binding protein complex
    • Etchison D., Milburn S.C., Edery I., Sonenberg N., Hershey J.W. Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220,000-dalton polypeptide associated with eucaryotic initiation factor 3 and a cap binding protein complex. J. Biol. Chem. 257:1982;14806-14810.
    • (1982) J. Biol. Chem. , vol.257 , pp. 14806-14810
    • Etchison, D.1    Milburn, S.C.2    Edery, I.3    Sonenberg, N.4    Hershey, J.W.5
  • 15
    • 0343217078 scopus 로고
    • Expression of membrane interleukin 1 by fibroblasts transfected with murine pro-interleukin 1 alpha cDNA
    • Fuhlbrigge R.C., Fine S.M., Unanue E.R., Chaplin D.D. Expression of membrane interleukin 1 by fibroblasts transfected with murine pro-interleukin 1 alpha cDNA. Proc. Natl. Acad. Sci. USA. 85:1988;5649-5653.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5649-5653
    • Fuhlbrigge, R.C.1    Fine, S.M.2    Unanue, E.R.3    Chaplin, D.D.4
  • 17
    • 0001583837 scopus 로고    scopus 로고
    • Photodynamic therapy induces caspase-3 activation in HL-60 cells
    • Granville D.J., Levy J.G., Hunt D.W. Photodynamic therapy induces caspase-3 activation in HL-60 cells. Cell Death Differ. 4:1997;623-629.
    • (1997) Cell Death Differ. , vol.4 , pp. 623-629
    • Granville, D.J.1    Levy, J.G.2    Hunt, D.W.3
  • 20
    • 0031060175 scopus 로고    scopus 로고
    • Tyrosine phosphorylation events during coxsackievirus B3 replication
    • Huber M., Selinka H.C., Kandolf R. Tyrosine phosphorylation events during coxsackievirus B3 replication. J. Virol. 71:1997;595-600.
    • (1997) J. Virol. , vol.71 , pp. 595-600
    • Huber, M.1    Selinka, H.C.2    Kandolf, R.3
  • 21
    • 0031754123 scopus 로고    scopus 로고
    • Visualization of enteroviral replication in myocardial tissue by ultrastructural in situ hybridization: Identification of target cells and cytopathic effects
    • Klingel K., Rieger P., Mall G., Selinka H.C., Huber M., Kandolf R. Visualization of enteroviral replication in myocardial tissue by ultrastructural in situ hybridization identification of target cells and cytopathic effects . Lab. Invest. 78:1998;1227-1237.
    • (1998) Lab. Invest. , vol.78 , pp. 1227-1237
    • Klingel, K.1    Rieger, P.2    Mall, G.3    Selinka, H.C.4    Huber, M.5    Kandolf, R.6
  • 22
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck R.M., Bossy-Wetzel E., Green D.R., Newmeyer D.D. The release of cytochrome c from mitochondria a primary site for Bcl-2 regulation of apoptosis . Science. 275:1997;1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 23
    • 0037162833 scopus 로고    scopus 로고
    • Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization
    • Lassus P., Opitz-Araya X., Lazebnik Y. Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization. Science. 297:2002;1352-1354.
    • (2002) Science , vol.297 , pp. 1352-1354
    • Lassus, P.1    Opitz-Araya, X.2    Lazebnik, Y.3
  • 24
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • Li L.Y., Luo X., Wang X. Endonuclease G is an apoptotic DNase when released from mitochondria. Nature. 412:2001;95-99.
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 25
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P., Nijhawan D., Budihardjo I., Srinivasula S.M., Ahmad M., Alnemri E.S., Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell. 91:1997;479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 27
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H., Zhu H., Xu C.J., Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell. 94:1998;491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 28
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X., Kim C.N., Yang J., Jemmerson R., Wang Z. Induction of apoptotic program in cell-free extracts requirement for dATP and cytochrome c . Cell. 86:1996;147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, Z.5
  • 29
    • 0032502855 scopus 로고    scopus 로고
    • Activation of caspases triggered by cytochrome c in vitro
    • Pan G., Humke E.W., Dixit V.M. Activation of caspases triggered by cytochrome c in vitro. FEBS Lett. 426:1998;151-154.
    • (1998) FEBS Lett. , vol.426 , pp. 151-154
    • Pan, G.1    Humke, E.W.2    Dixit, V.M.3
  • 30
    • 0036308059 scopus 로고    scopus 로고
    • Mitochondria, the killer organelles and their weapons
    • Ravagnan L., Roumier T., Kroemer G. Mitochondria, the killer organelles and their weapons. J. Cell. Physiol. 192:2002;131-137.
    • (2002) J. Cell. Physiol. , vol.192 , pp. 131-137
    • Ravagnan, L.1    Roumier, T.2    Kroemer, G.3
  • 33
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival application to proliferation and cytotoxicity assays . J. Immunol. Methods. 57:1983;55-60.
    • (1983) J. Immunol. Methods , vol.57 , pp. 55-60
    • Mosmann, T.1
  • 37
    • 0034733665 scopus 로고    scopus 로고
    • 2A proteinase of human rhinovirus cleaves cytokeratin 8 in infected HeLa cells
    • Seipelt J., Liebig H.D., Sommergruber W., Gerner C., Kuechler E. 2A proteinase of human rhinovirus cleaves cytokeratin 8 in infected HeLa cells. J. Biol. Chem. 275:2000;20084-20089.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20084-20089
    • Seipelt, J.1    Liebig, H.D.2    Sommergruber, W.3    Gerner, C.4    Kuechler, E.5
  • 41
    • 0034785591 scopus 로고    scopus 로고
    • A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death
    • Suzuki Y., Imai Y., Nakayama H., Takahashi K., Takio K., Takahashi R. A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Mol. Cell. 8:2001;613-621.
    • (2001) Mol. Cell. , vol.8 , pp. 613-621
    • Suzuki, Y.1    Imai, Y.2    Nakayama, H.3    Takahashi, K.4    Takio, K.5    Takahashi, R.6
  • 44
    • 0031041172 scopus 로고    scopus 로고
    • Regulation of apoptosis by viral gene products
    • Teodoro J., Branton P. Regulation of apoptosis by viral gene products. J. Virol. 71:1997;1739-1746.
    • (1997) J. Virol. , vol.71 , pp. 1739-1746
    • Teodoro, J.1    Branton, P.2
  • 45
    • 0033971901 scopus 로고    scopus 로고
    • Bcl-2 family: Life-or-death switch
    • Tsujimoto Y., Shimizu S. Bcl-2 family life-or-death switch . FEBS Lett. 466:2000;6-10.
    • (2000) FEBS Lett. , vol.466 , pp. 6-10
    • Tsujimoto, Y.1    Shimizu, S.2
  • 46
    • 0030998947 scopus 로고    scopus 로고
    • Intracellular viral localization in murine coxsackievirus-B3 myocarditis. Ultrastructural study by electron microscopic in situ hybridization
    • Ukimura A., Deguchi H., Kitaura Y., Fujioka S., Hirasawa M., Kawamura K., Hirai K. Intracellular viral localization in murine coxsackievirus-B3 myocarditis. Ultrastructural study by electron microscopic in situ hybridization. Am. J. Pathol. 150:1997;2061-2074.
    • (1997) Am. J. Pathol. , vol.150 , pp. 2061-2074
    • Ukimura, A.1    Deguchi, H.2    Kitaura, Y.3    Fujioka, S.4    Hirasawa, M.5    Kawamura, K.6    Hirai, K.7
  • 47
    • 0030928285 scopus 로고    scopus 로고
    • Coxsackievirus protein 2B modifies endoplasmic reticulum membrane and plasma membrane permeability and facilitates virus release
    • van Kuppeveld F.J., Hoenderop J.G., Smeets R.L., Willems P.H., Dijkman H.B., Galama J.M., Melchers W.J. Coxsackievirus protein 2B modifies endoplasmic reticulum membrane and plasma membrane permeability and facilitates virus release. EMBO J. 16:1997;3519-3532.
    • (1997) EMBO J. , vol.16 , pp. 3519-3532
    • Van Kuppeveld, F.J.1    Hoenderop, J.G.2    Smeets, R.L.3    Willems, P.H.4    Dijkman, H.B.5    Galama, J.M.6    Melchers, W.J.7
  • 51
    • 0034605121 scopus 로고    scopus 로고
    • Preservation of mitochondrial structure and function after Bid- or Bax-mediated cytochrome c release
    • von Ahsen O., Renken C., Perkins G., Kluck R.M., Bossy-Wetzel E., Newmeyer D.D. Preservation of mitochondrial structure and function after Bid- or Bax-mediated cytochrome c release. J. Cell. Biol. 150:2000;1027-1036.
    • (2000) J. Cell. Biol. , vol.150 , pp. 1027-1036
    • Von Ahsen, O.1    Renken, C.2    Perkins, G.3    Kluck, R.M.4    Bossy-Wetzel, E.5    Newmeyer, D.D.6
  • 52
    • 0027336114 scopus 로고
    • Ionophoric interaction with the myocyte sarcolemma: A new insight into the pathophysiology of degenerative myocardial disease
    • Waldenstrom A., Ronquist G., Fohlman J., Gerdin B., Ilback N.G. Ionophoric interaction with the myocyte sarcolemma a new insight into the pathophysiology of degenerative myocardial disease . Scand. J. Infect. Dis. Suppl. 88:1993;131-134.
    • (1993) Scand. J. Infect. Dis. Suppl. , vol.88 , pp. 131-134
    • Waldenstrom, A.1    Ronquist, G.2    Fohlman, J.3    Gerdin, B.4    Ilback, N.G.5
  • 54
    • 0036344498 scopus 로고    scopus 로고
    • Dystrophin deficiency markedly increases enterovirus-induced cardiomyopathy: A genetic predisposition to viral heart disease
    • Xiong D., Lee G.H., Badorff C., Dorner A., Lee S., Wolf P., Knowlton K.U. Dystrophin deficiency markedly increases enterovirus-induced cardiomyopathy a genetic predisposition to viral heart disease . Nat. Med. 8:2002;872-877.
    • (2002) Nat. Med. , vol.8 , pp. 872-877
    • Xiong, D.1    Lee, G.H.2    Badorff, C.3    Dorner, A.4    Lee, S.5    Wolf, P.6    Knowlton, K.U.7
  • 55
    • 0030753160 scopus 로고    scopus 로고
    • Poliovirus-encoded protease 2APro cleaves the TATA-binding protein but does not inhibit host cell RNA polymerase II transcription in vitro
    • Yalamanchili P., Banerjee R., Dasgupta A. Poliovirus-encoded protease 2APro cleaves the TATA-binding protein but does not inhibit host cell RNA polymerase II transcription in vitro. J. Virol. 71:1997;6881-6886.
    • (1997) J. Virol. , vol.71 , pp. 6881-6886
    • Yalamanchili, P.1    Banerjee, R.2    Dasgupta, A.3
  • 56
    • 0031016644 scopus 로고    scopus 로고
    • Inhibition of host cell transcription by poliovirus: Cleavage of transcription factor CREB by poliovirus-encoded protease 3Cpro
    • Yalamanchili P., Datta U., Dasgupta A. Inhibition of host cell transcription by poliovirus cleavage of transcription factor CREB by poliovirus-encoded protease 3Cpro . J. Virol. 71:1997;1220-1226.
    • (1997) J. Virol. , vol.71 , pp. 1220-1226
    • Yalamanchili, P.1    Datta, U.2    Dasgupta, A.3
  • 57
    • 0029925258 scopus 로고    scopus 로고
    • Inhibition of basal transcription by poliovirus: A virus-encoded protease (3Cpro) inhibits formation of TBP-TATA box complex in vitro
    • Yalamanchili P., Harris K., Wimmer E., Dasgupta A. Inhibition of basal transcription by poliovirus a virus-encoded protease (3Cpro) inhibits formation of TBP-TATA box complex in vitro . J. Virol. 70:1996;2922-2929.
    • (1996) J. Virol. , vol.70 , pp. 2922-2929
    • Yalamanchili, P.1    Harris, K.2    Wimmer, E.3    Dasgupta, A.4
  • 58
    • 0031458316 scopus 로고    scopus 로고
    • Cleavage of transcriptional activator Oct-1 by poliovirus encoded protease 3Cpro
    • Yalamanchili P., Weidman K., Dasgupta A. Cleavage of transcriptional activator Oct-1 by poliovirus encoded protease 3Cpro. Virology. 239:1997;176-185.
    • (1997) Virology , vol.239 , pp. 176-185
    • Yalamanchili, P.1    Weidman, K.2    Dasgupta, A.3
  • 59
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang J., Liu X., Bhalla K., et al. Prevention of apoptosis by Bcl-2 release of cytochrome c from mitochondria blocked . Science. 275:1997;1129-1132.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3
  • 60
    • 0030294374 scopus 로고    scopus 로고
    • A mitochondrial membrane protein defined by a novel monoclonal antibody is preferentially detected in apoptotic cells
    • Zhang C., Ao Z., Seth A., Schlossman S.F. A mitochondrial membrane protein defined by a novel monoclonal antibody is preferentially detected in apoptotic cells. J. Immunol. 157:1996;3980-3987.
    • (1996) J. Immunol. , vol.157 , pp. 3980-3987
    • Zhang, C.1    Ao, Z.2    Seth, A.3    Schlossman, S.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.