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Volumn 117, Issue 6, 2004, Pages 773-786

Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CASPASE; PROTEIN P75; PROTEIN SUBUNIT;

EID: 2942581328     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2004.05.008     Document Type: Article
Times cited : (518)

References (50)
  • 2
    • 0037147267 scopus 로고    scopus 로고
    • NADPH oxidase-dependent oxidation and externalization of phosphatidylserine during apoptosis in Me2SO-differentiated HL-60 cells. Role in phagocytic clearance
    • Arroyo A., Modriansky M., Serinkan F.B., Bello R.I., Matsura T., Jiang J., Tyurin V.A., Tyurina Y.Y., Fadeel B., Kagan V.E. NADPH oxidase-dependent oxidation and externalization of phosphatidylserine during apoptosis in Me2SO-differentiated HL-60 cells. Role in phagocytic clearance. J. Biol. Chem. 277:2002;49965-49975
    • (2002) J. Biol. Chem. , vol.277 , pp. 49965-49975
    • Arroyo, A.1    Modriansky, M.2    Serinkan, F.B.3    Bello, R.I.4    Matsura, T.5    Jiang, J.6    Tyurin, V.A.7    Tyurina, Y.Y.8    Fadeel, B.9    Kagan, V.E.10
  • 3
    • 0033611057 scopus 로고    scopus 로고
    • Adenine nucleotide translocase-1, a component of the permeability transition pore, can dominantly induce apoptosis
    • Bauer M.K., Schubert A., Rocks O., Grimm S. Adenine nucleotide translocase-1, a component of the permeability transition pore, can dominantly induce apoptosis. J. Cell Biol. 147:1999;1493-1502
    • (1999) J. Cell Biol. , vol.147 , pp. 1493-1502
    • Bauer, M.K.1    Schubert, A.2    Rocks, O.3    Grimm, S.4
  • 5
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier C. Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 256:1981;1604-1607
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 6
    • 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
    • 0032472329 scopus 로고    scopus 로고
    • Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization
    • Bossy-Wetzel E., Newmeyer D.D., Green D.R. Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization. EMBO J. 17:1998;37-49
    • (1998) EMBO J. , vol.17 , pp. 37-49
    • Bossy-Wetzel, E.1    Newmeyer, D.D.2    Green, D.R.3
  • 9
    • 0032544449 scopus 로고    scopus 로고
    • Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development
    • Cecconi F., Alvarez-Bolado G., Meyer B.I., Roth K.A., Gruss P. Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development. Cell. 94:1998;727-737
    • (1998) Cell , vol.94 , pp. 727-737
    • Cecconi, F.1    Alvarez-Bolado, G.2    Meyer, B.I.3    Roth, K.A.4    Gruss, P.5
  • 10
    • 0035072953 scopus 로고    scopus 로고
    • Membrane blebbing during apoptosis results from caspase-mediated activation of ROCK I
    • Coleman M.L., Sahai E.A., Yeo M., Bosch M., Dewar A., Olson M.F. Membrane blebbing during apoptosis results from caspase-mediated activation of ROCK I. Nat. Cell Biol. 3:2001;339-345
    • (2001) Nat. Cell Biol. , vol.3 , pp. 339-345
    • Coleman, M.L.1    Sahai, E.A.2    Yeo, M.3    Bosch, M.4    Dewar, A.5    Olson, M.F.6
  • 12
    • 0032778902 scopus 로고    scopus 로고
    • Redistribution of cytochrome c precedes the caspase-dependent formation of ultracondensed mitochondria, with a reduced inner membrane potential, in apoptotic monocytes
    • Dinsdale D., Zhuang J., Cohen G.M. Redistribution of cytochrome c precedes the caspase-dependent formation of ultracondensed mitochondria, with a reduced inner membrane potential, in apoptotic monocytes. Am. J. Pathol. 155:1999;607-618
    • (1999) Am. J. Pathol. , vol.155 , pp. 607-618
    • Dinsdale, D.1    Zhuang, J.2    Cohen, G.M.3
  • 13
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • Earnshaw W.C., Martins L.M., Kaufmann S.H. Mammalian caspases. structure, activation, substrates, and functions during apoptosis Annu. Rev. Biochem. 68:1999;383-424
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 14
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M., Sakahira H., Yokoyama H., Okawa K., Iwamatsu A., Nagata S. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature. 391:1998;43-50
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 16
    • 0242432345 scopus 로고    scopus 로고
    • Many cuts to ruin: A comprehensive update of caspase substrates
    • Fischer U., Janicke R.U., Schulze-Osthoff K. Many cuts to ruin. a comprehensive update of caspase substrates Cell Death Differ. 10:2003;76-100
    • (2003) Cell Death Differ. , vol.10 , pp. 76-100
    • Fischer, U.1    Janicke, R.U.2    Schulze-Osthoff, K.3
  • 17
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki Y., Hubbard A.L., Fowler S., Lazarow P.B. Isolation of intracellular membranes by means of sodium carbonate treatment. application to endoplasmic reticulum J. Cell Biol. 93:1982;97-102
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 18
    • 0037157104 scopus 로고    scopus 로고
    • Fas-triggered phosphatidylserine exposure is modulated by intracellular ATP
    • Gleiss B., Gogvadze V., Orrenius S., Fadeel B. Fas-triggered phosphatidylserine exposure is modulated by intracellular ATP. FEBS Lett. 519:2002;153-158
    • (2002) FEBS Lett. , vol.519 , pp. 153-158
    • Gleiss, B.1    Gogvadze, V.2    Orrenius, S.3    Fadeel, B.4
  • 19
    • 0033781027 scopus 로고    scopus 로고
    • The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant
    • Goldstein J.C., Waterhouse N.J., Juin P., Evan G.I., Green D.R. The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant. Nat. Cell Biol. 2:2000;156-162
    • (2000) Nat. Cell Biol. , vol.2 , pp. 156-162
    • Goldstein, J.C.1    Waterhouse, N.J.2    Juin, P.3    Evan, G.I.4    Green, D.R.5
  • 20
    • 0036463405 scopus 로고    scopus 로고
    • A matter of life and death
    • Green D.R., Evan G.I. A matter of life and death. Cancer Cell. 1:2002;19-30
    • (2002) Cancer Cell , vol.1 , pp. 19-30
    • Green, D.R.1    Evan, G.I.2
  • 23
    • 0038731167 scopus 로고    scopus 로고
    • Caspase-independent cell death in T lymphocytes
    • Jaattela M., Tschopp J. Caspase-independent cell death in T lymphocytes. Nat. Immunol. 4:2003;416-423
    • (2003) Nat. Immunol. , vol.4 , pp. 416-423
    • Jaattela, M.1    Tschopp, J.2
  • 26
    • 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
    • 0037424245 scopus 로고    scopus 로고
    • Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production
    • Li N., Ragheb K., Lawler G., Sturgis J., Rajwa B., Melendez J.A., Robinson J.P. Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production. J. Biol. Chem. 278:2003;8516-8525
    • (2003) J. Biol. Chem. , vol.278 , pp. 8516-8525
    • Li, N.1    Ragheb, K.2    Lawler, G.3    Sturgis, J.4    Rajwa, B.5    Melendez, J.A.6    Robinson, J.P.7
  • 30
    • 0028800947 scopus 로고
    • Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: Inhibition by overexpression of Bcl-2 and Abl
    • Martin S.J., Reutelingsperger C.P., McGahon A.J., Rader J.A., van Schie R.C., LaFace D.M., Green D.R. Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus. inhibition by overexpression of Bcl-2 and Abl J. Exp. Med. 182:1995;1545-1556
    • (1995) J. Exp. Med. , vol.182 , pp. 1545-1556
    • Martin, S.J.1    Reutelingsperger, C.P.2    McGahon, A.J.3    Rader, J.A.4    Van Schie, R.C.5    Laface, D.M.6    Green, D.R.7
  • 32
    • 0037205754 scopus 로고    scopus 로고
    • Phosphatidylserine peroxidation/externalization during staurosporineinduced apoptosis in HL-60 cells
    • Matsura T., Serinkan B.F., Jiang J., Kagan V.E. Phosphatidylserine peroxidation/externalization during staurosporineinduced apoptosis in HL-60 cells. FEBS Lett. 524:2002;25-30
    • (2002) FEBS Lett. , vol.524 , pp. 25-30
    • Matsura, T.1    Serinkan, B.F.2    Jiang, J.3    Kagan, V.E.4
  • 33
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: Releasing power for life and unleashing the machineries of death
    • Newmeyer D.D., Ferguson-Miller S. Mitochondria. releasing power for life and unleashing the machineries of death Cell. 112:2003;481-490
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 34
    • 0021958744 scopus 로고
    • EPR studies of iron-sulfur clusters in isolated subunits and subfractions of NADH-ubiquinone oxidoreductase
    • Ohnishi T., Ragan C.I., Hatefi Y. EPR studies of iron-sulfur clusters in isolated subunits and subfractions of NADH-ubiquinone oxidoreductase. J. Biol. Chem. 260:1985;2782-2788
    • (1985) J. Biol. Chem. , vol.260 , pp. 2782-2788
    • Ohnishi, T.1    Ragan, C.I.2    Hatefi, Y.3
  • 35
    • 0037421221 scopus 로고    scopus 로고
    • Caspase-mediated loss of mitochondrial function and generation of reactive oxygen species during apoptosis
    • a
    • Ricci J.E., Gottlieb R.A., Green D.R. Caspase-mediated loss of mitochondrial function and generation of reactive oxygen species during apoptosis. J. Cell Biol. 160:2003;65-75. a
    • (2003) J. Cell Biol. , vol.160 , pp. 65-75
    • Ricci, J.E.1    Gottlieb, R.A.2    Green, D.R.3
  • 36
    • 0038146907 scopus 로고    scopus 로고
    • Mitochondrial functions during cell death, a complex (I-V) dilemma
    • Ricci, J.E., Waterhouse, N.J., and Green, D.R. (2003b). Mitochondrial functions during cell death, a complex (I-V) dilemma. Cell Death Differ 10, 488-492.
    • (2003) Cell Death Differ , vol.10 , pp. 488-492
    • Ricci, J.E.1    Waterhouse, N.J.2    Green, D.R.3
  • 37
    • 0032490099 scopus 로고    scopus 로고
    • Human complex I deficiency: Clinical spectrum and involvement of oxygen free radicals in the pathogenicity of the defect
    • Robinson B.H. Human complex I deficiency. clinical spectrum and involvement of oxygen free radicals in the pathogenicity of the defect Biochim. Biophys. Acta. 1364:1998;271-286
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 271-286
    • Robinson, B.H.1
  • 38
    • 0031907887 scopus 로고    scopus 로고
    • P21-activated kinase (PAK) is required for Fas-induced JNK activation in Jurkat cells
    • Rudel T., Zenke F.T., Chuang T.H., Bokoch G.M. p21-activated kinase (PAK) is required for Fas-induced JNK activation in Jurkat cells. J. Immunol. 160:1998;7-11
    • (1998) J. Immunol. , vol.160 , pp. 7-11
    • Rudel, T.1    Zenke, F.T.2    Chuang, T.H.3    Bokoch, G.M.4
  • 39
    • 0033539067 scopus 로고    scopus 로고
    • Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation
    • Sahara S., Aoto M., Eguchi Y., Imamoto N., Yoneda Y., Tsujimoto Y. Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation. Nature. 401:1999;168-173
    • (1999) Nature , vol.401 , pp. 168-173
    • Sahara, S.1    Aoto, M.2    Eguchi, Y.3    Imamoto, N.4    Yoneda, Y.5    Tsujimoto, Y.6
  • 40
    • 0026713818 scopus 로고
    • Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial functions. Evidence for the involvement of mitochondrial radical generation
    • Schulze-Osthoff K., Bakker A.C., Vanhaesebroeck B., Beyaert R., Jacob W.A., Fiers W. Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial functions. Evidence for the involvement of mitochondrial radical generation. J. Biol. Chem. 267:1992;5317-5323
    • (1992) J. Biol. Chem. , vol.267 , pp. 5317-5323
    • Schulze-Osthoff, K.1    Bakker, A.C.2    Vanhaesebroeck, B.3    Beyaert, R.4    Jacob, W.A.5    Fiers, W.6
  • 41
    • 0018980419 scopus 로고
    • The organization of NADH dehydrogenase polypeptides in the inner mitochondrial membrane
    • Smith S., Ragan C.I. The organization of NADH dehydrogenase polypeptides in the inner mitochondrial membrane. Biochem. J. 185:1980;315-326
    • (1980) Biochem. J. , vol.185 , pp. 315-326
    • Smith, S.1    Ragan, C.I.2
  • 42
    • 0034283578 scopus 로고    scopus 로고
    • Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8
    • Stennicke H.R., Renatus M., Meldal M., Salvesen G.S. Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8. Biochem. J. 350:2000;563-568
    • (2000) Biochem. J. , vol.350 , pp. 563-568
    • Stennicke, H.R.1    Renatus, M.2    Meldal, M.3    Salvesen, G.S.4
  • 43
    • 0038202902 scopus 로고    scopus 로고
    • Phosphatidylserine exposure in Fas type I cells is mitochondria-dependent
    • Uthaisang W., Nutt L.K., Orrenius S., Fadeel B. Phosphatidylserine exposure in Fas type I cells is mitochondria-dependent. FEBS Lett. 545:2003;110-114
    • (2003) FEBS Lett. , vol.545 , pp. 110-114
    • Uthaisang, W.1    Nutt, L.K.2    Orrenius, S.3    Fadeel, B.4
  • 44
    • 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
  • 45
    • 0027104114 scopus 로고
    • The nadh:ubiquinone oxidoreductase (complex i) of respiratory chains
    • Walker J.E. The nadh:ubiquinone oxidoreductase (complex i) of respiratory chains. Q. Rev. Biophys. 25:1992;253-324
    • (1992) Q. Rev. Biophys. , vol.25 , pp. 253-324
    • Walker, J.E.1
  • 46
    • 0035897408 scopus 로고    scopus 로고
    • Cytochrome c maintains mitochondrial transmembrane potential and ATP generation after outer mitochondrial membrane permeabilization during the apoptotic process
    • Waterhouse N.J., Goldstein J.C., von Ahsen O., Schuler M., Newmeyer D.D., Green D.R. Cytochrome c maintains mitochondrial transmembrane potential and ATP generation after outer mitochondrial membrane permeabilization during the apoptotic process. J. Cell Biol. 153:2001;319-328
    • (2001) J. Cell Biol. , vol.153 , pp. 319-328
    • Waterhouse, N.J.1    Goldstein, J.C.2    Von Ahsen, O.3    Schuler, M.4    Newmeyer, D.D.5    Green, D.R.6
  • 48
    • 0028903933 scopus 로고
    • Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo
    • b
    • Zamzami N., Marchetti P., Castedo M., Zanin C., Vayssiere J.L., Petit P.X., Kroemer G. Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo. J. Exp. Med. 181:1995;1661-1672. b
    • (1995) J. Exp. Med. , vol.181 , pp. 1661-1672
    • Zamzami, N.1    Marchetti, P.2    Castedo, M.3    Zanin, C.4    Vayssiere, J.L.5    Petit, P.X.6    Kroemer, G.7
  • 49
    • 0031795088 scopus 로고    scopus 로고
    • Apoptosis, in human monocytic THP.1 cells, results in the release of cytochrome c from mitochondria prior to their ultracondensation, formation of outer membrane discontinuities and reduction in inner membrane potential
    • Zhuang J., Dinsdale D., Cohen G.M. Apoptosis, in human monocytic THP.1 cells, results in the release of cytochrome c from mitochondria prior to their ultracondensation, formation of outer membrane discontinuities and reduction in inner membrane potential. Cell Death Differ. 5:1998;953-962
    • (1998) Cell Death Differ. , vol.5 , pp. 953-962
    • Zhuang, J.1    Dinsdale, D.2    Cohen, G.M.3
  • 50
    • 0037128923 scopus 로고    scopus 로고
    • The role of ARK in stress-induced apoptosis in Drosophila cells
    • Zimmermann K.C., Ricci J.E., Droin N.M., Green D.R. The role of ARK in stress-induced apoptosis in Drosophila cells. J. Cell Biol. 156:2002;1077-1087
    • (2002) J. Cell Biol. , vol.156 , pp. 1077-1087
    • Zimmermann, K.C.1    Ricci, J.E.2    Droin, N.M.3    Green, D.R.4


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