메뉴 건너뛰기




Volumn 15, Issue 5, 2010, Pages 563-573

Cytochrome c is rapidly reduced in the cytosol after mitochondrial outer membrane permeabilization

Author keywords

Caspase; Cytochrome c; Cytochrome oxidase; Electron transport chain (ETC); Mitochondrial outer membrane permeabilization (MOMP); Oxidation state

Indexed keywords

ANISOMYCIN; CASPASE 3; CASPASE 9; CYTOCHROME C; CYTOCHROME C OXIDASE; MITOCHONDRIAL PROTEIN; OUTER MEMBRANE PROTEIN; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 77951666026     PISSN: 13608185     EISSN: 1573675X     Source Type: Journal    
DOI: 10.1007/s10495-010-0455-2     Document Type: Article
Times cited : (52)

References (30)
  • 1
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • DOI 10.1126/science.1099320
    • DR Green G Kroemer 2004 The pathophysiology of mitochondrial cell death Science 305 626 629 10.1126/science.1099320 15286356 1:CAS:528: DC%2BD2cXmtFWqsrc%3D (Pubitemid 39006738)
    • (2004) Science , vol.305 , Issue.5684 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 2
    • 35848962271 scopus 로고    scopus 로고
    • C-Myc blazing a trail of death: Coupling of the mitochondrial and death receptor apoptosis pathways by c-Myc
    • 17914284 1:CAS:528:DC%2BD2sXhsVahtr7K
    • AI Nieminen JI Partanen J Klefstrom 2007 c-Myc blazing a trail of death: coupling of the mitochondrial and death receptor apoptosis pathways by c-Myc Cell Cycle 6 2464 2472 17914284 1:CAS:528:DC%2BD2sXhsVahtr7K
    • (2007) Cell Cycle , vol.6 , pp. 2464-2472
    • Nieminen, A.I.1    Partanen, J.I.2    Klefstrom, J.3
  • 3
    • 34247345833 scopus 로고    scopus 로고
    • The apoptosome: Signalling platform of cell death
    • DOI 10.1038/nrm2153, PII NRM2153
    • SJ Riedl GS Salvesen 2007 The apoptosome: signalling platform of cell death Nat Rev Mol Cell Biol 8 405 413 10.1038/nrm2153 17377525 1:CAS:528:DC%2BD2sXksFSjsr4%3D (Pubitemid 46643237)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.5 , pp. 405-413
    • Riedl, S.J.1    Salvesen, G.S.2
  • 4
    • 0023832894 scopus 로고
    • Electron conduction between b cytochromes of the mitochondrial respiratory chain in the presence of antimycin plus myxothiazol
    • DOI 10.1016/0005-2728(88)90053-9
    • IC West P Mitchell PR Rich 1988 Electron conduction between b cytochromes of the mitochondrial respiratory chain in the presence of antimycin plus myxothiazol Biochim Biophys Acta 933 35 41 10.1016/0005-2728(88)90053-9 3349068 1:CAS:528:DyaL1cXhvVags7o%3D (Pubitemid 18086627)
    • (1988) Biochimica et Biophysica Acta - Bioenergetics , vol.933 , Issue.1 , pp. 35-41
    • West, I.C.1    Mitchell, P.2    Rich, P.R.3
  • 5
    • 0023821272 scopus 로고
    • The location of CuA in mammalian cytochrome c oxidase
    • 10.1016/0014-5793(88)81349-8 2454843 1:CAS:528:DyaL1cXltVKqu70%3D
    • PR Rich IC West P Mitchell 1988 The location of CuA in mammalian cytochrome c oxidase FEBS Lett 233 25 30 10.1016/0014-5793(88)81349-8 2454843 1:CAS:528:DyaL1cXltVKqu70%3D
    • (1988) FEBS Lett , vol.233 , pp. 25-30
    • Rich, P.R.1    West, I.C.2    Mitchell, P.3
  • 6
    • 78651031094 scopus 로고
    • The respiratory chain and oxidative phosphorylation
    • 10.1002/9780470122624.ch2 1:CAS:528:DyaG2sXktlKgsw%3D%3D
    • B Chance GR Williams 1956 The respiratory chain and oxidative phosphorylation Adv Enzymol Relat Areas Mol Biol 17 65 134 10.1002/ 9780470122624.ch2 1:CAS:528:DyaG2sXktlKgsw%3D%3D
    • (1956) Adv Enzymol Relat Areas Mol Biol , vol.17 , pp. 65-134
    • Chance, B.1    Williams, G.R.2
  • 7
    • 0023869404 scopus 로고
    • The oxygen dependence of mitochondrial oxidative phosphorylation measured by a new optical method for measuring oxygen concentration
    • 2830260 1:CAS:528:DyaL1cXhs1egtLw%3D
    • DF Wilson WL Rumsey TJ Green JM Vanderkooi 1988 The oxygen dependence of mitochondrial oxidative phosphorylation measured by a new optical method for measuring oxygen concentration J Biol Chem 263 2712 2718 2830260 1:CAS:528:DyaL1cXhs1egtLw%3D
    • (1988) J Biol Chem , vol.263 , pp. 2712-2718
    • Wilson, D.F.1    Rumsey, W.L.2    Green, T.J.3    Vanderkooi, J.M.4
  • 8
    • 0345490800 scopus 로고    scopus 로고
    • Monitoring cytochrome redox changes in the mitochondria of intact cells using multi-wavelength visible light spectroscopy
    • DOI 10.1016/j.bbabio.2003.09.012
    • VS Hollis M Palacios-Callender RJ Springett DT Delpy S Moncada 2003 Monitoring cytochrome redox changes in the mitochondria of intact cells using multi-wavelength visible light spectroscopy Biochim Biophys Acta 1607 191 202 10.1016/j.bbabio.2003.09.012 14670609 1:CAS:528:DC%2BD3sXptlOqtrg%3D (Pubitemid 37500845)
    • (2003) Biochimica et Biophysica Acta - Bioenergetics , vol.1607 , Issue.2-3 , pp. 191-202
    • Hollis, V.S.1    Palacios-Callender, M.2    Springett, R.J.3    Delpy, D.T.4    Moncada, S.5
  • 9
    • 0031973203 scopus 로고    scopus 로고
    • Importance of the redox state of cytochrome c during caspase activation in cytosolic extracts
    • 9405280 1:CAS:528:DyaK1cXltFehsA%3D%3D
    • MB Hampton B Zhivotovsky AF Slater DH Burgess S Orrenius 1998 Importance of the redox state of cytochrome c during caspase activation in cytosolic extracts Biochem J 329 1 95 99 9405280 1:CAS:528:DyaK1cXltFehsA%3D%3D
    • (1998) Biochem J , vol.329 , Issue.1 , pp. 95-99
    • Hampton, M.B.1    Zhivotovsky, B.2    Slater, A.F.3    Burgess, D.H.4    Orrenius, S.5
  • 10
    • 0032793203 scopus 로고    scopus 로고
    • Analysis of redox regulation of cytochrome c-induced apoptosis in a cell-free system
    • 10.1038/sj.cdd.4400544 10453079 1:CAS:528:DyaK1MXltlOhur8%3D
    • Z Pan DW Voehringer RE Meyn 1999 Analysis of redox regulation of cytochrome c-induced apoptosis in a cell-free system Cell Death Differ 6 683 688 10.1038/sj.cdd.4400544 10453079 1:CAS:528:DyaK1MXltlOhur8%3D
    • (1999) Cell Death Differ , vol.6 , pp. 683-688
    • Pan, Z.1    Voehringer, D.W.2    Meyn, R.E.3
  • 11
    • 29144432723 scopus 로고    scopus 로고
    • Suppression of the pro-apoptotic function of cytochrome c by singlet oxygen via a haem redox state-independent mechanism
    • DOI 10.1042/BJ20050580
    • D Suto K Sato Y Ohba T Yoshimura J Fujii 2005 Suppression of the pro-apoptotic function of cytochrome c by singlet oxygen via a haem redox state-independent mechanism Biochem J 392 399 406 10.1042/BJ20050580 15966870 1:CAS:528:DC%2BD2MXht1CrtLfF (Pubitemid 41796529)
    • (2005) Biochemical Journal , vol.392 , Issue.2 , pp. 399-406
    • Suto, D.1    Sato, K.2    Ohba, Y.3    Yoshimura, T.4    Fujii, J.5
  • 12
    • 35748954935 scopus 로고    scopus 로고
    • Mitochondrial regulation of caspase activation by cytochrome oxidase and tetramethylphenylenediamine via cytosolic cytochrome c redox state
    • DOI 10.1074/jbc.M700322200
    • V Borutaite GC Brown 2007 Mitochondrial regulation of caspase activation by cytochrome oxidase and tetramethylphenylenediamine via cytosolic cytochrome c redox state J Biol Chem 282 31124 31130 10.1074/jbc.M700322200 17690099 1:CAS:528:DC%2BD2sXhtFykurrN (Pubitemid 350044866)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.43 , pp. 31124-31130
    • Borutaite, V.1    Brown, G.C.2
  • 13
    • 0028081969 scopus 로고
    • Use of the water absorption spectrum to quantify tissue chromophore concentration changes in near-infrared spectroscopy
    • 10.1088/0031-9155/39/1/011 7651995 1:STN:280:DyaK2MzotVCmtQ%3D%3D
    • SJ Matcher M Cope DT Delpy 1994 Use of the water absorption spectrum to quantify tissue chromophore concentration changes in near-infrared spectroscopy Phys Med Biol 39 177 196 10.1088/0031-9155/39/1/011 7651995 1:STN:280: DyaK2MzotVCmtQ%3D%3D
    • (1994) Phys Med Biol , vol.39 , pp. 177-196
    • Matcher, S.J.1    Cope, M.2    Delpy, D.T.3
  • 14
    • 0032415254 scopus 로고    scopus 로고
    • Simultaneous release of adenylate kinase and cytochrome c in cell death
    • 10.1038/sj.cdd.4400462 9894606 1:CAS:528:DyaK1MXktFKktg%3D%3D
    • B Single M Leist P Nicotera 1998 Simultaneous release of adenylate kinase and cytochrome c in cell death Cell Death Differ 5 1001 1003 10.1038/sj.cdd.4400462 9894606 1:CAS:528:DyaK1MXktFKktg%3D%3D
    • (1998) Cell Death Differ , vol.5 , pp. 1001-1003
    • Single, B.1    Leist, M.2    Nicotera, P.3
  • 15
    • 0036291021 scopus 로고    scopus 로고
    • L and calyculin a prevent translocation of bax to mitochondria during apoptosis
    • DOI 10.1006/bbrc.2002.6584
    • N Ganju A Eastman 2002 Bcl-X(L) and calyculin A prevent translocation of Bax to mitochondria during apoptosis Biochem Biophys Res Commun 291 1258 1264 10.1006/bbrc.2002.6584 11883953 1:CAS:528:DC%2BD38XhslWns7w%3D (Pubitemid 34694325)
    • (2002) Biochemical and Biophysical Research Communications , vol.291 , Issue.5 , pp. 1258-1264
    • Ganju, N.1    Eastman, A.2
  • 16
    • 45849085339 scopus 로고    scopus 로고
    • Cytochrome c: Functions beyond respiration
    • DOI 10.1038/nrm2434, PII NRM2434
    • YL Ow DR Green Z Hao TW Mak 2008 Cytochrome c: functions beyond respiration Nat Rev Mol Cell Biol 9 532 542 10.1038/nrm2434 18568041 1:CAS:528:DC%2BD1cXnsFGgu7k%3D (Pubitemid 351881842)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.7 , pp. 532-542
    • Ow, Y.-L.P.1    Green, D.R.2    Hao, Z.3    Mak, T.W.4
  • 17
    • 0033781027 scopus 로고    scopus 로고
    • The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant
    • 10.1038/35004029 10707086 1:CAS:528:DC%2BD3cXhvVGnt74%3D
    • JC Goldstein NJ Waterhouse P Juin GI Evan DR Green 2000 The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant Nat Cell Biol 2 156 162 10.1038/35004029 10707086 1:CAS:528: DC%2BD3cXhvVGnt74%3D
    • (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
  • 18
    • 0019888247 scopus 로고
    • Cytochrome c as an electron shuttle between the outer and inner mitochondrial membranes
    • 6265441 1:CAS:528:DyaL3MXkslGlsb0%3D
    • P Bernardi GF Azzone 1981 Cytochrome c as an electron shuttle between the outer and inner mitochondrial membranes J Biol Chem 256 7187 7192 6265441 1:CAS:528:DyaL3MXkslGlsb0%3D
    • (1981) J Biol Chem , vol.256 , pp. 7187-7192
    • Bernardi, P.1    Azzone, G.F.2
  • 19
    • 0036799548 scopus 로고    scopus 로고
    • Biphasic translocation of Bax to mitochondria
    • DOI 10.1042/BJ20020805
    • M Capano M Crompton 2002 Biphasic translocation of Bax to mitochondria Biochem J 367 169 178 10.1042/BJ20020805 12097139 1:CAS:528:DC%2BD38XotVWls70%3D (Pubitemid 35176903)
    • (2002) Biochemical Journal , vol.367 , Issue.1 , pp. 169-178
    • Capano, M.1    Crompton, M.2
  • 20
    • 0025876396 scopus 로고
    • Mechanistic stoichiometry of mitochondrial oxidative phosphorylation
    • 10.1021/bi00228a031 2012815 1:CAS:528:DyaK3MXhsF2hsL8%3D
    • PC Hinkle MA Kumar A Resetar DL Harris 1991 Mechanistic stoichiometry of mitochondrial oxidative phosphorylation Biochemistry 30 3576 3582 10.1021/bi00228a031 2012815 1:CAS:528:DyaK3MXhsF2hsL8%3D
    • (1991) Biochemistry , vol.30 , pp. 3576-3582
    • Hinkle, P.C.1    Kumar, M.A.2    Resetar, A.3    Harris, D.L.4
  • 21
    • 0041803002 scopus 로고    scopus 로고
    • Cytochrome c, released from cerebellar granule cells undergoing apoptosis or excytotoxic death, can generate protonmotive force and drive ATP synthesis in isolated mitochondria
    • DOI 10.1046/j.1471-4159.2003.01863.x
    • A Atlante L de Bari A Bobba E Marra P Calissano S Passarella 2003 Cytochrome c, released from cerebellar granule cells undergoing apoptosis or excytotoxic death, can generate protonmotive force and drive ATP synthesis in isolated mitochondria J Neurochem 86 591 604 10.1046/j.1471-4159.2003.01863.x 12859673 1:CAS:528:DC%2BD3sXlvF2ntbg%3D (Pubitemid 36897440)
    • (2003) Journal of Neurochemistry , vol.86 , Issue.3 , pp. 591-604
    • Atlante, A.1    De Bari, L.2    Bobba, A.3    Marra, E.4    Calissano, P.5    Passarella, S.6
  • 23
    • 0035451525 scopus 로고    scopus 로고
    • Does the redox status of cytochrome C act as a fail-safe mechanism in the regulation of programmed cell death?
    • DOI 10.1016/S0891-5849(01)00646-3, PII S0891584901006463
    • JT Hancock R Desikan SJ Neill 2001 Does the redox status of cytochrome C act as a fail-safe mechanism in the regulation of programmed cell death? Free Radic Biol Med 31 697 703 10.1016/S0891-5849(01)00646-3 11522455 1:CAS:528:DC%2BD3MXmtV2lurc%3D (Pubitemid 32777871)
    • (2001) Free Radical Biology and Medicine , vol.31 , Issue.5 , pp. 697-703
    • Hancock, J.T.1    Desikan, R.2    Neill, S.J.3
  • 24
    • 0026612806 scopus 로고
    • Ca2+/calmodulin-dependent cytochrome c reductase activity of brain nitric oxide synthase
    • 1375940 1:CAS:528:DyaK38XkvVGks7Y%3D
    • P Klatt B Heinzel M John M Kastner E Bohme B Mayer 1992 Ca2+/calmodulin-dependent cytochrome c reductase activity of brain nitric oxide synthase J Biol Chem 267 11374 11378 1375940 1:CAS:528:DyaK38XkvVGks7Y%3D
    • (1992) J Biol Chem , vol.267 , pp. 11374-11378
    • Klatt, P.1    Heinzel, B.2    John, M.3    Kastner, M.4    Bohme, E.5    Mayer, B.6
  • 25
    • 33748181931 scopus 로고    scopus 로고
    • 5 and cytochrome c
    • DOI 10.1016/j.febslet.2006.08.003, PII S0014579306009598
    • A Fago AJ Mathews L Moens S Dewilde T Brittain 2006 The reaction of neuroglobin with potential redox protein partners cytochrome b5 and cytochrome c FEBS Lett 580 4884 4888 10.1016/j.febslet.2006.08.003 16914148 1:CAS:528:DC%2BD28XovVels7s%3D (Pubitemid 44308330)
    • (2006) FEBS Letters , vol.580 , Issue.20 , pp. 4884-4888
    • Fago, A.1    Mathews, A.J.2    Moens, L.3    Dewilde, S.4    Brittain, T.5
  • 26
    • 1842509253 scopus 로고    scopus 로고
    • Electron transfer by diflavin reductases
    • 15063311 1:CAS:528:DC%2BD2cXivVCqsbg%3D
    • MB Murataliev R Feyereisen FA Walker 2004 Electron transfer by diflavin reductases Biochim Biophys Acta 1698 1 26 15063311 1:CAS:528: DC%2BD2cXivVCqsbg%3D
    • (2004) Biochim Biophys Acta , vol.1698 , pp. 1-26
    • Murataliev, M.B.1    Feyereisen, R.2    Walker, F.A.3
  • 27
    • 0345505668 scopus 로고    scopus 로고
    • Determination of the redox potentials and electron transfer properties of the FAD- and FMN-binding domains of the human oxidoreductase NR1
    • DOI 10.1046/j.1432-1033.2003.03474.x
    • RD Finn J Basran O Roitel CR Wolf AW Munro MJ Paine NS Scrutton 2003 Determination of the redox potentials and electron transfer properties of the FAD- and FMN-binding domains of the human oxidoreductase NR1 Eur J Biochem 270 1164 1175 10.1046/j.1432-1033.2003.03474.x 12631275 1:CAS:528: DC%2BD3sXivVSkt7g%3D (Pubitemid 36384449)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.6 , pp. 1164-1175
    • Finn, R.D.1    Basran, J.2    Roitel, O.3    Wolf, C.R.4    Munro, A.W.5    Paine, M.J.I.6    Scrutton, N.S.7
  • 28
    • 0018344726 scopus 로고
    • The mechanism of reduction of single-site redox proteins by ascorbic acid
    • 35158 1:CAS:528:DyaE1MXkslSisLc%3D
    • AI Al-Ayash MT Wilson 1979 The mechanism of reduction of single-site redox proteins by ascorbic acid Biochem J 177 641 648 35158 1:CAS:528: DyaE1MXkslSisLc%3D
    • (1979) Biochem J , vol.177 , pp. 641-648
    • Al-Ayash, A.I.1    Wilson, M.T.2
  • 29
    • 0018788773 scopus 로고
    • Kinetics and mechanism of the reduction of horse heart ferricytochrome c by glutathione
    • 10.1021/bi00579a037 36137 1:CAS:528:DyaE1MXktFGnsLo%3D
    • J Everse N Kujundzic 1979 Kinetics and mechanism of the reduction of horse heart ferricytochrome c by glutathione Biochemistry 18 2668 2673 10.1021/bi00579a037 36137 1:CAS:528:DyaE1MXktFGnsLo%3D
    • (1979) Biochemistry , vol.18 , pp. 2668-2673
    • Everse, J.1    Kujundzic, N.2
  • 30
    • 0033569714 scopus 로고    scopus 로고
    • Cytochrome c-mediated apoptosis in cells lacking mitochondrial DNA. Signaling pathway involving release and caspase 3 activation is conserved
    • DOI 10.1074/jbc.274.42.29905
    • S Jiang J Cai DC Wallace DP Jones 1999 Cytochrome c-mediated apoptosis in cells lacking mitochondrial DNA. Signaling pathway involving release and caspase 3 activation is conserved J Biol Chem 274 29905 29911 10.1074/jbc.274.42.29905 10514472 1:CAS:528:DyaK1MXmvVajsbk%3D (Pubitemid 29483369)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.42 , pp. 29905-29911
    • Jiang, S.1    Cai, J.2    Wallace, D.C.3    Jones, D.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.