메뉴 건너뛰기




Volumn 122, Issue 2, 2005, Pages 221-233

Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; HYDROGEN PEROXIDE; PROTEIN P66; REACTIVE OXYGEN METABOLITE;

EID: 22744447211     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2005.05.011     Document Type: Article
Times cited : (1006)

References (36)
  • 1
    • 0036026536 scopus 로고    scopus 로고
    • Insights from protein film voltammetry into mechanisms of complex biological electron-transfer reactions
    • F.A. Armstrong Insights from protein film voltammetry into mechanisms of complex biological electron-transfer reactions J. Chem. Soc., Dalton Trans. 5 2002 661
    • (2002) J. Chem. Soc., Dalton Trans. , vol.5 , pp. 661
    • Armstrong, F.A.1
  • 3
    • 1142297598 scopus 로고    scopus 로고
    • New concepts in reactive oxygen species and cardiovascular reperfusion physiology
    • L.B. Becker New concepts in reactive oxygen species and cardiovascular reperfusion physiology Cardiovasc. Res. 61 2004 461 470
    • (2004) Cardiovasc. Res. , vol.61 , pp. 461-470
    • Becker, L.B.1
  • 4
    • 0019888247 scopus 로고
    • Cytochrome c as an electron shuttle between the outer and inner mitochondrial membranes
    • P. Bernardi, and G.F. Azzone Cytochrome c as an electron shuttle between the outer and inner mitochondrial membranes J. Biol. Chem. 256 1981 7187 7192
    • (1981) J. Biol. Chem. , vol.256 , pp. 7187-7192
    • Bernardi, P.1    Azzone, G.F.2
  • 6
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • M. Brownlee Biochemistry and molecular cell biology of diabetic complications Nature 414 2001 813 820
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 7
    • 0032496143 scopus 로고    scopus 로고
    • Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss
    • J. Cai, and D.P. Jones Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss J. Biol. Chem. 273 1998 11401 11404
    • (1998) J. Biol. Chem. , vol.273 , pp. 11401-11404
    • Cai, J.1    Jones, D.P.2
  • 9
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • B. Chance, H. Sies, and A. Boveris Hydroperoxide metabolism in mammalian organs Physiol. Rev. 59 1979 527 605
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 10
    • 0037015367 scopus 로고    scopus 로고
    • Redox properties of cytochrome c adsorbed on self-assembled monolayers: A probe for protein conformation and orientation
    • X. Chen, R. Ferrigno, J. Yang, and G.M. Whitesides Redox properties of cytochrome c adsorbed on self-assembled monolayers: a probe for protein conformation and orientation Langmuir 18 2002 7009 7015
    • (2002) Langmuir , vol.18 , pp. 7009-7015
    • Chen, X.1    Ferrigno, R.2    Yang, J.3    Whitesides, G.M.4
  • 11
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: Critical control points
    • N.N. Danial, and S.J. Korsmeyer Cell death: critical control points Cell 116 2004 205 219
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 12
    • 0023870541 scopus 로고
    • Enhanced uptake of spermidine and methylglyoxal-bis(guanylhydrazone) by rat liver mitochondria following outer membrane lysis
    • J.J. Diwan, H.H. Yune, R. Bawa, T. Haley, and C.A. Mannella Enhanced uptake of spermidine and methylglyoxal-bis(guanylhydrazone) by rat liver mitochondria following outer membrane lysis Biochem. Pharmacol. 37 1988 957 961
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 957-961
    • Diwan, J.J.1    Yune, H.H.2    Bawa, R.3    Haley, T.4    Mannella, C.A.5
  • 14
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • D.R. Green, and G. Kroemer The pathophysiology of mitochondrial cell death Science 305 2004 626 629
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 15
    • 2442421118 scopus 로고    scopus 로고
    • Loss of the intermembrane space protein Mgm1/OPA1 induces swelling and localized constrictions along the lengths of mitochondria
    • L. Griparic, N.N. van der Wel, I.J. Orozco, P.J. Peters, and A.M. van der Bliek Loss of the intermembrane space protein Mgm1/OPA1 induces swelling and localized constrictions along the lengths of mitochondria J. Biol. Chem. 279 2004 18792 18798
    • (2004) J. Biol. Chem. , vol.279 , pp. 18792-18798
    • Griparic, L.1    Van Der Wel, N.N.2    Orozco, I.J.3    Peters, P.J.4    Van Der Bliek, A.M.5
  • 16
    • 0026554428 scopus 로고
    • Evaluation of the probe 2′,7′-dichlorofluorescin as an indicator of reactive oxygen species formation and oxidative stress
    • C.P. LeBel, H. Ischiropoulos, and S.C. Bondy Evaluation of the probe 2′,7′-dichlorofluorescin as an indicator of reactive oxygen species formation and oxidative stress Chem. Res. Toxicol. 5 1992 227 231
    • (1992) Chem. Res. Toxicol. , vol.5 , pp. 227-231
    • Lebel, C.P.1    Ischiropoulos, H.2    Bondy, S.C.3
  • 17
    • 0028169881 scopus 로고
    • N-acetyl-L-cysteine is a pluripotent protector against cell death and enhancer of trophic factor-mediated cell survival in vitro
    • M. Mayer, and M. Noble N-acetyl-L-cysteine is a pluripotent protector against cell death and enhancer of trophic factor-mediated cell survival in vitro Proc. Natl. Acad. Sci. USA 91 1994 7496 7500
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7496-7500
    • Mayer, M.1    Noble, M.2
  • 21
    • 0037192473 scopus 로고    scopus 로고
    • Redox regulation of forkhead proteins through a p66shc dependent signaling pathway
    • S. Nemoto, and T. Finkel Redox regulation of forkhead proteins through a p66shc dependent signaling pathway Science 295 2002 2450 2452
    • (2002) Science , vol.295 , pp. 2450-2452
    • Nemoto, S.1    Finkel, T.2
  • 24
    • 1542781658 scopus 로고    scopus 로고
    • Do tumor-suppressive mechanisms contribute to organism aging by inducing stem cell senescence?
    • P.G. Pelicci Do tumor-suppressive mechanisms contribute to organism aging by inducing stem cell senescence? J. Clin. Invest. 113 2004 4 7
    • (2004) J. Clin. Invest. , vol.113 , pp. 4-7
    • Pelicci, P.G.1
  • 26
    • 0028239794 scopus 로고
    • The voltage sensor of the mitochondrial permeability transition pore is tuned by the oxidation-reduction state of vicinal thiols. Increase of the gating potential by oxidants and its reversal by reducing agents
    • V. Petronilli, P. Costantini, L. Scorrano, R. Colonna, S. Passamonti, and P. Bernardi The voltage sensor of the mitochondrial permeability transition pore is tuned by the oxidation-reduction state of vicinal thiols. Increase of the gating potential by oxidants and its reversal by reducing agents J. Biol. Chem. 269 1994 16638 16642
    • (1994) J. Biol. Chem. , vol.269 , pp. 16638-16642
    • Petronilli, V.1    Costantini, P.2    Scorrano, L.3    Colonna, R.4    Passamonti, S.5    Bernardi, P.6
  • 30
    • 0037427412 scopus 로고    scopus 로고
    • Mechanisms of cytochrome c release by proapoptotic BCL-2 family members
    • L. Scorrano, and S.J. Korsmeyer Mechanisms of cytochrome c release by proapoptotic BCL-2 family members Biochem. Biophys. Res. Commun. 304 2003 437 444
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 437-444
    • Scorrano, L.1    Korsmeyer, S.J.2
  • 31
  • 32
    • 0347087425 scopus 로고    scopus 로고
    • A cryptic targeting signal induces isoform-specific localization of p46Shc to mitochondria
    • A. Ventura, M. Maccarana, V.A. Raker, and P.G. Pelicci A cryptic targeting signal induces isoform-specific localization of p46Shc to mitochondria J. Biol. Chem. 279 2004 2299 2306
    • (2004) J. Biol. Chem. , vol.279 , pp. 2299-2306
    • Ventura, A.1    MacCarana, M.2    Raker, V.A.3    Pelicci, P.G.4
  • 33
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial diseases in man and mouse
    • D.C. Wallace Mitochondrial diseases in man and mouse Science 283 1999 1482 1488
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1
  • 35
    • 0038368985 scopus 로고    scopus 로고
    • Superoxide reacts with hydroethidine but forms a fluorescent product that is distinctly different from ethidium: Potential implications in intracellular fluorescence detection of superoxide
    • H. Zhao, S. Kalivendi, H. Zhang, J. Joseph, K. Nithipatikom, J. Vasquez-Vivar, and B. Kalyanaraman Superoxide reacts with hydroethidine but forms a fluorescent product that is distinctly different from ethidium: potential implications in intracellular fluorescence detection of superoxide Free Radic. Biol. Med. 34 2003 1359 1368
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 1359-1368
    • Zhao, H.1    Kalivendi, S.2    Zhang, H.3    Joseph, J.4    Nithipatikom, K.5    Vasquez-Vivar, J.6    Kalyanaraman, B.7
  • 36
    • 0033621394 scopus 로고    scopus 로고
    • Definition of the interaction domain for cytochrome c on cytochrome c oxidase. I. Biochemical, spectral, and kinetic characterization of surface mutants in subunit ii of Rhodobacter sphaeroides cytochrome aa(3)
    • Y. Zhen, C.W. Hoganson, G.T. Babcock, and S. Ferguson-Miller Definition of the interaction domain for cytochrome c on cytochrome c oxidase. I. Biochemical, spectral, and kinetic characterization of surface mutants in subunit ii of Rhodobacter sphaeroides cytochrome aa(3) J. Biol. Chem. 274 1999 38032 38041
    • (1999) J. Biol. Chem. , vol.274 , pp. 38032-38041
    • Zhen, Y.1    Hoganson, C.W.2    Babcock, G.T.3    Ferguson-Miller, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.