메뉴 건너뛰기




Volumn 84, Issue 1, 2003, Pages 112-118

Quantitative relationship between inhibition of respiratory complexes and formation of reactive oxygen species in isolated nerve terminals

Author keywords

Complex I; Parkinson's disease; Reactive oxygen species; Reactive oxygen species formation; Respiratory complexes

Indexed keywords

ACONITATE HYDRATASE; CITRININ; CYANIDE; CYTOCHROME C OXIDASE; REACTIVE OXYGEN METABOLITE; ROTENONE;

EID: 0037269343     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2003.01513.x     Document Type: Article
Times cited : (169)

References (35)
  • 1
    • 0032547309 scopus 로고    scopus 로고
    • Inactivation of aconitase and oxoglutarate dihydrogenase in skeletal muscle in vitro by superoxide anions and/or nitric oxide
    • Andersson U., Leighton B., Young M. E., Blomstrand E. and Newsholme E. A. (1998) Inactivation of aconitase and oxoglutarate dihydrogenase in skeletal muscle in vitro by superoxide anions and/or nitric oxide. Biochem. Biophys. Res. Commun. 249, 512-516.
    • (1998) Biochem. Biophys. Res. Commun. , vol.249 , pp. 512-516
    • Andersson, U.1    Leighton, B.2    Young, M.E.3    Blomstrand, E.4    Newsholme, E.A.5
  • 2
    • 0030273295 scopus 로고    scopus 로고
    • Mitochondria, free radicals, and neurodegeneration
    • Beal M. F. (1996) Mitochondria, free radicals, and neurodegeneration. Curr Opin. Neurobiol. 6, 661-666.
    • (1996) Curr Opin. Neurobiol. , vol.6 , pp. 661-666
    • Beal, M.F.1
  • 3
    • 0032504710 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in neurodegenerative diseases
    • Beal M. F. (1998) Mitochondrial dysfunction in neurodegenerative diseases. Biochim. Biophys. Acta 1366, 211-223.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 211-223
    • Beal, M.F.1
  • 5
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide: General properties and effect of hyperbaric oxygen
    • Boveris A. and Chance B. (1973) The mitochondrial generation of hydrogen peroxide: general properties and effect of hyperbaric oxygen. Biochem. J. 134, 707-716.
    • (1973) Biochem. J. , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 6
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • Boveris A., Oshino N. and Chance B. (1972) The cellular production of hydrogen peroxide. Biochem. J. 128, 617-630.
    • (1972) Biochem. J. , vol.128 , pp. 617-630
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 7
    • 0017154414 scopus 로고
    • Role of ubiquinone in the mitochondrial generation of hydrogen peroxide
    • Boveris A., Cadenas E. and Stoppani A. O. M. (1976) Role of ubiquinone in the mitochondrial generation of hydrogen peroxide. Biochem. J. 156, 435-444.
    • (1976) Biochem. J. , vol.156 , pp. 435-444
    • Boveris, A.1    Cadenas, E.2    Stoppani, A.O.M.3
  • 8
    • 0017406503 scopus 로고
    • Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria
    • Cadenas E., Boveris A., Ragan C. I. and Stoppani A. O. (1977) Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria. Arch. Biochem. Biophys. 180, 248-257.
    • (1977) Arch. Biochem. Biophys. , vol.180 , pp. 248-257
    • Cadenas, E.1    Boveris, A.2    Ragan, C.I.3    Stoppani, A.O.4
  • 9
    • 0035162338 scopus 로고    scopus 로고
    • Mitochondria deficient in complex I activity are depolarized by hydrogen peroxide in nerve terminals: Relevance to Parkinson's disease
    • Chinopoulos C. and Adam-Vizi V. (2001) Mitochondria deficient in complex I activity are depolarized by hydrogen peroxide in nerve terminals: relevance to Parkinson's disease. J. Neurochem. 76, 302-306.
    • (2001) J. Neurochem. , vol.76 , pp. 302-306
    • Chinopoulos, C.1    Adam-Vizi, V.2
  • 10
    • 0029873904 scopus 로고    scopus 로고
    • Threshold effects and control of oxidative phosphorylation in nonsynaptic rat brain mitochondria
    • Davey G. P. and Clark J. B. (1996) Threshold effects and control of oxidative phosphorylation in nonsynaptic rat brain mitochondria. J. Neurochem. 66, 1617-1624.
    • (1996) J. Neurochem. , vol.66 , pp. 1617-1624
    • Davey, G.P.1    Clark, J.B.2
  • 11
    • 0032557511 scopus 로고    scopus 로고
    • Energy thresholds in brain mitochondria. Potential involvement in neurodegeneration
    • Davey G. P., Peuchen S. and Clark J. B. (1998) Energy thresholds in brain mitochondria. Potential involvement in neurodegeneration. J. Biol. Chem. 273, 12753-12757.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12753-12757
    • Davey, G.P.1    Peuchen, S.2    Clark, J.B.3
  • 12
    • 0030939089 scopus 로고    scopus 로고
    • On the virtual existence of superoxide anions in mitochondria: Thoughts regarding its role in pathophysiology
    • Forman H. J. and Azzi A. (1997) On the virtual existence of superoxide anions in mitochondria: thoughts regarding its role in pathophysiology. FASEB J. 11, 374-375.
    • (1997) FASEB J. , vol.11 , pp. 374-375
    • Forman, H.J.1    Azzi, A.2
  • 13
    • 0029064257 scopus 로고
    • Superoxide radical and iron modulate aconitase activity in mammalian cells
    • Gardner P. R., Raineri I., Epstein L. B. and White C. W. (1995) Superoxide radical and iron modulate aconitase activity in mammalian cells. J. Biol. Chem. 270, 13399-13405.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13399-13405
    • Gardner, P.R.1    Raineri, I.2    Epstein, L.B.3    White, C.W.4
  • 15
    • 0027452550 scopus 로고
    • Regulating the fate of mRNA: The control of cellular iron metabolism
    • Klausner R. D., Rouault T. A. and Harford J. B. (1993) Regulating the fate of mRNA: the control of cellular iron metabolism. Cell 72, 19-28.
    • (1993) Cell , vol.72 , pp. 19-28
    • Klausner, R.D.1    Rouault, T.A.2    Harford, J.B.3
  • 16
    • 0034212341 scopus 로고    scopus 로고
    • Neuronal cell death in Huntington's disease: A potential role for dopamine
    • Jakel R. J. and Maragos W. F. (2000) Neuronal cell death in Huntington's disease: a potential role for dopamine. Trends Neurosci. 23, 239-245.
    • (2000) Trends Neurosci. , vol.23 , pp. 239-245
    • Jakel, R.J.1    Maragos, W.F.2
  • 17
    • 0029819752 scopus 로고    scopus 로고
    • Measuring nitric oxide and superoxide: Rate constants for aconitase activity
    • Hausladen A. and Fridovich I. (1996) Measuring nitric oxide and superoxide: rate constants for aconitase activity. Meth Enzymol. 269, 37-41.
    • (1996) Meth Enzymol. , vol.269 , pp. 37-41
    • Hausladen, A.1    Fridovich, I.2
  • 18
    • 0034883512 scopus 로고    scopus 로고
    • Dependence of excitotoxic neurodegeneration on mitochondrial aconitase inactivation
    • Li Q.-Y., Pedersen C., Day B. J. and Patel M. (2001) Dependence of excitotoxic neurodegeneration on mitochondrial aconitase inactivation. J. Neurochem. 78, 746-755.
    • (2001) J. Neurochem. , vol.78 , pp. 746-755
    • Li, Q.-Y.1    Pedersen, C.2    Day, B.J.3    Patel, M.4
  • 19
    • 0034669186 scopus 로고    scopus 로고
    • Mitochondrial superoxide production in kainite-induced hippocampal damage
    • Liang L. P., Ho Y. S. and Patel M. (2000) Mitochondrial superoxide production in kainite-induced hippocampal damage. Neurosci. 101, 563-570.
    • (2000) Neurosci , vol.101 , pp. 563-570
    • Liang, L.P.1    Ho, Y.S.2    Patel, M.3
  • 20
    • 0036319021 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by the mitochondrial electron transport chain
    • Liu Y., Fiskum G. and Schubert D. (2002) Generation of reactive oxygen species by the mitochondrial electron transport chain. J. Neurochem. 80, 780-787.
    • (2002) J. Neurochem. , vol.80 , pp. 780-787
    • Liu, Y.1    Fiskum, G.2    Schubert, D.3
  • 22
    • 0015694375 scopus 로고
    • 2 formation: Relationship with energy conservation
    • 2 formation: relationship with energy conservation. FEBS Lett. 18, 84-88.
    • (1973) FEBS Lett. , vol.18 , pp. 84-88
    • Lochen, G.1    Azzi, A.2    Flohe, L.3
  • 24
    • 0028110234 scopus 로고
    • Cortical cytochrome oxidase activity is reduced in Alzheimer's disease
    • Mutisya E. M., Bowling A. C. and Beal M. F. (1994) Cortical cytochrome oxidase activity is reduced in Alzheimer's disease. J. Neurochem. 63, 2179-2184.
    • (1994) J. Neurochem. , vol.63 , pp. 2179-2184
    • Mutisya, E.M.1    Bowling, A.C.2    Beal, M.F.3
  • 27
    • 0001889165 scopus 로고
    • Subfractionation of mitochondria, and isolation of the proteins of oxidative phosphorylation
    • Darley-Usmar V. M., Rickwood D. and Wilson M. T., eds. IRL Press. London
    • Ragan C. I., Wilson M. T., Darley-Usmar V. M. and Lowe P. N. (1987) Subfractionation of mitochondria, and isolation of the proteins of oxidative phosphorylation, in Mitochondria, a Practical Approach. (Darley-Usmar V. M., Rickwood D. and Wilson M. T., eds), pp. 79-112. IRL Press. London.
    • (1987) Mitochondria, A Practical Approach , pp. 79-112
    • Ragan, C.I.1    Wilson, M.T.2    Darley-Usmar, V.M.3    Lowe, P.N.4
  • 28
    • 77956985297 scopus 로고
    • Preparation and properties of reduced coenzyme Q-cytochrome c reductase
    • Rieske J. S. (1967) Preparation and properties of reduced coenzyme Q-cytochrome c reductase. Meth Enzymol. 10, 239-245.
    • (1967) Meth Enzymol. , vol.10 , pp. 239-245
    • Rieske, J.S.1
  • 30
    • 0034671429 scopus 로고    scopus 로고
    • Inhibition of Krebs cycle enzymes by hydrogen peroxide: A key role of α-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress
    • Tretter L. and Adam-Vizi V. (2000) Inhibition of Krebs cycle enzymes by hydrogen peroxide: a key role of α-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress. J. Neurosci. 20, 8972-8979.
    • (2000) J. Neurosci. , vol.20 , pp. 8972-8979
    • Tretter, L.1    Adam-Vizi, V.2
  • 31
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • Turrens J. F. and Boveris A. (1980) Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem. J. 191, 421-427.
    • (1980) Biochem. J. , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 32
    • 0039174315 scopus 로고    scopus 로고
    • Mitochondrial aconitase is a source of hydroxyl radical
    • Vasquez-Vivar J., Kalyanaraman B. and Kennedy M. C. (2000) Mitochondrial aconitase is a source of hydroxyl radical. J. Biol. Chem. 275, 14064-14069.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14064-14069
    • Vasquez-Vivar, J.1    Kalyanaraman, B.2    Kennedy, M.C.3
  • 33
    • 0034740585 scopus 로고    scopus 로고
    • m-dependent and -independent production of reactive oxygen species by rat brain mitochondria
    • m-dependent and -independent production of reactive oxygen species by rat brain mitochondria. J. Neurochem. 79, 266-277.
    • (2001) J. Neurochem. , vol.79 , pp. 266-277
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 34
    • 2042432480 scopus 로고
    • Cytochrome oxidase from beef heart mitochondria
    • Wharton D. C. and Tzagoloff A. (1967) Cytochrome oxidase from beef heart mitochondria. Meth. Enzymol. 10, 245-250.
    • (1967) Meth. Enzymol. , vol.10 , pp. 245-250
    • Wharton, D.C.1    Tzagoloff, A.2
  • 35
    • 0024996681 scopus 로고
    • The oxidative inactivation of mitochondrial electron transport chain components and ATPase
    • Zhang Y., Marcillat O., Giulivi C., Ernster L. and Davies K. J. (1990) The oxidative inactivation of mitochondrial electron transport chain components and ATPase. J. Biol. Chem. 265, 16330-16336.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16330-16336
    • Zhang, Y.1    Marcillat, O.2    Giulivi, C.3    Ernster, L.4    Davies, K.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.