메뉴 건너뛰기




Volumn 29, Issue 3, 2004, Pages 569-577

Initiation of Neuronal Damage by Complex I Deficiency and Oxidative Stress in Parkinson's Disease

Author keywords

Complex I deficiency; Dopaminergic neurons; Oxidative stress; Parkinson's disease; Reactive oxygen species

Indexed keywords

ADENOSINE TRIPHOSPHATE; HYDROGEN PEROXIDE; OXOGLUTARATE DEHYDROGENASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);

EID: 1542318096     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:NERE.0000014827.94562.4b     Document Type: Review
Times cited : (170)

References (104)
  • 1
    • 0031848638 scopus 로고    scopus 로고
    • Neurochemical and neurogenetic correlates of Parkinson's disease
    • Mizuno, Y., Hattori, N., and Matsumine, H. 1998. Neurochemical and neurogenetic correlates of Parkinson's disease. J. Neurochem. 71:893-902.
    • (1998) J. Neurochem. , vol.71 , pp. 893-902
    • Mizuno, Y.1    Hattori, N.2    Matsumine, H.3
  • 3
    • 0036182026 scopus 로고    scopus 로고
    • Mitochondrial involvement in Parkinson's disease
    • Orth, M. and Schapira, A. H. 2002. Mitochondrial involvement in Parkinson's disease. Neurochem. Int. 40:533-541.
    • (2002) Neurochem. Int. , vol.40 , pp. 533-541
    • Orth, M.1    Schapira, A.H.2
  • 4
    • 0027104114 scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains
    • Walker, J. E. 1992. The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Q. Rev. Biophys. 25:253-324.
    • (1992) Q. Rev. Biophys. , vol.25 , pp. 253-324
    • Walker, J.E.1
  • 6
    • 0037029133 scopus 로고    scopus 로고
    • Mutations in human nuclear genes encoding for subunits of mitochondrial respiratory complex I: The NDUFS4 gene
    • Petruzzella, V. and Papa, S. 2002. Mutations in human nuclear genes encoding for subunits of mitochondrial respiratory complex I: The NDUFS4 gene. Gene 286:149-154.
    • (2002) Gene , vol.286 , pp. 149-154
    • Petruzzella, V.1    Papa, S.2
  • 7
    • 0021810979 scopus 로고
    • Inhibition of NADH-linked oxidation in brain mitochondria by 1-methyl-4-phenyl-pyridine, a metabolite of the neurotoxin, 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine
    • Nicklas, W. J., Vyas, I., and Heikkila, R. E. 1985. Inhibition of NADH-linked oxidation in brain mitochondria by 1-methyl-4-phenyl-pyridine, a metabolite of the neurotoxin, 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine. Life Sci. 36:2503-2508.
    • (1985) Life Sci. , vol.36 , pp. 2503-2508
    • Nicklas, W.J.1    Vyas, I.2    Heikkila, R.E.3
  • 8
    • 0022516015 scopus 로고
    • Inhibition of mitochondrial NADH dehydrogenase by pyridine derivatives and its possible relation to experimental and idiopathic parkinsonism
    • Ramsay, R. R., Salach, J. I., Dadgar, J., and Singer, T. P. 1986. Inhibition of mitochondrial NADH dehydrogenase by pyridine derivatives and its possible relation to experimental and idiopathic parkinsonism. Biochem. Biophys. Res. Commun. 135:269-275.
    • (1986) Biochem. Biophys. Res. Commun. , vol.135 , pp. 269-275
    • Ramsay, R.R.1    Salach, J.I.2    Dadgar, J.3    Singer, T.P.4
  • 9
    • 0027504297 scopus 로고
    • Advances in our understanding of the mechanisms of the neurotoxicity of MPTP and related compounds
    • Tipton, K. F. and Singer, T. P. 1993. Advances in our understanding of the mechanisms of the neurotoxicity of MPTP and related compounds. J. Neurochem. 61:1191-1206.
    • (1993) J. Neurochem. , vol.61 , pp. 1191-1206
    • Tipton, K.F.1    Singer, T.P.2
  • 10
    • 0020680904 scopus 로고
    • Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis
    • Langston, J. W., Ballard, P., Tetrud, J. W., and Irwin, I. 1983. Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis. Science 219:979-980.
    • (1983) Science , vol.219 , pp. 979-980
    • Langston, J.W.1    Ballard, P.2    Tetrud, J.W.3    Irwin, I.4
  • 11
    • 0021337873 scopus 로고
    • Selective nigral toxicity after systemic administration of 1-methyl-4-phenyl-1,2,5,6-tetrahydropyrine (MPTP) in the squirrel monkey
    • Langston, J. W., Forno, L. S., Rebert, C. S., and Irwin, I. 1984. Selective nigral toxicity after systemic administration of 1-methyl-4-phenyl-1,2,5,6-tetrahydropyrine (MPTP) in the squirrel monkey. Brain Res. 292:390-394.
    • (1984) Brain Res. , vol.292 , pp. 390-394
    • Langston, J.W.1    Forno, L.S.2    Rebert, C.S.3    Irwin, I.4
  • 12
    • 0022477535 scopus 로고
    • Fate of nigrostriatal neurons in young mature mice given 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine: A neurochemical and morphological reassessment
    • Ricaurte, G. A., Langston, J. W., Delanney, L. E., Irwin, I., Peroutka, S. J., and Forno, L. S. 1986. Fate of nigrostriatal neurons in young mature mice given 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine: A neurochemical and morphological reassessment. Brain Res. 376:117-124.
    • (1986) Brain Res. , vol.376 , pp. 117-124
    • Ricaurte, G.A.1    Langston, J.W.2    Delanney, L.E.3    Irwin, I.4    Peroutka, S.J.5    Forno, L.S.6
  • 14
    • 0024848034 scopus 로고
    • Abnormalities of the electron transport chain in idiopathic Parkinson's disease
    • Parker, W. D. Jr., Boyson, S. J., and Parks, J. K. 1989. Abnormalities of the electron transport chain in idiopathic Parkinson's disease. Ann. Neurol. 26:719-723.
    • (1989) Ann. Neurol. , vol.26 , pp. 719-723
    • Parker Jr., W.D.1    Boyson, S.J.2    Parks, J.K.3
  • 17
    • 0026718086 scopus 로고
    • Brain, skeletal muscle and platelet homogenate mitochondrial function in Parkinson's disease
    • Mann, V. M., Cooper, J. M., Krige, D., Daniel, S. E., Schapira, A. H., and Marsden, C. D. 1992. Brain, skeletal muscle and platelet homogenate mitochondrial function in Parkinson's disease. Brain 115:333-342.
    • (1992) Brain , vol.115 , pp. 333-342
    • Mann, V.M.1    Cooper, J.M.2    Krige, D.3    Daniel, S.E.4    Schapira, A.H.5    Marsden, C.D.6
  • 19
    • 0031017696 scopus 로고    scopus 로고
    • Altered calcium homeostasis in cells transformed by mitochondria from individuals with Parkinson's disease
    • Sheehan, J. P., Swerdlow, R. H., Parker, W. D., Miller, S. W., Davis, R. E., and Tuttle, J. B. 1997. Altered calcium homeostasis in cells transformed by mitochondria from individuals with Parkinson's disease. J. Neurochem. 68:1221-1233.
    • (1997) J. Neurochem. , vol.68 , pp. 1221-1233
    • Sheehan, J.P.1    Swerdlow, R.H.2    Parker, W.D.3    Miller, S.W.4    Davis, R.E.5    Tuttle, J.B.6
  • 22
    • 0035341492 scopus 로고    scopus 로고
    • Parkinson's disease, pesticides and mitochondrial dysfunction
    • Jenner, P. 2001. Parkinson's disease, pesticides and mitochondrial dysfunction. Trends Neurosci. 24:245-247.
    • (2001) Trends Neurosci. , vol.24 , pp. 245-247
    • Jenner, P.1
  • 23
    • 0032904412 scopus 로고    scopus 로고
    • An evaluation of the role of mitochondria in neurodegenerative diseases: Mitochondrial mutations and oxidative pathology, protective nuclear responses, and cell death in neurodegeneration
    • Cassarino, D. S. and Bennett, J. P. Jr. 1999. An evaluation of the role of mitochondria in neurodegenerative diseases: Mitochondrial mutations and oxidative pathology, protective nuclear responses, and cell death in neurodegeneration. Brain Res. Brain Res. Rev. 29:1-25.
    • (1999) Brain Res. Brain Res. Rev. , vol.29 , pp. 1-25
    • Cassarino, D.S.1    Bennett Jr., J.P.2
  • 24
    • 0033032999 scopus 로고    scopus 로고
    • Mitochondrial involvement in Parkinson's disease. Huntington's disease, hereditary spastic paraplegia and Friedreich's ataxia
    • Schapira, A. H. 1999. Mitochondrial involvement in Parkinson's disease, Huntington's disease, hereditary spastic paraplegia and Friedreich's ataxia. Biochim. Biophys. Acta 1410:159-170.
    • (1999) Biochim. Biophys. Acta , vol.1410 , pp. 159-170
    • Schapira, A.H.1
  • 25
    • 0037096193 scopus 로고    scopus 로고
    • The relationship between oxidative/nitrative stress and pathological inclusions in Alzheimer's and Parkinson's disease
    • Giasson, B. I., Ischiropoulos, H., Lee, V. M., and Trojanowski, J. Q. 2002. The relationship between oxidative/nitrative stress and pathological inclusions in Alzheimer's and Parkinson's disease. Free Radic. Biol. Med. 32:1264-1275.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1264-1275
    • Giasson, B.I.1    Ischiropoulos, H.2    Lee, V.M.3    Trojanowski, J.Q.4
  • 26
    • 0037314215 scopus 로고    scopus 로고
    • Neuronal degeneration and mitochondrial dysfunction
    • Schon, E. A. and Manfredi, G. 2003. Neuronal degeneration and mitochondrial dysfunction. J. Clin. Invest 111:303-312.
    • (2003) J. Clin. Invest. , vol.111 , pp. 303-312
    • Schon, E.A.1    Manfredi, G.2
  • 29
    • 0028176592 scopus 로고
    • An immunohistochemical study on alpha-ketoglutarate dehydrogenase complex in Parkinson's disease
    • Mizuno, Y., Matuda, S., Yoshino, H., Mori, H., Hattori, N., and Ikebe, S. 1994. An immunohistochemical study on alpha-ketoglutarate dehydrogenase complex in Parkinson's disease. Ann. Neurol. 35:204-210.
    • (1994) Ann. Neurol. , vol.35 , pp. 204-210
    • Mizuno, Y.1    Matuda, S.2    Yoshino, H.3    Mori, H.4    Hattori, N.5    Ikebe, S.6
  • 30
    • 0026663828 scopus 로고
    • Mitochondrial ATP-synthase activity in cardiomyocytes after aerobic-anaerobic metabolic transition
    • Noll, T., Koop, A., and Piper, H. M. 1992. Mitochondrial ATP-synthase activity in cardiomyocytes after aerobic-anaerobic metabolic transition. Am. J. Physiol 262:C1297-C1303.
    • (1992) Am. J. Physiol. , vol.262
    • Noll, T.1    Koop, A.2    Piper, H.M.3
  • 31
    • 0025116342 scopus 로고
    • Mechanism of the neurotoxicity of MPTP: An update
    • Singer, T. P. and Ramsay, R. R. 1990. Mechanism of the neurotoxicity of MPTP: An update. FEBS Lett. 274:1-8.
    • (1990) FEBS Lett. , vol.274 , pp. 1-8
    • Singer, T.P.1    Ramsay, R.R.2
  • 32
    • 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
  • 33
    • 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
  • 34
    • 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
  • 35
    • 0018864653 scopus 로고
    • Energy transduction in intact synaptosomes: Influence of plasma-membrane depolarization on the respiration and membrane potential of internal mitochondria determined in situ
    • Scott, I. D. and Nicholls, D. G. 1980. Energy transduction in intact synaptosomes: Influence of plasma-membrane depolarization on the respiration and membrane potential of internal mitochondria determined in situ. Biochem. J. 186:21-33.
    • (1980) Biochem. J. , vol.186 , pp. 21-33
    • Scott, I.D.1    Nicholls, D.G.2
  • 36
    • 0029827804 scopus 로고    scopus 로고
    • Mitochondria, calcium regulation, and acute glutamate excitotoxicity in cultured cerebellar granule cells
    • Budd, S. L. and Nicholls, D. G. 1996. Mitochondria, calcium regulation, and acute glutamate excitotoxicity in cultured cerebellar granule cells. J. Neurochem. 67:2282-2291.
    • (1996) J. Neurochem. , vol.67 , pp. 2282-2291
    • Budd, S.L.1    Nicholls, D.G.2
  • 37
    • 0033522924 scopus 로고    scopus 로고
    • Titrating the effects of mitochondrial complex I impairment in the cell physiology
    • Barrientos, A. and Moraes, C. T. 1999. Titrating the effects of mitochondrial complex I impairment in the cell physiology. J. Biol. Chem. 274:16188-16197.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16188-16197
    • Barrientos, A.1    Moraes, C.T.2
  • 38
    • 0029125857 scopus 로고
    • Aging, energy, and oxidative stress in neurodegenerative diseases
    • Beal, M. F. 1995. Aging, energy, and oxidative stress in neurodegenerative diseases. Ann. Neurol. 38:357-366.
    • (1995) Ann. Neurol. , vol.38 , pp. 357-366
    • Beal, M.F.1
  • 39
    • 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
  • 40
    • 0003234960 scopus 로고
    • Mitochondrial dysfunction in neurodegenerative disorders and aging
    • Schapira, A. H. and DiMauro, S. (eds.), Butterworth-Heinemann, Oxford
    • Schapira, A. H. 1994. Mitochondrial dysfunction in neurodegenerative disorders and aging. Pages 227-244, in Schapira, A. H. and DiMauro, S. (eds.), Mitochondrial Disorders in Neurology, Butterworth-Heinemann, Oxford.
    • (1994) Mitochondrial Disorders in Neurology , pp. 227-244
    • Schapira, A.H.1
  • 41
    • 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
  • 42
    • 0000163281 scopus 로고    scopus 로고
    • Antioxydant defence enzymes: The gluthatione peroxidase family
    • Halliwell, B. and Gutteridge, J. M. C. (eds.), Oxford University Press, Oxford
    • Halliwell, B. and Gutteridge, J. M. C. 1999. Antioxydant defence enzymes: The gluthatione peroxidase family. Pages 140-146, in Halliwell, B. and Gutteridge, J. M. C. (eds.), Free Radicals in Biology and Medicine, Oxford University Press, Oxford.
    • (1999) Free Radicals in Biology and Medicine , pp. 140-146
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 43
    • 0021167030 scopus 로고
    • The role of hydroperoxides as calcium release agents in rat brain mitochondria
    • Satrustegui, J. and Richter, C. 1984. The role of hydroperoxides as calcium release agents in rat brain mitochondria. Arch. Biochem. Biophys. 233:736-740.
    • (1984) Arch. Biochem. Biophys. , vol.233 , pp. 736-740
    • Satrustegui, J.1    Richter, C.2
  • 44
    • 0029990439 scopus 로고    scopus 로고
    • Astrocytes protect neurons from hydrogen peroxide toxicity
    • Desagher, S., Glowinski, J., and Premont, J. 1996. Astrocytes protect neurons from hydrogen peroxide toxicity. J. Neurosci. 16:2553-2562.
    • (1996) J. Neurosci. , vol.16 , pp. 2553-2562
    • Desagher, S.1    Glowinski, J.2    Premont, J.3
  • 45
    • 0032974143 scopus 로고    scopus 로고
    • The glutathione system of peroxide detoxification is less efficient in neurons than in astroglial cells
    • Dringen, R., Kussmaul, L., Gutterer, J. M., Hirrlinger, J., and Hamprecht, B. 1999. The glutathione system of peroxide detoxification is less efficient in neurons than in astroglial cells. J. Neurochem. 72:2523-2530.
    • (1999) J. Neurochem. , vol.72 , pp. 2523-2530
    • Dringen, R.1    Kussmaul, L.2    Gutterer, J.M.3    Hirrlinger, J.4    Hamprecht, B.5
  • 47
    • 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
  • 48
    • 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
  • 49
    • 0020308323 scopus 로고
    • Parkinson's disease: A disorder due to nigral glutathione deficiency?
    • Perry, T. L., Godin, D. V., and Hansen, S. 1982. Parkinson's disease: A disorder due to nigral glutathione deficiency? Neurosci. Lett. 33:305-310.
    • (1982) Neurosci. Lett. , vol.33 , pp. 305-310
    • Perry, T.L.1    Godin, D.V.2    Hansen, S.3
  • 50
    • 0022553605 scopus 로고
    • Idiopathic Parkinson's disease, progressive supranuclear palsy and glutathione metabolism in the substantia nigra of patients
    • Perry, T. L. and Yong, V. W. 1986. Idiopathic Parkinson's disease, progressive supranuclear palsy and glutathione metabolism in the substantia nigra of patients. Neurosci. Lett. 67:269-274.
    • (1986) Neurosci. Lett. , vol.67 , pp. 269-274
    • Perry, T.L.1    Yong, V.W.2
  • 51
    • 0026514643 scopus 로고
    • What process causes nigral cell death in Parkinson's disease?
    • Jenner, P. 1992. What process causes nigral cell death in Parkinson's disease? Neurol. Clin. 10:387-403.
    • (1992) Neurol. Clin. , vol.10 , pp. 387-403
    • Jenner, P.1
  • 52
    • 0024321178 scopus 로고
    • A selective increase in particulate superoxide dismutase activity in parkinsonian substantia nigra
    • Saggu, H., Cooksey, J., Dexter, D., Wells, F. R., Lees, A., Jenner, P., and Marsden, C. D. 1989. A selective increase in particulate superoxide dismutase activity in parkinsonian substantia nigra. J. Neurochem. 53:692-697.
    • (1989) J. Neurochem. , vol.53 , pp. 692-697
    • Saggu, H.1    Cooksey, J.2    Dexter, D.3    Wells, F.R.4    Lees, A.5    Jenner, P.6    Marsden, C.D.7
  • 54
    • 0026683140 scopus 로고
    • Enhanced hydroxyl radical generation by 2′-methyl analog of MPTP: Suppression by clorgyline and deprenyl
    • Chiueh, C. C., Huang, S. J., and Murphy, D. L. 1992. Enhanced hydroxyl radical generation by 2′-methyl analog of MPTP: Suppression by clorgyline and deprenyl. Synapse 11:346-348.
    • (1992) Synapse , vol.11 , pp. 346-348
    • Chiueh, C.C.1    Huang, S.J.2    Murphy, D.L.3
  • 55
    • 0027171873 scopus 로고
    • MPP+ and MPDP+ induced oxygen radical formation with mitochondrial enzymes
    • Adams, J. D. Jr., Klaidman, L. K., and Leung, A. C. 1993. MPP+ and MPDP+ induced oxygen radical formation with mitochondrial enzymes. Free Radic. Biol. Med. 15:181-186.
    • (1993) Free Radic. Biol. Med. , vol.15 , pp. 181-186
    • Adams Jr., J.D.1    Klaidman, L.K.2    Leung, A.C.3
  • 56
    • 0027941334 scopus 로고
    • MPTP-induced oxidative stress and neurotoxicity are age-dependent: Evidence from measures of reactive oxygen species and striatal dopamine levels
    • Ali, S. F., David, S. N., Newport, G. D., Cadet, J. L., and Slikker, W. Jr. 1994. MPTP-induced oxidative stress and neurotoxicity are age-dependent: Evidence from measures of reactive oxygen species and striatal dopamine levels. Synapse 18:27-34.
    • (1994) Synapse , vol.18 , pp. 27-34
    • Ali, S.F.1    David, S.N.2    Newport, G.D.3    Cadet, J.L.4    Slikker Jr., W.5
  • 58
    • 0028971624 scopus 로고
    • Effect of MPTP and L-deprenyl on antioxidant enzymes and lipid peroxidation levels in mouse brain
    • Thiffault, C., Aumont, N., Quirion, R., and Poirier, J. 1995. Effect of MPTP and L-deprenyl on antioxidant enzymes and lipid peroxidation levels in mouse brain. J. Neurochem. 65:2725-2733.
    • (1995) J. Neurochem. , vol.65 , pp. 2725-2733
    • Thiffault, C.1    Aumont, N.2    Quirion, R.3    Poirier, J.4
  • 61
    • 0026635461 scopus 로고
    • Oxidative stress as a cause of nigral cell death in Parkinson's disease and incidental Lewy body disease: The Royal Kings and Queens Parkinson's Disease Research Group
    • Jenner, P., Dexter, D. T., Sian, J., Schapira, A. H., and Marsden, C. D. 1992. Oxidative stress as a cause of nigral cell death in Parkinson's disease and incidental Lewy body disease: The Royal Kings and Queens Parkinson's Disease Research Group. Ann. Neurol. 32(Suppl):S82-S87.
    • (1992) Ann. Neurol. , vol.32 , Issue.SUPPL.
    • Jenner, P.1    Dexter, D.T.2    Sian, J.3    Schapira, A.H.4    Marsden, C.D.5
  • 63
    • 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
  • 64
    • 0018837597 scopus 로고
    • Enhancement of hydrogen peroxide formation by protophores and ionophores in antimycin-supplemented mitochondria
    • Cadenas, E. and Boveris, A. 1980. Enhancement of hydrogen peroxide formation by protophores and ionophores in antimycin-supplemented mitochondria. Biochem. J. 188:31-37.
    • (1980) Biochem. J. , vol.188 , pp. 31-37
    • Cadenas, E.1    Boveris, A.2
  • 65
    • 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
  • 66
    • 0034740585 scopus 로고    scopus 로고
    • DeltaPsi(m)-dependent and -independent production of reactive oxygen species by rat brain mitochondria
    • Votyakova, T. V. and Reynolds, I. J. 2001. DeltaPsi(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
  • 67
    • 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
  • 68
    • 0037269343 scopus 로고    scopus 로고
    • Quantitative relationship between inhibition of respiratory complexes and formation of reactive oxygen species in isolated nerve terminals
    • Sipos, I., Tretter, L., and Adam-Vizi, V. 2003. Quantitative relationship between inhibition of respiratory complexes and formation of reactive oxygen species in isolated nerve terminals. J. Neurochem. 84:112-118.
    • (2003) J. Neurochem. , vol.84 , pp. 112-118
    • Sipos, I.1    Tretter, L.2    Adam-Vizi, V.3
  • 69
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals: I. General aspects
    • Davies, K. J. 1987. Protein damage and degradation by oxygen radicals: I. general aspects. J. Biol. Chem. 262:9895-9901.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9895-9901
    • Davies, K.J.1
  • 70
    • 0021759809 scopus 로고
    • Free radicals, lipid peroxidation, and cell damage
    • Halliwell, B. and Gutteridge, J. M. 1984. Free radicals, lipid peroxidation, and cell damage. Lancet 2:1095.
    • (1984) Lancet , vol.2 , pp. 1095
    • Halliwell, B.1    Gutteridge, J.M.2
  • 71
    • 0028927261 scopus 로고
    • Reactions of oxyl radicals with DNA
    • Breen, A. P. and Murphy, J. A. 1995. Reactions of oxyl radicals with DNA. Free Radic. Biol. Med. 18:1033-1077.
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 1033-1077
    • Breen, A.P.1    Murphy, J.A.2
  • 72
    • 0028064964 scopus 로고
    • Effects of 1-methyl-4-phenylpyridinium on isolated rat brain mitochondria: Evidence for a primary involvement of energy depletion
    • Bates, T. E., Heales, S. J., Davies, S. E., Boakye, P., and Clark, J. B. 1994. Effects of 1-methyl-4-phenylpyridinium on isolated rat brain mitochondria: Evidence for a primary involvement of energy depletion. J. Neurochem. 63:640-648.
    • (1994) J. Neurochem. , vol.63 , pp. 640-648
    • Bates, T.E.1    Heales, S.J.2    Davies, S.E.3    Boakye, P.4    Clark, J.B.5
  • 73
    • 0028952832 scopus 로고
    • Effect of peroxynitrite on the mitochondrial respiratory chain: Differential susceptibility of neurones and astrocytes in primary culture
    • Bolanos, J. P., Heales, S. J., Land, J. M., and Clark, J. B. 1995. Effect of peroxynitrite on the mitochondrial respiratory chain: Differential susceptibility of neurones and astrocytes in primary culture. J. Neurochem. 64:1965-1972.
    • (1995) J. Neurochem. , vol.64 , pp. 1965-1972
    • Bolanos, J.P.1    Heales, S.J.2    Land, J.M.3    Clark, J.B.4
  • 75
    • 0029910556 scopus 로고    scopus 로고
    • Nitric oxide-mediated mitochondrial damage: A potential neuroprotective role for glutathione
    • Bolanos, J. P., Heales, S. J., Peuchen, S., Barker, J. E., Land, J. M., and Clark, J. B. 1996. Nitric oxide-mediated mitochondrial damage: A potential neuroprotective role for glutathione. Free Radic. Biol. Med. 21:995-1001.
    • (1996) Free Radic. Biol. Med. , vol.21 , pp. 995-1001
    • Bolanos, J.P.1    Heales, S.J.2    Peuchen, S.3    Barker, J.E.4    Land, J.M.5    Clark, J.B.6
  • 77
    • 0036479054 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in acute neurodegeneration
    • Friberg, H. and Wieloch, T. 2002. Mitochondrial permeability transition in acute neurodegeneration. Biochimie 84:241-250.
    • (2002) Biochimie , vol.84 , pp. 241-250
    • Friberg, H.1    Wieloch, T.2
  • 78
    • 0033000269 scopus 로고    scopus 로고
    • Depolarization of in situ mitochondria due to hydrogen peroxide-induced oxidative stress in nerve terminals: Inhibition of alpha-ketoglutarate dehydrogenase
    • Chinopoulos, C., Tretter, L., and Adam-Vizi, V. 1999. Depolarization of in situ mitochondria due to hydrogen peroxide-induced oxidative stress in nerve terminals: Inhibition of alpha-ketoglutarate dehydrogenase. J. Neurochem. 73:220-228.
    • (1999) J. Neurochem. , vol.73 , pp. 220-228
    • Chinopoulos, C.1    Tretter, L.2    Adam-Vizi, V.3
  • 80
    • 0030658986 scopus 로고    scopus 로고
    • Enhanced depolarization-evoked calcium signal and reduced [ATP]/[ADP] ratio are unrelated events induced by oxidative stress in synaptosomes
    • Tretter, L., Chinopoulos, C., and Adam-Vizi, V. 1997. Enhanced depolarization-evoked calcium signal and reduced [ATP]/[ADP] ratio are unrelated events induced by oxidative stress in synaptosomes. J. Neurochem. 69:2529-2537.
    • (1997) J. Neurochem. , vol.69 , pp. 2529-2537
    • Tretter, L.1    Chinopoulos, C.2    Adam-Vizi, V.3
  • 81
    • 0023874677 scopus 로고
    • Mechanisms of oxidant-mediated cell injury: The glycolytic and mitochondrial pathways of ADP phosphorylation are major intracellular targets inactivated by hydrogen peroxide
    • Hyslop, P. A., Hinshaw, D. B., Halsey, W. A. Jr., Schraufstatter, I. U., Sauerheber, R. D., Spragg, R. G., Jackson, J. H., and Cochrane, C. G. 1988. Mechanisms of oxidant-mediated cell injury: The glycolytic and mitochondrial pathways of ADP phosphorylation are major intracellular targets inactivated by hydrogen peroxide. J. Biol. Chem. 263:1665-1675.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1665-1675
    • Hyslop, P.A.1    Hinshaw, D.B.2    Halsey Jr., W.A.3    Schraufstatter, I.U.4    Sauerheber, R.D.5    Spragg, R.G.6    Jackson, J.H.7    Cochrane, C.G.8
  • 82
    • 0027157981 scopus 로고
    • Hydrogen peroxide-induced oxidative stress to the mammalian heart-muscle cell (cardiomyocyte): Nonperoxidative purine and pyrimidine nucleotide depletion
    • Janero, D. R., Hreniuk, D., and Sharif, H. M. 1993. Hydrogen peroxide-induced oxidative stress to the mammalian heart-muscle cell (cardiomyocyte): Nonperoxidative purine and pyrimidine nucleotide depletion. J. Cell Physiol. 155:494-504.
    • (1993) J. Cell Physiol. , vol.155 , pp. 494-504
    • Janero, D.R.1    Hreniuk, D.2    Sharif, H.M.3
  • 83
    • 0034671429 scopus 로고    scopus 로고
    • Inhibition of Krebs cycle enzymes by hydrogen peroxide: A key role of [alpha]-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 [alpha]-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
  • 84
    • 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
  • 85
    • 0030052530 scopus 로고    scopus 로고
    • Requirement for superoxide in excitotoxic cell death
    • Patel, M., Day, B. J., Crapo, J. D., Fridovich, I., and McNamara, J. O. 1996. Requirement for superoxide in excitotoxic cell death. Neuron 16:345-355.
    • (1996) Neuron , vol.16 , pp. 345-355
    • Patel, M.1    Day, B.J.2    Crapo, J.D.3    Fridovich, I.4    McNamara, J.O.5
  • 86
    • 0029819752 scopus 로고    scopus 로고
    • Measuring nitrix oxide and superoxide: Rate constants for aconitase activity
    • Hausladen, A. and Fridovich, I. 1996. Measuring nitrix oxide and superoxide: Rate constants for aconitase activity. Methods Enzymol. 269:37-41.
    • (1996) Methods Enzymol. , vol.269 , pp. 37-41
    • Hausladen, A.1    Fridovich, I.2
  • 87
    • 0032547309 scopus 로고    scopus 로고
    • Inactivation of aconitase and oxoglutarate dehydrogenase 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 dehydrogenase 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
  • 88
    • 0034669186 scopus 로고    scopus 로고
    • Mitochondrial superoxide production in kainate-induced hippocampal damage
    • Liang, L. P., Ho, Y. S., and Patel, M. 2000. Mitochondrial superoxide production in kainate-induced hippocampal damage. Neuroscience 101:563-570.
    • (2000) Neuroscience , vol.101 , pp. 563-570
    • Liang, L.P.1    Ho, Y.S.2    Patel, M.3
  • 89
    • 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
  • 90
    • 0039174315 scopus 로고    scopus 로고
    • Mitochondrial aconitase is a source of hydroxyl radical: An electron spin resonance investigation
    • Vasquez-Vivar, J., Kalyanaraman, B., and Kennedy, M. C. 2000. Mitochondrial aconitase is a source of hydroxyl radical: An electron spin resonance investigation. 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
  • 91
    • 0032506040 scopus 로고    scopus 로고
    • Selective inactivation of alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase: Reaction of lipoic acid with 4-hydroxy-2-nonenal
    • Humphries, K. M. and Szweda, L. I. 1998. Selective inactivation of alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase: Reaction of lipoic acid with 4-hydroxy-2-nonenal. Biochemistry 37:15835-15841.
    • (1998) Biochemistry , vol.37 , pp. 15835-15841
    • Humphries, K.M.1    Szweda, L.I.2
  • 92
    • 0033048258 scopus 로고    scopus 로고
    • Metabolic impairment induces oxidative stress, compromises inflammatory responses, and inactivates a key mitochondrial enzyme in microglia
    • Park, L. C., Zhang, H., Sheu, K. F., Calingasan, N. Y., Kristal, B. S., Lindsay, J. G., and Gibson, G. E. 1999. Metabolic impairment induces oxidative stress, compromises inflammatory responses, and inactivates a key mitochondrial enzyme in microglia. J. Neurochem. 72:1948-1958.
    • (1999) J. Neurochem. , vol.72 , pp. 1948-1958
    • Park, L.C.1    Zhang, H.2    Sheu, K.F.3    Calingasan, N.Y.4    Kristal, B.S.5    Lindsay, J.G.6    Gibson, G.E.7
  • 94
    • 0023111239 scopus 로고
    • Inhibition of mitochondrial alpha-ketoglutarate dehydrogenase by 1-methyl-4-phenylpyridinium ion
    • Mizuno, Y., Saitoh, T., and Sone, N. 1987. Inhibition of mitochondrial alpha-ketoglutarate dehydrogenase by 1-methyl-4-phenylpyridinium ion. Biochem. Biophys. Res. Commun. 143:971-976.
    • (1987) Biochem. Biophys. Res. Commun. , vol.143 , pp. 971-976
    • Mizuno, Y.1    Saitoh, T.2    Sone, N.3
  • 95
    • 0034653388 scopus 로고    scopus 로고
    • Exacerbated responses to oxidative stress by an Na(+) load in isolated nerve terminals: The role of ATP depletion and rise of [Ca(2+)](i)
    • Chinopoulos, C., Tretter, L., Rozsa, A., and Adam-Vizi, V. 2000. Exacerbated responses to oxidative stress by an Na(+) load in isolated nerve terminals: The role of ATP depletion and rise of [Ca(2+)](i). J. Neurosci. 20:2094-2103.
    • (2000) J. Neurosci. , vol.20 , pp. 2094-2103
    • Chinopoulos, C.1    Tretter, L.2    Rozsa, A.3    Adam-Vizi, V.4
  • 96
    • 0029737355 scopus 로고    scopus 로고
    • + channels, glutamate release, and NMDA receptors mediates delayed neurodegeneration through nitric oxide formation
    • + channels, glutamate release, and NMDA receptors mediates delayed neurodegeneration through nitric oxide formation. J. Neurosci. 16:5004-5013.
    • (1996) J. Neurosci. , vol.16 , pp. 5004-5013
    • Strijbos, P.J.1    Leach, M.J.2    Garthwaite, J.3
  • 97
    • 0031797319 scopus 로고    scopus 로고
    • Effects of oxidants and glutamate receptor activation on mitochondrial membrane potential in rat forebrain neurons
    • Scanlon, J. M. and Reynolds, I. J. 1998. Effects of oxidants and glutamate receptor activation on mitochondrial membrane potential in rat forebrain neurons. J. Neurochem. 71:2392-2400.
    • (1998) J. Neurochem. , vol.71 , pp. 2392-2400
    • Scanlon, J.M.1    Reynolds, I.J.2
  • 98
    • 0029052829 scopus 로고
    • A selective toxicity toward cultured mesencephalic dopaminergic neurons is induced by the synergistic effects of energetic metabolism impairment and NMDA receptor activation
    • Marey-Semper, I., Gelman, M., and Levi-Strauss, M. 1995. A selective toxicity toward cultured mesencephalic dopaminergic neurons is induced by the synergistic effects of energetic metabolism impairment and NMDA receptor activation. J. Neurosci. 15:5912-5918.
    • (1995) J. Neurosci. , vol.15 , pp. 5912-5918
    • Marey-Semper, I.1    Gelman, M.2    Levi-Strauss, M.3
  • 99
    • 0027221998 scopus 로고
    • NMDA-dependent superoxide production and neurotoxicity
    • Lafon-Cazal, M., Pietri, S., Culcasi, M., and Bockaert, J. 1993. NMDA-dependent superoxide production and neurotoxicity. Nature 364:535-537.
    • (1993) Nature , vol.364 , pp. 535-537
    • Lafon-Cazal, M.1    Pietri, S.2    Culcasi, M.3    Bockaert, J.4
  • 100
    • 0028882764 scopus 로고
    • Mitochondrial production of reactive oxygen species in cortical neurons following exposure to N-methyl-D-aspartate
    • Dugan, L. L., Sensi, S. L., Canzoniero, L. M., Handran, S. D., Rothman, S. M., Lin, T. S., Goldberg, M. P., and Choi, D. W. 1995. Mitochondrial production of reactive oxygen species in cortical neurons following exposure to N-methyl-D-aspartate. J. Neurosci. 15:6377-6388.
    • (1995) J. Neurosci. , vol.15 , pp. 6377-6388
    • Dugan, L.L.1    Sensi, S.L.2    Canzoniero, L.M.3    Handran, S.D.4    Rothman, S.M.5    Lin, T.S.6    Goldberg, M.P.7    Choi, D.W.8
  • 101
    • 0029064518 scopus 로고
    • Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation
    • Reynolds, I. J. and Hastings, T. G. 1995. Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation. J. Neurosci. 15:3318-3327.
    • (1995) J. Neurosci. , vol.15 , pp. 3318-3327
    • Reynolds, I.J.1    Hastings, T.G.2
  • 102
    • 0018148688 scopus 로고
    • Autoxidation versus covalent binding of quinones as the mechanism of toxicity of dopamine, 6-hydroxydopamine, and related compounds toward C1300 neuroblastoma cells in vitro
    • Graham, D. G., Tiffany, S. M., Bell, W. R. Jr., and Gutknecht, W. F. 1978. Autoxidation versus covalent binding of quinones as the mechanism of toxicity of dopamine, 6-hydroxydopamine, and related compounds toward C1300 neuroblastoma cells in vitro. Mol. Pharmacol. 14:644-653.
    • (1978) Mol. Pharmacol. , vol.14 , pp. 644-653
    • Graham, D.G.1    Tiffany, S.M.2    Bell Jr., W.R.3    Gutknecht, W.F.4
  • 103
    • 0032842038 scopus 로고    scopus 로고
    • Dopamine oxidation alters mitochondrial respiration and induces permeability transition in brain mitochondria: Implications for Parkinson's disease
    • Berman, S. B. and Hastings, T. G. 1999. Dopamine oxidation alters mitochondrial respiration and induces permeability transition in brain mitochondria: Implications for Parkinson's disease. J. Neurochem. 73:1127-1137.
    • (1999) J. Neurochem. , vol.73 , pp. 1127-1137
    • Berman, S.B.1    Hastings, T.G.2
  • 104
    • 0031010596 scopus 로고    scopus 로고
    • Parkinson disease: A new link between monoamine oxidase and mitochondrial electron flow
    • Cohen, G., Farooqui, R., and Kesler, N. 1997. Parkinson disease: A new link between monoamine oxidase and mitochondrial electron flow. Proc. Natl. Acad. Sci. USA 94:4890-4894.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4890-4894
    • Cohen, G.1    Farooqui, R.2    Kesler, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.