메뉴 건너뛰기




Volumn 7, Issue 5-6, 2005, Pages 662-672

Energy status, ubiquitin proteasomal function, and oxidative stress during chronic and acute complex I inhibition with rotenone in mesencephalic cultures

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CHYMOTRYPSIN; DOPAMINE; FREE RADICAL; GLUCOSE; LACTIC ACID; NEURON SPECIFIC ENOLASE; PROTEASOME; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); ROTENONE; TYROSINE 3 MONOOXYGENASE; UBIQUITIN;

EID: 17644411438     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2005.7.662     Document Type: Article
Times cited : (22)

References (55)
  • 1
    • 0033522924 scopus 로고    scopus 로고
    • Titrating the effects of mitochondrial complex 1 impairment in the cell physiology
    • Barrientos A and Moraes CT. Titrating the effects of mitochondrial complex 1 impairment in the cell physiology. J Biol Chem 274: 16188-16197, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 16188-16197
    • Barrientos, A.1    Moraes, C.T.2
  • 4
    • 0037227378 scopus 로고    scopus 로고
    • Mitochondrial complex inhibitors preferentially damage substantia nigra dopamine neurons in rat brain slices
    • Bywood PT and Johnson SM. Mitochondrial complex inhibitors preferentially damage substantia nigra dopamine neurons in rat brain slices. Exp Neurol 179: 47-59, 2002.
    • (2002) Exp Neurol , vol.179 , pp. 47-59
    • Bywood, P.T.1    Johnson, S.M.2
  • 5
    • 0018992813 scopus 로고
    • ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation
    • Ciechanover A, Heller H, Elias S, Haas AL, and Hershko A. ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation. Proc Natl Acad Sci USA 77: 1365-1368, 1980.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1365-1368
    • Ciechanover, A.1    Heller, H.2    Elias, S.3    Haas, A.L.4    Hershko, A.5
  • 6
    • 0021140995 scopus 로고
    • Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85
    • Ciechanover A, Finley D, and Varshavsky A. Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85. Cell 37: 57-66, 1984.
    • (1984) Cell , vol.37 , pp. 57-66
    • Ciechanover, A.1    Finley, D.2    Varshavsky, A.3
  • 7
    • 0032557511 scopus 로고    scopus 로고
    • Energy thresholds in brain mitochondria. Potential involvement in neurodegeneration
    • Davey GP, Peuchen S, and Clark JB. Energy thresholds in brain mitochondria. Potential involvement in neurodegeneration. J Biol Chem 273: 12753-12757, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 12753-12757
    • Davey, G.P.1    Peuchen, S.2    Clark, J.B.3
  • 8
    • 0015714956 scopus 로고
    • Metabolic alterations in brain during anoxic-anoxia and subsequent recovery
    • Drewes L, Gilboe DD, and Betz LA. Metabolic alterations in brain during anoxic-anoxia and subsequent recovery. Arch Neurol 29: 385-390, 1973.
    • (1973) Arch Neurol , vol.29 , pp. 385-390
    • Drewes, L.1    Gilboe, D.D.2    Betz, L.A.3
  • 9
    • 0027429163 scopus 로고
    • Damage to neurons in culture following medium change: Role of glutamine and extracellular generation of glutamate
    • Driscoll BF, Deibler GE, Law MJ, and Crane AM. Damage to neurons in culture following medium change: role of glutamine and extracellular generation of glutamate. J Neurochem 61: 1795-1800, 1993.
    • (1993) J Neurochem , vol.61 , pp. 1795-1800
    • Driscoll, B.F.1    Deibler, G.E.2    Law, M.J.3    Crane, A.M.4
  • 10
    • 0034975804 scopus 로고    scopus 로고
    • Hydrogen peroxide removal and glutathione mixed disulfide formation during metabolic inhibition in mesencephalic cultures
    • Ehrhart J and Zeevalk GD. Hydrogen peroxide removal and glutathione mixed disulfide formation during metabolic inhibition in mesencephalic cultures. J Neurochem 77: 1496-1507, 2001.
    • (2001) J Neurochem , vol.77 , pp. 1496-1507
    • Ehrhart, J.1    Zeevalk, G.D.2
  • 11
    • 0027512740 scopus 로고
    • Physiological stimulation increases nonoxidative glucose metabolism in the brain of the freely moving rat
    • Fellows LK, Boutelle MG, and Fillenze M. Physiological stimulation increases nonoxidative glucose metabolism in the brain of the freely moving rat. J Neurochem 60: 1258-1263, 1993.
    • (1993) J Neurochem , vol.60 , pp. 1258-1263
    • Fellows, L.K.1    Boutelle, M.G.2    Fillenze, M.3
  • 12
    • 0029688041 scopus 로고    scopus 로고
    • Electron microscopy of Lewy bodies in the amygdala-parahippocampal region
    • Forno LS, DeLanney IE, Irwin I, and Langston JW. Electron microscopy of Lewy bodies in the amygdala-parahippocampal region. Adv Neurol 69: 217-228, 1996.
    • (1996) Adv Neurol , vol.69 , pp. 217-228
    • Forno, L.S.1    DeLanney, I.E.2    Irwin, I.3    Langston, J.W.4
  • 13
    • 0023780085 scopus 로고
    • Non-oxidative glucose consumption during focal physiologic neural activity
    • Fox PT, Raichle ME, Mintun MA, and Dence C. Non-oxidative glucose consumption during focal physiologic neural activity. Science 241: 462-464, 1988.
    • (1988) Science , vol.241 , pp. 462-464
    • Fox, P.T.1    Raichle, M.E.2    Mintun, M.A.3    Dence, C.4
  • 14
    • 0036470165 scopus 로고    scopus 로고
    • Distinct role for microglia in rotenone-induced degeneration of dopaminergic neurons
    • Gao H-M, Hong J-S, Zhang W, and Liu B. Distinct role for microglia in rotenone-induced degeneration of dopaminergic neurons. J Neurosci 22: 782-790, 2002.
    • (2002) J Neurosci , vol.22 , pp. 782-790
    • Gao, H.-M.1    Hong, J.-S.2    Zhang, W.3    Liu, B.4
  • 15
    • 0030982143 scopus 로고    scopus 로고
    • Degradation of oxidized proteins in mammalian cells
    • Grune T, Reinheckel T, and Davies KJA. Degradation of oxidized proteins in mammalian cells. FASEB J 11: 526-534, 1997.
    • (1997) FASEB J , vol.11 , pp. 526-534
    • Grune, T.1    Reinheckel, T.2    Davies, K.J.A.3
  • 16
    • 0029050583 scopus 로고
    • Low platelet mitochondrial complex I and complex II/III activity in early untreated Parkinson's disease
    • Haas RH, Nasirian F, Nakano K, Ward D, Pay RN, Hill R, and Shults CW. Low platelet mitochondrial complex I and complex II/III activity in early untreated Parkinson's disease. Ann Neurol 37: 714-722, 1995.
    • (1995) Ann Neurol , vol.37 , pp. 714-722
    • Haas, R.H.1    Nasirian, F.2    Nakano, K.3    Ward, D.4    Pay, R.N.5    Hill, R.6    Shults, C.W.7
  • 17
    • 0021280826 scopus 로고
    • Dopaminergic neurotoxicity of 1-methyl-4-phenyl-1,2,5,6- tetrahydropyridine in mice
    • Heikkila RE, Hess A, and Duvoisin RC. Dopaminergic neurotoxicity of 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine in mice. Science 224: 1451-1453, 1984.
    • (1984) Science , vol.224 , pp. 1451-1453
    • Heikkila, R.E.1    Hess, A.2    Duvoisin, R.C.3
  • 18
    • 0031771518 scopus 로고    scopus 로고
    • Interaction of alpha-phenyl-N-tert-butyl nitrone and alternative electron acceptors with complex I indicates a substrate reduction site upstream from the rotenone binding site
    • Hensley K, Pye QN, Maidt ML, Stewart CA, Robinson KA, Jaffrey F, and Floyd RA. Interaction of alpha-phenyl-N-tert-butyl nitrone and alternative electron acceptors with complex I indicates a substrate reduction site upstream from the rotenone binding site. J Neurochem 71: 2549-2557, 1998.
    • (1998) J Neurochem , vol.71 , pp. 2549-2557
    • Hensley, K.1    Pye, Q.N.2    Maidt, M.L.3    Stewart, C.A.4    Robinson, K.A.5    Jaffrey, F.6    Floyd, R.A.7
  • 19
    • 0019000271 scopus 로고
    • Proposed role of ATP in protein breakdown: Conjugation of proteins with miltiple chains of the polypeptide of ATP-dependent proteolysis
    • Hershko A, Ciechanover A, Heller H, Haas AL, and Rose IA. Proposed role of ATP in protein breakdown: conjugation of proteins with miltiple chains of the polypeptide of ATP-dependent proteolysis. Proc Natl Acad Sci USA 77: 1783-1786, 1980.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1783-1786
    • Hershko, A.1    Ciechanover, A.2    Heller, H.3    Haas, A.L.4    Rose, I.A.5
  • 22
    • 0020680904 scopus 로고
    • Chronic parkinsonism in humans due to a product of meperidine analog synthesis
    • Langston JW, Ballard PA, Tetrud JW, and Irwin I. Chronic parkinsonism in humans due to a product of meperidine analog synthesis. Science 219: 979-980, 1983.
    • (1983) Science , vol.219 , pp. 979-980
    • Langston, J.W.1    Ballard, P.A.2    Tetrud, J.W.3    Irwin, I.4
  • 23
    • 0021337873 scopus 로고
    • Selective nigral toxicity after systemic administration of 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine (MPTP) in the squirrel monkey
    • Langsten JW, Forno LS, Rebert CS, and Irwin I. Selective nigral toxicity after systemic administration of 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine (MPTP) in the squirrel monkey. Brain Res 292: 390-394, 1984.
    • (1984) Brain Res , vol.292 , pp. 390-394
    • Langsten, J.W.1    Forno, L.S.2    Rebert, C.S.3    Irwin, I.4
  • 26
    • 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 JA, and Robinson JP. Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production. J Biol Chem 278: 8516-8525, 2003.
    • (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
  • 28
    • 0024386801 scopus 로고
    • 1-Methyl-4-(2′-methylphenyl)-1,2,3,6-tetrahydropyridine (2′CH3-MPTP)-induced degeneration of mesostriatal dopaminergic neurons in the mouse: Biochemical and neuroanatomical studies
    • Manaye KF, Sonsalla PK, Barnett G, Heikkila RE, Woodward DJ, Smith WK, and German DC. 1-Methyl-4-(2′-methylphenyl)-1,2,3,6-tetrahydropyridine (2′CH3-MPTP)-induced degeneration of mesostriatal dopaminergic neurons in the mouse: biochemical and neuroanatomical studies. Brain Res 491: 307-315, 1989.
    • (1989) Brain Res , vol.491 , pp. 307-315
    • Manaye, K.F.1    Sonsalla, P.K.2    Barnett, G.3    Heikkila, R.E.4    Woodward, D.J.5    Smith, W.K.6    German, D.C.7
  • 29
    • 0027304231 scopus 로고
    • The high sensitivity to rotenone of striatal dopamine uptake suggests the existence of a constitutive metabolic deficiency in dopaminergic neurons from the substantia nigra
    • Marey-Semper I, Gelman M, and Levi-Strauss ML. The high sensitivity to rotenone of striatal dopamine uptake suggests the existence of a constitutive metabolic deficiency in dopaminergic neurons from the substantia nigra. Eur J Neurosci 5: 1029-1034, 1993.
    • (1993) Eur J Neurosci , vol.5 , pp. 1029-1034
    • Marey-Semper, I.1    Gelman, M.2    Levi-Strauss, M.L.3
  • 30
    • 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. 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.
    • (1995) J Neurosci , vol.15 , pp. 5912-5918
    • Marey-Semper, I.1    Gelman, M.2    Levi-Strauss, M.3
  • 31
    • 0035910634 scopus 로고    scopus 로고
    • Proteasomal function is impaired in substantia nigra in Parkinson's disease
    • McNaught KS and Jenner P. Proteasomal function is impaired in substantia nigra in Parkinson's disease. Neurosci Lett 297: 191-194, 2001.
    • (2001) Neurosci Lett , vol.297 , pp. 191-194
    • McNaught, K.S.1    Jenner, P.2
  • 32
    • 0028176592 scopus 로고
    • An immunohistochemical study on αketoglutarate dehydrogenase complex in Parkinson's disease
    • Mizuno Y, Matsuda S, Yoshino H, Mori H, Hattori N, and Ikebe SI. An immunohistochemical study on αketoglutarate dehydrogenase complex in Parkinson's disease. Ann Neurol 35: 204-210, 1994.
    • (1994) Ann Neurol , vol.35 , pp. 204-210
    • Mizuno, Y.1    Matsuda, S.2    Yoshino, H.3    Mori, H.4    Hattori, N.5    Ikebe, S.I.6
  • 33
    • 0037154184 scopus 로고    scopus 로고
    • Recent advances in the genetics and pathogenesis of Parkinson disease
    • Mouradain MM. Recent advances in the genetics and pathogenesis of Parkinson disease. Neurology 58: 179-185, 2002.
    • (2002) Neurology , vol.58 , pp. 179-185
    • Mouradain, M.M.1
  • 34
    • 0034026634 scopus 로고    scopus 로고
    • Role for dopamine in malonate-induced damage in vivo in striatum and in vitro in mesencephalic cultures
    • Moy LY, Zeevalk GD, and Sonsalla PK. Role for dopamine in malonate-induced damage in vivo in striatum and in vitro in mesencephalic cultures. J Neurochem 74: 1656-1665, 2000.
    • (2000) J Neurochem , vol.74 , pp. 1656-1665
    • Moy, L.Y.1    Zeevalk, G.D.2    Sonsalla, P.K.3
  • 36
    • 0021810979 scopus 로고
    • Inhibition of NADH-linked oxidation in brain mitochondria by 1-methyl-4-phenylpyridine, a metabolite of the neurotoxin, 1-methyl-4-phenyl-1, 2,5,6-tetrahydropyridine
    • Nicklas WJ, Vyas I, and Heikkila RE. Inhibition of NADH-linked oxidation in brain mitochondria by 1-methyl-4-phenylpyridine, a metabolite of the neurotoxin, 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine. Life Sci 36: 2503-2508, 1985.
    • (1985) Life Sci , vol.36 , pp. 2503-2508
    • Nicklas, W.J.1    Vyas, I.2    Heikkila, R.E.3
  • 37
    • 0024843661 scopus 로고
    • Macroxyproteinase (MPO): A 670 kDa proteinase complex that degrades oxidatively denatured proteins in red blood cells
    • Pacifici RE, Salo DC, and Davies KJA. Macroxyproteinase (MPO): a 670 kDa proteinase complex that degrades oxidatively denatured proteins in red blood cells. Free Radic Biol Med 7: 521-536, 1989.
    • (1989) Free Radic Biol Med , vol.7 , pp. 521-536
    • Pacifici, R.E.1    Salo, D.C.2    Davies, K.J.A.3
  • 38
    • 0024848034 scopus 로고
    • Abnormalities of the electron transport chain in idiopathic Parkinson's disease
    • Parker WD, Boyson SJ, and Parks JK. Abnormalities of the electron transport chain in idiopathic Parkinson's disease. Ann Neurol 26: 719-733, 1989.
    • (1989) Ann Neurol , vol.26 , pp. 719-733
    • Parker, W.D.1    Boyson, S.J.2    Parks, J.K.3
  • 40
    • 0034884622 scopus 로고    scopus 로고
    • Proteasomal inhibition leads to formation of ubiquitin/alpha-synuclein- immunoreactive inclusions in PC12 cells
    • Rideout HJ, Larsen KE, Sulzer D, and Stefanis L. Proteasomal inhibition leads to formation of ubiquitin/alpha-synuclein-immunoreactive inclusions in PC12 cells. J Neurochem 78: 899-908, 2001.
    • (2001) J Neurochem , vol.78 , pp. 899-908
    • Rideout, H.J.1    Larsen, K.E.2    Sulzer, D.3    Stefanis, L.4
  • 41
    • 0034088395 scopus 로고    scopus 로고
    • Parkinson's disease mortality and pesticide exposure in California 1984-1994
    • Ritz B and Yu F. Parkinson's disease mortality and pesticide exposure in California 1984-1994. Int J Epidemiol 29: 323-329, 2000.
    • (2000) Int J Epidemiol , vol.29 , pp. 323-329
    • Ritz, B.1    Yu, F.2
  • 42
    • 0025358959 scopus 로고
    • Superoxide dismutase undergoes proteolysis and fragmentation following oxidative modification and inactivation
    • Salo DC, Pacifici RE, and Davies KJA. Superoxide dismutase undergoes proteolysis and fragmentation following oxidative modification and inactivation. J Biol Chem 265: 11919-11927, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 11919-11927
    • Salo, D.C.1    Pacifici, R.E.2    Davies, K.J.A.3
  • 45
    • 0037104723 scopus 로고    scopus 로고
    • An in vitro model of Parkinson's disease: Linking mitochondrial impairment to altered alpha-synuclein metabolism and oxidative damage
    • Sherer TB, Betarbet R, Stout AK, Lund S, Baptista M, Panov AV, Cookson MR, and Greenamyre JT. An in vitro model of Parkinson's disease: linking mitochondrial impairment to altered alpha-synuclein metabolism and oxidative damage. J Neurosci 22: 7006-7015, 2002.
    • (2002) J Neurosci , vol.22 , pp. 7006-7015
    • Sherer, T.B.1    Betarbet, R.2    Stout, A.K.3    Lund, S.4    Baptista, M.5    Panov, A.V.6    Cookson, M.R.7    Greenamyre, J.T.8
  • 46
    • 0037229425 scopus 로고    scopus 로고
    • Subcutaneous rotenone exposure causes highly selective dopaminergic degeneration and alpha-synuclein aggregation
    • Sherer TB, Kim J-H, Betarbet R, and Greenamyre JT. Subcutaneous rotenone exposure causes highly selective dopaminergic degeneration and alpha-synuclein aggregation. Exp Neurol 179: 9-16, 2003.
    • (2003) Exp Neurol , vol.179 , pp. 9-16
    • Sherer, T.B.1    Kim, J.-H.2    Betarbet, R.3    Greenamyre, J.T.4
  • 48
    • 0030612117 scopus 로고    scopus 로고
    • Coenzyme Q10 levels correlate with the activities of complexes I and 11/111 in mitochondria from parkinsonian and nonparkinsonian subjects
    • Shults CW, Haas RH, Passov D, and Beal MF. Coenzyme Q10 levels correlate with the activities of complexes I and 11/111 in mitochondria from parkinsonian and nonparkinsonian subjects. Ann Neurol 42: 261-264, 1997.
    • (1997) Ann Neurol , vol.42 , pp. 261-264
    • Shults, C.W.1    Haas, R.H.2    Passov, D.3    Beal, M.F.4
  • 49
    • 0035894855 scopus 로고    scopus 로고
    • Expression of A53T mutant but not wild-type alpha-synuclein in PC 12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death
    • Stefanis L, Larsen KE, Rideout HJ, Sulzer D, and Greene LA. Expression of A53T mutant but not wild-type alpha-synuclein in PC 12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death. J Neurosci 21: 9549-9560, 2001.
    • (2001) J Neurosci , vol.21 , pp. 9549-9560
    • Stefanis, L.1    Larsen, K.E.2    Rideout, H.J.3    Sulzer, D.4    Greene, L.A.5
  • 51
    • 0036777211 scopus 로고    scopus 로고
    • Parkinson's disease and related synucleinopathies are a new class of nervous system amyloidoses
    • Trojanowski JQ and Lee VMY. Parkinson's disease and related synucleinopathies are a new class of nervous system amyloidoses. Neurotoxicology 23: 457-460, 2002.
    • (2002) Neurotoxicology , vol.23 , pp. 457-460
    • Trojanowski, J.Q.1    Lee, V.M.Y.2
  • 52
    • 0030867774 scopus 로고    scopus 로고
    • The ubiquitin system
    • Varshavsky A. The ubiquitin system. Trends Biochem Sci 22: 383-387, 1997.
    • (1997) Trends Biochem Sci , vol.22 , pp. 383-387
    • Varshavsky, A.1
  • 53
    • 0019427234 scopus 로고
    • Glycolytic and oxidative metabolism in relation to retinal function
    • Winkler BS. Glycolytic and oxidative metabolism in relation to retinal function. J Gen Physiol 77: 667-692, 1981.
    • (1981) J Gen Physiol , vol.77 , pp. 667-692
    • Winkler, B.S.1
  • 54
    • 0025290130 scopus 로고
    • Chemically induced hypoglycemia and anoxia: Relationship to glutamate receptor-mediated toxicity in retina
    • Zeevalk GD and Nicklas WJ. Chemically induced hypoglycemia and anoxia: relationship to glutamate receptor-mediated toxicity in retina. J Pharmacol Exp Ther 253: 1285-1292, 1990.
    • (1990) J Pharmacol Exp Ther , vol.253 , pp. 1285-1292
    • Zeevalk, G.D.1    Nicklas, W.J.2
  • 55
    • 0034892993 scopus 로고    scopus 로고
    • Differential sensitivity of mesencephalic neurons to inhibition of phosphatase 2A
    • Zeevalk GD, Bernard LP, Manzino L, and Sonsalla PK. Differential sensitivity of mesencephalic neurons to inhibition of phosphatase 2A. J Pharmacol Exp Ther 298: 925-933, 2001.
    • (2001) J Pharmacol Exp Ther , vol.298 , pp. 925-933
    • Zeevalk, G.D.1    Bernard, L.P.2    Manzino, L.3    Sonsalla, P.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.