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Volumn 45, Issue 6, 2008, Pages 820-825

Mitochondria and ubiquitin-proteasomal system interplay: Relevance to Parkinson's disease

Author keywords

Mitochondria; Mitochondrial DNA depleted cells; MPP+; Parkinson's disease; Reactive oxygen species; Ubiquitin proteasome system

Indexed keywords

1 METHYL 4 PHENYLPYRIDINIUM; CARBONYL DERIVATIVE; CHYMOTRYPSIN; LACTACYSTIN; MITOCHONDRIAL DNA; PROTEASOME; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UBIQUITIN;

EID: 54949100005     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2008.06.007     Document Type: Article
Times cited : (38)

References (38)
  • 3
    • 20244370595 scopus 로고    scopus 로고
    • Alterations in the solubility and intracellular localization of parkin by several familial Parkinson's disease-linked point mutations
    • Wang C., Tan J.M., Ho M.W., Zaiden N., Wong S.H., Chew C.L., Eng P.W., Lim T.M., Dawson T.M., and Lim K.L. Alterations in the solubility and intracellular localization of parkin by several familial Parkinson's disease-linked point mutations. J. Neurochem. 93 (2005) 422-431
    • (2005) J. Neurochem. , vol.93 , pp. 422-431
    • Wang, C.1    Tan, J.M.2    Ho, M.W.3    Zaiden, N.4    Wong, S.H.5    Chew, C.L.6    Eng, P.W.7    Lim, T.M.8    Dawson, T.M.9    Lim, K.L.10
  • 5
    • 0024992208 scopus 로고
    • Ubiquitin, cell stress and diseases of the nervous system
    • Lowe J., and Mayer R.J. Ubiquitin, cell stress and diseases of the nervous system. Neuropathol. Appl. Neurobiol. 16 (1990) 281-291
    • (1990) Neuropathol. Appl. Neurobiol. , vol.16 , pp. 281-291
    • Lowe, J.1    Mayer, R.J.2
  • 8
    • 0037131567 scopus 로고    scopus 로고
    • The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility
    • Liu Y., Fallon L., Lashuel H.A., Liu Z., and Lansbury Jr. P.T. The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility. Cell 111 (2002) 209-218
    • (2002) Cell , vol.111 , pp. 209-218
    • Liu, Y.1    Fallon, L.2    Lashuel, H.A.3    Liu, Z.4    Lansbury Jr., P.T.5
  • 9
    • 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 Jr. W.R., and Gutknecht W.F. 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 (1978) 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
  • 10
    • 0019445484 scopus 로고
    • Regional activities of metabolic enzymes and glutamate decarboxylase in human brain
    • Maker H.S., Weiss C., Weissbarth S., Silides D.J., and Whetsell W. Regional activities of metabolic enzymes and glutamate decarboxylase in human brain. Ann. Neurol. 10 (1981) 377-383
    • (1981) Ann. Neurol. , vol.10 , pp. 377-383
    • Maker, H.S.1    Weiss, C.2    Weissbarth, S.3    Silides, D.J.4    Whetsell, W.5
  • 11
    • 18144406539 scopus 로고    scopus 로고
    • Oxidative stress and inflammation in Parkinson's disease: is there a causal link?
    • Hald A., and Lotharius J. Oxidative stress and inflammation in Parkinson's disease: is there a causal link?. Exp. Neurol. 193 (2005) 279-290
    • (2005) Exp. Neurol. , vol.193 , pp. 279-290
    • Hald, A.1    Lotharius, J.2
  • 13
    • 22544445837 scopus 로고    scopus 로고
    • Molecular characterization of mtDNA depleted and repleted NT2 cell lines
    • Binder D.R., Dunn Jr. W.H., and Swerdlow R.H. Molecular characterization of mtDNA depleted and repleted NT2 cell lines. Mitochondrion 5 (2005) 255-265
    • (2005) Mitochondrion , vol.5 , pp. 255-265
    • Binder, D.R.1    Dunn Jr., W.H.2    Swerdlow, R.H.3
  • 14
    • 0001889165 scopus 로고
    • Subfractionation of mitochondria, and isolation of the proteins of oxidative phosphorylationdrial DNA depleted cells
    • IRL Press, London
    • Ragan C.I., Wilson M.T., Darley-Usmar V.M., and Lowe P.N. Subfractionation of mitochondria, and isolation of the proteins of oxidative phosphorylationdrial DNA depleted cells. Mitochondria, a practical approach (1987), IRL Press, London 79-112
    • (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
  • 15
    • 0021996231 scopus 로고
    • Simultaneous extraction and reverse-phase high-performance liquid chromatographic determination of adenine and pyridine nucleotides in human red blood cells
    • Stocchi V., Cucchiarini L., Magnani M., Chiarantini L., Palma P., and Crescentini G. Simultaneous extraction and reverse-phase high-performance liquid chromatographic determination of adenine and pyridine nucleotides in human red blood cells. Anal. Biochem. 146 (1985) 118-124
    • (1985) Anal. Biochem. , vol.146 , pp. 118-124
    • Stocchi, V.1    Cucchiarini, L.2    Magnani, M.3    Chiarantini, L.4    Palma, P.5    Crescentini, G.6
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0141838915 scopus 로고    scopus 로고
    • Inhibition of NF-kB renders cells more vulnerable to apoptosis induced by amyloid beta peptides
    • Cardoso S.M., and Oliveira C.R. Inhibition of NF-kB renders cells more vulnerable to apoptosis induced by amyloid beta peptides. Free Radic. Res. 37 (2003) 967-973
    • (2003) Free Radic. Res. , vol.37 , pp. 967-973
    • Cardoso, S.M.1    Oliveira, C.R.2
  • 20
    • 0036829946 scopus 로고    scopus 로고
    • Neuroprotective and neurorestorative strategies for Parkinson's disease
    • Dawson T.M., and Dawson V.L. Neuroprotective and neurorestorative strategies for Parkinson's disease. Nat. Neurosci. 5 (2002) 1058-1061
    • (2002) Nat. Neurosci. , vol.5 , pp. 1058-1061
    • Dawson, T.M.1    Dawson, V.L.2
  • 21
    • 39049179635 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of Parkinson's disease: neurotoxins, causative genes, and inflammatory cytokines
    • Nagatsu T., and Sawada M. Cellular and molecular mechanisms of Parkinson's disease: neurotoxins, causative genes, and inflammatory cytokines. Cell. Mol. Neurobiol. 26 (2006) 781-802
    • (2006) Cell. Mol. Neurobiol. , vol.26 , pp. 781-802
    • Nagatsu, T.1    Sawada, M.2
  • 23
    • 2942618660 scopus 로고    scopus 로고
    • The role of the ubiquitin-proteasomal pathway in Parkinson's disease and other neurodegenerative disorders
    • Chung K.K., Dawson V.L., and Dawson T.M. The role of the ubiquitin-proteasomal pathway in Parkinson's disease and other neurodegenerative disorders. Trends Neurosci. 24 (2001) S7-14
    • (2001) Trends Neurosci. , vol.24
    • Chung, K.K.1    Dawson, V.L.2    Dawson, T.M.3
  • 24
    • 0037378898 scopus 로고    scopus 로고
    • Proteolytic stress: a unifying concept for the etiopathogenesis of Parkinson's disease
    • McNaught K.S., and Olanow C.W. Proteolytic stress: a unifying concept for the etiopathogenesis of Parkinson's disease. Ann. Neurol. 53 Suppl. 3 (2003) S73-S84
    • (2003) Ann. Neurol. , vol.53 , Issue.SUPPL. 3
    • McNaught, K.S.1    Olanow, C.W.2
  • 25
    • 0034766344 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system and neurodegenerative disease
    • Tanaka K. The ubiquitin-proteasome system and neurodegenerative disease. No To Shinkei 53 (2001) 935-942
    • (2001) No To Shinkei , vol.53 , pp. 935-942
    • Tanaka, K.1
  • 26
    • 0035894855 scopus 로고    scopus 로고
    • Expression of A53T mutant but not wild-type alpha-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death
    • Stefanis L., Larsen K.E., Rideout H.J., Sulzer D., and Greene L.A. Expression of A53T mutant but not wild-type alpha-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death. J. Neurosci. 21 (2001) 9549-9560
    • (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
  • 27
    • 33745140532 scopus 로고    scopus 로고
    • Proteasome dysfunction in aged human alpha-synuclein transgenic mice
    • Chen L., Thiruchelvam M.J., Madura K., and Richfield E.K. Proteasome dysfunction in aged human alpha-synuclein transgenic mice. Neurobiol. Dis. 23 (2006) 120-126
    • (2006) Neurobiol. Dis. , vol.23 , pp. 120-126
    • Chen, L.1    Thiruchelvam, M.J.2    Madura, K.3    Richfield, E.K.4
  • 28
    • 0030830270 scopus 로고    scopus 로고
    • Immunocytochemical co-localization of the proteasome in ubiquitinated structures in neurodegenerative diseases and the elderly
    • Ii K., Ito H., Tanaka K., and Hirano A. Immunocytochemical co-localization of the proteasome in ubiquitinated structures in neurodegenerative diseases and the elderly. J. Neuropathol. Exp. Neurol. 56 (1997) 125-131
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 125-131
    • Ii, K.1    Ito, H.2    Tanaka, K.3    Hirano, A.4
  • 29
    • 0033669319 scopus 로고    scopus 로고
    • In situ and in vitro study of colocalization and segregation of alpha-synuclein, ubiquitin, and lipids in Lewy bodies
    • Gai W.P., Yuan H.X., Li X.Q., Power J.T., Blumbergs P.C., and Jensen P.H. In situ and in vitro study of colocalization and segregation of alpha-synuclein, ubiquitin, and lipids in Lewy bodies. Exp. Neurol. 166 (2000) 324-333
    • (2000) Exp. Neurol. , vol.166 , pp. 324-333
    • Gai, W.P.1    Yuan, H.X.2    Li, X.Q.3    Power, J.T.4    Blumbergs, P.C.5    Jensen, P.H.6
  • 33
    • 0022515217 scopus 로고
    • Comparative studies on the mechanisms of paraquat and 1-methyl-4-phenylpyridine (MPP+) cytotoxicity
    • Di M.D., Sandy M.S., Ekstrom G., and Smith M.T. Comparative studies on the mechanisms of paraquat and 1-methyl-4-phenylpyridine (MPP+) cytotoxicity. Biochem. Biophys. Res. Commun. 137 (1986) 303-309
    • (1986) Biochem. Biophys. Res. Commun. , vol.137 , pp. 303-309
    • Di, M.D.1    Sandy, M.S.2    Ekstrom, G.3    Smith, M.T.4
  • 34
    • 15544365143 scopus 로고    scopus 로고
    • Rotenone induces oxidative stress and dopaminergic neuron damage in organotypic substantia nigra cultures
    • Testa C.M., Sherer T.B., and Greenamyre J.T. Rotenone induces oxidative stress and dopaminergic neuron damage in organotypic substantia nigra cultures. Brain Res. Mol. Brain Res. 134 (2005) 109-118
    • (2005) Brain Res. Mol. Brain Res. , vol.134 , pp. 109-118
    • Testa, C.M.1    Sherer, T.B.2    Greenamyre, J.T.3
  • 35
    • 1542318096 scopus 로고    scopus 로고
    • Initiation of neuronal damage by complex I deficiency and oxidative stress in Parkinson's disease
    • Tretter L., Sipos I., and dam-Vizi V. Initiation of neuronal damage by complex I deficiency and oxidative stress in Parkinson's disease. Neurochem. Res. 29 (2004) 569-577
    • (2004) Neurochem. Res. , vol.29 , pp. 569-577
    • Tretter, L.1    Sipos, I.2    dam-Vizi, V.3
  • 37
    • 0034194227 scopus 로고    scopus 로고
    • Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress
    • Reinheckel T., Ullrich O., Sitte N., and Grune T. Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress. Arch. Biochem. Biophys. 377 (2000) 65-68
    • (2000) Arch. Biochem. Biophys. , vol.377 , pp. 65-68
    • Reinheckel, T.1    Ullrich, O.2    Sitte, N.3    Grune, T.4


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