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Volumn 75, Issue , 2016, Pages 34-44

The novel mechanism of rotenone-induced α-synuclein phosphorylation via reduced protein phosphatase 2A activity

Author keywords

a Synuclein; Parkinson's disease; Phosphorylation; Protein phosphatase 2A; Rotenone

Indexed keywords

ALPHA SYNUCLEIN; BOSUTINIB; CALMODULIN; CERAMIDE; PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEIN TYROSINE KINASE; ROTENONE; PHOSPHOPROTEIN PHOSPHATASE 2; PROTEIN AGGREGATE; TYROSINE;

EID: 84961895910     PISSN: 13572725     EISSN: 18785875     Source Type: Journal    
DOI: 10.1016/j.biocel.2016.03.007     Document Type: Article
Times cited : (26)

References (33)
  • 2
    • 84893774898 scopus 로고    scopus 로고
    • Nigral iron elevation is an invariable feature of Parkinson's disease and is a sufficient cause of neurodegeneration
    • S. Ayton, and P. Lei Nigral iron elevation is an invariable feature of Parkinson's disease and is a sufficient cause of neurodegeneration Biomed. Res. Int. 2014 2014 581256
    • (2014) Biomed. Res. Int. , vol.2014
    • Ayton, S.1    Lei, P.2
  • 5
    • 67650496503 scopus 로고    scopus 로고
    • Relationship between alpha synuclein phosphorylation, proteasomal inhibition and cell death: Relevance to Parkinson's disease pathogenesis
    • K.Y. Chau, H.L. Ching, A.H. Schapira, and J.M. Cooper Relationship between alpha synuclein phosphorylation, proteasomal inhibition and cell death: relevance to Parkinson's disease pathogenesis J. Neurochem. 110 2009 1005 1013
    • (2009) J. Neurochem. , vol.110 , pp. 1005-1013
    • Chau, K.Y.1    Ching, H.L.2    Schapira, A.H.3    Cooper, J.M.4
  • 6
    • 17844406856 scopus 로고    scopus 로고
    • Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease
    • L. Chen, and M.B. Feany Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease Nat. Neurosci. 8 2005 657 663
    • (2005) Nat. Neurosci. , vol.8 , pp. 657-663
    • Chen, L.1    Feany, M.B.2
  • 7
    • 0026786471 scopus 로고
    • Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation
    • J. Chen, B.L. Martin, and D.L. Brautigan Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation Science 257 1992 1261 1264
    • (1992) Science , vol.257 , pp. 1261-1264
    • Chen, J.1    Martin, B.L.2    Brautigan, D.L.3
  • 8
    • 33846118688 scopus 로고    scopus 로고
    • Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme
    • U.S. Cho, and W. Xu Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme Nature 445 2007 53 57
    • (2007) Nature , vol.445 , pp. 53-57
    • Cho, U.S.1    Xu, W.2
  • 9
    • 0022445670 scopus 로고
    • Rapid colorimetric assay for cell growth and survival. Modifications to the tetrazolium dye procedure giving improved sensitivity and reliability
    • F. Denizot, and R. Lang Rapid colorimetric assay for cell growth and survival. Modifications to the tetrazolium dye procedure giving improved sensitivity and reliability J. Immunol. Methods 89 1986 271 277
    • (1986) J. Immunol. Methods , vol.89 , pp. 271-277
    • Denizot, F.1    Lang, R.2
  • 12
    • 9644289489 scopus 로고    scopus 로고
    • An intermittent, controlled-rate, slow progressive degeneration model of Parkinson's disease: Antiparkinson effects of Sinemet and protective effects of methylphenidate
    • S.M. Fleming, Y. Delville, and T. Schallert An intermittent, controlled-rate, slow progressive degeneration model of Parkinson's disease: antiparkinson effects of Sinemet and protective effects of methylphenidate Behav. Brain Res. 156 2005 201 213
    • (2005) Behav. Brain Res. , vol.156 , pp. 201-213
    • Fleming, S.M.1    Delville, Y.2    Schallert, T.3
  • 13
    • 0029981526 scopus 로고    scopus 로고
    • Neuropathology of Parkinson's disease
    • L.S. Forno Neuropathology of Parkinson's disease J. Neuropathol. Exp. Neurol. 55 1996 259 272
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 259-272
    • Forno, L.S.1
  • 15
    • 0027477103 scopus 로고
    • Autophosphorylation-activated protein kinase phosphorylates and inactivates protein phosphatase 2A
    • H. Guo, and Z. Damuni Autophosphorylation-activated protein kinase phosphorylates and inactivates protein phosphatase 2A Proc. Natl. Acad. Sci. U. S. A. 90 1993 2500 2504
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 2500-2504
    • Guo, H.1    Damuni, Z.2
  • 16
    • 0029073053 scopus 로고
    • The dimeric and catalytic subunit forms of protein phosphatase 2A from rat brain are stimulated by C2-ceramide
    • B. Law, and S. Rossie The dimeric and catalytic subunit forms of protein phosphatase 2A from rat brain are stimulated by C2-ceramide J. Biol. Chem. 270 1995 12808 12813
    • (1995) J. Biol. Chem. , vol.270 , pp. 12808-12813
    • Law, B.1    Rossie, S.2
  • 17
    • 0037424245 scopus 로고    scopus 로고
    • Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production
    • N. Li, K. Ragheb, G. Lawler, J. Sturgis, B. Rajwa, J.A. Melendez, and J.P. Robinson Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production J. Biol. Chem. 278 2003 8516 8525
    • (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
  • 18
    • 0042477558 scopus 로고    scopus 로고
    • Alpha-synuclein and presynaptic function: Implications for Parkinson's disease
    • S. Lykkebo, and P.H. Jensen Alpha-synuclein and presynaptic function: implications for Parkinson's disease Neuromolecular Med. 2 2002 115 129
    • (2002) Neuromolecular Med. , vol.2 , pp. 115-129
    • Lykkebo, S.1    Jensen, P.H.2
  • 19
    • 84870552532 scopus 로고    scopus 로고
    • Deletion in exon 5 of the SNCA gene and exposure to rotenone leads to oligomerization of alpha-synuclein and toxicity to PC12 cells
    • K.L. Ma, L.K. Song, W.A. Long, Y.H. Yuan, Y. Zhang, X.Y. Song, F. Niu, N. Han, and N.H. Chen Deletion in exon 5 of the SNCA gene and exposure to rotenone leads to oligomerization of alpha-synuclein and toxicity to PC12 cells Brain Res. Bull. 90 2013 127 131
    • (2013) Brain Res. Bull. , vol.90 , pp. 127-131
    • Ma, K.L.1    Song, L.K.2    Long, W.A.3    Yuan, Y.H.4    Zhang, Y.5    Song, X.Y.6    Niu, F.7    Han, N.8    Chen, N.H.9
  • 21
    • 84916898834 scopus 로고    scopus 로고
    • Unveiling the role of the pesticides paraquat and rotenone on alpha-synuclein fibrillation in vitro
    • M.G. Maturana, A.S. Pinheiro, T.L. Souza, and C. Follmer Unveiling the role of the pesticides paraquat and rotenone on alpha-synuclein fibrillation in vitro Neurotoxicology 46 2015 35 43
    • (2015) Neurotoxicology , vol.46 , pp. 35-43
    • Maturana, M.G.1    Pinheiro, A.S.2    Souza, T.L.3    Follmer, C.4
  • 22
    • 33646431738 scopus 로고    scopus 로고
    • Age-related severity of dopaminergic neurodegeneration to MPTP neurotoxicity causes motor dysfunction in C57BL/6 mice
    • S. Ohashi, A. Mori, N. Kurihara, Y. Mitsumoto, and M. Nakai Age-related severity of dopaminergic neurodegeneration to MPTP neurotoxicity causes motor dysfunction in C57BL/6 mice Neurosci. Lett. 401 2006 183 187
    • (2006) Neurosci. Lett. , vol.401 , pp. 183-187
    • Ohashi, S.1    Mori, A.2    Kurihara, N.3    Mitsumoto, Y.4    Nakai, M.5
  • 23
    • 84906751686 scopus 로고    scopus 로고
    • Linking alpha-synuclein phosphorylation to reactive oxygen species formation and mitochondrial dysfunction in SH-SY5Y cells
    • R. Perfeito, D.F. Lazaro, T.F. Outeiro, and A.C. Rego Linking alpha-synuclein phosphorylation to reactive oxygen species formation and mitochondrial dysfunction in SH-SY5Y cells Mol. Cell. Neurosci. 62 2014 51 59
    • (2014) Mol. Cell. Neurosci. , vol.62 , pp. 51-59
    • Perfeito, R.1    Lazaro, D.F.2    Outeiro, T.F.3    Rego, A.C.4
  • 26
    • 0037229425 scopus 로고    scopus 로고
    • Subcutaneous rotenone exposure causes highly selective dopaminergic degeneration and alpha-synuclein aggregation
    • T.B. Sherer, J.H. Kim, R. Betarbet, and J.T. Greenamyre Subcutaneous rotenone exposure causes highly selective dopaminergic degeneration and alpha-synuclein aggregation Exp. Neurol. 179 2003 9 16
    • (2003) Exp. Neurol. , vol.179 , pp. 9-16
    • Sherer, T.B.1    Kim, J.H.2    Betarbet, R.3    Greenamyre, J.T.4
  • 31
    • 77952882422 scopus 로고    scopus 로고
    • A study to correlate rotenone induced biochemical changes and cerebral damage in brain areas with neuromuscular coordination in rats
    • S. Swarnkar, S. Singh, R. Mathur, I.K. Patro, and C. Nath A study to correlate rotenone induced biochemical changes and cerebral damage in brain areas with neuromuscular coordination in rats Toxicology 272 2010 17 22
    • (2010) Toxicology , vol.272 , pp. 17-22
    • Swarnkar, S.1    Singh, S.2    Mathur, R.3    Patro, I.K.4    Nath, C.5
  • 32
    • 84870481575 scopus 로고    scopus 로고
    • Zinc induces protein phosphatase 2A inactivation and tau hyperphosphorylation through Src dependent PP2A (tyrosine 307) phosphorylation
    • Y. Xiong, X.P. Jing, X.W. Zhou, X.L. Wang, Y. Yang, X.Y. Sun, M. Qiu, F.Y. Cao, Y.M. Lu, R. Liu, and J.Z. Wang Zinc induces protein phosphatase 2A inactivation and tau hyperphosphorylation through Src dependent PP2A (tyrosine 307) phosphorylation Neurobiol. Aging 34 2013 745 756
    • (2013) Neurobiol. Aging , vol.34 , pp. 745-756
    • Xiong, Y.1    Jing, X.P.2    Zhou, X.W.3    Wang, X.L.4    Yang, Y.5    Sun, X.Y.6    Qiu, M.7    Cao, F.Y.8    Lu, Y.M.9    Liu, R.10    Wang, J.Z.11
  • 33
    • 84922169955 scopus 로고    scopus 로고
    • The molecular mechanism of rotenone-induced alpha-synuclein aggregation: Emphasizing the role of the calcium/GSK3beta pathway
    • Y.H. Yuan, W.F. Yan, J.D. Sun, J.Y. Huang, Z. Mu, and N.H. Chen The molecular mechanism of rotenone-induced alpha-synuclein aggregation: emphasizing the role of the calcium/GSK3beta pathway Toxicol. Lett. 233 2015 163 171
    • (2015) Toxicol. Lett. , vol.233 , pp. 163-171
    • Yuan, Y.H.1    Yan, W.F.2    Sun, J.D.3    Huang, J.Y.4    Mu, Z.5    Chen, N.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.