메뉴 건너뛰기




Volumn 48, Issue 3, 2010, Pages 377-383

Oxidants induce alternative splicing of α-synuclein: Implications for Parkinson's disease

Author keywords

Alternative splicing; Dopamine neurons; MPTP; Neurotoxicity; Oxidative stress; Parkinson's disease; Synuclein

Indexed keywords

1 METHYL 4 PHENYLPYRIDINIUM; ALPHA SYNUCLEIN; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE 1; PROTEASOME; ROTENONE;

EID: 73449099224     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2009.10.045     Document Type: Article
Times cited : (41)

References (41)
  • 2
    • 0242363670 scopus 로고    scopus 로고
    • Molecular pathways of neurodegeneration in Parkinson's disease
    • Dawson T.M., and Dawson V.L. Molecular pathways of neurodegeneration in Parkinson's disease. Science 302 (2003) 819-822
    • (2003) Science , vol.302 , pp. 819-822
    • Dawson, T.M.1    Dawson, V.L.2
  • 3
    • 0031907128 scopus 로고    scopus 로고
    • Abnormal accumulation of NACP/alpha-synuclein in neurodegenerative disorders
    • Takeda A., Mallory M., Sundsmo M., Honer W., Hansen L., and Masliah E. Abnormal accumulation of NACP/alpha-synuclein in neurodegenerative disorders. Am. J. Pathol. 152 (1998) 367-372
    • (1998) Am. J. Pathol. , vol.152 , pp. 367-372
    • Takeda, A.1    Mallory, M.2    Sundsmo, M.3    Honer, W.4    Hansen, L.5    Masliah, E.6
  • 5
    • 0037154184 scopus 로고    scopus 로고
    • Recent advances in the genetics and pathogenesis of Parkinson disease
    • Mouradian M.M. Recent advances in the genetics and pathogenesis of Parkinson disease. Neurology 58 (2002) 179-185
    • (2002) Neurology , vol.58 , pp. 179-185
    • Mouradian, M.M.1
  • 6
    • 68149123529 scopus 로고    scopus 로고
    • Alterations in lysosomal and proteasomal markers in Parkinson's disease: relationship to alpha-synuclein inclusions
    • Chu Y., Dodiya H., Aebischer P., Olanow C.W., and Kordower J.H. Alterations in lysosomal and proteasomal markers in Parkinson's disease: relationship to alpha-synuclein inclusions. Neurobiol. Dis. 3 (2009) 385-398
    • (2009) Neurobiol. Dis. , vol.3 , pp. 385-398
    • Chu, Y.1    Dodiya, H.2    Aebischer, P.3    Olanow, C.W.4    Kordower, J.H.5
  • 7
    • 0003148419 scopus 로고    scopus 로고
    • Rowland L.P. (Ed), Lippincott, Williams & Wilkins, New York
    • Fahan S., and Przedborski S. In: Rowland L.P. (Ed). Merritt's neurology (2000), Lippincott, Williams & Wilkins, New York 679-695
    • (2000) Merritt's neurology , pp. 679-695
    • Fahan, S.1    Przedborski, S.2
  • 8
    • 0041430614 scopus 로고    scopus 로고
    • Dysfunction of mitochondrial complex I and the proteasome: interactions between two biochemical deficits in a cellular model of Parkinson's disease
    • Hoglinger G.U., Carrard G., Michel P.P., Medja F., Lombes A., Ruberg M., Friguet B., and Hirsch E.C. Dysfunction of mitochondrial complex I and the proteasome: interactions between two biochemical deficits in a cellular model of Parkinson's disease. J. Neurochem. 86 (2003) 1297-1307
    • (2003) J. Neurochem. , vol.86 , pp. 1297-1307
    • Hoglinger, G.U.1    Carrard, G.2    Michel, P.P.3    Medja, F.4    Lombes, A.5    Ruberg, M.6    Friguet, B.7    Hirsch, E.C.8
  • 9
    • 0035214256 scopus 로고    scopus 로고
    • Neurochemical findings in the MPTP model of Parkinson's disease
    • Schmidt N., and Ferger B. Neurochemical findings in the MPTP model of Parkinson's disease. J. Neural. Transm. 108 (2001) 1263-1282
    • (2001) J. Neural. Transm. , vol.108 , pp. 1263-1282
    • Schmidt, N.1    Ferger, B.2
  • 10
    • 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 T.B., Betarbet R., Stout A.K., Lund S., Baptista M., Panov A.V., Cookson M.R., and Greenamyre J.T. An in vitro model of Parkinson's disease: linking mitochondrial impairment to altered alpha-synuclein metabolism and oxidative damage. J. Neurosci. 22 (2002) 7006-7015
    • (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
  • 11
    • 2442494278 scopus 로고    scopus 로고
    • Alpha-synuclein up-regulation and aggregation during MPP+-induced apoptosis in neuroblastoma cells: intermediacy of transferrin receptor iron and hydrogen peroxide
    • Kalivendi S.V., Cunningham S., Kotamraju S., Joseph J., Hillard C.J., and Kalyanaraman B. Alpha-synuclein up-regulation and aggregation during MPP+-induced apoptosis in neuroblastoma cells: intermediacy of transferrin receptor iron and hydrogen peroxide. J. Biol. Chem. 279 (2004) 15240-15247
    • (2004) J. Biol. Chem. , vol.279 , pp. 15240-15247
    • Kalivendi, S.V.1    Cunningham, S.2    Kotamraju, S.3    Joseph, J.4    Hillard, C.J.5    Kalyanaraman, B.6
  • 12
    • 0032492689 scopus 로고    scopus 로고
    • Regulation of phospholipase D2: selective inhibition of mammalian phospholipase D isoenzymes by alpha- and beta-synucleinsm
    • Jenco J.M., Rawlingson A., Daniels B., and Morris A.J. Regulation of phospholipase D2: selective inhibition of mammalian phospholipase D isoenzymes by alpha- and beta-synucleinsm. Biochemistry 37 (1998) 4901-4909
    • (1998) Biochemistry , vol.37 , pp. 4901-4909
    • Jenco, J.M.1    Rawlingson, A.2    Daniels, B.3    Morris, A.J.4
  • 13
    • 1642264194 scopus 로고    scopus 로고
    • Structural determinants of PLD2 inhibition by alpha-synuclein
    • Payton J.E., Perrin R.J., Woods W.S., and George J.M. Structural determinants of PLD2 inhibition by alpha-synuclein. J. Mol. Biol. 337 (2004) 1001-1009
    • (2004) J. Mol. Biol. , vol.337 , pp. 1001-1009
    • Payton, J.E.1    Perrin, R.J.2    Woods, W.S.3    George, J.M.4
  • 14
    • 0035066885 scopus 로고    scopus 로고
    • Direct binding and functional coupling of alpha-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis
    • Lee F.J., Liu F., Pristupa Z.B., and Niznik H.B. Direct binding and functional coupling of alpha-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis. FASEB J. 15 (2001) 916-926
    • (2001) FASEB J. , vol.15 , pp. 916-926
    • Lee, F.J.1    Liu, F.2    Pristupa, Z.B.3    Niznik, H.B.4
  • 16
    • 0037047371 scopus 로고    scopus 로고
    • Distinct roles of the N-terminal-binding domain and the C-terminal-solubilizing domain of alpha-synuclein, a molecular chaperone
    • Park S.M., Jung H.Y., Kim T.D., Park J.H., Yang C.H., and Kim J. Distinct roles of the N-terminal-binding domain and the C-terminal-solubilizing domain of alpha-synuclein, a molecular chaperone. J. Biol. Chem. 277 (2002) 28512-28520
    • (2002) J. Biol. Chem. , vol.277 , pp. 28512-28520
    • Park, S.M.1    Jung, H.Y.2    Kim, T.D.3    Park, J.H.4    Yang, C.H.5    Kim, J.6
  • 17
    • 0036736218 scopus 로고    scopus 로고
    • Amyloid precursor protein, presenilins, and alpha-synuclein: molecular pathogenesis and pharmacological applications in Alzheimer's disease
    • Suh Y.H., and Checler F. Amyloid precursor protein, presenilins, and alpha-synuclein: molecular pathogenesis and pharmacological applications in Alzheimer's disease. Pharmacol. Rev. 54 (2002) 469-525
    • (2002) Pharmacol. Rev. , vol.54 , pp. 469-525
    • Suh, Y.H.1    Checler, F.2
  • 18
    • 0034755275 scopus 로고    scopus 로고
    • Characterization of the human alpha-synuclein gene: genomic structure, transcription start site, promoter region and polymorphisms
    • Xia Y., Saitoh T., Ueda K., Tanaka S., Chen X., Hashimoto M., Hsu L., Conrad C., Sundsmo M., Yoshimoto M., et al. Characterization of the human alpha-synuclein gene: genomic structure, transcription start site, promoter region and polymorphisms. J. Alzheimers Dis. 3 (2001) 485-494
    • (2001) J. Alzheimers Dis. , vol.3 , pp. 485-494
    • Xia, Y.1    Saitoh, T.2    Ueda, K.3    Tanaka, S.4    Chen, X.5    Hashimoto, M.6    Hsu, L.7    Conrad, C.8    Sundsmo, M.9    Yoshimoto, M.10
  • 19
    • 8544264002 scopus 로고    scopus 로고
    • Impact of the acidic C-terminal region comprising amino acids 109-140 on alpha-synuclein aggregation in vitro
    • Hoyer W., Cherny D., Subramaniam V., and Jovin T.M. Impact of the acidic C-terminal region comprising amino acids 109-140 on alpha-synuclein aggregation in vitro. Biochemistry 43 (2004) 16233-16242
    • (2004) Biochemistry , vol.43 , pp. 16233-16242
    • Hoyer, W.1    Cherny, D.2    Subramaniam, V.3    Jovin, T.M.4
  • 20
    • 0037137224 scopus 로고    scopus 로고
    • Structural and functional implications of C-terminal regions of alpha-synuclein
    • Kim T.D., Paik S.R., and Yang C.H. Structural and functional implications of C-terminal regions of alpha-synuclein. Biochemistry 41 (2002) 13782-13790
    • (2002) Biochemistry , vol.41 , pp. 13782-13790
    • Kim, T.D.1    Paik, S.R.2    Yang, C.H.3
  • 21
    • 13844320376 scopus 로고    scopus 로고
    • Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations
    • Li W., West N., Colla E., Pletnikova O., Troncoso J.C., Marsh L., Dawson T.M., Jakala P., Hartmann T., Price D.L., et al. Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 2162-2167
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 2162-2167
    • Li, W.1    West, N.2    Colla, E.3    Pletnikova, O.4    Troncoso, J.C.5    Marsh, L.6    Dawson, T.M.7    Jakala, P.8    Hartmann, T.9    Price, D.L.10
  • 22
    • 0028618190 scopus 로고
    • Tissue-dependent alternative splicing of mRNA for NACP, the precursor of non-A beta component of Alzheimer's disease amyloid
    • Ueda K., Saitoh T., and Mori H. Tissue-dependent alternative splicing of mRNA for NACP, the precursor of non-A beta component of Alzheimer's disease amyloid. Biochem. Biophys. Res. Commun. 205 (1994) 1366-1372
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 1366-1372
    • Ueda, K.1    Saitoh, T.2    Mori, H.3
  • 23
    • 0029056115 scopus 로고
    • NACP, the precursor protein of the non-amyloid beta/A4 protein (A beta) component of Alzheimer disease amyloid, binds A beta and stimulates A beta aggregation
    • Yoshimoto M., Iwai A., Kang D., Otero D.A., Xia Y., and Saitoh T. NACP, the precursor protein of the non-amyloid beta/A4 protein (A beta) component of Alzheimer disease amyloid, binds A beta and stimulates A beta aggregation. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 9141-9145
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 9141-9145
    • Yoshimoto, M.1    Iwai, A.2    Kang, D.3    Otero, D.A.4    Xia, Y.5    Saitoh, T.6
  • 24
    • 0030881589 scopus 로고    scopus 로고
    • Development and survival of rat embryonic mesencephalic dopaminergic neurones in serum-free, antioxidant-rich primary cultures
    • Cheung N.S., Hickling Y.M., and Beart P.M. Development and survival of rat embryonic mesencephalic dopaminergic neurones in serum-free, antioxidant-rich primary cultures. Neurosci. Lett. 233 (1997) 13-16
    • (1997) Neurosci. Lett. , vol.233 , pp. 13-16
    • Cheung, N.S.1    Hickling, Y.M.2    Beart, P.M.3
  • 26
    • 0035861687 scopus 로고    scopus 로고
    • Doxorubicin-induced apoptosis is associated with increased transcription of endothelial nitric-oxide synthase. Effect of antiapoptotic antioxidants and calcium
    • Kalivendi S.V., Kotamraju S., Zhao H., Joseph J., and Kalyanaraman B. Doxorubicin-induced apoptosis is associated with increased transcription of endothelial nitric-oxide synthase. Effect of antiapoptotic antioxidants and calcium. J. Biol. Chem. 276 (2001) 47266-47276
    • (2001) J. Biol. Chem. , vol.276 , pp. 47266-47276
    • Kalivendi, S.V.1    Kotamraju, S.2    Zhao, H.3    Joseph, J.4    Kalyanaraman, B.5
  • 27
    • 0037012778 scopus 로고    scopus 로고
    • An alternatively spliced form of rodent alpha-synuclein forms intracellular inclusions in vitro: role of the carboxy-terminus in alpha-synuclein aggregation
    • McLean P.J., and Hyman B.T. An alternatively spliced form of rodent alpha-synuclein forms intracellular inclusions in vitro: role of the carboxy-terminus in alpha-synuclein aggregation. Neurosci. Lett. 323 (2002) 219-223
    • (2002) Neurosci. Lett. , vol.323 , pp. 219-223
    • McLean, P.J.1    Hyman, B.T.2
  • 28
    • 11344262265 scopus 로고    scopus 로고
    • Ubiquitin-proteasome system and Parkinson's diseases
    • Betarbet R., Sherer T.B., and Greenmayre T. Ubiquitin-proteasome system and Parkinson's diseases. Exp. Neurol. 191 (2005) S17-S27
    • (2005) Exp. Neurol. , vol.191
    • Betarbet, R.1    Sherer, T.B.2    Greenmayre, T.3
  • 29
    • 0035910634 scopus 로고    scopus 로고
    • Proteasomal function is impaired in substantia nigra in Parkinson's disease
    • McNaught K.P., and Jenner P. Proteasomal function is impaired in substantia nigra in Parkinson's disease. Neurosci. Lett. 297 (2001) 191-194
    • (2001) Neurosci. Lett. , vol.297 , pp. 191-194
    • McNaught, K.P.1    Jenner, P.2
  • 31
    • 0038389681 scopus 로고    scopus 로고
    • Oxidative modifications of alpha-synuclein
    • Ischiropoulos H. Oxidative modifications of alpha-synuclein. Ann. N. Y. Acad. Sci. 991 (2003) 93-100
    • (2003) Ann. N. Y. Acad. Sci. , vol.991 , pp. 93-100
    • Ischiropoulos, H.1
  • 33
    • 0037237927 scopus 로고    scopus 로고
    • Oxidative stress and nitration in neurodegeneration: cause, effect, or association?
    • Ischiropoulos H., and Beckman J.S. Oxidative stress and nitration in neurodegeneration: cause, effect, or association?. J. Clin. Invest. 111 (2003) 163-169
    • (2003) J. Clin. Invest. , vol.111 , pp. 163-169
    • Ischiropoulos, H.1    Beckman, J.S.2
  • 35
    • 0035976959 scopus 로고    scopus 로고
    • Alpha-synuclein affects the MAPK pathway and accelerates cell death
    • Iwata A., Maruyama M., Kanazawa I., and Nukina N. Alpha-synuclein affects the MAPK pathway and accelerates cell death. J. Biol. Chem. 276 (2001) 45320-45329
    • (2001) J. Biol. Chem. , vol.276 , pp. 45320-45329
    • Iwata, A.1    Maruyama, M.2    Kanazawa, I.3    Nukina, N.4
  • 36
    • 0038472472 scopus 로고    scopus 로고
    • Alpha-synuclein up-regulates expression of caveolin-1 and down-regulates extracellular signal-regulated kinase activity in B103 neuroblastoma cells: role in the pathogenesis of Parkinson's disease
    • Hashimoto M., Takenouchi T., Rockenstein E., and Masliah E. Alpha-synuclein up-regulates expression of caveolin-1 and down-regulates extracellular signal-regulated kinase activity in B103 neuroblastoma cells: role in the pathogenesis of Parkinson's disease. J. Neurochem. 85 (2003) 1468-1479
    • (2003) J. Neurochem. , vol.85 , pp. 1468-1479
    • Hashimoto, M.1    Takenouchi, T.2    Rockenstein, E.3    Masliah, E.4
  • 37
    • 0037069651 scopus 로고    scopus 로고
    • Signal-dependent regulation of splicing via phosphorylation of Sam68
    • Matter N., Herrlich P., and Konig H. Signal-dependent regulation of splicing via phosphorylation of Sam68. Nature 420 (2002) 691-695
    • (2002) Nature , vol.420 , pp. 691-695
    • Matter, N.1    Herrlich, P.2    Konig, H.3
  • 38
    • 0035421277 scopus 로고    scopus 로고
    • Regulation of alternative pre-mRNA splicing by the ERK MAP-kinase pathway
    • Weg-Remers S., Ponta H., Herrlich P., and Konig H. Regulation of alternative pre-mRNA splicing by the ERK MAP-kinase pathway. EMBO J. 20 (2001) 4194-4203
    • (2001) EMBO J. , vol.20 , pp. 4194-4203
    • Weg-Remers, S.1    Ponta, H.2    Herrlich, P.3    Konig, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.