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Volumn 36, Issue 9, 2015, Pages 2649-2659

Increased oligomerization and phosphorylation of α-synuclein are associated with decreased activity of glucocerebrosidase and protein phosphatase 2A in aging monkey brains

Author keywords

Aging; Cynomolgus monkey; Dementia with lewy bodies; Glucocerebrosidase; Parkinson's disease; Synuclein

Indexed keywords

ALPHA SYNUCLEIN; GLUCOSYLCERAMIDASE; OLIGOMER; PHOSPHOPROTEIN PHOSPHATASE 2A; SERINE; PEPTIDE; PHOSPHOPROTEIN PHOSPHATASE 2;

EID: 84940467091     PISSN: 01974580     EISSN: 15581497     Source Type: Journal    
DOI: 10.1016/j.neurobiolaging.2015.06.004     Document Type: Article
Times cited : (51)

References (65)
  • 3
    • 0031941058 scopus 로고    scopus 로고
    • Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies
    • Baba M., Nakajo S., Tu P.H., Tomita T., Nakaya K., Lee V.M., Trojanowski J.Q., Iwatsubo T. Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies. Am. J. Pathol. 1998, 152:879-884.
    • (1998) Am. J. Pathol. , vol.152 , pp. 879-884
    • Baba, M.1    Nakajo, S.2    Tu, P.H.3    Tomita, T.4    Nakaya, K.5    Lee, V.M.6    Trojanowski, J.Q.7    Iwatsubo, T.8
  • 5
    • 0033575310 scopus 로고    scopus 로고
    • Long chain ceramides activate protein phosphatase-1 and protein phosphatase-2A. Activation is stereospecific and regulated by phosphatidic acid
    • Chalfant C.E., Kishikawa K., Mumby M.C., Kamibayashi C., Bielawska A., Hannun Y.A. Long chain ceramides activate protein phosphatase-1 and protein phosphatase-2A. Activation is stereospecific and regulated by phosphatidic acid. J.Biol. Chem. 1999, 274:20313-20317.
    • (1999) J.Biol. Chem. , vol.274 , pp. 20313-20317
    • Chalfant, C.E.1    Kishikawa, K.2    Mumby, M.C.3    Kamibayashi, C.4    Bielawska, A.5    Hannun, Y.A.6
  • 7
    • 78049383132 scopus 로고    scopus 로고
    • Mitochondrial α-synuclein accumulation impairs complex I function in dopaminergic neuronsand results in increased mitophagy invivo
    • Chinta S.J., Mallajosyula J.K., Rane A., Andersen J.K. Mitochondrial α-synuclein accumulation impairs complex I function in dopaminergic neuronsand results in increased mitophagy invivo. Neurosci. Lett. 2010, 486:235-239.
    • (2010) Neurosci. Lett. , vol.486 , pp. 235-239
    • Chinta, S.J.1    Mallajosyula, J.K.2    Rane, A.3    Andersen, J.K.4
  • 11
    • 44749085250 scopus 로고    scopus 로고
    • Mitochondrial translocation of alpha-synuclein is promoted by intracellular acidification
    • Cole N.B., Dieuliis D., Leo P., Mitchell D.C., Nussbaum R.L. Mitochondrial translocation of alpha-synuclein is promoted by intracellular acidification. Exp. Cell Res. 2008, 314:2076-2089.
    • (2008) Exp. Cell Res. , vol.314 , pp. 2076-2089
    • Cole, N.B.1    Dieuliis, D.2    Leo, P.3    Mitchell, D.C.4    Nussbaum, R.L.5
  • 12
    • 84863229691 scopus 로고    scopus 로고
    • Accumulation of toxic α-synuclein oligomer within endoplasmic reticulum occurs in alpha-synucleinopathy invivo
    • Colla E., Jensen P.H., Pletnikova O., Troncoso J.C., Glabe C., Lee M.K. Accumulation of toxic α-synuclein oligomer within endoplasmic reticulum occurs in alpha-synucleinopathy invivo. J.Neurosci. 2012, 32:3301-3305.
    • (2012) J.Neurosci. , vol.32 , pp. 3301-3305
    • Colla, E.1    Jensen, P.H.2    Pletnikova, O.3    Troncoso, J.C.4    Glabe, C.5    Lee, M.K.6
  • 14
    • 0026781572 scopus 로고
    • Anovel N18TG29 mesencephalon cell hybrid expresses properties that suggest a dopaminergic cell line of substantia nigra origin
    • Crawford G.D., Le W.D., Smith R.G., Xie W.J., Stefani E., Appel S.H. Anovel N18TG29 mesencephalon cell hybrid expresses properties that suggest a dopaminergic cell line of substantia nigra origin. J.Neurosci. 1992, 12:3392-3398.
    • (1992) J.Neurosci. , vol.12 , pp. 3392-3398
    • Crawford, G.D.1    Le, W.D.2    Smith, R.G.3    Xie, W.J.4    Stefani, E.5    Appel, S.H.6
  • 15
    • 26444530166 scopus 로고    scopus 로고
    • Age-related changes in neutral sphingomyelin-specific phospholipase C activity in striatum, hippocampus, and frontal cortex: implication for sensitivity to stress and inflammation
    • Crivello N.A., Rosenberg I.H., Dallal G.E., Bielinski D., Joseph J.A. Age-related changes in neutral sphingomyelin-specific phospholipase C activity in striatum, hippocampus, and frontal cortex: implication for sensitivity to stress and inflammation. Neurochem. Int. 2005, 47:573-579.
    • (2005) Neurochem. Int. , vol.47 , pp. 573-579
    • Crivello, N.A.1    Rosenberg, I.H.2    Dallal, G.E.3    Bielinski, D.4    Joseph, J.A.5
  • 16
    • 84875967929 scopus 로고    scopus 로고
    • Loss of β-glucocerebrosidase activity does not affect alpha-synuclein levels or lysosomal function in neuronal cells
    • Dermentzaki G., Dimitriou E., Xilouri M., Michelakakis H., Stefanis L. Loss of β-glucocerebrosidase activity does not affect alpha-synuclein levels or lysosomal function in neuronal cells. PLoS One 2013, 8:e60674.
    • (2013) PLoS One , vol.8 , pp. e60674
    • Dermentzaki, G.1    Dimitriou, E.2    Xilouri, M.3    Michelakakis, H.4    Stefanis, L.5
  • 17
    • 44049099669 scopus 로고    scopus 로고
    • Mitochondrial import and accumulation of alpha-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain
    • Devi L., Raghavendran V., Prabhu B.M., Avadhani N.G., Anandatheerthavarada H.K. Mitochondrial import and accumulation of alpha-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain. J.Biol. Chem. 2008, 283:9089-9100.
    • (2008) J.Biol. Chem. , vol.283 , pp. 9089-9100
    • Devi, L.1    Raghavendran, V.2    Prabhu, B.M.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 21
    • 79956196722 scopus 로고    scopus 로고
    • Neuropathology of sporadic Parkinson disease before the appearance of parkinsonism: preclinical Parkinson disease
    • Ferrer I., Martinez A., Blanco R., Dalfó E., Carmona M. Neuropathology of sporadic Parkinson disease before the appearance of parkinsonism: preclinical Parkinson disease. J.Neural Transm. 2011, 118:821-839.
    • (2011) J.Neural Transm. , vol.118 , pp. 821-839
    • Ferrer, I.1    Martinez, A.2    Blanco, R.3    Dalfó, E.4    Carmona, M.5
  • 22
    • 34848914455 scopus 로고    scopus 로고
    • Oxidative inhibition of protein phosphatase 2A activity: role of catalytic subunit disulfides
    • Foley T.D., Petro L.A., Stredny C.M., Coppa T.M. Oxidative inhibition of protein phosphatase 2A activity: role of catalytic subunit disulfides. Neurochem. Res. 2007, 32:1957-1964.
    • (2007) Neurochem. Res. , vol.32 , pp. 1957-1964
    • Foley, T.D.1    Petro, L.A.2    Stredny, C.M.3    Coppa, T.M.4
  • 24
    • 0032529707 scopus 로고    scopus 로고
    • Multiple-system atrophy: a new alpha-synuclein disease?
    • Gai W.P., Power J.H., Blumbergs P.C., Blessing W.W. Multiple-system atrophy: a new alpha-synuclein disease?. Lancet 1998, 352:547-548.
    • (1998) Lancet , vol.352 , pp. 547-548
    • Gai, W.P.1    Power, J.H.2    Blumbergs, P.C.3    Blessing, W.W.4
  • 25
    • 78149410222 scopus 로고    scopus 로고
    • Glucocerebrosidase is present in α-synuclein inclusions in Lewy body disorders
    • Goker-Alpan O., Stubblefield B.K., Giasson B.I., Sidransky E. Glucocerebrosidase is present in α-synuclein inclusions in Lewy body disorders. Acta Neuropathol. 2010, 120:641-649.
    • (2010) Acta Neuropathol. , vol.120 , pp. 641-649
    • Goker-Alpan, O.1    Stubblefield, B.K.2    Giasson, B.I.3    Sidransky, E.4
  • 26
    • 53049096591 scopus 로고    scopus 로고
    • Phenotype, diagnosis, and treatment of Gaucher's disease
    • Grabowski G.A. Phenotype, diagnosis, and treatment of Gaucher's disease. Lancet 2008, 372:1263-1271.
    • (2008) Lancet , vol.372 , pp. 1263-1271
    • Grabowski, G.A.1
  • 27
    • 0142200947 scopus 로고    scopus 로고
    • Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer's and Parkinson's diseases
    • Hashimoto M., Rockenstein E., Crews L., Masliah E. Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer's and Parkinson's diseases. Neuromolecular Med. 2003, 4:21-36.
    • (2003) Neuromolecular Med. , vol.4 , pp. 21-36
    • Hashimoto, M.1    Rockenstein, E.2    Crews, L.3    Masliah, E.4
  • 28
    • 0042974099 scopus 로고    scopus 로고
    • Alpha-synuclein pathology in Parkinson's and Alzheimer's disease brain: incidence and topographic distribution-a pilot study
    • Jellinger K.A. Alpha-synuclein pathology in Parkinson's and Alzheimer's disease brain: incidence and topographic distribution-a pilot study. Acta Neuropathol. 2003, 106:191-201.
    • (2003) Acta Neuropathol. , vol.106 , pp. 191-201
    • Jellinger, K.A.1
  • 29
    • 7944238570 scopus 로고    scopus 로고
    • Lewy body-related alpha-synucleinopathy in the aged human brain
    • Jellinger K.A. Lewy body-related alpha-synucleinopathy in the aged human brain. J.Neural Transm. 2004, 111:1219-1235.
    • (2004) J.Neural Transm. , vol.111 , pp. 1219-1235
    • Jellinger, K.A.1
  • 31
    • 33846997878 scopus 로고    scopus 로고
    • Presynaptic alpha-synuclein aggregates, not Lewy bodies, cause neurodegeneration in dementia with Lewy bodies
    • Kramer M.L., Schulz-Schaeffer W.J. Presynaptic alpha-synuclein aggregates, not Lewy bodies, cause neurodegeneration in dementia with Lewy bodies. J.Neurosci. 2007, 27:1405-1410.
    • (2007) J.Neurosci. , vol.27 , pp. 1405-1410
    • Kramer, M.L.1    Schulz-Schaeffer, W.J.2
  • 34
    • 63449093494 scopus 로고    scopus 로고
    • Alpha-Synuclein is differentially expressed in mitochondria from different rat brain regions and dose-dependently down-regulates complex I activity
    • Liu G., Zhang C., Yin J., Li X., Cheng F., Li Y., Yang H., Uéda K., Chan P., Yu S. alpha-Synuclein is differentially expressed in mitochondria from different rat brain regions and dose-dependently down-regulates complex I activity. Neurosci. Lett. 2009, 454:187-192.
    • (2009) Neurosci. Lett. , vol.454 , pp. 187-192
    • Liu, G.1    Zhang, C.2    Yin, J.3    Li, X.4    Cheng, F.5    Li, Y.6    Yang, H.7    Uéda, K.8    Chan, P.9    Yu, S.10
  • 43
    • 80052949842 scopus 로고    scopus 로고
    • Loss of PINK1 function decreases PP2A activity and promotes autophagy in dopaminergic cells and a murine model
    • Qi Z., Yang W., Liu Y., Cui T., Gao H., Duan C., Lu L., Zhao C., Zhao H., Yang H. Loss of PINK1 function decreases PP2A activity and promotes autophagy in dopaminergic cells and a murine model. Neurochem. Int. 2011, 59:572-581.
    • (2011) Neurochem. Int. , vol.59 , pp. 572-581
    • Qi, Z.1    Yang, W.2    Liu, Y.3    Cui, T.4    Gao, H.5    Duan, C.6    Lu, L.7    Zhao, C.8    Zhao, H.9    Yang, H.10
  • 44
    • 84872458771 scopus 로고    scopus 로고
    • Aggregation and neurotoxicity of recombinant alpha-synuclein aggregates initiated by dimerization
    • Roostaee A., Beaudoin S., Staskevicius A., Roucou X. Aggregation and neurotoxicity of recombinant alpha-synuclein aggregates initiated by dimerization. Mol. Neurodegener. 2013, 8:5.
    • (2013) Mol. Neurodegener. , vol.8 , pp. 5
    • Roostaee, A.1    Beaudoin, S.2    Staskevicius, A.3    Roucou, X.4
  • 47
    • 77957264418 scopus 로고    scopus 로고
    • The synaptic pathology of alpha-synuclein aggregation in dementia with Lewy bodies, Parkinson's disease and Parkinson's disease dementia
    • Schulz-Schaeffer W.J. The synaptic pathology of alpha-synuclein aggregation in dementia with Lewy bodies, Parkinson's disease and Parkinson's disease dementia. Acta Neuropathol. 2010, 120:131-143.
    • (2010) Acta Neuropathol. , vol.120 , pp. 131-143
    • Schulz-Schaeffer, W.J.1
  • 49
    • 84867616698 scopus 로고    scopus 로고
    • The link between the GBA gene and parkinsonism
    • Sidransky E., Lopez G. The link between the GBA gene and parkinsonism. Lancet Neurol. 2012, 11:986-998.
    • (2012) Lancet Neurol. , vol.11 , pp. 986-998
    • Sidransky, E.1    Lopez, G.2
  • 51
    • 0032568534 scopus 로고    scopus 로고
    • Alpha-synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies
    • Spillantini M.G., Crowther R.A., Jakes R., Hasegawa M., Goedert M. Alpha-synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:6469-6473.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6469-6473
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Hasegawa, M.4    Goedert, M.5
  • 52
    • 77952900626 scopus 로고    scopus 로고
    • Alpha-synuclein delays endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells by antagonizing ER/Golgi SNAREs
    • Thayanidhi N., Helm J.R., Nycz D.C., Bentley M., Liang Y., Hay J.C. Alpha-synuclein delays endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells by antagonizing ER/Golgi SNAREs. Mol. Biol. Cell 2010, 21:1850-1863.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1850-1863
    • Thayanidhi, N.1    Helm, J.R.2    Nycz, D.C.3    Bentley, M.4    Liang, Y.5    Hay, J.C.6
  • 53
    • 77956649080 scopus 로고    scopus 로고
    • Neuroimaging for Lewy body disease: is the invivo molecular imaging of alpha-synuclein neuropathology required and feasible?
    • Vernon A.C., Ballard C., Modo M. Neuroimaging for Lewy body disease: is the invivo molecular imaging of alpha-synuclein neuropathology required and feasible?. Brain Res. Rev. 2010, 65:28-55.
    • (2010) Brain Res. Rev. , vol.65 , pp. 28-55
    • Vernon, A.C.1    Ballard, C.2    Modo, M.3
  • 54
    • 0038386274 scopus 로고    scopus 로고
    • Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease
    • Volles M.J., Lansbury P.T. Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease. Biochemistry 2003, 42:7871-7878.
    • (2003) Biochemistry , vol.42 , pp. 7871-7878
    • Volles, M.J.1    Lansbury, P.T.2
  • 59
    • 79959925894 scopus 로고    scopus 로고
    • Alpha-synuclein interacts with Glucocerebrosidase providing a molecular link between Parkinson and Gaucher diseases
    • Yap T.L., Gruschus J.M., Velayati A., Westbroek W., Goldin E., Moaven N., Sidransky E., Lee J.C. Alpha-synuclein interacts with Glucocerebrosidase providing a molecular link between Parkinson and Gaucher diseases. J.Biol. Chem. 2011, 286:28080-28088.
    • (2011) J.Biol. Chem. , vol.286 , pp. 28080-28088
    • Yap, T.L.1    Gruschus, J.M.2    Velayati, A.3    Westbroek, W.4    Goldin, E.5    Moaven, N.6    Sidransky, E.7    Lee, J.C.8
  • 60
    • 33847649977 scopus 로고    scopus 로고
    • Extensive nuclear localization of alpha-synuclein in normal rat brain neurons revealed by a novel monoclonal antibody
    • Yu S., Li X., Liu G., Han J., Zhang C., Li Y., Xu S., Liu C., Gao Y., Yang H., Uéda K., Chan P. Extensive nuclear localization of alpha-synuclein in normal rat brain neurons revealed by a novel monoclonal antibody. Neuroscience 2007, 145:539-555.
    • (2007) Neuroscience , vol.145 , pp. 539-555
    • Yu, S.1    Li, X.2    Liu, G.3    Han, J.4    Zhang, C.5    Li, Y.6    Xu, S.7    Liu, C.8    Gao, Y.9    Yang, H.10    Uéda, K.11    Chan, P.12
  • 61
    • 43049165482 scopus 로고    scopus 로고
    • Hypoxic preconditioning up-regulates glucose transport activity and glucose transporter (GLUT1 and GLUT3) gene expression after acute anoxic exposure in the cultured rat hippocampal neurons and astrocytes
    • Yu S., Zhao T., Guo M., Fang H., Ma J., Ding A., Wang F., Chan P., Fan M. Hypoxic preconditioning up-regulates glucose transport activity and glucose transporter (GLUT1 and GLUT3) gene expression after acute anoxic exposure in the cultured rat hippocampal neurons and astrocytes. Brain Res. 2008, 1211:22-29.
    • (2008) Brain Res. , vol.1211 , pp. 22-29
    • Yu, S.1    Zhao, T.2    Guo, M.3    Fang, H.4    Ma, J.5    Ding, A.6    Wang, F.7    Chan, P.8    Fan, M.9
  • 62
    • 4043107784 scopus 로고    scopus 로고
    • Inhibition of tyrosine hydroxylase expression in alpha-synuclein-transfected dopaminergic neuronal cells
    • Yu S., Zuo X., Li Y., Zhang C., Zhou M., Zhang Y.A., Uéda K., Chan P. Inhibition of tyrosine hydroxylase expression in alpha-synuclein-transfected dopaminergic neuronal cells. Neurosci. Lett. 2004, 367:34-39.
    • (2004) Neurosci. Lett. , vol.367 , pp. 34-39
    • Yu, S.1    Zuo, X.2    Li, Y.3    Zhang, C.4    Zhou, M.5    Zhang, Y.A.6    Uéda, K.7    Chan, P.8


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