Cited by 686Parkinson's Disease Mechanisms and TreatmentsNeuroinflammation and Neurodegeneration MechanismsNuclear Receptors and Signaling

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Glial cytoplasmic inclusions in white matter oligodendrocytes of multiple system atrophy brains contain insoluble α‐synuclein

Tu, Pang‐hsien, Galvin, James E., Baba, Minami, Giasson, Benoit, Tomita, Taisuke, Leight, Susan, Nakajo, Shigeo, Iwatsubo, Takeshi, Trojanowski, John Q., Lee, Virginia M.‐Y.·1998·Annals of Neurology

DOI 10.1002/ana.410440324

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Abstract

Recently, α‐synuclein was shown to be a structural component of the filaments in Lewy bodies (LBs) of Parkinson's disease (PD), dementia with LBs (DLB) as well as the LB variant of Alzheimer's disease, and this suggests that α‐synuclein could play a mechanistic role in the pathogenesis of these disorders. To determine whether α‐synuclein is a building block of inclusions in other neurodegenerative movement disorders, we examined brains from patients with multiple system atrophy (MSA) and detected α‐synuclein, but not β‐ or γ‐synuclein, in glial cytoplasmic inclusions (GCIs) throughout the MSA brain. In MSA white matter, α‐synuclein–positive GCIs were restricted to oligodendrocytes, and α‐synuclein accumulated selectively in MSA white matter with α‐synuclein–positive GCIs. Taken together with evidence that LBs contain insoluble α‐synuclein, our data suggest that a reduction in the solubility of α‐synuclein may induce this protein to form filaments that aggregate into cytoplasmic inclusions, which contribute to the dysfunction or death of glial cells as well as neurons in neurodegenerative disorders with different phenotypes.

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α-Synuclein in Lewy bodies
Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382
Self-citation
Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240
AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
Krüger, R., Kuhn, W., Müller, T., Woitalla, D., Graeber, M., Kösel, S., Przuntek, H., Epplen, J. T., Schols, L., & Riess, O. (1998) · Nature Genetics · doi:10.1038/ng0298-106 · Cited by 3,836
α-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. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6469 · Cited by 2,868
Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal
Maroteaux, L., Campanelli, J., & Scheller, R. (1988) · Journal of Neuroscience · doi:10.1523/jneurosci.08-08-02804.1988 · Cited by 1,646
Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies.
(1998) · Europe PMC (PubMed Central) · Cited by 1,594
Self-citation
Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease.
Uéda, K., Fukushima, H., Masliah, E., Xia, Y., Iwai, A., Yoshimoto, M., Otero, D. A., Kondo, J. D. M., Ihara, Y., & Saitoh, T. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11282 · Cited by 1,502
The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system
Iwai, A., Masliah, E., Yoshimoto, M., Ge, N., Flanagan, L., Rohan de Silva, H. A., Kittel, A., & Saitoh, T. (1995) · Neuron · doi:10.1016/0896-6273(95)90302-x · Cited by 1,316
Identification of two distinct synucleins from human brain
Jakes, R., Spillantini, M. G., & Goedert, M. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00395-5 · Cited by 1,080
Glial cytoplasmic inclusions in the CNS of patients with multiple system atrophy (striatonigral degeneration, olivopontocerebellar atrophy and Shy-Drager syndrome)
Papp, M. I., Kahn, J. E., & Lantos, P. L. (1989) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(89)90219-0 · Cited by 991

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Yamazaki, M., Arai, Y., Baba, M., Iwatsubo, T., Mori, O., Katayama, Y., & Oyanagi, K. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.7.585 · Cited by 98
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BackgroundSelf-citation
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BackgroundSelf-citation
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Takahashi, T., Yamashita, H., Nakamura, T., Nagano, Y., & Nakamura, S. (2002) · Brain Research · doi:10.1016/s0006-8993(02)02498-8 · Cited by 97
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“Despite the identification of GCIs as the neuropathological hallmark of MSA in 1989 [36], α-synuclein was not recognized as the primary protein component until 1998 [44, 49, 50].”
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Iwata, A., Miura, S., Kanazawa, I., Sawada, M., & Nukina, N. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.t01-1-00232.x · Cited by 98
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Self-citation
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“Accumulation of these pathogenic aggregates led to oligodendrocyte cell death and neurotoxicity (Tu et al., 1998; Narasimhan et al., 2020), adding further complexity to the non-cell autonomous interactions contributing to the spread of pathogenic protein aggregation and progression of neurodegeneration.”
Background
Oligomeric α-synuclein inhibits tubulin polymerization
Chen, L., Jin, J., Davis, J., Zhou, Y. F., Wang, Y., Liu, J., Lockhart, P. J., & Zhang, J. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.02.163 · Cited by 94
Glial cell death induced by overexpression of α‐synuclein
Stefanova, N., Klimaschewski, L., Poewe, W., Wenning, G. K., & Reindl, M. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.1171 · Cited by 93
“…event in these disorders causing apoptosis of glial cells, disturbing the functional integrity of axons and dendrites and actually preceding neuronal cell death. a-Synuclein is a specific marker of the glial cytoplasmic inclusions (GCIs) observed in oligodendrocytes of MSA brains (Tu et al., 1998).”
BackgroundInfluential
Recent developments in multiple system atrophy
Wenning, G. K., & Stefanova, N. (2009) · Journal of Neurology · doi:10.1007/s00415-009-5173-8 · Cited by 92
“Some years ago, glial cytoplasmic inclusions (GCIs) containing alpha-synuclein filaments have been defined as a cellular hallmark of MSA [92, 129, 169, 182, 193, 204].”
Background
α-synuclein fibrils constitute the central core of oligodendroglial inclusion filaments in multiple system atrophy
Gai, W. P., Pountney, D. L., Power, J. H. T., Li, Q. X., Culvenor, J. G., McLean, C., Jensen, P. H., & Blumbergs, P. C. (2003) · Experimental Neurology · doi:10.1016/s0014-4886(03)00004-9 · Cited by 96
Differential Expression and Distribution of α-, β-, and γ-Synuclein in the Developing Human Substantia Nigra
Galvin, J. E., Schuck, T., Lee, V. M. ‐., & Trojanowski, J. Q. (2001) · Experimental Neurology · doi:10.1006/exnr.2000.7615 · Cited by 92
Self-citation
Toll-like receptor 4 stimulation with monophosphoryl lipid A ameliorates motor deficits and nigral neurodegeneration triggered by extraneuronal α-synucleinopathy
Venezia, S., Refolo, V., Polissidis, A., Stefanis, L., Wenning, G. K., & Stefanova, N. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0195-7 · Cited by 93
Are We Ready for Detecting α-Synuclein Prone to Aggregation in Patients? The Case of “Protein-Misfolding Cyclic Amplification” and “Real-Time Quaking-Induced Conversion” as Diagnostic Tools
Paciotti, S., Bellomo, G., Gatticchi, L., & Parnetti, L. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00415 · Cited by 93
Clinical and neuropathological correlates of Lewy body disease
Hishikawa, N., Hashizume, Y., Yoshida, M., & Sobue, G. (2003) · Acta Neuropathologica · doi:10.1007/s00401-002-0651-4 · Cited by 90
Selective vulnerability in α-synucleinopathies
Alegre‐Abarrategui, J., Brimblecombe, K. R., Roberts, R. F., Velentza‐Almpani, E., Tilley, B. S., Bengoa‐Vergniory, N., & Proukakis, C. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02010-2 · Cited by 90
“While accumulation of α-syn in the glial cells has been described in α-synucleinopathies [169, 180], α-syn accumulation was not detected neither in microglia nor astrocytes in a study with a primate MPTP model [115].”
Background
An autopsy case of early (“minimal change”) olivopontocerebellar atrophy (multiple system atrophy-cerebellar)
Wakabayashi, K., Mori, F., Nishie, M., Oyama, Y., Kurihara, A., Yoshimoto, M., & Kuroda, N. (2005) · Acta Neuropathologica · doi:10.1007/s00401-005-1029-1 · Cited by 87
“Since the discovery of a-synuclein as a major component of glial and neuronal inclusions in MSA [2, 6, 17, 22, 31- 33 ], two neurodegenerative processes have been considered in this disease: one is the widespread occurrence of GCIs associated with oligodendroglial-myelin degeneration in the central nervous system, and…”
Structure/function of α‐synuclein in health and disease: rational development of animal models for Parkinson's and related diseases
Kahle, P. J., Haass, C., Kretzschmar, H. A., & Neumann, M. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01020.x · Cited by 86
“Finally, aSYN was identified as the building block of the GCIs that characterize MSA (Gai et al. 1998; Tu et al. 1998; Wakabayashi et al. 1998).”
Background
The effect of truncation on prion-like properties of α-synuclein
Terada, M., Suzuki, G., Nonaka, T., Kametani, F., Tamaoka, A., & Hasegawa, M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.001862 · Cited by 85
The significance of tau and α-synuclein inclusions in neurodegenerative diseases
Goedert, M. (2001) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(00)00200-8 · Cited by 86
Fluoxetine ameliorates behavioral and neuropathological deficits in a transgenic model mouse of α-synucleinopathy
Ubhi, K. K., Inglis, C. A., Mante, M., Patrick, C., Adame, A., Spencer, B. J., Rockenstein, E. M., May, V. E. L., Winkler, J., & Masliah, E. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.01.008 · Cited by 87
“The characteristic oligodendrocytic neuropathological lesions are known as glial cytoplasmic inclusions (GCI) (Arima et al., 1998; Tu et al., 1998; Wakabayashi et al., 1998a, 1998b).”
Background
α‐Synuclein pathology is highly dependent on the case selection
Parkkinen, L., Soininen, H. S., Laakso, M., & Alafuzoff, I. I. (2001) · Neuropathology and Applied Neurobiology · doi:10.1046/j.0305-1846.2001.00342.x · Cited by 86
Synucleins in glaucoma: Implication of γ‐synuclein in glaucomatous alterations in the optic nerve
Surgucheva, I. G., McMahan, B., Ahmed, F. A. K. M., Tomarev, S. I., Wax, M. B., & Surguchov, A. P. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10198 · Cited by 86
“, 1998), and glial cytoplasmic inclusions in multiple system atrophy (Tu et al., 1998; Dickson et al., 1999).”
Background
Alpha-synuclein dysfunction in Lewy body diseases
Tofaris, G. K., & Spillantini, M. G. (2005) · Movement Disorders · doi:10.1002/mds.20538 · Cited by 87
Sensitization of Neuronal Cells to Oxidative Stress with Mutated Human α‐Synuclein
Ko, L., Mehta, N. D., Farrer, M. J., Easson, C., Hussey, J., Yen, S. H., Hardy, J., & Yen, S.-H. C. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0752546.x · Cited by 86
“…(synucleinopathy) constitutes a cardinal feature shared by numerous neurodegenerative disorders including Parkinson’s disease (PD), diffuse Lewy body disease, multiple system atrophy, and AD (Arima et al., 1998a,b; Baba et al., 1998; Mezey et al., 1998a; Spillantini et al., 1998; Tu et al., 1998).”
Background
Immunohistochemical comparison of α- and β-synuclein in adult rat central nervous system
Mori, F., Tanji, K., Yoshimoto, M., Takahashi, H., & Wakabayashi, K. (2002) · Brain Research · doi:10.1016/s0006-8993(02)02643-4 · Cited by 84
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Butler, B., Sambo, D. O., & Khoshbouei, H. (2016) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2016.06.001 · Cited by 90
“Despite its role in a number of pathological conditions coined synucleinopathies, which include Parkinson’s disease and Dementia with Lewy Bodies and Multiple Systems Atrophy (Spillantini et al., 1997; Ueda et al., 1993; Recchia et al., 2004; Tu et al., 1998; Baba et al., 1998), the exact physiological function/s of a…”
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Wakabayashi, K., Engelender, S., Tanaka, Y., Yoshimoto, M., Mori, F., Tsuji, S., Ross, C. A., & Takahashi, H. (2001) · Acta Neuropathologica · doi:10.1007/s004010100451 · Cited by 84
C-terminal α-synuclein immunoreactivity in structures other than Lewy bodies in neurodegenerative disorders
Takeda, A., Hashimoto, M., Mallory, M., Sundsumo, M., Hansen, L., & Masliah, E. (2000) · Acta Neuropathologica · doi:10.1007/pl00007441 · Cited by 83
“Furthermore, recent studies have shown that α-synuclein immunoreactivity is also present in the filamentous inclusions of multiple system atrophy (MSA) [7, 22, 26 , 29, 30], but not apparently in neurofibrillary tangles (NFTs) and Pick bodies [25, 30].”
BackgroundMethod
Sensitivity and specificity of a seed amplification assay for diagnosis of multiple system atrophy: a multicentre cohort study
Ma, Y., Farris, C. M., Weber, S., Schade, S., Nguyen, H., Pérez‐Soriano, A., Giraldo, D. M., Fernández, M., Soto, M., Cámara, A., et al. (2024) · The Lancet Neurology · doi:10.1016/s1474-4422(24)00395-8 · Cited by 84
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Jo, E., Darabie, A. A., Han, K. A., Tandon, A., Fraser, P. E., & McLaurin, J. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04250.x · Cited by 83
“Immunocytochemistry has revealed a-synuclein positive inclusions within astrocytes and oligodendrocytes of PD-patients and glial and neuronal inclusions of multiple system atrophy patients [9–14].”
Background
Pathologic Modifications of α-Synuclein in 1-Methyl-4-Phenyl-1,2,3,6-Tetrahydropyridine (MPTP)-Treated Squirrel Monkeys
McCormack, A. L., Mak, S. K., Shenasa, M., Langston, J. W., Forno, L. S., & Monte, D. A. D. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318180f0bd · Cited by 89
“Accumulation of >-synuclein within nonneuronal cells, including astrocytes and oligodendroglia, has been described in PD, multiple system atrophy, and other synucleinopathies (5, 25, 26).”
Neuronal and glial accumulation of α- and β-synucleins in human lipidoses
Suzuki, K., Iseki, E., Togo, T., Yamaguchi, A., Katsuse, O., Katsuyama, K., Kanzaki, S., Shiozaki, K., Kawanishi, C., Yamashita, S., et al. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0264-z · Cited by 83
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Self-citation
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Waxman, E. A., Duda, J. E., & Giasson, B. I. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0375-1 · Cited by 79
Self-citation
A novel, high‐efficiency cellular model of fibrillar α‐synuclein inclusions and the examination of mutations that inhibit amyloid formation
Waxman, E. A., & Giasson, B. I. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06592.x · Cited by 85
Self-citation
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Spillantini, M. G. (1999) · Parkinsonism & Related Disorders · doi:10.1016/s1353-8020(99)00031-0 · Cited by 80
Widespread occurrence of argyrophilic glial inclusions in Parkinson's disease
Hishikawa, N., Hashizume, Y., Yoshida, M., & Sobue, G. (2001) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.2001.00345.x · Cited by 83
Atypical multiple system atrophy is a new subtype of frontotemporal lobar degeneration: frontotemporal lobar degeneration associated with α-synuclein
Aoki, N., Boyer, P. J., Lund, C., Lin, W.-L., Koga, S., Ross, O. A., Weiner, M., Lipton, A. M., Powers, J. M., White, C. L., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1442-z · Cited by 82
“The discovery that GCI were composed of α-synuclein led to classification of MSA as an α-synucleinopathy, a designation shared with Lewy body disease (LBD) presenting clinically as Parkinson’s disease or dementia with Lewy bodies [8, 36, 38, 43].”
Defined α-synuclein prion-like molecular assemblies spreading in cell culture
Aulić, S., Le, T. T. N., Moda, F., Abounit, S., Corvaglia, S., Casalis, L., Gustincich, S., Zurzolo, C., Tagliavini, F., & Legname, G. (2014) · BMC Neuroscience · doi:10.1186/1471-2202-15-69 · Cited by 84
“Neurons containing LBs are the hallmark of PD and DLB, whereas in MSA α-syn is deposited in oligodendrocytes referred to as glial cytoplasmic inclusions (GCIs) [2-4].”
Background
Chapter 33 The history of movement disorders
Lanska, D. J. (2009) · Handbook of clinical neurology · doi:10.1016/s0072-9752(08)02133-7 · Cited by 83
Active immunization therapies for Parkinson's disease and multiple system atrophy
Schneeberger, A., Tierney, L., & Mandler, M. (2015) · Movement Disorders · doi:10.1002/mds.26377 · Cited by 86
Expression of ??-synuclein in a human glioma cell line and its up-regulation by interleukin-1??
Tanji, K., Imaizumi, T., Yoshida, H., Mori, F., Yoshimoto, M., Satoh, K., & Wakabayashi, K. (2001) · Neuroreport · doi:10.1097/00001756-200107030-00028 · Cited by 81
Mechanisms of cell death in neurodegenerative disorders
Jellinger, K. A., & Stadelmann, C. (2000) · Springer eBooks · doi:10.1007/978-3-7091-6781-6_13 · Cited by 80
Increased α-synuclein phosphorylation and nitration in the aging primate substantia nigra
McCormack, A. L., Mak, S. K., & Monte, D. A. D. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.50 · Cited by 80
“pathic Parkinson’s disease (PD) and other age-related neurodegenerative disorders such as dementia with Lewy bodies and multiple system atrophy.(1,2) Intraneuronal accumulation of insoluble a-synuclein, as reflected by the formation Lewy bodies and Lewy neurites, is typically observed in postmortem brains of all PD pa…”
Background
Properties of NACP/α-synuclein and its role in Alzheimer’s disease
Iwai, A. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00036-3 · Cited by 78
Mitochondrial inhibitor 3‐nitroproprionic acid enhances oxidative modification of alpha‐synuclein in a transgenic mouse model of multiple system atrophy
Ubhi, K. K., Lee, P. H., Adame, A., Inglis, C. A., Mante, M., Rockenstein, E. M., Stefanova, N., Wenning, G. K., & Masliah, E. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22089 · Cited by 83
“…modified asyn forms a major component of the inclusions observed in MSA (Burn and Jaros, 2001; Duda et al., 2000b; Kikuchi et al., 2002; Tu et al., 1998; Yamashita et al., 2000), and other asyn nucleopathies (Duda et al., 2000a; Giasson et al., 2000; Gomez-Tortosa et al., 2002; Kikuchi…”
Background
Different α-synuclein prion strains cause dementia with Lewy bodies and multiple system atrophy
Ayers, J. I., Lee, J., Monteiro, O., Woerman, A. L., Lazar, A., Condello, C., Paras, N. A., & Prusiner, S. B. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2113489119 · Cited by 79
Smoking habits in multiple system atrophy and progressive supranuclear palsy
Vanacore, N., Bonifati, V., Fabbrini, G., Colosimo, C., Marconi, R., Nicholl, D. J., Bonuccelli, U., Stocchi, F., Lamberti, P., Volpe, G., et al. (2000) · Neurology · doi:10.1212/wnl.54.1.114 · Cited by 79
Alpha-synuclein potentiates Ca2+ influx through voltage-dependent Ca2+ channels
Adamczyk, A., & Strosznajder, J. B. (2006) · Neuroreport · doi:10.1097/wnr.0b013e3280115185 · Cited by 79
Characterization of kinases involved in the phosphorylation of aggregated α‐synuclein
Waxman, E. A., & Giasson, B. I. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22537 · Cited by 78
“a-Syn is also the major component of pathological inclusions in other neurodegenerative diseases, including dementia with Lewy bodies (DLB), Lewy body variant of Alzheimer’s disease (LBVAD), and multiple systems atrophy (MSA), collectively termed a-synucleinopathies (Spillantini et al., 1997, 1998; Tu et al., 1998; Li…”
BackgroundSelf-citation
α-Synuclein Accumulates in Purkinje Cells in Lewy Body Disease but not in Multiple System Atrophy
Mori, F., Piao, Y.-S., Hayashi, S., Fujiwara, H., Hasegawa, M., Yoshimoto, M., Iwatsubo, T., Takahashi, H., & Wakabayashi, K. (2003) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/62.8.812 · Cited by 79
Self-citation
Co-localization of α-synuclein and phosphorylated tau in neuronal and glial cytoplasmic inclusions in a patient with multiple system atrophy of long duration
Piao, Y.-S., Hayashi, S., Hasegawa, M., Wakabayashi, K., Yamada, M., Yoshimoto, M., Ishikawa, A., Iwatsubo, T., & Takahashi, H. (2001) · Acta Neuropathologica · doi:10.1007/s004010000292 · Cited by 78
“Importantly, it has also been shown recently that, like Lewy bodies (LBs) in Parkinson’s disease (PD) and diffuse Lewy body disease (DLBD), these NCIs and GCIs in MSA contain α -synuclein [3, 10, 12, 36, 41 , 44, 45], the precursor protein of the non-Aβ component of Alzheimer’s disease (AD) amyloid (NACP) [20, 42].”
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A characterization of Gaucher iPS-derived astrocytes: Potential implications for Parkinson's disease
Aflaki, E., Stubblefield, B. K., McGlinchey, R. P., McMahon, B., Ory, D. S., & Sidransky, E. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104647 · Cited by 77
“While astrocytes express extremely low levels of α-syn, some studies in both PD and DLB have shown the presence of aggregated α-syn in astrocytes and oligodendrocytes (Braak et al., 2007; Tu et al., 1998).”
Background
Annular α‐synuclein species from purified multiple system atrophy inclusions
Pountney, D. L., Lowe, R. D., Quilty, M. C., Vickers, J. C., Voelcker, N. H., & Gai, W. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02533.x · Cited by 77
“GCIs are composed primarily of the protein, a-synuclein (Gai et al. 1998; Spillantini et al. 1998; Tu et al. 1998; Wakabayashi et al. 1998), just like the neuronal cytoplasmic inclusions, Lewy bodies (LB), found in Parkinson’s disease (PD) and dementia with Lewy bodies (DLB) (Duda et al. 2000;…”
Background
Modulating Self‐Assembly of Amyloidogenic Proteins as a Therapeutic Approach for Neurodegenerative Diseases: Strategies and Mechanisms
Liu, T., & Bitan, G. (2012) · ChemMedChem · doi:10.1002/cmdc.201100585 · Cited by 77
Cell cycle aberrations by α-synuclein over-expression and cyclin B immunoreactivity in Lewy bodies
Lee, S. S., Kim, Y. M., Junn, E., Lee, G., Park, K. H., Tanaka, M., Ronchetti, R., Quezado, M., & Mouradian, M. M. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00196-3 · Cited by 75
“For example, in the brains of patients with multi-system atrophy (MSA), -synuclein-positive inclusions are found in the cytoplasm of oligodendrocytes and neurons [4,74] as well as in the nuclei of neurons [69].”
Background
Mechanisms of alpha-synuclein toxicity: An update and outlook
Brás, I. C., Xylaki, M., & Outeiro, T. F. (2019) · Progress in brain research · doi:10.1016/bs.pbr.2019.10.005 · Cited by 78
Proteolytic Stress Causes Heat Shock Protein Induction, Tau Ubiquitination, and the Recruitment of Ubiquitin to Tau-Positive Aggregates in Oligodendrocytes in Culture
Goldbaum, O., & Richter‐Landsberg, C. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1307-04.2004 · Cited by 75
Abundant neuritic inclusions and microvacuolar changes in a case of diffuse Lewy body disease with the A53T mutation in the α-synuclein gene
Yamaguchi, K., Cochran, E. J., Murrell, J. R., Polymeropoulos, M. H., Shannon, K. M., Crowther, R. A., Goedert, M., & Ghetti, B. F. (2005) · Acta Neuropathologica · doi:10.1007/s00401-005-1042-4 · Cited by 77
“In addition, the filamentous glial and neuronal inclusions of multiple system atrophy (MSA) have also been found to contain a-synuclein as a major component [35, 38 , 39].”
Background
A simple, versatile and robust centrifugation‐based filtration protocol for the isolation and quantification of α‐synuclein monomers, oligomers and fibrils: Towards improving experimental reproducibility in α‐synuclein research
Kumar, S. T., Donzelli, S., Chiki, A., Syed, M. M. K., & Lashuel, H. A. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.14955 · Cited by 69
Glial cytoplasmic inclusions and tissue injury in multiple system atrophy: A quantitative study in white matter (olivopontocerebellar system) and gray matter (nigrostriatal system)
Ishizawa, K., Komori, T., Arai, N., Mizutani, T., & Hirose, T. (2008) · Neuropathology · doi:10.1111/j.1440-1789.2007.00855.x · Cited by 74
“In a native condition, a-syn is soluble with little secondary structure;20,22 however, in a-synucleinopathies, a-syn acquires physiological insolubility by taking on b-sheet-like structures and aggregates into filaments in GCIs and LBs.6,9,20,23 Phosphorylation of a-syn is another important factor that contributes to…”
Background
Long-term deep brain stimulation in a patient with essential tremor: clinical response and postmortem correlation with stimulator termination sites in ventral thalamus
Boockvar, J. A., Telfeian, A. E., Baltuch, G. H., Skolnick, B. E., Simuni, T., Stern, M., Schmidt, M. L., & Trojanowski, J. Q. (2000) · Journal of neurosurgery · doi:10.3171/jns.2000.93.1.0140 · Cited by 73
Self-citation
Proteasome Inhibition Stabilizes Tau Inclusions in Oligodendroglial Cells that Occur after Treatment with Okadaic Acid
Goldbaum, O., Oppermann, M., Handschuh, M., Dabir, D. V., Zhang, B., Forman, M. S., Trojanowski, J. Q., Lee, V. M. ‐., & Richter‐Landsberg, C. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-26-08872.2003 · Cited by 73
“GCIs are composed of a meshwork of loosely packed filaments and stained with antibodies against tau, ubiquitin, -synuclein, and the small heat-shock protein (HSP) Bcrystallin, although -synuclein is the major building block of these inclusions (Chin and Goldman, 1996; Tu et al., 1998; Komori, 1999).”
BackgroundMethodSelf-citation
The role of lipids in α-synuclein misfolding and neurotoxicity
Ugalde, C. L., Lawson, V., Finkelstein, D. I., & Hill, A. F. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.007500 · Cited by 77
Attenuated Neurodegenerative Disease Phenotype in Tau Transgenic Mouse Lacking Neurofilaments
Ishihara, T., Higuchi, M., Zhang, B., Yoshiyama, Y., Hong, M., Trojanowski, J. Q., & Lee, V. M. ‐. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-16-06026.2001 · Cited by 71
“NFs are also detected in Lewy bodies in which they coexist with -synuclein (Tu et al., 1998).”
BackgroundSelf-citation
Multiple system atrophy: An update
Wenning, G. K., Geser, F., Stampfer‐Kountchev, M., & Tison, F. (2003) · Movement Disorders · doi:10.1002/mds.10561 · Cited by 71
Glia cells in amyotrophic lateral sclerosis: New clues to understanding an old disease?
Neusch, C., Bähr, M., & Schneider‐Gold, C. (2007) · Muscle & Nerve · doi:10.1002/mus.20768 · Cited by 69
The Prion Hypothesis of Parkinson’s Disease
Chu, Y., & Kordower, J. H. (2015) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-015-0549-x · Cited by 74
The interrelationship of proteasome impairment and oligomeric intermediates in neurodegeneration
Deger, J. M., Gerson, J. E., & Kayed, R. (2015) · Aging Cell · doi:10.1111/acel.12359 · Cited by 69
“…with sporadic and familial AD, Down’s syndrome, multiple system atrophy, and in a small fraction of Hallervorden-Spatz cases (Lippa et al., 1998; Tu et al., 1998). a-synuclein has implications for a multitude of major neurodegenerative diseases and is therefore at the center of intensive…”
Background
α-Synuclein-immunoreactive structure formation is enhanced in sympathetic ganglia of patients with multiple system atrophy
Sone, M., Yoshida, M., Hashizume, Y., Hishikawa, N., & Sobue, G. (2005) · Acta Neuropathologica · doi:10.1007/s00401-005-1013-9 · Cited by 69
Progression of alpha‐synuclein pathology in multiple system atrophy of the cerebellar type
Brettschneider, J., Irwin, D. J., Boluda, S., Byrne, M., Fang, L., Lee, E. B., Robinson, J. L., Suh, E. R., Deerlin, V. M. V., Toledo, J. B., et al. (2016) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12362 · Cited by 70
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Novel biphasic effect of pyrrolidine dithiocarbamate on neuronal cell viability is mediated by the differential regulation of intracellular zinc and copper ion levels, NF-?b, and MAP kinases
Chung, K. C., Park, J. H., Kim, C. H., Lee, H. W., Sato, N., Uchiyama, Y., & Ahn, Y. S. (2000) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(20000101)59:1 · Cited by 74
Progressive striatonigral degeneration in a transgenic mouse model of multiple system atrophy: translational implications for interventional therapies
Refolo, V., Bez, F., Polissidis, A., Kuzdas-Wood, D., Sturm, E., Kamaratou, M., Poewe, W., Stefanis, L., Angela Cenci, M., Romero-Ramos, M., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0504-y · Cited by 67
“The major component of the GCIs is filamentous α-synuclein (α-syn) [31, 53, 63, 67].”
Background
Primary progressive aphasia as the initial manifestation of corticobasal degeneration and unusual tauopathies
Ferrer, I., Hern�ndez, I., Boada, M., Llorente, A., Rey, M. J., Cardozo, A., Ezquerra, M., & Puig, B. (2003) · Acta Neuropathologica · doi:10.1007/s00401-003-0756-4 · Cited by 67
Multiple system atrophy of the cerebellar type: Clinical state of the art
Lin, D. J., Hermann, K. L., & Schmahmann, J. D. (2014) · Movement Disorders · doi:10.1002/mds.25847 · Cited by 67
Hallucinations in Neurodegenerative Diseases
Burghaus, L., Eggers, C., Timmermann, L., Fink, G. R., & Diederich, N. J. (2011) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2011.00247.x · Cited by 68
“In MSA, aggregated alpha-synuclein is also a component of glial cytoplasmatic inclusions [6].”
Background
Alpha-synuclein at the intracellular and the extracellular side: functional and dysfunctional implications
Ottolini, D., Calí, T., Szabó, I., & Brini, M. (2016) · Biological Chemistry · doi:10.1515/hsz-2016-0201 · Cited by 65
α-Synuclein: Its Biological Function and Role in Neurodegenerative Diseases
Kaplan, B., Ratner, V., & Haas, E. (2003) · Journal of Molecular Neuroscience · doi:10.1385/jmn:20:2:83 · Cited by 64
An Update on the Critical Role of α-Synuclein in Parkinson’s Disease and Other Synucleinopathies: from Tissue to Cellular and Molecular Levels
Serratos, I. N., Hernández‐Pérez, E., Campos, C., Aschner, M., & Santamarı́a, A. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02596-3 · Cited by 70
Therapeutic functions of astrocytes to treat α-synuclein pathology in Parkinson’s disease
Yang, Y., Song, J., Choi, Y. R., Kim, S. H., Seok, M., Wulansari, N., Darsono, W. H. W., Kwon, O., Chang, M., Park, S. M., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2110746119 · Cited by 61
α-Synuclein aggregates amplified from patient-derived Lewy bodies recapitulate Lewy body diseases in mice
Uemura, N., Marotta, N. P., Ara, J. E., Meymand, E. S., Zhang, B., Kameda, H., Koike, M., Luk, K. C., Trojanowski, J. Q., & Lee, V. M. ‐. (2023) · Nature Communications · doi:10.1038/s41467-023-42705-5 · Cited by 64
Self-citation
Alteration of autophagosomal proteins in the brain of multiple system atrophy
Tanji, K., Odagiri, S., Maruyama, A., Mori, F., Kakita, A., Takahashi, H., & Wakabayashi, K. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.08.017 · Cited by 64
“Indeed, experimental evidence indicates that autophagic impairment results in neurodegenerative symptom in model mice (Hara et al., 2006; Komatsu et al., 2006; Wang et al., 2006; Komatsu et al., 2007), and also autophagy-related proteins are biochemically and pathologically altered in PD and DLB (Alvarez-Erviti et al.…”
Influential
Role of TPPP/p25 on α-synuclein-mediated oligodendroglial degeneration and the protective effect of SIRT2 inhibition in a cellular model of multiple system atrophy
Hasegawa, T., Baba, T., Kobayashi, M., Konno, M., Sugeno, N., Kikuchi, A., Itoyama, Y., & Takeda, A. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2010.09.002 · Cited by 64
“GCIs were initially detected with sliver stains and ubiquitin immunostaining; however, the most sensitive and specific marker for GCIs is a-SYN, which is a 140-amino acid presynaptic protein that is also seen in the filamentous neuronal Lewy bodies (LBs) in Parkinson’s disease (PD) (Arima et al., 1998; Spillantini et…”
The pathogenesis linked to coenzyme Q10 insufficiency in iPSC-derived neurons from patients with multiple-system atrophy
Nakamoto, F. K., Okamoto, S., Mitsui, J., Sone, T., Ishikawa, M., Yamamoto, Y., Kanegae, Y., Nakatake, Y., Imaizumi, K., Ishiura, H., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-32573-1 · Cited by 64
Endogenous oligodendroglial alpha-synuclein and TPPP/p25α orchestrate alpha-synuclein pathology in experimental multiple system atrophy models
Mavroeidi, P., Arvanitaki, F., Karakitsou, A.-K., Vetsi, M., Kloukina, I., Zweckstetter, M., Giller, K., Becker, S., Sorrentino, Z. A., Giasson, B. I., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02014-y · Cited by 66
“Neuropathologically, MSA is characterized by the accumulation of the neuronal presynaptic protein alpha-synuclein (aSyn) within oligodendrocytes, the myelin-producing cells of the central nervous system, forming glial cytoplasmic inclusions (GCIs), which represent the main histopathological hallmark of MSA [67, 73].”
Self-citation
Juvenile-onset generalized neuroaxonal dystrophy (Hallervorden-Spatz disease) with diffuse neurofibrillary and Lewy body pathology
Wakabayashi, K., Fukushima, T., Koide, R., Horikawa, Y., Hasegawa, M., Watanabe, Y., Noda, T., Eguchi, I., Morita, T., Yoshimoto, M., et al. (2000) · Acta Neuropathologica · doi:10.1007/s004010050049 · Cited by 64
“In agreement with previous studies [3, 37 ], these LBs were strongly immunolabeled with anti-ubiquitin and anti- α-synuclein antibodies (Fig. 2 I). α-Synuclein-positive degenerating neurites (also called Lewy neurites) were also found in the hippocampus, basal ganglia, brain stem and spinal gray matter.”
ResultSelf-citation
Role of Oxidative Damage in Protein Aggregation Associated with Parkinson's Disease and Related Disorders
Norris, E. H., & Giasson, B. I. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.672 · Cited by 61
Self-citation
Oligodendrogliopathy in neurodegenerative diseases with abnormal protein aggregates: The forgotten partner
Ferrer, I. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.07.004 · Cited by 65
Late‐onset neurodegenerative diseases—the role of protein insolubility
Johnson, W. G. (2000) · Journal of Anatomy · doi:10.1046/j.1469-7580.2000.19640609.x · Cited by 61
No mutation in the entire coding region of the α-synuclein gene in pathologically confirmed cases of multiple system atrophy
Ozawa, T., Takano, H., Onodera, O., Kobayashi, H., Ikeuchi, T., Koide, R., Okuizumi, K., Shimohata, T., Wakabayashi, K., Takahashi, H., et al. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00475-9 · Cited by 61
Cerebral mitochondrial electron transport chain dysfunction in multiple system atrophy and Parkinson’s disease
Foti, S. C., Hargreaves, I. P., Carrington, S., Kiely, A. P., Houlden, H., & Holton, J. L. (2019) · Scientific Reports · doi:10.1038/s41598-019-42902-7 · Cited by 58
Widespread occurrence of α‐synuclein/NACP‐immunoreactive neuronal inclusions in juvenileand adult‐onset Hallervorden–Spatz diseasewith Lewy bodies
Wakabayashi, Yoshimoto, Fukushima, Koide, R., Horikawa, Morita, & Takahashi, Y. (1999) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.1999.00193.x · Cited by 61

Authors: Tu, P., Galvin, J. E., Baba, M., Giasson, B., Tomita, T., Leight, S., Nakajo, S., Iwatsubo, T., Trojanowski, J. Q., & Lee, V. M. ‐.
Affiliations: University of Pennsylvania (US)
The University of Tokyo (JP)
SHOWA Medical University (JP)
Corresponding author: Lee, Virginia M.‐Y.
ORCID: Tu, Pang‐hsien
Galvin, James E.
Giasson, Benoit
Tomita, Taisuke
Iwatsubo, Takeshi
Trojanowski, John Q.
Lee, Virginia M.‐Y.
Venue: Annals of Neurology
Publisher: Wiley
Published: 1998-09
Volume: 44
Issue: 3
Pages: 415-422
ISSN: 0364-5134 (ISSN-L)
1531-8249
DOI: 10.1002/ana.410440324
OpenAlex: W2133068803
Cited by: 686
References: 43
Citations by year: 2026: 14 · 2025: 21 · 2024: 33 · 2023: 23 · 2022: 25 · 2021: 28 · 2020: 21 · 2019: 24 · 2018: 21 · 2017: 23 · 2016: 12 · 2015: 20 · 2014: 24 · 2013: 18 · 2012: 17
FWCI: 30.21
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 2229 d)
Locations: Annals of Neurology (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of Mental Health (MH.NS 31862)
Topics: Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
Keywords: alpha-synuclein, glial cytoplasmic inclusions, multiple system atrophy, oligodendrocytes, white matter, Lewy bodies, protein aggregation, neurodegenerative movement disorders, immunoelectron microscopy, synuclein
MeSH terms: Adult, Aged, Aged, 80 and over, Antibodies, Inclusion Bodies, Female, Humans, Male, Actin Cytoskeleton, Middle Aged, Myelin Sheath, Nerve Tissue Proteins, Neuroglia, Oligodendroglia, Solubility, Multiple System Atrophy, Synucleins, alpha-Synuclein, gamma-Synuclein

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Glial cytoplasmic inclusions in white matter oligodendrocytes of multiple system atrophy brains contain insoluble α‐synuclein

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