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Ultrastructure of alpha-synuclein-positive aggregations in U373 astrocytoma and rat primary glial cells

Stefanova, N; Emgård-Mattson, Mia LU ; Klimaschewski, L; Wenning, GK and Reindl, M (2002) In Neuroscience Letters 323(1). p.37-40
Abstract
Abnormal alpha-synuclein-positive glial cytoplasmic inclusions are found in Parkinson's disease, multiple system atrophy and dementia with Lewy bodies. We have recently developed an in vitro model of alpha-synuclein-immunoreactive aggregations in U373 astrocytoma cells. We have additionally overexpressed wild-type and a C-terminally truncated form of alpha-synuclein in primary rat glial cells. Astrocytes and oligodendrocytes were found to form alpha-synuclein-positive aggregations in vitro perinuclearly or in the processes of the cells. The morphological studies presented here demonstrate that the aggregations we have observed in vitro are not limited by a membrane but have unclear borders. They have an amorphous dense core that is... (More)
Abnormal alpha-synuclein-positive glial cytoplasmic inclusions are found in Parkinson's disease, multiple system atrophy and dementia with Lewy bodies. We have recently developed an in vitro model of alpha-synuclein-immunoreactive aggregations in U373 astrocytoma cells. We have additionally overexpressed wild-type and a C-terminally truncated form of alpha-synuclein in primary rat glial cells. Astrocytes and oligodendrocytes were found to form alpha-synuclein-positive aggregations in vitro perinuclearly or in the processes of the cells. The morphological studies presented here demonstrate that the aggregations we have observed in vitro are not limited by a membrane but have unclear borders. They have an amorphous dense core that is intensely alpha-synuclein-immunopositive and a predominantly filamentous halo around. Mainly filamentous structures at the border area between the halo and the core are alpha-synuclein-immunoreactive. We conclude that this in vitro model of alpha-synuclein-positive glial aggregations mimics the morphology of the abnormal glial inclusions described in neuroclegenerative disorders and could be a suitable model for studying their role in the pathogenesis of these diseases. (C) 2002 Elsevier Science Ireland Ltd. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
glial cytoplasmic inclusions, ultrastructure, alpha-synuclein, glia, Lewy bodies, neurodegeneration
in
Neuroscience Letters
volume
323
issue
1
pages
37 - 40
publisher
Elsevier
external identifiers
  • pmid:11911985
  • wos:000174853100010
  • scopus:0037134107
ISSN
0304-3940
DOI
10.1016/S0304-3940(02)00117-9
language
English
LU publication?
yes
id
1a2bb052-c2b3-47b3-b34d-70f700c2f4a9 (old id 340572)
date added to LUP
2007-11-14 14:13:14
date last changed
2017-07-30 03:52:30
@article{1a2bb052-c2b3-47b3-b34d-70f700c2f4a9,
  abstract     = {Abnormal alpha-synuclein-positive glial cytoplasmic inclusions are found in Parkinson's disease, multiple system atrophy and dementia with Lewy bodies. We have recently developed an in vitro model of alpha-synuclein-immunoreactive aggregations in U373 astrocytoma cells. We have additionally overexpressed wild-type and a C-terminally truncated form of alpha-synuclein in primary rat glial cells. Astrocytes and oligodendrocytes were found to form alpha-synuclein-positive aggregations in vitro perinuclearly or in the processes of the cells. The morphological studies presented here demonstrate that the aggregations we have observed in vitro are not limited by a membrane but have unclear borders. They have an amorphous dense core that is intensely alpha-synuclein-immunopositive and a predominantly filamentous halo around. Mainly filamentous structures at the border area between the halo and the core are alpha-synuclein-immunoreactive. We conclude that this in vitro model of alpha-synuclein-positive glial aggregations mimics the morphology of the abnormal glial inclusions described in neuroclegenerative disorders and could be a suitable model for studying their role in the pathogenesis of these diseases. (C) 2002 Elsevier Science Ireland Ltd. All rights reserved.},
  author       = {Stefanova, N and Emgård-Mattson, Mia and Klimaschewski, L and Wenning, GK and Reindl, M},
  issn         = {0304-3940},
  keyword      = {glial cytoplasmic inclusions,ultrastructure,alpha-synuclein,glia,Lewy bodies,neurodegeneration},
  language     = {eng},
  number       = {1},
  pages        = {37--40},
  publisher    = {Elsevier},
  series       = {Neuroscience Letters},
  title        = {Ultrastructure of alpha-synuclein-positive aggregations in U373 astrocytoma and rat primary glial cells},
  url          = {http://dx.doi.org/10.1016/S0304-3940(02)00117-9},
  volume       = {323},
  year         = {2002},
}