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| Content Provider | Springer Nature Link |
|---|---|
| Author | Pountney, D. L. Treweek, T. M. Chataway, T. Huang, Y. Chegini, F. Blumbergs, P. C. Raftery, M. J Gai, W. P. |
| Copyright Year | 2005 |
| Abstract | Multiple system atrophy (MSA) is characterized by the formation of oligodendroglial cytoplasmic inclusions (GCIs) consisting of α-synuclein filaments. αB-crystallin, a small chaperone protein that binds to unfolded proteins and inhibits aggregation, has been documented in GCIs. We investigated the relative abundance and speciation of αB-crystallin in GCIs in MSA brains. We also examined the influence of αB-crystallin on the formation of cytoplasmic inclusions in cultured glial cells. Immunohistochemistry and confocal microscopy revealed αB-crystallin is a prominent component of GCIs, more abundant than in Lewy bodies in Lewy body dementia. One- and two-dimensional gel electrophoresis and mass spectrometric analysis of GCIs immunopurified from MSA brains indicated that αB-crystallin is a major protein component with multiple post-translationally modified species. In cultured C6 glioma cells treated with the proteasomal inhibitor, lactacystin, to induce accumulation of ubiquitinated proteins, a subset of cells showed increased cytoplasmic staining for αB-crystallin. Proteasomeinhibited cells transfected with GFP-tagged α-synuclein resulted in ubiquitin- and αB-crystallin-positive aggregates resembling GCIs in MSA brains. Our results indicate that αB-crystallin is a major chaperone in MSA, and suggest a role of the protein in the formation of inclusion bodies in glial cells. |
| Starting Page | 77 |
| Ending Page | 85 |
| Page Count | 9 |
| File Format | |
| ISSN | 10298428 |
| Journal | Neurotoxicity Research |
| Volume Number | 7 |
| Issue Number | 1-2 |
| e-ISSN | 14763524 |
| Language | English |
| Publisher | Springer-Verlag |
| Publisher Date | 2005-01-01 |
| Publisher Place | New York |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | αB-Crystallin α-Synuclein Multiple system atrophy Post-translational modification Inclusion body Aggresome Chaperone Neurodegeneration Neurosciences Pharmaceutical Sciences/Technology Neurology Neurochemistry Pharmacology/Toxicology Neurobiology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Neuroscience Toxicology |
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