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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Iwase, Tamaki Yazawa, Ikuru Suzuki, Yasuyo Jin, Chenghua |
| Description | Author Affiliation: Suzuki Y ( From the Laboratory of Research Resources, Research Institute, National Center for Geriatrics and Gerontology, 35 Gengo, Morioka, Obu-shi, Aichi 474-8511, Japan and.); Jin C ( From the Laboratory of Research Resources, Research Institute, National Center for Geriatrics and Gerontology, 35 Gengo, Morioka, Obu-shi, Aichi 474-8511, Japan and.); Iwase T ( the Department of Neurology, Nagoya City Koseiin Medical Welfare Center, Aichi 465-8610, Japan.); Yazawa I ( From the Laboratory of Research Resources, Research Institute, National Center for Geriatrics and Gerontology, 35 Gengo, Morioka, Obu-shi, Aichi 474-8511, Japan and yazawaik@ncgg.go.jp.) |
| Abstract | Multiple system atrophy (MSA) is a neurodegenerative disease caused by -synuclein aggregation in oligodendrocytes and neurons. Using a transgenic mouse model overexpressing human -synuclein in oligodendrocytes, we previously demonstrated that oligodendrocytic -synuclein inclusions induce neuronal -synuclein accumulation and progressive neuronal degeneration. -Synuclein binds to ß-III tubulin, leading to the neuronal accumulation of insoluble -synuclein in an MSA mouse model. The present study demonstrates that -synuclein co-localizes with ß-III tubulin in the brain tissue from patients with MSA and MSA model transgenic mice as well as neurons cultured from these mice. Accumulation of insoluble -synuclein in MSA mouse neurons was blocked by the peptide fragment ß-III tubulin (residues 235-282). We have determined the -synuclein-binding domain of ß-III tubulin and demonstrated that a short fragment containing this domain can suppress -synuclein accumulation in the primary cultured cells. Administration of a short -synuclein-binding fragment of ß-III tubulin may be a novel therapeutic strategy for MSA. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 35 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-08-29 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Multiple System Atrophy Metabolism Tubulin Physiology Alpha-Synuclein Animals Cells, Cultured DNA Primers Disease Models, Animal Mice Mice, Transgenic Neurons Protein Binding Chemistry Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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