2011 Fiscal Year Final Research Report
Analyses on the mode of proteolysis and aggregation of synphilin-1 that constitutes the core of Lewy bodies
| Project/Area Number |
21591085
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Neurology
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| Research Institution | Hiroshima University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
MATSUMOTO Masayasu 広島大学, 大学院・医歯薬学総合研究科, 教授 (20192346)
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| Project Period (FY) |
2009 – 2011
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| Keywords | 脳神経疾患 / 神経科学 / 蛋白質 |
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| Research Abstract |
Impairments in the proteolytic process of disease-specific proteins have been assumed to be the cause of the formation of neuronal inclusions and subsequent neuronal cell death. In Parkinson' s disease, Synphilin-1 is one of the constituents of Lewy bodies that characterize Parkinson' s disease pathologically. We hypothesized that the perturbation of intracellular vesicle trafficking is the underlying cause which leads to the formation of neuronal inclusion, and elucidated that ESCRT(endosomal sorting complex required for transport) pathway is implicated in the Lewy bodies formation. We also demonstrated that ubiquitination of Synphilin-1 by Siah-1 is a signal that recruit Synphilin-1 to ESCRT pathway.
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[Journal Article] Simulated Microgravity Maintains the Undifferentiated State and Enhances the Neural Repair Potential of Bone Marrow Stromal Cells2011
Author(s)
Yuge L, Sasaki A, Kawahara Y, Wu SL, Matsumoto M, Manabe T, Kajiume T, Takeda M, Magaki T, Takahashi T, Kurisu K, Matsumoto M.
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Journal Title
Stem Cells Dev
Volume: 20(5)
Pages: 893-900
Peer Reviewed
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