| Project/Area Number |
21890086
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| Research Category |
Grant-in-Aid for Research Activity Start-up
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| Allocation Type | Single-year Grants |
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| Research Field |
Pathological medical chemistry
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| Research Institution | Kyoto University (2010)
Kanazawa University (2009) |
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Principal Investigator |
OZAWA Kentaro Kyoto University, 薬学研究科, 特定助教 (80507393)
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| Project Period (FY) |
2009 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥2,652,000 (Direct Cost: ¥2,040,000、Indirect Cost: ¥612,000)
Fiscal Year 2010: ¥1,261,000 (Direct Cost: ¥970,000、Indirect Cost: ¥291,000)
Fiscal Year 2009: ¥1,391,000 (Direct Cost: ¥1,070,000、Indirect Cost: ¥321,000)
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| Keywords | パーキンソン病 / 一酸化窒素 / タンパク質翻訳後修飾 / 神経細胞死 / 翻訳後タンパク質修飾 |
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| Research Abstract |
It is reported that S-nitrosylation of Parkin regulates its activity and might play a role in the pathogenesis of Parkinson's disease, however, its function in physiological or pathophysiological situation is incompletely understood. I have tried to identify cysteine residue(s) S-nitrosylated in Parkin by proteomics method using MS and generating truncated forms of Parkin. I found some candidate cysteines but did not comfirm that those are S-nitrosylated in physiological conditions. On the other hand, I found Synhilin-1, which is reported to be ubiqutinated by Parkin, was S-nitrosylated by nNOS. These data indicate not only Parkin itself but substrate of Parkin is regulated via S-nitrosylation.
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