2010 Fiscal Year Final Research Report

Investigation for rolesof post translational modificationbynitric oxide (NO) in Parkinson's disease.

Research Project

Project/Area Number	21890086
Research Category	Grant-in-Aid for Research Activity Start-up
Allocation Type	Single-year Grants
Research Field	Pathological medical chemistry
Research Institution	Kyoto University (2010) Kanazawa University (2009)
Principal Investigator	OZAWA Kentaro Kyoto University, 薬学研究科, 特定助教 (80507393)
Project Period (FY)	2009 – 2010
Keywords	パーキンソン病 / 一酸化窒素 / タンパク質翻訳後修飾
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.