| Project/Area Number |
17K17583
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
General physiology
General pharmacology
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| Research Institution | Tohoku University |
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Principal Investigator |
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| Research Collaborator |
Morita Masanobu
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| Project Period (FY) |
2017-04-01 – 2019-03-31
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| Project Status |
Completed (Fiscal Year 2018)
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| Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2018: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2017: ¥3,120,000 (Direct Cost: ¥2,400,000、Indirect Cost: ¥720,000)
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| Keywords | タンパク質ポリスルフィド化 / システインパースルフィド / アルコールデヒドロゲナーゼ / レドックスシグナル |
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| Outline of Final Research Achievements |
In this study, we investigated biological roles of protein polysulfidation of alcohol dehydrogenase 5 (ADH5) in a regulatory mechanism for redox signaling. It was revealed that human ADH5 protein was highly polysulfidated and the Cys174 residue, is known to be coordinated to the active site, played the important role to maintain its protein polysulfidation. Furthermore, we found that the protein polysufidation level of ADH5 correlated with the enzymatic activity. These results suggest that polysulfidation at the active site of ADH5 protein may involve in the regulation of nitric oxide- and formaldehyde-related redox signaling.
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| Academic Significance and Societal Importance of the Research Achievements |
本研究で着目したアルコールデヒドロゲナーゼ５（ADH5）は、生体内で一酸化窒素（NO）を代謝する主要酵素の一つである。本研究により世界で初めて、ADH5酵素活性がタンパク質ポリスルフィドによって制御されていることを明らかにした。ADH5タンパク質ポリスルフィドによる生体内NO代謝機構をより詳細に解析することにより、感染・炎症などのNO・酸化ストレスが関与する疾患・病態の治療・予防戦略の開発への貢献が期待できる。
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