| Project/Area Number |
25870549
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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 |
Chemical biology
General medical chemistry
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| Research Institution | Tohoku University |
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Principal Investigator |
IDA Tomoaki 東北大学, 医学(系)研究科(研究院), 助教 (70570406)
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| Project Period (FY) |
2013-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
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| Keywords | 8-SH-cGMP / 8-ニトロ-cGMP / 活性イオウ分子種 / S-S-グアニル化 / S-ポリチオール化タンパク質 / タンパク質翻訳後修飾 / 酸化ストレス / システインパースルフィド / タンパク質S-ポリチオール化 / レドックスシグナル / 活性酸素 / 一酸化窒素 / 8-Nitro-cGMP / ポリサルファ |
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| Outline of Final Research Achievements |
The cyclic nucleotide 8-SH-cGMP is produced by the metabolism of 8-nitro-cGMP, which serves as a secondary messenger for NO and reactive oxygen species signaling. However, the mechanisms controlling the formation and levels of intracellular 8-SH-cGMP have not yet been identified. In this study, the principal investigator precisely quantified the formation of 8-SH-GMP via a mass spectrometry-based metabolomic method. The results revealed that 8-SH-cGMP is produced from 8-nitro-cGMP via sulfhydration by reactive sulfur species generated from the cystathione beta-synthase and cystathionine gamma-lyase systems. Moreover, the formation of S-S-guanylation (cGMP adduction to the thiol group of the protein via disulfide linkage) was specifically identified using proteome analysis of S-polythiolation.
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