| Project/Area Number |
25650040
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Functional biochemistry
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| Research Institution | Tokai University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
ITO Yukishige 理化学研究所, 伊藤細胞制御化学研究室, 主任研究員 (80168385)
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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 |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2014: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2013: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | セレノシステイン / グルタチオン / フォールディング / 品質管理機構 / シャペロン / タンパク質ジスルフィドイソメラーゼ / 酸化ストレス / 酸化還元酵素 / ジスルフィド結合 / レドックス / 酵素 |
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| Outline of Final Research Achievements |
The enzymes related on redox regulatory system work on the maintenance of the intracellular environment from reactive oxygen species (ROS) providing oxidative stress. Especially, it was reported that inactivation or decrease in chaperone activity of protein disulfide isomerase (PDI) cause accumulation of misfolded proteins resulting incidence of Alzheimer's disease. In this study, we pay attention to selenocysteine, the 21th amino acid, to introduce it into the active sites of glutathione or PDI. The difference in reactivity of cysteine and selenocysteine bring on the difference of reactivity to the molecules. We compared the effects on folding of misfolded proteins between glutathione (GSSG) and selenoglutathione (GSeSeG) by detecting the rate of recovered activity of misfolded RNase. The enhancement effect derived from GSeSeG was superior to that from GSSG on both chaperone activity of PDI and refolding of misfolded enzymes.
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