| Project/Area Number |
15K15060
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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 |
General medical chemistry
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| Research Institution | Tohoku University |
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Principal Investigator |
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| Project Period (FY) |
2015-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2016: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2015: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | 蛋白質シトルリン化 / 翻訳後修飾 / PAD4 / 好中球 |
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| Outline of Final Research Achievements |
Arginine residues in some proteins are citrullinated, which is mediated by calcium- dependent enzymes PADs. The citrullination often affects their functions such as epigenetic control of gene expression, tumorigenesis, autoimmune diseases, since positively-charged arginine is changed into neutral citrulline. However, much remains unclear in the regulation of PAD activity. We found a PAD4 regulating factor and named it iPAD1 that positively regulated PAD4. While mM order of calcium ion has been required for the efficient activity of PAD4 in vitro, iPAD1 drastically enhanced the calcium-sensitivity. Further, we performed affinity purification with several proteins that have been reported to undergo citrullination to identify their binding proteins that change the affinity. Among them. we found a few proteins that change their affinity to ING4, a critical factor for cell growth. Currently, we are investigating functional relevance about the affinity-change in the protein function.
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