Physiology and application of deimination of humnan hair follicle S100A3
| Project/Area Number |
20591358
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Dermatology
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| Research Institution | Kinki University |
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Principal Investigator |
KAWADA Akira Kinki University, 医学部, 教授 (90160986)
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| Co-Investigator(Kenkyū-buntansha) |
TAKAHARA Hidenari 茨城大学, 農学部, 教授 (30122063)
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| Project Period (FY) |
2008 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2010: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2009: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2008: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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| Keywords | S100A3,脱イミノ化反応 / ヒト毛嚢 / peptidylarginine deimase / 線構造解析 / カルシウム結合タンパク質 / S100A3 / Ca^<2+>結合蛋白質 / ヒト毛嚢キューテクル / 脱イミノ化 / 結晶化 / X線 / シトルリン残基 / ヒト毛嚢キューティクル / 架橋反応 / トランスグルタミナーゼ / 蛍光分光分析 / 小角散乱 / シトルリン残 |
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| Research Abstract |
S100A3 protein specifically expressed in the cuticular cells of hair follicle. Human S100A3 is characterized by two disulphide bridges, a preformed Zn^<2+>-binding site, and a specific citrullination site by deimination. Conversion to the citrulline residues, symmetrically located on the S100A3 dimer plane-causes the assembly of the Ca^<2+>-bound S100A3 homotetramer. S100A3 acts as a Ca^<2+> buffering protein providing Ca^<2+> ions in turn to the deimination.
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Report
(4 results)
Research Products
(6 results)
