| Project/Area Number |
23591459
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
膠原病・アレルギー・感染症内科学
|
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| Research Institution | Ochanomizu University (2012-2013)
The University of Tokyo (2011) |
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Principal Investigator |
HONDA Zen-ichiro お茶の水女子大学, 保健管理センター, 教授 (70238814)
|
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| Co-Investigator(Kenkyū-buntansha) |
HONDA Hiroaki 広島大学, 原爆放射線医科学研究所, 教授 (40245064)
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2013: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2012: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2011: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
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| Keywords | Fc受容体 / 膜貫通部位 / 遺伝子多型 / シグナル伝達 / 自己免疫疾患 / 免疫グロブリンFc受容体 / 細胞膜貫通部位 / 多型 / タンパク質間結合 / 治療標的 / 膜貫通ドメイン |
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| Research Abstract |
We have prepared 28 Cys mutants spanning the transmembrane domain of FcgRIIA, stably expressed in human B cells, and the cells were analyzed for Cys crosslinking under unligated, and ligated conditions. We identified unexpectedly complicated TMD assembly and reassembly mechanisms under resting, and activated conditions, and these structural alterations are all responsible for the signal stabilization, and the signal activation. We extrapolated the findings in FcgRIIA to FcgRIIB I232T autoimmune disease promoting polymorphism, and found that the amino acid substitution does alter the mode of the TMD association.
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