| Project/Area Number |
24390074
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
General medical chemistry
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| Research Institution | Ehime University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
FUKUDA Shinji 愛媛大学, プロテオサイエンスセンター, 助教 (70398238)
INOUE Hirofumi 愛媛大学, 大学院医学系研究科, 講師 (70321635)
MATSUSHITA Natsuki 愛媛大学, 医学部附属病院, 研究員 (40271556)
JHO Takashi 名古屋市立大学, 大学院医学系研究科, 教授 (30231369)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥18,720,000 (Direct Cost: ¥14,400,000、Indirect Cost: ¥4,320,000)
Fiscal Year 2014: ¥5,980,000 (Direct Cost: ¥4,600,000、Indirect Cost: ¥1,380,000)
Fiscal Year 2013: ¥5,720,000 (Direct Cost: ¥4,400,000、Indirect Cost: ¥1,320,000)
Fiscal Year 2012: ¥7,020,000 (Direct Cost: ¥5,400,000、Indirect Cost: ¥1,620,000)
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| Keywords | ectodomian shedding / ADAM17 / proHB-EGF / proamphiregulin / proTNF-α / annexin / レムナントペプチドシグナル / Shedding / HB-EGF / amphiregulin / TNF-alpha / 細胞膜蛋白質 / Ectodomain Shedding / TNF-α |
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| Outline of Final Research Achievements |
ADAM17, a transmembrane-type metalloprotease, sheds various transmembrane proteins on cell surface, which regulates cell signaling. Both type I transmembrane protein proHB-EGF and proAREG, and type II transmembrane protein proTNF-α are equally shed. However, ADAM17 binding proteins annexin reversibly affected on their ADAM17-induced shedding. We propose that the catalytic domain of ADAM17 can swing by binding different member of annexin and access to the different types of membrane proteins.
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