Analysis of the machinery of ectodomain shedding and its possible role for the action of HB-EGF
| Project/Area Number |
22790319
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Pathological medical chemistry
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| Research Institution | Ehime University |
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Principal Investigator |
FUKUDA Shinji 愛媛大学, 大学院・医学系研究科, 助教 (70398238)
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| Project Period (FY) |
2010 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2011: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2010: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | 膜型増殖因子 / ectodomain shedding / HB-EGF / Amphiregulin / アネキシン / ADAM17 |
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| Research Abstract |
We identified cell surface-annexins as components of their shedding complex. Annexin family members, annexin A2(ANXA2), A8, and A9 interacted with ADAM17 on the cell surface. Shedding of proHB-EGF was increased when ANXA2 was knocked down, but decreased with ANXA8 knockdown. Taken together with studies of its related ligand, Amphiregulin, we propose that annexins on the cell surface function as" shedding platform" proteins to determine the substrate selectivity of ADAM17, with possible therapeutic potential in ADAM-related diseases.
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Report
(3 results)
Research Products
(24 results)
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[Journal Article] BAZF, a novel component of cullin3-based E3 ligase complex, mediates VEGFR and Notch cross-signaling in angiogenesis2012
Author(s)
Ohnuki H, Inoue H, Takemori N, Nakayama H, Sakaue T, Fukuda S, Miwa D, Nishiwaki E, Hatano M, Tokuhisa T, Endo Y, Nose M, Higashiyama S
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Journal Title
Blood
Volume: 119(11)
Pages: 2688-2698
Related Report
Peer Reviewed
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