Analysis of the structure and interaction of apoptotic signaling molecules via Fas
| Project/Area Number |
10680606
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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 |
Functional biochemistry
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
SAKAMAKI Kazuhiro Kyoto University, Institute for Virus Research Associate Professor, ウイルス研究所, 助教授 (20271017)
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| Co-Investigator(Kenkyū-buntansha) |
YONEHARA Shin Kyoto University, Institute for Virus Research Professor, ウイルス研究所, 教授 (00124503)
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| Project Period (FY) |
1998 – 1999
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| Project Status |
Completed (Fiscal Year 1999)
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| Budget Amount *help |
¥3,400,000 (Direct Cost: ¥3,400,000)
Fiscal Year 1999: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1998: ¥2,700,000 (Direct Cost: ¥2,700,000)
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| Keywords | apoptosis / Death Effector Domain / Caspase-8 / FADD / MC159 / デス・エフェクター・ドメイン / デス-エフェクター・ドメイン / Caspase-8 |
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| Research Abstract |
The death effector domain(DED), which is essential for protein interaction, is involved in apoptotic signal transudation. Cysteine protease caspase-8 and viral protein MC159 have two tandemly repeated DEDs, respectively. The DEDs of caspase-8 could induce apoptosis whereas that of MC159 inhibits apoptosis. To examine binding and biological activities of the DED domains, we generated deletion and chimera mutants of DEDs derived from caspase-8 and MC159. These mutants did not work compare to wild type of caspase-8 and MC159. Therefore, we concluded that the combination of the two-repeated DEDs is necessary for the DED-containing proteins to stimulate or inhibit apoptosis.
By searching DED-containing proteins on Genbank database, we found a new molecule which contains two tandemly repeated DEDs at the amino-terminal portion. We detected high expression of this molecules in the mouse testis by northern blot analysis. We suppose that this molecule may have a new function for signal transduction.
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Report
(3 results)
Research Products
(5 results)
