| Project/Area Number |
12670990
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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 |
Hematology
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| Research Institution | HIROSHIMA UNIVERSITY |
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Principal Investigator |
FUJIMURA Kingo School of Medicine, Hiroshima Univ., Professor, 医学部, 教授 (80034114)
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| Co-Investigator(Kenkyū-buntansha) |
SHIMOMURA Takeshi University Hospital, Hiroshima Univ., 医学部・附属病院, 助手 (20263741)
FUJIMOTO Tetsuro School of Medicine, Hiroshima Univ., Associate Professor, 医学部, 助教授 (00221549)
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| Project Period (FY) |
2000 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 2001: ¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 2000: ¥1,500,000 (Direct Cost: ¥1,500,000)
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| Keywords | platelets / GPV / von Willebrand factor receptor / GPIb-IX complex / Two hybrid system / filamin / FBLP-1 / cytoplasmic domain / トロンビン / 巨核球 |
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| Research Abstract |
In order to determine the function of membrane glycoprotein V (GPV) on platelet activation, proteins which bind to the cytoplasmic domain of GPV were identified by yeast two hybrid screening. Since the cytoplasmic tail of murine GPV cDNA and murine megakaryocytic cell lines. One positive clone was identified. In addition, proteins that bind to filamins were also identified by years two hybrid screening since filamin was known as a binding protein to the von Willebrand factor receptor GPIb-V-IX complex. One clone was a novel cDNA, which encoded 375 amino acids and 45kDa protein. Deduced amino acid sequence showed that it contained a proline-rich domain at its N-terminal half and two LIM domains at C-terminus. We therefore, named it as FBLP-1 (Filamin Binding LIM Protein-1). Subcellular localization analysis showed that FBLP-1 co-localized with stress fibers, which stretched from focal adhesions. The cells, which over-expressed FBLP-1, spread more effectively than the cells which did not express FBLP-1, suggesting that FBLP-1 plays a significant role on platelet adhesion. Further investigation of the associated protein would clarify the function of platelet GPV.
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