| Project/Area Number |
11557007
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| Research Category |
Grant-in-Aid for Scientific Research (B).
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| Allocation Type | Single-year Grants |
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| Section | 展開研究 |
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| Research Field |
General medical chemistry
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| Research Institution | Kansai Medical University |
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Principal Investigator |
KUROSAKI Tomohiro Kansai Medical University, Department of Medicine, Professor, 医学部, 教授 (50178125)
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| Co-Investigator(Kenkyū-buntansha) |
OKAWA Katsuya Kirin Brewery Co., LTD., Investigator, 研究員
IWAMATSU Akihiro Kirin Brewery Co., LTD., Principal Investigator, 主任研究員
ISHIAI Masamichi Kansai Medical University, Department of Medicine, Assistant Professor, 医学部, 助手 (90298844)
前田 明人 関西医科大学, 医学部, 講師 (50298882)
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| Project Period (FY) |
1999 – 2000
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| Project Status |
Completed (Fiscal Year 2000)
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| Budget Amount *help |
¥14,700,000 (Direct Cost: ¥14,700,000)
Fiscal Year 2000: ¥5,400,000 (Direct Cost: ¥5,400,000)
Fiscal Year 1999: ¥9,300,000 (Direct Cost: ¥9,300,000)
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| Keywords | BCR signaling / Syk / BLNK / BCAP / apoptosis / 遺伝子欠損 / 微量蛋白質精製 |
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| Research Abstract |
The ability of B cells to respond to antigen relies on signals transmitted through the B cell antigen receptor (BCR) complex. Activation of cytoplasmic protein tyrosine kinases (PTKs) is the earliest measurable biochemical response to BCR cross-linking. The initial event leads to the generation of secondary signals including Ras activation, phosphatidylinositol 3-kinase (PI-3K) activation, phospholipase C (PLC)-γ2 activation.
Based upon our previous evidence that Syk, a BCR-associated PTK, is essential for PLC-γ2 activation, we purified tyrosine-phosphorylated proteins mediated by Syk. Among 15 purified proteins, two molecules (BLNK and BCAP) were turned out to play an important role in BCR-mediated apoptosis. In fact, BLNK-deficient B cells abolished apoptosis, whereas this BCR-mediated apoptosis was enhanced by loss of BCAP.
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