| Project/Area Number |
09660137
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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 |
食品科学・栄養科学
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
FUKUOKA Shin-Ichi Kyoto University, Research Institute For Food Science, Associate Professor, 食糧科学研究所, 助教授 (20183923)
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| Project Period (FY) |
1997 – 1998
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| Project Status |
Completed (Fiscal Year 1998)
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| Budget Amount *help |
¥3,300,000 (Direct Cost: ¥3,300,000)
Fiscal Year 1998: ¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 1997: ¥1,700,000 (Direct Cost: ¥1,700,000)
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| Keywords | phospholipaseA_2 / lipocortin / ATP / ATPase / membranefusion / ホスホリパーゼA2 / アネキシン / ZAP |
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| Research Abstract |
In this study the author tried the detection of changes in phospholipids from rat pancreatic acinar AR42J cells before and after secretory stimulation. As a result, the incrememt of lysophosphatidylethanolamine (lysoPE) was observed after secretory stimulation, indicating the involvement of phospholipase A_2 (PLA_2) in the membrane fusion. Lysophospholipids are shown to be a direct inducer of the membrane fusion event which is a final stage in the regulated exocytosis. It is possible that lysoPE and/or free fatty acid produced at the same time are the actual triggers that destabilize lipid bilayers to start membrane fusion. The author found and cloned the zymogen granule membrane associated protein with molecular mass of 36 kDa (ZAP36) which was a novel member of the annexin family, which includes a PLA_2 inhibitory protein, lipocortin. ZAP36 was a cytoplasmic protein although it was located on the zymogen granule membranes. Several results and observations suggest that ZAP36 may be involved in the regulated exocytosis. Biochemical properties of ZAP36 were investigated. ZAP36 showed an ATPase activity in vitro and inhibited PLA_2 activity in vitro . Based on these findings, the author has proposed the hypothesis of the function of ZAP36 in the membrane fusion where ZAP36 is thought to be a PLA_2 inhibitory protein functioning in response to the stimulations.
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