The Mechanism of Arachidonic Acid Release in Collagen-activated Human Platelets
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概要
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The mechanism of arachidonic acid (AA) release in collagen-activated human platelets was studied. An arachidonic acid metabolite, thromboxane B_2 (TXB_2), was formed in parallel with the formation of phosphatidic acid (PA) without formation of lysophosphatidic acid (lysoPA) or lysophosphatidylinositol (lysoPI) in the absence of extracellular Ca^<2+>, suggesting that AA was released from PI via a PI-specific phospholipase C (PI-PLC)/diacylglycerol (DG) lipase/monoacylglycerol (MG) lipase pathway under the cytosolic low Ca^<2+> concentrations. Moreover, solubilized DG lipase and MG lipase could hydrolyze the substrates at basal cytosolic free Ca^<2+> concentrations. Subsequently, the relationship of cytosolic free Ca^<2+> concentrations and formation of AA metabolites was analyzed using Ca^<2+> ionophre, A23187. Collagen was able to induce a release of small amounts of AA under basal cytosolic Ca^<2+> conditions. However, a release of large amounts of AA was induced by phospholipase A_2 activated by both collagen-receptor occupancy and elevated Ca^<2+> levels. A TXA_2 mimetic agonist, STA_2 induced all the responses except for AA release. From these results, the mechanism of AA release and signal transduction in collagen-activated human platelets is discussed.
- 社団法人日本農芸化学会の論文
- 1994-01-23
著者
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KITO Makoto
Research Institute for Food Science, Kyoto University
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OKI Manabu
Kyoto Red Cross Blood Center
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Wada Kazuteru
Research Institute For Food Science Kyoto University
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Moriyama Tatsuya
Research Institute For Food Science Kyoto University
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Kito Makoto
Research Institute For Food Science Kyoto University
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Matsuura Takao
Kyoto Red Cross Blood Center
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Matsuura T
Kyoto Red Cross Blood Center
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