Lysophosphatidic acid activates phosphoinositide 3-kinase and phospholipase C in human platelets: inhibitory effects of Wortmannin on phosphoinositide 3-kinase and aggregation.
Lysophosphatidic acid activates phosphoinositide 3-kinase and phospholipase C in human platelets: inhibitory effects of Wortmannin on phosphoinositide 3-kinase and aggregation.
复制标题
溶血磷脂酸激活人血小板中的磷酸肌醇 3-激酶和磷脂酶 C:渥曼青霉素对磷酸肌醇 3-激酶和聚集的抑制作用。
DOI:
10.1006/bbrc.1995.1839
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发表时间:
1995
期刊:
影响因子:
--
通讯作者:
Rittenhouse,SE
中科院分区:
文献类型:
--
作者:
Zhang,J;Rittenhouse,SE
Lysophosphatidic acid is a biologically active serum phospholipid known to have growth factor-like activities and to cause platelet aggregation. Activated phosphoinositide 3-kinase has been suggested to be involved in cytoskeletal reorganization and mitogenesis. We report that lysophosphatidic acid causes platelet phosphoinositide 3-kinase activation, leading to accumulation of phosphatidylinositol (3.4,5)P3and phosphatidylinositol (3,4)P2and stimulates phospholipase C. Wortmannin, a potent inhibitor of phosphoinositide 3-kinase, blocks platelet aggregation induced by lysophosphatidic acid without impairing phospholipase C activation. Eristostatin, an antagonist of fibrinogen binding to platelet integrin, completely blocks platelet aggregation without inhibiting phosphoinositide 3-kinase or phospholipase C. We suggest that lysophosphatidic acid, in activating phosphoinositide 3-kinase, promotes platelet aggregation, but that platelet aggregation in response to lysophosphatidic acid does not significantly enhance phosphoinositide 3-kinase activation.