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首页> 外文期刊>Journal of Cellular Physiology >Thrombin-stimulated phosphatidylinositol 3-kinase activity in platelets is associated with activation of PYK2 tyrosine kinase: activation of both enzymes is aggregation independent.
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Thrombin-stimulated phosphatidylinositol 3-kinase activity in platelets is associated with activation of PYK2 tyrosine kinase: activation of both enzymes is aggregation independent.

机译:Thrombin-stimulated磷脂酰肌醇3-kinase血小板的活动相关联PYK2酪氨酸激酶激活:激活的这两种酶聚合独立。

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摘要

In this study, we investigated the activation of a new member of the focal adhesion kinase family of tyrosine kinases, the proline-rich tyrosine kinase, or PYK2, in platelets. We show that PYK2 is tyrosine phosphorylated and its activity is increased during early stages of platelet aggregation. This activation coincided with increased association of phosphatidylinositol (PI) 3-kinase and PYK2, as determined by both anti-PI 3-kinase and anti-PYK2 immunoprecipitates. However, under basal conditions, some association of PYK2 and PI 3-kinase was consistently observed, even though little or no tyrosine phosphorylated PYK2 could be detected. In addition, both increased PI 3-kinase activity and increased PYK2 activity could be detected in immunoprecipitates following thrombin stimulation. All of these events were unaffected by blocking platelet aggregation with arginine-glycine-aspartate-serine (RGDS) peptide, which interferes with binding of the platelet integrin alpha(IIb)beta(3) to fibrinogen. Neither was the activation of the PYK2 kinase activity affected by blocking PI 3-kinase activity. These results support a model in which PYK2 is associated with PI 3-kinase in unstimulated platelets and following activation of platelets, there is an increase in tyrosine phosphorylation of PYK2, increased PYK2 activity, and increased association of PYK2 with PI 3-kinase, which may contribute to the increase in PI 3-kinase activity. All of these were found to be early events independent of subsequent platelet aggregation. Copyright 2000 Wiley-Liss, Inc.
机译:在这项研究中,我们调查的激活粘着斑激酶家族的新成员酪氨酸激酶,脯氨酸酪氨酸激酶或PYK2血小板。酪氨酸磷酸化及其活动是吗增加血小板的早期阶段聚合。增加协会的磷脂酰肌醇(PI) 3-kinase PYK2,由两个决定anti-PI 3-kinase和anti-PYK2免疫沉淀反应。条件下,一些PYK2协会和π3-kinase一直观察到,尽管很少或没有酪氨酸磷酸化PYK2被检测出来。3-kinase活动和PYK2活动增加可以检测到免疫沉淀反应后凝血酶刺激。通过阻止血小板聚集的影响arginine-glycine-aspartate-serine (RGDS)肽,这干扰血小板的绑定吗整合素α(IIb)β(3)纤维蛋白原。的激活PYK2激酶活性受阻塞π3-kinase活动。PYK2结果支持模型如果与π3-kinase有关血小板和血小板激活后,有酪氨酸磷酸化的增加PYK2 PYK2活动增加,增加与π3-kinase PYK2协会,这可能为π3-kinase的增加作出贡献活动。事件独立于随后的血小板聚合。

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