PLATELET TYROSINE-SPECIFIC PROTEIN-PHOSPHORYLATION IS REGULATED BY THROMBIN
PLATELET TYROSINE-SPECIFIC PROTEIN-PHOSPHORYLATION IS REGULATED BY THROMBIN
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DOI：
10.1128/mcb.8.9.3603
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发表时间：
1988-09-01
影响因子：
5.3
通讯作者：
MARTIN, GS
中科院分区：
文献类型：
--
作者：
FERRELL, JE;MARTIN, GS
完整的人血小板，终末分化的细胞，没有生长潜力，被发现具有异常高水平的酪氨酸特异性蛋白磷酸化。生理性血小板激活剂凝血酶可短暂升高血小板磷酸酪氨酸含量，这显然是通过刺激一种或多种酪氨酸特异性蛋白激酶实现的。抗磷酸酪氨酸抗血清的免疫印迹表明，凝血酶引起了显着的变化，在酪氨酸磷酸化的一些个别蛋白质带，这些变化发生在三个不同的时间波。大多数但不是所有的蛋白质条带在酪氨酸磷酸化的凝血酶也酪氨酸磷酸化的冷冻或离子载体A23187和tetradecanoylphorbol醋酸酯的组合。凝血酶刺激酪氨酸激酶pp 60 c-src的磷酸化，主要是在Ser-12和Tyr-527，虽然这些磷酸化对血小板pp 60 c-src功能的影响并不明显。总之，这些结果表明，酪氨酸特异性蛋白激酶的身份不确定参与血小板中的信号转导。
Intact human platelets, terminally differentiated cells with no growth potential, were found to possess unusually high levels of tyrosine-specific protein phosphorylation. The physiological platelet activator thrombin transiently elevated platelet phosphotyrosine content, apparently through stimulation of one or more tyrosine-specific protein kinases. Immunoblotting with antiphosphotyrosine antiserum showed that thrombin caused dramatic changes in the tyrosine phosphorylation of a number of individual protein bands and that these changes occurred in three distinct temporal waves. Most but not all of the protein bands phosphorylated at tyrosine in response to thrombin were also tyrosine phosphorylated in response to chilling or the combination of ionophore A23187 and tetradecanoylphorbol acetate. Thrombin stimulated the phosphorylation of the tyrosine kinase pp60c-src, primarily at Ser-12 and Tyr-527, although the effects of these phosphorylations on platelet pp60c-src function were not apparent. Together, these results suggest that tyrosine-specific protein kinases of uncertain identity are involved in signal transduction in platelets.