Tyrosine unphosphorylated platelet SHP-1 is a substrate for calpain.
摘要：
The platelet phosphotyrosine () is tyrosine phosphorylated during -induced activation. Stimulation of platelets by the A23187 in the presence of induced a dependent cleavage of . proteolysis was undetectable during -induced stimulation. When was tyrosine phosphorylated by , further addition of A23187 failed to induce its cleavage. In the presence of tyrphostin to inhibit -induced tyrosine , was cleaved. Thus, only the tyrosine unphosphorylated form of was a substrate for . A23187 induced the disappearance of all platelet phosphotyrosine proteins and a two-fold increase in activity, both inhibited by pervanadate, a inhibitor, but unaffected by calpeptin, a . The data show that is either tyrosine phosphorylated or cleaved by , and suggest that cleavage does not contribute to A23187-induced activity.
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关键词：
Blood Platelets Humans Calcium Chloride Vanadates Calcimycin Calpain Thrombin Tyrosine Intracellular Signaling Peptides and Proteins Enzyme Activation
DOI：
10.1006/bbrc.1998.9593
被引量：
年份：
1998
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