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Signal transduction in neutrophil activation Phosphatidylinositol 3-kinase is stimulated without tyrosine phosphorylation

✍ Scribed by Chris J. Vlahos; William F. Matter

Book ID
115926462
Publisher
Elsevier Science
Year
1992
Tongue
English
Weight
873 KB
Volume
309
Category
Article
ISSN
0014-5793

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Thrombin-stimulated phosphatidylinositol
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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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