Abstract
Despite the diversity of platelet agonists, ranging from soluble molecules that bind to receptors on the platelet surface to shear stress (Kroll et al. 1993) and various artificial surfaces (Ware et al. 1991), the changes in platelet function that they induce are stereotypical. These include cytoskeletal reorganization (shape change), conversion of the αIIb-β3 integrin complex to a ligand-binding form, release of contents from storage granules, and clot retraction. Moreover, the pathways leading to expression of these diverse functions involve the generation of second messengers in a pattern that is somewhat similar among the agonists (Ware and Coller 1994); these mediators in turn interact with intracellular effectors, of which the most widely studied are protein kinases, enzymes that transfer phosphoryl groups from ATP to an acceptor polypeptide substrate. Two general categories of protein kinases have been identified: those that mediate the phosphorylation of proteins on tyrosine residues and those that phosphorylate substrates on serine or threonine residues.
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Ware, J.A., Chang, J.D. (1997). Protein Kinase C and Its Interactions with Other Serine-Threonine Kinases. In: von Bruchhausen, F., Walter, U. (eds) Platelets and Their Factors. Handbook of Experimental Pharmacology, vol 126. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-60639-7_12
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