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Protein-tyrosine phosphorylation and p72syk activation in human platelets stimulated with collagen is dependent upon glycoprotein Ia/IIa and actin polymerization

Protein-tyrosine phosphorylation and p72syk activation in human platelets stimulated with collagen is dependent upon glycoprotein Ia/IIa and actin polymerization

Thrombosis and Haemostasis 75(4): 648-654

ISSN/ISBN: 0340-6245

PMID: 8743194

In human platelets treated with acetylsalicylic acid, collagen induced protein-tyrosine-phosphorylation of several proteins. The major 75 kDa band included cortactin and autophosphorylated p72-syk, p72-syk activity rapidly increased upon collagen stimulation, whereas p60-c-src activation was below detectable levels. A combination of inhibitors to remove the effects of extracellular and intracellular Ca-2+, released ADP, and fibrinogen binding to GPIIb/IIIa delayed and attenuated the major 75 kDa band. By contrast, p72-syk activation was not inhibited by these treatments. Cytochalasin D completely inhibited protein tyrosine phosphorylation and p72-syk activation. It also potently inhibited aggregation and (Ca-2+)-i elevation. Anti-GPIa/IIa MoAb in a concentration-dependent manner partially attenuated protein tyrosine phosphorylation and p72-syk activation. Its inhibitory effects on intracellular Ca-2+ mobilization, release of intracellular granule contents, and aggregation also were partial. No tyrosine kinase activity was coprecipitated with GPIa/IIa. These results suggest that p72-syk activation lies upstream of protein tyrosine phosphorylation, Ca-2+ mobilization, ADP release, thromboxane A-2 production and aggregation. GPIa/IIa plays a key role in p72-syk activation induced by collagen, but other collagen receptors may work in synergy to fully activate p72-syk. Actin polymerization is a prerequisite for both p72-syk activation and other intracellular signal transduction pathways.

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Accession: 009268308

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