Echistatin inhibits pp72~syk and pp125~FAK phosphorylation in fibrinogen-adherent platelets

摘要

The adhesion of ADP-stimulated platelets to immobilized fibrinogen induces the tyrosine phosphorylation of multiple proteins which include pp72~syk and pp125~FAK. The phosphorylation of these two proteins increases as function of time of platelet adhesion to fibrinogen; however, pp72~syk results strongly phosphorylated already after 15 min, whereas pp125~FAK reaches high levels of phosphorylation after 1 h of platelet adhesion.