作者: K M Pumiglia , L F Lau , C K Huang , S Burroughs , M B Feinstein
DOI: 10.1042/BJ2860441
关键词: Tyrosine 、 Biochemistry 、 Tyrosine-kinase inhibitor 、 Protein kinase C 、 Tyrosine phosphorylation 、 Protein kinase A 、 Biology 、 Protein phosphorylation 、 Protein tyrosine phosphatase 、 Phosphorylation
摘要: The protein tyrosine phosphatase (PTPase) inhibitor pervanadate (vanadyl hydroperoxide) stimulated phosphorylation 29-fold more than did thrombin in intact and saponin-permeabilized platelets. Increased preceded, or was coincident with, a fall PtdIns(4,5)P2 levels, production of PtdIns(3,4)P2 phosphatidic acid, mobilization intracellular Ca2+, stimulation kinase C-dependent phosphorylation, secretion dense alpha-granules, increased actin polymerization, shape change aggregation which required fibrinogen mediated by surface expression GPIIb-IIIa. RG 50864 totally prevented induction pervanadate, as well all other responses measured; contrast, the inactive structural analogue, tyrphostin #1, had no effect. Dense-granule induced C activity; however, alpha-granule were independent C. In platelets phospholipase activity GTP-independent GTP-dependent mechanisms respectively. We conclude that PTPases are important regulators signal transduction