Abstract
We show that p72syk is rapidly activated following the stimulation of thromboxane A2 mimetics, U44069 and STA2 in porcine platelets. The activity of p72syk reached a maximum at 10 s and decreased to a basal level within 60 s after 1 μM U44069 stimulation. This activation was enhanced in a dose-dependent manner and completely canceled by the pretreatment of platelet suspension with ONO3708, a specific antagonist of thromboxane A2. Pretreatment of platelets with aspirin as well as apyrase did not affect the activation of p72syk. When both extra- and intra-cellular Ca2+ were depleted, the activation of p72syk was still persistent; in contrast, the deactivation process was completely abrogated even at 120 s after U44069 stimulation. These results suggest that p72sykis a responsible enzyme to the protein-tyrosine phosphorylation events, and that p72syk functions mainly before Ca2+ recruitment in thromboxane A2-stimulated platelets.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochemical and Biophysical Research Communications
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
