Activity of pp60c-src and association of pp60c-src, pp54/58lyn, pp60fyn, and pp72syk with the cytoskeleton in platelets activated by collagen.

Abstract

Collagen stimulation of platelets induced an increase in the specific activity of pp60c-src immunoprecipitated from the Triton-soluble fraction. The earliest time after collagen stimulation that an increase in pp60c-src activity was observed was 30 s. However, the maximum activity of pp60c-src in the Triton-soluble fraction was observed 60 s after collagen stimulation. At this time an approximately twofold increase of pp60c-src activity towards phosphorylation of KVEKIGEGTYGVVKK specific peptide and enolase and a 4.5-fold increase towards phosphorylation of pp60c-src itself was measured. Furthermore, the majority of pp60c-src as well as pp54/58lyn, pp60fyn, and pp72syk were found in the Triton-soluble fraction in resting platelets. Collagen induced, to different extents and velocities, translocation of all of these proteins from the Triton-soluble fraction to the Triton-insoluble, cytoskeleton-rich, platelets fraction. These results provide direct evidence that collagen stimulation of platelets increases the tyrosine kinase activity of pp60c-src and suggest that the platelet cytoskeleton plays an important role in collagen-induced signal transduction by localizing signaling molecules.

Cite this paper

@article{Kralisz2000ActivityOP, title={Activity of pp60c-src and association of pp60c-src, pp54/58lyn, pp60fyn, and pp72syk with the cytoskeleton in platelets activated by collagen.}, author={Urszula Kralisz and Czesław S. Cierniewski}, journal={IUBMB life}, year={2000}, volume={49 1}, pages={33-42} }