Phosphorylation of JAK2 in thrombin-stimulated human platelets.

Abstract

We show the presence of the tyrosine kinase JAK2 in human platelets and demonstrate that it undergoes phosphorylation on tyrosine residues on challenge with the G protein receptor stimulus, thrombin, or the tyrosine phosphatase inhibitor, peroxovanadate. Thrombin-induced phosphorylation of JAK2 is inhibited by two structurally distinct inhibitors of tyrosine kinases, staurosporine and the tyrphostin ST271. The protein kinase C (PKC) inhibitor, Ro 31-8220, and intracellular Ca2+ chelator, BAPTA-AM, also inhibit thrombin-induced phosphorylation of JAK2, while the phorbol ester, phorbol dibutyrate (PDBu), and Ca2+ ionophore, A23187, induce tyrosine phosphorylation of JAK2. These results suggest that tyrosine phosphorylation of JAK2 stimulated by thrombin may be mediated downstream of phosphoinositide metabolism.

Statistics

0102030'98'00'02'04'06'08'10'12'14'16
Citations per Year

68 Citations

Semantic Scholar estimates that this publication has 68 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{RodrguezLiares1994PhosphorylationOJ, title={Phosphorylation of JAK2 in thrombin-stimulated human platelets.}, author={B Rodr{\'i}guez-Li{\~n}ares and Stephen P. Watson}, journal={FEBS letters}, year={1994}, volume={352 3}, pages={335-8} }