Thrombin treatment induces rapid changes in tyrosine phosphorylation in platelets.
Open Access
- 1 February 1989
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 86 (3), 901-905
- https://doi.org/10.1073/pnas.86.3.901
Abstract
We previously demonstrated that platelets express high levels of the tyrosine protein kinase pp60c-src. By a quantitative immunoblot assay, it is shown in this report that pp60c-src represents 0.2-0.4% of total platelet protein. The expression of high levels of pp60c-src in platelets correlated with high levels of total cell phosphotyrosine. Unstimulated platelets were shown to possess numerous phosphotyrosine-containing proteins by immunoblot analysis using antibodies that specifically recognize phosphotyrosine residues. To examine whether the pattern of phosphotyrosine-containing proteins changes upon platelet activation, lysates from thrombin- and phorbol ester-treated platelets were subjected to immunoblot analysis. Novel phosphotyrosine-containing proteins were detected within seconds following platelet stimulation. These results suggest that tyrosine phosphorylation, perhaps mediated by pp60c-src, may be involved in events associated with platelet activation.This publication has 41 references indexed in Scilit:
- The CD4 and CD8 T cell surface antigens are associated with the internal membrane tyrosine-protein kinase p56lckCell, 1988
- Cell Transformation by the Viral src OncogeneAnnual Review of Cell Biology, 1987
- RECEPTORS FOR EPIDERMAL GROWTH FACTOR AND OTHER POLYPEPTIDE MITOGENSAnnual Review of Biochemistry, 1987
- Tyrosine kinases in normal human blood cellsFEBS Letters, 1986
- Site-Specific Increased Phosphorylation of pp60
v-
src
After Treatment of RSV-Transformed Cells with a Tumor PromoterScience, 1985
- Two separate tyrosine protein kinases in human plateletsFEBS Letters, 1985
- Highly specific antibody to Rous sarcoma virus src gene product recognizes a novel population of pp60v-src and pp60c-src molecules.The Journal of cell biology, 1985
- Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membraneNature, 1984
- High tyrosine kinase activity in normal nonproliferating cellsNature, 1983
- Thrombin-induced protein phosphorylation in human platelets.JCI Insight, 1975