Open AccessThrombin treatment induces rapid changes in tyrosine phosphorylation in platelets.
Author(s) -
Andy Golden,
Joan S. Brugge
Publication year - 1989
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.86.3.901
Subject(s) - platelet , phosphorylation , tyrosine phosphorylation , thrombin , tyrosine , proto oncogene tyrosine protein kinase src , platelet activation , biochemistry , tyrosine kinase , protein phosphorylation , biology , microbiology and biotechnology , sh2 domain , chemistry , signal transduction , protein kinase a , immunology
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.