Shape change is independent of tyrosine phosphorylation of p130 in human platelets

Silvia Riondino, Pier Paolo Gazzaniga, Fabio M. Pulcinelli

Research output: Contribution to journalArticle

Abstract

It has been previously suggested that tyrosine phosphorylation of p62, p68, and p130 might be necessary for the platelet shape change to occur. In preliminary studies we observed that high concentrations (30 μM) of a protein kinase C inhibitor, Ro 31-8220, selectively suppressed p130 tyrosine phosphorylation induced by thrombin, the thromboxane synthetic analogue (U46619) and ADP. Therefore, we have investigated the correlation, if any, between p130 tyrosine phosphorylation and platelet shape change induced by the same agonists in the presence of Ro 31-8220. Our results demonstrated that high concentrations of this compound almost completely abolished p130 tyrosine phosphorylation, whereas they had no effect on platelet shape change, thus proving a dissociation between these two phenomena. Our data support the hypothesis that a role in platelet shape change might be played by tyrosine phosphorylation of proteins other than p130.

Original languageEnglish
Pages (from-to)73-78
Number of pages6
JournalThrombosis Research
Volume92
Issue number2
DOIs
Publication statusPublished - Oct 15 1998

Keywords

  • p130
  • Platelet shape change
  • Tyrosine kinases

ASJC Scopus subject areas

  • Cardiology and Cardiovascular Medicine
  • Hematology

Fingerprint Dive into the research topics of 'Shape change is independent of tyrosine phosphorylation of p130 in human platelets'. Together they form a unique fingerprint.

  • Cite this