Thrombopoietin modulates platelet activation in vitro through protein-tyrosine phosphorylation

Stem Cells. 1996 Jul;14(4):439-44. doi: 10.1002/stem.140439.

Abstract

To determine the roles of thrombopoietin (TPO) in platelet function in vitro, we examined the effects of TPO on platelet aggregation. Although several proteins in platelets were tyrosine-phosphorylated by TPO treatment, TPO alone was unable to induce platelet aggregation. However, the secondary wave of platelet aggregation induced by adenosine diphosphate (ADP) was enhanced by TPO in a dose-dependent manner. TPO in conjunction with ADP augmented tyrosine phosphorylation of platelet proteins, including tyrosine-phosphorylated proteins induced by TPO alone. Genistein inhibited protein-tyrosine phosphorylation in platelets induced by TPO with ADP and suppressed TPO-enhanced platelet aggregation. Moreover, tyrosine phosphorylation of MAP-kinases induced by TPO alone and TPO with ADP was consistent with TPO-enhanced platelet aggregation. These findings in the present study suggest that signal transduction involved in TPO-enhanced platelet aggregation is mediated in part by tyrosine-phosphorylated proteins, including MAP-kinases, in platelets through TPO-stimulated c-Mpl, TPO receptor.

MeSH terms

  • Adenosine Diphosphate / pharmacology*
  • Blood Platelets / metabolism
  • Blood Platelets / physiology*
  • Cells, Cultured
  • Humans
  • Phosphorylation
  • Platelet Aggregation / drug effects*
  • Proteins / metabolism
  • Thrombopoietin / pharmacology*
  • Tyrosine / metabolism*

Substances

  • Proteins
  • Tyrosine
  • Adenosine Diphosphate
  • Thrombopoietin