Participation of tyrosine phosphorylation in cytoskeletal reorganization, alpha(IIb)beta(3) integrin receptor activation, and aspirin-insensitive mechanisms of thrombin-stimulated human platelets.

Autores de IIS La Fe

• Maria Teresa Santos Diaz

  Autor

• Antonio Moscardó Martínez

  Autor

• Juana Valles Giner

  Autor

• María Carmen Martínez Bisbal

  Autor

• Marta Piñon Saborit

  Autor

• Justo Aznar Lucea

  Autor

Participantes ajenos a IIS La Fe

• Broekman MJ
• Marcus AJ

Abstract

Fibrinogen binding to the active conformation of the alpha(IIb)beta(3) integrin receptor (glycoprotein IIb/IIIa) and cytoskeletal reorganization are important events in platelet function. Tyrosine phosphorylation of platelet proteins plays an essential role in platelet signal transduction pathways. We studied the participation of tyrosine kinases on these aspects of platelet reactivity and their importance in cyclooxygenase (COX)-1-independent mechanisms in thrombin-stimulated human platelets.

Keywords

• platelets; tyrosine kinases; glycoproteins; cytoskeleton; aspirin; thrombin