INHIBITION OF PLATELET-ADHESION TO FIBRONECTIN, FIBRINOGEN, AND VONWILLEBRAND-FACTOR SUBSTRATES BY A SYNTHETIC TETRAPEPTIDE DERIVED FROM THE CELL-BINDING DOMAIN OF FIBRONECTIN

Google Scholar
  • 1 January 1985
    • journal article
    • research article
    • Vol. 66  (4) , 946-952
Abstract
The role in platelet function of the cell-binding region of fibronectin was explored by the use of synthetic peptides. The prototypical peptide gly-arg-gly-asp-ser was capable of inhibiting thrombin-induced platelet aggregation without altering the degree of platelet activation as judged by the secretion of 14C-serotonin. The peptide also effectively inhibited, in a concentration-dependent manner, the binding of radiolabeled fibronectin to platelets and the adhesion of platlets to fibronectin substrates. The smallest peptide from the cell-binding region of fibronectin which retained full activity was arg-gly-asp-ser. Transposition of amino acids or conservative substitutions of amino acids within this short sequence resulted in inactive peptides. Peptides containing the arg-gly-asp-ser sequence were also capable of inhibiting the adhesion of platlets to fibrinogen and von Willebrand factor substrates. Examination of the entire panel of synthetic peptides for ability to inhibit adhesion to fibrinogen or von Willebrand factor substrates revealed the same structure-function relationships that had been determined in the studies with fibronectin.