Interaction of fibronectin with its receptor on platelets.

We report that the 12,000 dalton domain of fibronectin that interacts with fibroblast cell surfaces also binds specifically to thrombin-inducible, saturable receptors on platelets. Furthermore, we have used chemical cross-linking and monoclonal antibodies to show that the 12,000 dalton domain of fibronectin interacts directly with glycoprotein IIIa at the platelet cell surface. Both binding and cross-linking of this domain to platelets are competed by a hexapeptide previously shown to block fibroblast adhesion to fibronectin. Finally, we show that a complex of the platelet glycoproteins IIIa and IIb binds to affinity columns of a cell-attachment fragment of fibronectin. These results localize a major fibronectin-platelet interaction to a specific domain of fibronectin and to a specific platelet glycoprotein.