Faculty Research 1980 - 1989


Interaction of fibronectin with its receptor on platelets.

Document Type


Publication Date



Antigenic-Determinants, Binding-Sites, Blood-Platelets: me, Cell-Membrane: me, Cross-Linking-Reagents, Fibronectins: me, Glycoproteins: im, me, Human, Membrane-Proteins: im, me, Molecular-Weight, Receptors-Immunologic: im, me, SUPPORT-U-S-GOVT-P-H-S, Thrombin

JAX Source

Cell. 1985 Sep; 42(2):439-48.


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.

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