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J. Biol. Chem., Vol. 262, Issue 3, 947-950, Jan, 1987
SC Lam, EF Plow, MA Smith, A Andrieux, JJ Ryckwaert, G Marguerie and MH Ginsberg
Synthetic peptides corresponding to the carboxyl terminus of the fibrinogen
gamma chain inhibit the binding of fibrinogen, fibronectin, and von
Willebrand factor to platelets, yet the active decapeptide sequence has
only been found in fibrinogen to date. In contrast, all three proteins
contain Arg-Gly-Asp sequences, and peptides containing Arg-Gly-Asp are
potent inhibitors of their binding to activated platelets. We have analyzed
the relationship between these peptide sets by direct binding assays. H12
(gamma 400-411) inhibited the binding of an Arg-Gly-Asp-containing peptide
to platelets with similar dose response to inhibition of fibronectin
binding. We have previously reported that GPIIb-IIIa binds to immobilized
Arg-Gly-Asp peptides and can be eluted by Arg-Gly-Asp-containing peptides
in solution. Both H12 and L10 (gamma 402-411) completely eluted GPIIb-IIIa
bound to immobilized Arg-Gly-Asp peptides. Conversely, when GPIIb-IIIa was
bound to immobilized L10, either L10 or an Arg-Gly-Asp peptide could elute
it. Peptide specificity was established by the failure of Gly-Arg-Gly-
Glu-Ser-Pro or acetylated L10 to elute GPIIb-IIIa from the immobilized
peptides. These results indicate that the two peptide sets interact with
the same receptor which contains GPIIb-IIIa.
Evidence that arginyl-glycyl-aspartate peptides and fibrinogen gamma chain peptides share a common binding site on platelets
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