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J. Biol. Chem., Vol. 266, Issue 3, 1415-1421, Jan, 1991
IF Charo, L Nannizzi, DR Phillips, MA Hsu and RM Scarborough
The glycoprotein IIb-IIIa complex (GP IIb-IIIa) mediates platelet
aggregation and is a member of the cytoadhesin family of receptors that
bind adhesive proteins such as fibrinogen, fibronectin, and von Willebrand
factor. Despite the wide range of cell-substrate interactions mediated by
these receptors, ligand binding domains have not yet been identified on any
of the integrins. The present study was designed to determine potential
fibrinogen binding domain(s) on the GP IIb-IIIa complex. Synthetic peptides
derived from residues 1-288 of the amino-terminal portion of GP IIIa were
tested for their abilities to block the binding of fibrinogen to purified
GP IIb-IIIa in a solid- phase microtiter assay. Two overlapping peptides
encompassing residues 204-229 of GP IIIa were identified which blocked
fibrinogen binding in this assay. Polyclonal antibodies to these peptides
blocked fibrinogen binding to purified GP IIb-IIIa as well as platelet
aggregation. The overlapping residues of these two peptides GP IIIa
(211-222), SVSRNRDAPEGG-NH2, blocked the binding of fibronectin, von
Willebrand factor, and vitronectin to purified GP IIb-IIIa. Finally, direct
binding of GP IIIa (204-229) to fibrinogen and fibronectin was demonstrated
by enzyme-linked immunosorbent assay. We conclude from these studies that
the amino acid sequence 211-222 of GP IIIa is critically involved in
adhesive protein binding, and may represent an important portion of the GP
IIb-IIIa ligand binding domain.
Inhibition of fibrinogen binding to GP IIb-IIIa by a GP IIIa peptide
COR Therapeutics Inc., South San Francisco, California 94080.
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