Complex Formation of Platelet Membrane Glycoproteins IIb and IIIa with Fibrinogen

Overview

Journal J Clin Invest

Specialty General Medicine

Date 1982 Feb 1

PMID 6460044

Citations 58

Authors

R L Nachman

L L Leung

Affiliations

Soon will be listed here.

Abstract

We have recently reported the isolation of purified platelet membrane glycoproteins IIb and IIIa and the generation of monospecific antisera to these membrane proteins. Using these monospecific antisera in an enzyme-linked immunosorbent assay system, it is no demonstrated that glycoprotein IIb (GPIIb) and glycoprotein IIIa (GPIIIa) form a complex with purified human fibrinogen. The formation of this GPIIb-GPIIIa fibrinogen complex is calcium dependent, fibrinogen specific, saturable, and inhibited by specific amino sugars and amino acids. These observations suggest that the GPIIb-GPIIIa macromolecular complex on the platelet surface acts under the proper physiologic circumstances as the fibrinogen binding site required for normal platelet aggregation.

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