Abstract
Fibrinogen-related peptides, which inhibit the interaction of fibrinogen with the platelet membrane glycoprotein IIb IIIa complex ( GPIIb IIIa ) are under preclinical investigation now (1). Whereas peptides containing the Arg-Gly-Asp (RGD) sequence inhibit fibrinogen-dependent platelet aggregation by direct binding to GPIIb IIIa (2), GPRP inhibits fibrinogen polymerisation by direct binding to the fibrinogen polymerisation sites and modifying the glutamine residues in the α- and γ-chains of fibrinogen (3, 4). Since GPRP has been shown to inhibit ADP-induced platelet aggregation it has been suggested as antithrombotic agent (5). It has been demonstrated that in defibrinated plasma the amount of free thrombin generated after clotting activation is significantly higher than in normal plasma (6). The explanation for this observation is that in normal plasma free thrombin is partially adsorbed on generated fibrin (7). Since GPRP inhibits fibrinogen polymerisation, we investigated the generation of thrombin in platelet-rich plasma (PRP) containing GPRP.
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