Abstract
Glycoprotein IIb-IIIa (GPIIb-IIIa) is an externally exposed membrane complex on platelets which serves as an activation-dependent receptor for fibrinogen, fibronectin, von Willebrand factor and vitronectin. These ligands share an RGD sequence which binds to a specific site on GPIIIa. In addition, fibrinogen has a gamma chain dodecapeptide sequence that also interacts with GPIIb. Binding of fibrinogen to GPIIb-IIIa is directly responsible for cross-bridging adjacent platelets leading to platelet aggregate formation. In the search for pharmacologic anti-thrombotic agents, there has been considerable interest in drugs that inhibit platelet function, aspirin being the classic example. Recent efforts have been directed to the development of agents that target GPIIb-IIIa. Several synthetic peptides and peptidomimetic agents have been developed to compete with the RGD binding site on GPIIb-IIIa. Monoclonal antibodies directed against sites at or near the fibrinogen binding domains on GPIIb-IIIa have also been of considerable interest. The chimerised Fab fragment of the monoclonal antibody 7E3 (ReoPro, Centocor) has been approved by the US FDA to reduce the thrombotic complications of high risk angioplasty.
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