Adhesive reactions constitute extremely important cellular functions that are required to maintain certain physiological processes such as cell migration, proliferation, differentiation, and cellular activation. Adhesion can be mediated through cell-cell or cell-matrix interactions, and many are mediated by integrin glycoproteins, a major family of cellular adhesion receptors.1 The integrin superfamily of adhesion receptors is widely distributed and interacts with all of the key extracellular matrix proteins (e.g. collagens, laminin, fibronectin, vitronectin). Each integrin contains a single R- and â-subunit that forms a noncovalent complex, required for adhesive function. Currently known are 17 unique R-chains and 8 â-chains that give rise to greater than 20 characterized integrin complexes. Integrins can bind either unique single ligands or multiple ligands, thus determining a broad range of specificity with adhesive ligands.1 Beyond adhesive functions, integrins also mediate more traditional cellular signaling activities of a receptor, initiated by engagement through their relevant adhesive ligands.1 Integrins have been proposed to play significant roles in diseases and have been extensively studied in areas such as thrombosis, inflammation, angiogenesis, and osteoporosis.1 Of pioneering importance in this respect is the platelet and megakaryocyte-specific integrin, RIIbâ3 (also commonly know as GPIIb-IIIa), which has received considerable attention as a drug target due to its requisite role in platelet aggregation, a significant mechanism in mediating arterial thrombosis.2-8