Abstract
The adhesive plasme proteins such as fibrinogen, fibronectin, vitronectin and von Wil lebrand factor have the common cell attachment site; Arg-gly-Asp (RGD), which was recently identified. We investigated the role of platelet receptor-protein's ligand mechanism by using synthetic RGD-Ser (IDS) on the interaction between platelet and artificial surface. RGDS inhibited platelet adhesion, aggregation and shape change of adhered platelets on fibronectin-coated substrate in a dosedependent manner, but showed partial inhibition for fibrinogen even in high concentration. we can conclude that RGD receptor-ligand interaction between platelet and plasma proteins is the dominant factor for platelet adhesion, activation and aggregation on the artificial surface, although there may operate partly other interaction mechanism for adsorbed fibrinogen.
