Platelet binding and protein adsorption to titanium and gold after short time exposure to heparinized plasma and whole blood.

Protein adsorption from human plasma and platelet binding and activation were studied at short blood-titanium/gold contact times. The protein adsorption was studied by ellipsometry-antibody techniques in situ, and adhering platelets were visualized with fluorescein isothiocyanate-labelled anti-CD 61 antibodies. Adhering platelets were quantified by counting labelled cells in microscopic image fields. The spreading of platelets was studied by scanning electron microscopy. The results show that after 1 min of plasma exposure, fibrinogen, IgG and albumin were detectable with antibodies on both surfaces. The amount of deposited fibrinogen and complement decreased with time on titanium, and the amount of adsorbed anti-high molecular weight kininogen increased. No complement was detected on gold surfaces after plasma incubation, and the antibody binding pattern also remained unchanged after prolonged plasma exposure. The surface-bound platelets were found to spread on the gold but not on titanium surfaces. C1q has been shown to induce the expression of P-selectin, i.e. cause secretion reactions in platelets. In this study secreted platelet-microvesicles were found on gold, but not on the titanium surfaces that bound significant amounts of C1q. Thus, the results of the present study indicate that the mixture of fibrinogen, C1q and kininogens, whilst causing adhesion and aggregation, does not result in the activation and microvesicle secretion of platelets. Platelet activation on biomaterial surfaces thus seems to be governed by the mixture of proteins present on that surface, and no one particular protein need cause a known reaction in platelets as obtained when platelets are exposed only to that particular protein.