Abstract
The enhanced platelet adhesion on adhesive protein-coated surfaces was reduced by the addition of synthetic tetrapeptide, RGDS (Arg-Gly-Asp-Ser), which was identified as a common amino acid sequence of adhesive site of adhesive proteins. This was same as WBC in complement-inactivated serum. No significant effect was observed for WBC in complement-actvated. These indicate that RGDS ligand-receptor mechanism operates on adhesive protein-adsorbed surfaces for both cellular systems and that complement factor (C3b)-membrane receptor (CR3) interaction operates for WBC as complement is activated.
