Mechanistic aspects of cellular interactions with artificial dialyzer membrane surfaces.
The platelet adhesion on adhesive protein-coated surfaces was significantly reduced by the addition of the synthetic tetrapeptide, RGDS (Arg-Gly-Asp-Ser), which was identified as the common amino acid sequence of adhesive site of adhesive proteins. The inhibitory effect was also observed for leukocyte(WBC) in complement-inactivated serum. No significant effect was observed for WBC in complement-activated serum. These indicate that the RGDS ligand-receptor mechanism operates on adhesive protein-adsorbed surfaces for both cellular systems and that activated complement factor (C3b)-membrane receptor (CR3) interaction operates for WBC as the complement is activated.
Matsuda
T
T
Dept. of Bioengineering, National Cardiovascular Center, Osaka, Japan.
Takemoto
Y
Y
Kishimoto
T
T
Maekawa
M
M
Akutsu
T
T
D000595:Amino Acid Sequence; D001792:Blood Platelets / Q000502:physiology*; D002448:Cell Adhesion / Q000187:drug effects / Q000276:immunology / Q000502:physiology*; D002482:Cellulose; D003167:Complement Activation / Q000502:physiology; D006801:Humans; D039421:Integrin alpha2; D008422:Materials Testing; D008562:Membrane Glycoproteins; D008567:Membranes, Artificial; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000494:pharmacology; D010975:Platelet Aggregation Inhibitors / Q000494:pharmacology; D011142:Polyvinyl Alcohol; D011956:Receptors, Cell Surface / Q000502:physiology; D006435:Renal Dialysis
C056564:ITGA2B protein, human; D039421:Integrin alpha2; D008562:Membrane Glycoproteins; D008567:Membranes, Artificial; D009842:Oligopeptides; D010975:Platelet Aggregation Inhibitors; D011956:Receptors, Cell Surface; D011142:Polyvinyl Alcohol; D002482:Cellulose; C046617:arginyl-glycyl-aspartyl-serine