Platelet adhesion and prevention at blood-polymer interface.
It has been proposed that adsorbed glycoproteins such as fibrinogen and gamma-globulin induce platelet adhesion at blood-polymer interfaces. The importance of oligosaccharide groups in the glycoproteins proved to be responsible for platelet adhesion and aggregation via possible complex formation. Several studies have provided evidence that the proposed mechanism was involved in platelet adhesion on polymer surfaces. To minimize or prevent platelet adhesion on polymers, prostaglandins (PGs), potent inhibitors of platelet aggregation and PG-heparin (HEP) conjugate, were combined with polymers via physical dispersion or chemical immobilization on the surfaces. Albumin-HEP conjugate-adsorbed surfaces also showed significant reduction of platelet adhesion.
D000527:Alprostadil / Q000494:pharmacology; D001792:Blood Platelets / Q000187:drug effects / Q000502:physiology; D006493:Heparin / Q000494:pharmacology; D006801:Humans; D066298:In Vitro Techniques; D010973:Platelet Adhesiveness / Q000187:drug effects; D010974:Platelet Aggregation / Q000187:drug effects; D011108:Polymers; D012701:Serotonin / Q000378:metabolism; D012799:Sialyltransferases / Q000097:blood; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase
D011108:Polymers; D012701:Serotonin; D006493:Heparin; D012799:Sialyltransferases; D000527:Alprostadil; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase