The role of plasma fibronectin in platelet adhesion to collagen.
Human washed platelets were eluted from columns of Sepharose 4B linked to different preparations of collagen in order to evaluate cell adhesion. Collagen preparations characterized by low and high affinity toward platelets were identified. In our experiments, fibronectin purified from human plasma modified platelet adhesiveness, though not dramatically. When washed platelets, resuspended in a buffer containing fibronectin, were filtered on a low-affinity collagen-Sepharose, a significant increase in their adhesion occurred. A similar modification could be observed when platelets were allowed to adhere to the same collagen-Sepharose preconditioned with fibronectin. The effect of fibronectin was otherwise negligible when the high-affinity collagen was used for the experiments.
D002846:Chromatography, Affinity; D003094:Collagen / Q000502:physiology*; D004591:Electrophoresis, Polyacrylamide Gel; D005353:Fibronectins / Q000097:blood* / Q000494:pharmacology; D006801:Humans; D066298:In Vitro Techniques; D010973:Platelet Adhesiveness
D005353:Fibronectins; D003094:Collagen