Platelet-collagen adhesion-membrane fluidity and the development of high affinity adhesion through multiple interacting sites.
Multiple, linked interactions between the platelet surface and collagen fibers have been implicated in the initiation of platelet secretion and subsequent aggregation. The formation of such multiple simultaneous interactions could give rise to high affinity adhesion of platelets to collagen even though the affinity of the individual interactions may be much weaker. This concept has been tested by measuring the adhesion of platelets to collagen under conditions which could effect the formation of multiple interactions. Adhesion is markedly diminished at 4 degrees C but not at 23 or 37 degrees C. Metabolic inhibitors such as 2-deoxyglucose and Antimycin A do not inhibit adhesion although they virtually abolish subsequent aggregation. Brief formaldehyde fixation of platelets greatly reduces adhesion. These results are consistent with the concept that the formation of multiple linked interactions between the platelet surface and collagen are important in platelet-collagen adhesion and that mobility of platelet membrane components is required for the clustering of these interactions in focussed regions on the platelet surface.
D000968:Antimycin A / Q000494:pharmacology; D001665:Binding Sites; D001792:Blood Platelets / Q000187:drug effects / Q000378:metabolism*; D003094:Collagen / Q000097:blood*; D003847:Deoxyglucose / Q000494:pharmacology; D006801:Humans; D008560:Membrane Fluidity / Q000187:drug effects; D010974:Platelet Aggregation / Q000187:drug effects; D013499:Surface Properties; D000267:Tissue Adhesions
D000968:Antimycin A; D003094:Collagen; D003847:Deoxyglucose