Plasma clot-promoting effect of collagen in relation to collagen-platelet interaction.
The hemostatic function of several acid-soluble collagen preparations and a fibrillar-form collagen preparation have been compared. Pepsin-treated acid-soluble collagen isolated from burro and horse aortic tissue and acid-soluble collagen isolated from human umbilical cord readily promoted platelet aggregation, but failed to activate the coagulation mechanism even after prolonged incubation with plasma at 37 C. By contrast, fibrillar-form collagen isolated from burro aorta was both an efficient stimulant for the induction of platelet aggregation and a potent clot-promoting agent. Similar results were found for all the collagen preparations irrespective of whether the studies were conducted with sheep or with burro plasma. Heat denaturation studies showed that the hemostatic function of the fibrillar-form collagen was dependent on an intact triple-helical structure.
D000818:Animals; D001777:Blood Coagulation; D003094:Collagen / Q000502:physiology*; D006358:Hot Temperature; D006801:Humans; D007700:Kinetics; D008297:Male; D010527:Perissodactyla / Q000097:blood; D010974:Platelet Aggregation; D012756:Sheep / Q000097:blood
D003094:Collagen