Effect of Structural Changes of Collagen on Collagen-platelet Reaction

Abstract

Removal of telopeptides from the acid soluble calf skin collagen with proctase did not affect the platelet aggregation. Limited digestion with tadpole collagenase at 20° C maintained the ability of collagen to aggregate platelets, when it was measured at 20°C., although its ability was completely abolished at 37° C. Neither α1 and α2-components of collagen did show the ability to aggregate platelets. Denaturation of the soluble collagen by heating at 45° C for 10 min destroyed its ability to aggregate platelets, although an initial shape change of platelets was observed.These results suggest that there may be different mechanisms in relation to the structure of collagen in the adhesion of platelets and the aggregation of platelets as a sequential reaction and that the tertiary structure of the soluble collagen composed of three polypeptides chains with a some critical length may be necessary for the platelet aggregation.