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The interaction of blood platelets with collagen is the trigger of haemostasis and, at least partly, of thrombosis. Two types of fibrillar collagens (type I and type III), present in the vessel wall, can induce the adhesion of blood platelets. This study was designed to determine which part of their molecule is involved in that phenomenon. We then devised a quantitative test based upon differential filtration of non adhesive and adhesive 14c serotonin labeled platelets through a sepharose column for the evaluation of platelet adhesion to collagen or collagen derivatives. No differences were observed in the adhesive properties of calf-skin type I and type III collagens when the degree of multimerisation was identical. Isolated alpha 1 (I) and alpha 2 chains were not active ; but platelets adhered to reassociated (alpha .1 (I))3 trimers, not to (alpha 2)3 trimers ; in type I collagen, alpha 1 chains seems to have the most essential role for platelet adhesion. Various cyanogen bromide peptides were tested : only the 217 C-terminal amino acids alpha 1 CB6 from type I and the 149 central amino acids alpha 1 CB4 from type III were active.  The adhesive properties of collagen seems then associated with chemical groupings localized in these peptides : a random folding of the entire isolated chains could make these “sites” unavailable to the platelets, whereas in the triple helix characteristic of fibrillar trimers, they would be more accessible. This could explain why fibrils and small peptides are active, while isolated chains are not.

Platelet-Collagen Interaction : Adhesion to Alpha 1 (I) CB6 and Alpha 1 (III) CB4 Peptides from Calf-Skin Collagen