Fibrinogen-Collagen Interactions

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Abstract
Recently fibrinogen-collagen sponge preparations have been used surgically for tissue adhesion (Austria, BRD, Swiss). Therefore fibrinogen-collagen interactions were studied by affinity-chromatography and by investigation of fibrin crosslink formation in presence of collagen. Affinity chromatography of plasma on collagen-Sepharose yielded retention of fibrinogen on conjugates of native collagen type3 and denatured collagen typel. Vice versa these collagen types were adsorbed by fibrinogen-Sepharose. Fibrinogen-collagen mixtures were clotted by adding thrombin, Ca2+ and factor 13. In contrast to dissolved collagen, collagen fibers interfered with fibrin crosslinking, i.e. – dimer formation was restricted as shown by acrylamid gel elctrophoresis of the reduced coagulum. Covalent coupling of fibrin to collagen was not observed by DEAE and CM-cellulose chromatography. The affinity of collagen to fibrin was demonstrated by adhesion of collagen sponges (containing thrombin) with 10% fibrinogen. Breaking strength (p/cm2) is dependent on sponge. Studies on collagen-fibrinogen tissue adhesions are in progress. Scanning electron microscopic pictures showed inclusion of fibrin into collagen sponges. According to our results, collagen fibrinogen adhesion refer mainly to mechanic sticking. The affinity of plasma fibrinogen to collagen type3 will stimulate further investigations, since Gay et al.(Klin. Wschr. 53, 1975) have shown that collagen type3 is the main connective tissue component under endothelial cell-layers of arterial walls.

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