Lysis of Crosslinked and Non-Crosslinked Purified Fibrin

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Abstract
Several authors have reported that cross-linking by Factor XIII makes fibrin less susceptible to lysis by fibrinolytic enzymes, especially to plasminogen activators. However, the conclusions of most of these studies have been based on circumstantial evidence.To unambiguously establish a possible effect of cross-linking of fibrin on its resistance to lysis, the following experimental conditions are necessary (a) the use of preformed fibrin substrate, (b) the use of purified protein components, and (c) measurement of the extent of cross-linking. With due observance of these conditions, we determined lysis of both cross-linked and non cross-linked fibrin by plasmin, urokinase, and a human tissue activator by means of the fibrin plate assay. Purified preparations of fibrin, F XIII, and plasminogen were used. Cross-linking was determined by means of SDS polyacrylamide gel electrophoresis.The results revealed no differences in resistance to lysis of highly cross-linked and non-cross-linked fibrin.They suggest that the mechanism underlying the effect of F XIII on haemostasis is not directly related to a change in the resistance of the fibrin in the blood clot to lysis by fibrinolytic enzymes. For a better understanding of the role of F XIII in haemostasis, attention should be focused on processes which occur in the whole blood clot and not in purified fibrin.

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