ABSTRACT
Evidence is rapidly accumulating that there are multiple points of interaction between the processes of coagulation, fibrinolysis, and inflammation and that these are multiple facets of the general, basic homeostatic mechanisms for repair and regeneration. One point at which these processes may converge is through interaction with fibronectin. There is substantial evidence that plasma fibronectin interacts with fibrin during polymerization and is incorporated into the fibrin gel [1]. Immunofluorescence studies have shown that fibronectin is distributed along fibrin strands and raise 122the possibility of fibrin-fibronectin copolymerization [2]. The plasma concentration of fibronectin is about 320 £tg/dl [3]. The serum concentration is reported to be 20-50% less than the plasma level and is due to incorporation of the protein into the clot [4]. Fibronectin is, in fact, the major protein in the clot after fibrin and constitutes 4-5% of the total protein [3]. An understanding of the effect of fibronectin on fibrin structure and function requires an understanding of fibrin formation. The mechanism for fibronectin interaction with fibrin must be within the framework of the basic mechanism of fibrin gel formation from fibrinogen.
