Maintenance of fibrin solubility by plasma fibronectin.

The present study evaluated the influence of plasma fibronectin on the formation of fibrin and fibrin-collagen complexes. Experiments were performed in vitro in a homologous rat system consisting of urea solubilized 125I-fibrin monomer, plasma fibronectin, and insoluble particulate collagen. The formation of pelletable complexes was assessed after incubation at 37 degrees C. Fibronectin effectively inhibited the interactions reflected in pelletability in systems containing fibrin and fibrin-collagen. Solubility was equally well maintained during inhibition of plasminolysis. In addition, plasma fibronectin resolubilized performed pelletable complexes. The current results suggest a potential antithrombotic role for plasma fibronectin.