| Three mathematical models have been developed to describe the activation of TAFI and fibrinolysis; one focusing on structural aspects of a freely circulating clot. This extends previous models that only considered one-dimensional clots totally occluding a tubular blood vessel. It appears that thrombomodulin significantly increases the rate of TAFI activation and that TAFI could be a clinical fibrinolysis inhibitor as it can be activated at high levels. Reduction of α2-antiplasmin significantly increases the rate of fibrin degradation, dependent upon the inhibitory kinetic dissociation constant of its binding with free plasmin and its initial concentration. Fibrinolysis does not appear to significantly lower the circulating levels of t-PA or plasminogen which is in agreement with the absence of clinical deficiencies in these proteins. Clot lysis naturally is dependent on clot size and concentration of fibrinolytic enzymes, but not on fibrin density. |
