Abstract
T HE fibrinolytic system consists basically of fibrinogen, fibrin, plasminogen, plasmin, and activators of plasminogen. Plasmin, however, appears to be implicated in pathways other than fibrinolysis or fibrinogenolysis. For example, plasmin is capable of digesting factor Xlla to factor Xlla fragments which, in turn, are potent activators of prekallikrein.’ In this manner, plasmin can function in a capacity that controls the initiation of intrinsic blood coagulation and kallikrein formation by means of its action on factor Xlla. Additionally, plasmin is capable of activation of several complement zymogens, namely, Cl,’ C3,3 and C5.4 Plasmin has also been shown to substitute for factor D in the alternate pathway.5 Although the above facets of plasmin action have a great attraction in ascribing its possible role, only the well known fibrinolytic and iibrinogenolytic(’ activities of plasmin will be considered in this review. The intent of this article is to describe recent advances in the elucidation of the circulating structure of plasminogen, the mechanism of activation of plasminogen, and the role of antifibrinolytic amino acids in plasminogen activation.
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