ACTIVATION EFFECT OF THE SORBED PLASMIN. MODELLING IN VITRO
Abstract
One of the major factors of cancer and inflammatory processes development is excessive activation action of plasmin - a key enzyme of the fibrinolytic system. Such significant activation was caused not only physiological plasminogen binding on the fibrin mesh surface but also pathological-mediated interaction of plasminogen with dipole pairs of amino acid residues on the vessels surface. These amino acid pairs are structural analogues of ligands for lysine-binding sites of plasminogen. Their exposition on external side of cell membranes is result of interaction of protein and peptide products of endogenous intoxication with membranes phospholipids. Activation action of plasmin specifically sorbed on lysine-agarose state against soluble plasma prothrombin had been studied. The development of significant amidolytic thrombin-like activity that was insensitive to antithrombin III inhibition was noted. The obtained results show the ability of sorbed plasmin to proteolytic damage and non-functional activation of soluble proteins of blood. Mechanisms of formation of such activation in vivo and its possible role in the development of various pathologic states, particularly at disseminated intravascular coagulation were discussed.
Key words: plasmin, thrombin, disseminated intravascular coagulation.
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