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  • Title: Ambivalent roles of carboxypeptidase B in the lytic susceptibility of fibrin.
    Author: Kovács A, Szabó L, Longstaff C, Tenekedjiev K, Machovich R, Kolev K.
    Journal: Thromb Res; 2014 Jan; 133(1):80-7. PubMed ID: 24094605.
    Abstract:
    BACKGROUND: Removal of C-terminal lysine residues that are continuously exposed in lysing fibrin is an established anti-fibrinolytic mechanism dependent on the plasma carboxypeptidase TAFIa, which also removes arginines that are exposed at the time of fibrinogen clotting by thrombin. OBJECTIVE: To evaluate the impact of alterations in fibrin structure mediated by constitutive carboxypeptidase activity on the function of fibrin as a template for tissue plasminogen activator-(tPA) induced plasminogen activation and its susceptibility to digestion by plasmin. METHODS AND RESULTS: We used the stable carboxypeptidase B (CPB), which shows the same substrate specificity as TAFIa. If 1.5 - 6μM fibrinogen was clotted in the presence of 8U/mL CPB, a denser fibrin network was formed with thinner fibers (the median fiber diameter decreased from 138 - 144nm to 89 - 109nm as established with scanning electron microscopy). If clotting was initiated in the presence of 5 - 10μM arginine, a similar decrease in fiber diameter (82 -95nm) was measured. The fine structure of arginine-treated fibrin enhanced plasminogen activation by tPA, but slowed down lysis monitored using fluorescent tPA and confocal laser microscopy. However, if lysis was initiated with plasmin in CPB-treated fibrin, the rate of dissolution increased to a degree corresponding to doubling of the plasmin concentration. CONCLUSION: The present data evidence that CPB activity generates fine-mesh fibrin which is more difficult to lyse by tPA, but conversely, CPB and plasmin together can stimulate fibrinolysis, possibly by enhancing plasmin diffusion.
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