[Importance of the structure of the clot in thrombolysis].
Activation of plasminogen by tissue-type plasminogen activator (tpA) is potentiated by fibrin. We have demonstrated the role of fibrin polymerization in the potentiating effect of tpA-induced fibrinolysis. Therefore a pathogenic mechanism of thrombotic disorder may be related to an abnormal fibrin polymerization: the abnormal clot being less accessible to fibrinolysis than normal one. This defective lysis may be due to a defective enhancement by the abnormal fibrin of plasminogen activation by tpA, as demonstrated for fibrinogen Dusard, a congenital dysfibrinogenemia associated with a very severe thrombotic disorder. In some other cases, a decrease in the availability of the plasmin cleavage sites in fibrin clot may be involved. On the contrary, some antithrombotic drugs such as pentosane polysulfate in modifying clot structure allow a better degradation of fibrin clot by fibrinolytic enzymes. It is speculated that this enhanced fibrinolysis could explain, almost in part, the antithrombotic action of these drugs.
D001777:Blood Coagulation / Q000187:drug effects; D005337:Fibrin / Q000378:metabolism; D005342:Fibrinolysis / Q000187:drug effects; D006801:Humans; D010375:Pedigree; D010426:Pentosan Sulfuric Polyester / Q000494:pharmacology; D013577:Syndrome; D013917:Thrombin / Q000378:metabolism; D013927:Thrombosis / Q000097:blood* / Q000235:genetics
D010426:Pentosan Sulfuric Polyester; D005337:Fibrin; D013917:Thrombin
Importance de la structure du caillot sur la thrombolyse.