Soria C, Soria J, Mirshahi M, Desvignes P, Bonnet P, Caen J P
Ann Biol Clin (Paris). 1987;45(2):207-11.
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.
纤维蛋白可增强组织型纤溶酶原激活剂（tPA）对纤溶酶原的激活作用。我们已经证明了纤维蛋白聚合在tPA诱导的纤溶增强效应中的作用。因此，血栓形成性疾病的发病机制可能与纤维蛋白聚合异常有关：异常凝块比正常凝块更难被纤溶。这种纤溶缺陷可能是由于异常纤维蛋白对tPA激活纤溶酶原的增强作用存在缺陷，就像纤维蛋白原迪萨尔（Fibrinogen Dusard）那样，这是一种与非常严重的血栓形成性疾病相关的先天性异常纤维蛋白原血症。在其他一些情况下，可能涉及纤维蛋白凝块中纤溶酶裂解位点可用性的降低。相反，一些抗血栓药物，如戊聚糖多硫酸盐，在改变凝块结构时，可使纤维蛋白凝块更好地被纤溶酶降解。据推测，这种增强的纤溶作用几乎可以部分解释这些药物的抗血栓作用。
