Marchi R, Lundberg U, Grimbergen J, Koopman J, Torres A, de Bosch N B, Haverkate F, Arocha Piñango C L
Centro de Medicina Experimental, Laboratorio de Fisiopatología, Instituto Venezolano de Investigaciones Cientificas, IVIC, Caracas, Venezuela.
Thromb Haemost. 2000 Aug;84(2):263-70.
A new dysfibrinogenemia associated with thrombophilia has been identified in a Venezuelan kindred. Thrombin and Reptilase times were prolonged and the accelerating capacity of the patient's fibrin on the t-PA-induced plasminogen activation was decreased. In addition the affinity of fibrinogen for plasminogen was diminished. Permeability and electron microscopy studies revealed that the abnormal clot was made up of thin and densely packed fibres giving rise to a reduced fibrin gel porosity. This was confirmed by turbidity studies showing a decreased fibre mass/length ratio. Affected members were heterozygous for an Aalpha 532 Ser-->Cys mutation as demonstrated by genetic analyses. This abnormal fibrinogen has been designated as Fibrinogen Caracas V. The family study showed a convincing association between the mutation and thrombotic manifestations. The thrombotic tendency may be ascribed to lack of accelerating capacity of fibrin to induce fibrinolysis caused by an abnormal clot structure with thin fibres and reduced porosity.
在一个委内瑞拉家族中发现了一种与血栓形成倾向相关的新型异常纤维蛋白原血症。凝血酶时间和蛇毒凝血酶时间延长，患者纤维蛋白对组织型纤溶酶原激活物诱导的纤溶酶原激活的加速能力降低。此外，纤维蛋白原对纤溶酶原的亲和力减弱。通透性和电子显微镜研究显示，异常凝块由细而密集排列的纤维组成，导致纤维蛋白凝胶孔隙率降低。浊度研究证实了这一点，表明纤维质量/长度比降低。基因分析表明，受影响成员为Aα532 Ser→Cys突变的杂合子。这种异常纤维蛋白原被命名为纤维蛋白原加拉加斯V型。家族研究显示该突变与血栓形成表现之间存在令人信服的关联。血栓形成倾向可能归因于纤维蛋白诱导纤溶的加速能力缺乏，这是由具有细纤维和降低孔隙率的异常凝块结构引起的。
