Greenberg C S, Miraglia C C
Blood. 1985 Aug;66(2):466-9.
The effect of fibrin polymers on thrombin-catalyzed factor XIIIa formation was studied in afibrinogenemic plasma. Fibrin polymers derived from des A fibrinogen and des A,B fibrinogen increased sixfold the rate of thrombin-catalyzed factor XIIIa formation in the presence of EDTA. Calcium chloride accelerated factor XIIIa formation 14-fold in the presence of des A,B fibrinogen without increasing the rate of thrombin formation. Fibrinopeptides A and B had no effect on factor XIIIa formation in afibrinogenemic plasma. Des A,B fibrinogen reduced by 20- to 40-fold the thrombin concentration required to activate factor XIII. Glycyl-L-prolyl-L-arginyl-L-proline (gly-pro-arg-pro), a fibrin polymerization inhibitor, inhibited des A and des A,B fibrinogen from enhancing thrombin-catalyzed factor XIIIa formation. Gly-pro-arg-pro did not modify factor XIIIa formation in afibrinogenemic plasma and did not inhibit thrombin cleavage of the chromogenic substrate S-2238. These results demonstrate that fibrin polymers accelerate thrombin-catalyzed plasma factor XIIIa formation.
在无纤维蛋白原血浆中研究了纤维蛋白聚合物对凝血酶催化因子XIIIa形成的影响。在存在乙二胺四乙酸(EDTA)的情况下,源自去A纤维蛋白原和去A、B纤维蛋白原的纤维蛋白聚合物使凝血酶催化因子XIIIa形成的速率提高了六倍。在存在去A、B纤维蛋白原的情况下,氯化钙使因子XIIIa形成加速了14倍,而不增加凝血酶形成的速率。纤维蛋白肽A和B对无纤维蛋白原血浆中因子XIIIa的形成没有影响。去A、B纤维蛋白原将激活因子XIII所需的凝血酶浓度降低了20至40倍。甘氨酰-L-脯氨酰-L-精氨酰-L-脯氨酸(gly-pro-arg-pro),一种纤维蛋白聚合抑制剂,抑制去A和去A、B纤维蛋白原增强凝血酶催化因子XIIIa的形成。Gly-pro-arg-pro不改变无纤维蛋白原血浆中因子XIIIa的形成,也不抑制凝血酶对发色底物S-2238的裂解。这些结果表明,纤维蛋白聚合物加速凝血酶催化的血浆因子XIIIa的形成。