Rasche H
Klin Wochenschr. 1975 Dec 15;53(24):1137-45. doi: 10.1007/BF01476453.
Coagulation factor XIII (fibrin stabilizing factor, FSF) is detectable in plasma, platelets, placenta and various tissues. In the activated form FSF has the enzymatic properties of a transglutaminase and is capable of stabilizing fibrin by inducing covalent bondings between fibrin monomers. In patients with congenital factor XIII deficiency or acquired immune inhibitors of fibrin stabilization a severe bleeding tendency is evident. There is not yet enough information available concerning the significance of reduced FSF-activity as cofactor in hemorrhagic diathesis and wound healing disturbances in various disease states. There are some indications from experimental studies that there might be an influence of FSF on tumor growth and metastasis as well as arteriosclerosis. The quantitation of the enzyme by radiological and immunological techniques yield reproducible results. Fibrin in its stabilized or non stabilized form can be discriminated in polyacrylamide gel electrophoresis after reduction of fibrin clots.
凝血因子 XIII(纤维蛋白稳定因子,FSF)可在血浆、血小板、胎盘及多种组织中检测到。活化形式的 FSF 具有转谷氨酰胺酶的酶学特性,能够通过诱导纤维蛋白单体之间形成共价键来稳定纤维蛋白。在先天性因子 XIII 缺乏症患者或获得性纤维蛋白稳定免疫抑制剂患者中,严重的出血倾向很明显。关于在各种疾病状态下,FSF 活性降低作为出血素质和伤口愈合障碍辅助因子的意义,目前尚无足够信息。实验研究有一些迹象表明,FSF 可能对肿瘤生长、转移以及动脉硬化有影响。通过放射学和免疫学技术对该酶进行定量可得到可重复的结果。在还原纤维蛋白凝块后,可在聚丙烯酰胺凝胶电泳中区分稳定或未稳定形式的纤维蛋白。