Procyk R, Blomback B
Plasma Proteins-Coagulation, Lindsley F. Kimball Research Institute, New York Blood Center, NY 10021.
Biochim Biophys Acta. 1988 Nov 17;967(2):304-13. doi: 10.1016/0304-4165(88)90024-4.
In solutions containing fibrinogen and fibronectin, factor XIIIa catalyzes the formation of two types of crosslinked polymers: hybrid oligomers consisting of equimolar amounts of fibrinogen and fibronectin, and fibrinogen oligomers. The two types of oligomers are produced in amounts proportional to the starting concentration of fibronectin and fibrinogen in the reaction mixture. Increasing the fibronectin concentration relative to the fibrinogen concentration results in the production of more hybrid and less fibrinogen type oligomers. The lowest molecular weight hybrid oligomer, a dimer, is formed by ligation of one molecule of fibrinogen and fibronectin. The A alpha-chain of fibrinogen and one fibronectin subunit participate in the crosslinking. Larger size hybrid oligomers form by the joining of two hybrid dimers to each other via gamma-chain dimerization in the fibronectin moiety of the dimers. In fibrinogen oligomer formation, fibrinogen molecules are ligated by gamma-chain dimerization in a step-wise fashion producing fibrinogen dimers, trimers, tetramers, etc. without A alpha-chain crosslinking. The hybrid type and the fibrinogen type of oligomer grow in size and eventually become crosslinked to each other yielding large molecular weight complexes that interact to form a gel network.
在含有纤维蛋白原和纤连蛋白的溶液中,因子ⅩⅢa催化形成两种类型的交联聚合物:由等摩尔量的纤维蛋白原和纤连蛋白组成的杂合寡聚物以及纤维蛋白原寡聚物。这两种寡聚物的生成量与反应混合物中纤连蛋白和纤维蛋白原的起始浓度成正比。相对于纤维蛋白原浓度增加纤连蛋白浓度会导致产生更多的杂合寡聚物和更少的纤维蛋白原型寡聚物。最低分子量的杂合寡聚物,即二聚体,是由一分子纤维蛋白原和一分子纤连蛋白连接形成的。纤维蛋白原的Aα链和一个纤连蛋白亚基参与交联。更大尺寸的杂合寡聚物是由两个杂合二聚体通过二聚体纤连蛋白部分中的γ链二聚化相互连接形成的。在纤维蛋白原寡聚物形成过程中,纤维蛋白原分子通过γ链二聚化逐步连接,产生纤维蛋白原二聚体、三聚体、四聚体等,没有Aα链交联。杂合型和纤维蛋白原型寡聚物尺寸增大,最终相互交联形成高分子量复合物,这些复合物相互作用形成凝胶网络。