Usui T, Takagi J, Saito Y
Department of Biological Sciences, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Japan.
J Biol Chem. 1993 Jun 15;268(17):12311-6.
The propolypeptide of von Willebrand factor (pp-vWF) was found to serve as a substrate for Factor XIIIa (FXIIIa). FXIIIa catalyzed polymerization of pp-vWF as well as the incorporation of monodansylcadaverine and [14C]putrescine into pp-vWF in a Ca(2+)- and time-dependent manner. The amount of putrescine incorporated into pp-vWF was increased as a function of putrescine concentration and reached a maximum of 3 mol/mol of pp-vWF, indicating that there are at least 3 glutamine residues in the pp-vWF molecule responsible for the reaction. 125I-pp-vWF was incubated with FXIIIa in the presence of various adhesive glycoproteins. Laminin, among the proteins tested, specifically formed a large molecular weight complex with 125I-pp-vWF in a Ca(2+)- and time-dependent manner. It was also found that FXIIIa catalyzed polymerization of laminin as well as the incorporation of monodansylca-daverine into laminin. The high molecular weight complexes of 125I-pp-vWF (or 125I-laminin) formed in the presence of laminin (or pp-vWF) were immunoprecipitated with anti-laminin (or anti-pp-vWF) antibodies. Taking all the data together it can be concluded that both pp-vWF and laminin have glutamine and lysine residues responsive to FXIIIa and make copolymers by virtue of FXIIIa.
发现血管性血友病因子前体多肽（pp-vWF）是因子XIIIa（FXIIIa）的底物。FXIIIa以Ca(2+)和时间依赖性方式催化pp-vWF的聚合以及单丹磺酰尸胺和[14C]腐胺掺入pp-vWF。掺入pp-vWF的腐胺量随腐胺浓度增加而增加，最高达到每摩尔pp-vWF 3摩尔，这表明pp-vWF分子中至少有3个谷氨酰胺残基参与该反应。将125I-pp-vWF与FXIIIa在各种黏附糖蛋白存在下孵育。在所测试的蛋白质中，层粘连蛋白以Ca(2+)和时间依赖性方式与125I-pp-vWF特异性形成高分子量复合物。还发现FXIIIa催化层粘连蛋白的聚合以及单丹磺酰尸胺掺入层粘连蛋白。在层粘连蛋白（或pp-vWF）存在下形成的125I-pp-vWF（或125I-层粘连蛋白）的高分子量复合物用抗层粘连蛋白（或抗pp-vWF）抗体进行免疫沉淀。综合所有数据可以得出结论，pp-vWF和层粘连蛋白都具有对FXIIIa有反应的谷氨酰胺和赖氨酸残基，并借助FXIIIa形成共聚物。
