Fitzsimmons C M, Cockburn C G, Hornsey V, Prowse C V, Barnes M J
Edinburgh and South-East Scotland Regional Blood Transfusion Service, Royal Infirmary, UK.
Thromb Haemost. 1988 Apr 8;59(2):186-92.
Following fragmentation of the collagen molecule, we have examined the ability of the isolated fragments to bind vWf. In view of the importance of collagen tertiary and quaternary structure for binding, fragments were first renatured to restore triple-helical conformation and then polymerized. Results indicate the presence of specific vWf-binding sites in both the alpha 1(I)- and alpha 2(I)-chains of type I collagen. Cleavage of the alpha 1(I)-chain with cyanogen bromide suggests the presence of at least four (conceivably several more) binding sites implying a wide distribution of sites along the length of the collagen type I molecule. Collagen type III appears to possess a similar wide distribution of sites. Chemical modification of specific amino acid residues indicates that interaction involves arginyl residues in collagen and carboxyl groups in vWf. Although interaction between fibronectin and collagen fibres also involves collagen arginyl residues and carboxyl groups in fibronectin (authors' unpublished results), fibronectin does not compete with vWf in the binding to collagen fibres.
在胶原蛋白分子片段化之后，我们检测了分离出的片段结合血管性血友病因子（vWf）的能力。鉴于胶原蛋白三级和四级结构对于结合的重要性，首先使片段复性以恢复三螺旋构象，然后使其聚合。结果表明在I型胶原蛋白的α1（I）链和α2（I）链中均存在特定的vWf结合位点。用溴化氰切割α1（I）链表明至少存在四个（可能还有更多）结合位点，这意味着这些位点沿I型胶原蛋白分子的长度广泛分布。III型胶原蛋白似乎也具有类似的广泛分布的位点。对特定氨基酸残基的化学修饰表明，相互作用涉及胶原蛋白中的精氨酰残基和vWf中的羧基。尽管纤连蛋白与胶原纤维之间的相互作用也涉及胶原蛋白中的精氨酰残基和纤连蛋白中的羧基（作者未发表的结果），但纤连蛋白在与胶原纤维的结合中并不与vWf竞争。
