Lethias Claire, Carisey Alexandre, Comte Jane, Cluzel Caroline, Exposito Jean-Yves
Institut de Biologie et Chimie des Protéines, IFR 128 Biosciences Lyon-Gerland, CNRS UMR 5086, Université de Lyon, 7 Passage du Vercors, 69367 Lyon Cedex 07, France.
FEBS Lett. 2006 Nov 13;580(26):6281-5. doi: 10.1016/j.febslet.2006.10.037. Epub 2006 Oct 26.
Tenascin-X is an extracellular matrix protein whose absence leads to an Ehlers-Danlos syndrome in humans, characterized mainly by disorganisation of collagen and elastic fibril networks. After producing recombinant full-length tenascin-X in mammalian cells, we find that this protein assembled into disulfide-linked oligomers. Trimers were the predominant form observed using rotary shadowing. By solid phase interaction studies, we demonstrate that tenascin-X interacts with types I, III and V fibrillar collagen molecules when they are in native conformation. The use of tenascin-X variants with large regions deleted indicated that both epidermal growth factor repeats and the fibrinogen-like domain are involved in this interaction. Moreover, we demonstrate that tenascin-X binds to the fibril-associated types XII and XIV collagens. We thus suggest that tenascin-X, via trimerization and multiple interactions with components of collagenous fibrils, plays a crucial role in the organisation of extracellular matrices.
腱生蛋白-X是一种细胞外基质蛋白，其缺失会导致人类患埃勒斯-当洛综合征，主要特征为胶原蛋白和弹性纤维网络紊乱。在哺乳动物细胞中生产重组全长腱生蛋白-X后，我们发现该蛋白组装成二硫键连接的寡聚体。使用旋转阴影法观察到三聚体是主要形式。通过固相相互作用研究，我们证明腱生蛋白-X在I型、III型和V型纤维状胶原分子处于天然构象时与之相互作用。使用缺失大片段的腱生蛋白-X变体表明，表皮生长因子重复序列和纤维蛋白原样结构域都参与了这种相互作用。此外，我们证明腱生蛋白-X与纤维相关的XII型和XIV型胶原结合。因此，我们认为腱生蛋白-X通过三聚化以及与胶原纤维成分的多重相互作用，在细胞外基质的组织中起关键作用。
