A model of tenascin-X integration within the collagenous network
A model of tenascin-X integration within the collagenous network
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DOI：
10.1016/j.febslet.2006.10.037
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发表时间：
2006-11-13
期刊：
影响因子：
3.5
通讯作者：
Exposito, Jean-Yves
中科院分区：
文献类型：
--
作者：
Lethias, Claire;Carisey, Alexandre;Exposito, Jean-Yves
Tenascin-X 是一种细胞外基质蛋白，其缺失会导致人类出现 Ehlers-Danlos 综合征，其主要特征是胶原蛋白和弹性原纤维网络的解体。在哺乳动物细胞中产生重组全长生腱蛋白-X后，我们发现该蛋白质组装成二硫键连接的寡聚体。三聚体是使用旋转阴影观察到的主要形式。通过固相相互作用研究，我们证明生腱蛋白-X 与处于天然构象的 1、III 和 V 型纤维胶原分子相互作用。使用删除大区域的生腱蛋白-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，我们证明生腱蛋白-X 与原纤维相关的 XII 型和 XIV 型胶原蛋白结合。因此，我们认为生腱蛋白-X 通过三聚化和与胶原原纤维成分的多重相互作用，在细胞外基质的组织中发挥着至关重要的作用。 (c) 2006 年欧洲生化学会联合会。由 Elsevier B.V. 出版。保留所有权利。
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 1, 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. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.