期刊
FEBS LETTERS
卷 580, 期 26, 页码 6281-6285出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2006.10.037
关键词
extracellular matrix; Ehlers-Danlos syndrome; tenascin-X; collagen
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.
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