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. © 2006 Federation of European Biochemical Societies.
Lethias, C., Carisey, A., Comte, J., Cluzel, C., & Exposito, J. Y. (2006). A model of tenascin-X integration within the collagenous network. FEBS Letters, 580(26), 6281–6285. https://doi.org/10.1016/j.febslet.2006.10.037