Premium
A model of tenascin‐X integration within the collagenous network
Author(s) -
Lethias Claire,
Carisey Alexandre,
Comte Jane,
Cluzel Caroline,
Exposito Jean-Yves
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.10.037
Subject(s) - tenascin , tenascin c , extracellular matrix , fibril , chemistry , biophysics , extracellular , matrix (chemical analysis) , microbiology and biotechnology , biochemistry , fibronectin , biology , chromatography
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.