A model of tenascin-X integration within the collagenous network |
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Authors: | Lethias Claire Carisey Alexandre Comte Jane Cluzel Caroline Exposito Jean-Yves |
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Affiliation: | 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. c.lethias@ibcp.fr |
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Abstract: | 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. |
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Keywords: | Extracellular matrix Ehlers-Danlos syndrome Tenascin-X Collagen |
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