Tenascin-X: beyond the architectural function |
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Authors: | Ulrich Valcourt Lindsay B Alcaraz Jean-Yves Exposito Claire Lethias Laurent Bartholin |
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Institution: | 1. Inserm U1052, Centre de Recherche en Cancérologie de Lyon, Lyon, France;2. CNRS UMR 5286, Centre de Recherche en Cancérologie de Lyon, Lyon, France;3. Université de Lyon, Lyon, France;4. Université Lyon 1, Lyon, France;5. Centre Léon Bérard, Lyon, Franceulrich.valcourt@lyon.unicancer.fr;7. Centre Léon Bérard, Lyon, France;8. Institut de Biologie et Chimie des Protéines, FR3302, CNRS UMR 5305, Lyon, France |
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Abstract: | Tenascin-X is the largest member of the tenascin (TN) family of evolutionary conserved extracellular matrix glycoproteins, which also comprises TN-C, TN-R and TN-W. Among this family, TN-X is the only member described so far to exert a crucial architectural function as evidenced by a connective tissue disorder (a recessive form of Ehlers-Danlos syndrome) resulting from a loss-of-function of this glycoprotein in humans and mice. However, TN-X is more than an architectural protein, as it displays features of a matricellular protein by modulating cell adhesion. However, the cellular functions associated with the anti-adhesive properties of TN-X have not yet been revealed. Recent findings indicate that TN-X is also an extracellular regulator of signaling pathways. Indeed, TN-X has been shown to regulate the bioavailability of the Transforming Growth Factor (TGF)-β and to modulate epithelial cell plasticity. The next challenges will be to unravel whether the signaling functions of TN-X are functionally linked to its matricellular properties. |
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Keywords: | cell signaling Ehlers-Danlos syndrome (EDS) epithelial-to-mesenchymal transition (EMT) integrin α11β1 matricellular protein tenascin-X TGF-β activation |
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