Binding of tenascin-X to decorin
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Updated: Oct 8, 2026

A Protocol to Acquire the Degenerative Tenocyte from Humans
Published on: June 9, 2018
F Elefteriou1, J Y Exposito, R Garrone
1Institut de Biologie et Chimie des Protéines, CNRS UMR 5086, Université Claude Bernard, 7 passage du Vercors, 69367 Cedex 07, Lyon, France.
Abstract:
Tenascin-X (TN-X) is an extracellular matrix protein whose absence results in an alteration of the mechanical properties of connective tissue. To understand the mechanisms of integration of TN-X in the extracellular matrix, overlay blot assays were performed on skin extracts. A 100 kDa molecule interacting with TN-X was identified by this method and this interaction was abolished when the extract was digested by chondroitinase. By solid-phase assays, we showed that dermatan sulfate chains of decorin bind to the heparin-binding site included within the fibronectin-type III domains 10 and 11 of TN-X. We thus postulate that the association of TN-X with collagen fibrils is mediated by decorin and contributes to the integrity of the extracellular network.
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