Elefteriou F, Exposito J Y, Garrone R, Lethias C
Institut de Biologie et Chimie des Protéines, CNRS UMR 5086, Université Claude Bernard, 7 passage du Vercors, 69367 Cedex 07, Lyon, France.
FEBS Lett. 2001 Apr 20;495(1-2):44-7. doi: 10.1016/s0014-5793(01)02361-4.
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.
