Binding of tenascin-X to decorin.

Elefteriou F, Exposito JY, Garrone R, Lethias C
FEBS Lett. 2001 495 (1-2): 44-7

PMID: 11322944 · 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.

MeSH Terms (19)

Animals Biglycan Binding, Competitive Binding Sites Blotting, Western Cattle Chondroitin ABC Lyase Collagen Decorin Dose-Response Relationship, Drug Extracellular Matrix Proteins Glycosaminoglycans Heparin Protein Binding Protein Structure, Tertiary Proteoglycans Skin Tenascin Tissue Extracts

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