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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Biglycan
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Binding Sites / drug effects
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Binding Sites / physiology
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Binding, Competitive / drug effects
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Blotting, Western
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Cattle
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Chondroitin ABC Lyase / metabolism
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Collagen / metabolism
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Decorin
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Dose-Response Relationship, Drug
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Extracellular Matrix Proteins
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Glycosaminoglycans / metabolism
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Glycosaminoglycans / pharmacology
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Heparin / metabolism
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Protein Binding / drug effects
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Protein Binding / physiology
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Protein Structure, Tertiary / physiology
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Proteoglycans / metabolism*
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Proteoglycans / pharmacology
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Skin / chemistry
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Skin / embryology
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Tenascin / chemistry*
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Tenascin / metabolism*
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Tissue Extracts / chemistry
Substances
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Biglycan
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Decorin
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Extracellular Matrix Proteins
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Glycosaminoglycans
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Proteoglycans
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Tenascin
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Tissue Extracts
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tenascin X
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Heparin
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Collagen
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Chondroitin ABC Lyase