Binding of tenascin-X to decorin

被引:83
作者
Elefteriou, F [1 ]
Exposito, JY [1 ]
Garrone, R [1 ]
Lethias, C [1 ]
机构
[1] Univ Lyon 1, CNRS UMR 5086, Inst Biol & Chim Prot, F-69367 Lyon 07, France
关键词
extracellular matrix; Ehlers-Danlos syndrome; proteoglycan; tenascin-X;
D O I
10.1016/S0014-5793(01)02361-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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,vith TN-X was identified by this method and this interaction was abolished when the extract was digested by chondroitinase. BS solid-phase assays,,ve 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 bg decorin and contributes to the integrity of the extracellular network, (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:44 / 47
页数:4
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