Overlapping sites on the Link module of human TSG-6 mediate binding to hyaluronan and chondroitin-4-sulphate

被引:68
作者
Parkar, AA [1 ]
Day, AJ [1 ]
机构
[1] UNIV OXFORD,DEPT BIOCHEM,OXFORD OX1 3QU,ENGLAND
关键词
TSG-6; Link module; proteoglycan tandem repeat; hyaluronan; chondroitin-4-sulphate; inflammation;
D O I
10.1016/S0014-5793(97)00621-2
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
Link modules are hyaluronan-binding domains that are involved in the formation and stability of extracellular matrix and cell migration. We have examined the glycosaminoglycan specificity of the Link module from the arthritis-associated protein, human TSG-6, by microtitre plate-based assays employing biotinylated-hyaluronan or mono-biotinylated Link module. This domain was found to interact specifically,vith chondroitin-4-sulphate (C4S), with similar affinity to hyaluronan, but not with chondroitin-6-sulphate or heparin. Competition experiments indicate that C4S and hyaluronan have overlapping binding surfaces on the TSG-6 Link module. Disease-associated changes in C4S expression may influence the localisation and biological role of TSG-6. (C) 1997 Federation of European Biochemical Societies.
引用
收藏
页码:413 / 417
页数:5
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