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

FEBS Letters

Parkar, Ashfaq A¹  Day, Anthony J¹ 

[1] Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK

关键词: TSG-6;    Link module;    Proteoglycan tandem repeat;    Hyaluronan;    Chondroitin-4-sulphate;    Inflammation;    bA-Link_TSG6;    mono-biotinylated Link_TSG6;    bHA;    biotinylated hyaluronan;    C4S;    chondroitin-4-sulphate;    C6S;    chondroitin-6-sulphate;    DSequiv;    molar disaccharide equivalents;    ESI-MS;    electrospray ionisation mass spectrometry;    GAG;    glycosaminoglycan;    HPLC;    high-performance liquid chromatography;    IL-1;    interleukin-1;    Link_TSG6;    the Link module from TSG-6;    TFA;    trifluoroacetic acid;    TNF;    tumor necrosis factor;    TSG-6;    TNF-stimulated gene-6;   

DOI  :  10.1016/S0014-5793(97)00621-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 with 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.

【 授权许可】

Unknown