Overlapping sites on the Link module of human TSG-6 mediate binding to hyaluronan and chrondroitin-4-sulphate.
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.
Parkar
A A
AA
Department of Biochemistry, University of Oxford, UK.
Day
A J
AJ
D053674:Aggrecans; D001665:Binding Sites; D015815:Cell Adhesion Molecules / Q000378:metabolism*; D002809:Chondroitin Sulfates / Q000378:metabolism*; D016326:Extracellular Matrix Proteins; D006025:Glycosaminoglycans / Q000378:metabolism*; D006493:Heparin / Q000378:metabolism / Q000494:pharmacology; D006801:Humans; D006820:Hyaluronic Acid / Q000378:metabolism*; D037181:Lectins, C-Type; D011509:Proteoglycans / Q000378:metabolism
D053674:Aggrecans; D015815:Cell Adhesion Molecules; D016326:Extracellular Matrix Proteins; D006025:Glycosaminoglycans; D037181:Lectins, C-Type; D011509:Proteoglycans; C072273:TNFAIP6 protein, human; D006820:Hyaluronic Acid; D006493:Heparin; D002809:Chondroitin Sulfates