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High affinity binding of the leucocyte adhesion molecule L-selectin to 3'-sulphated Le-a and -Le-X oligosaccharides and the predominance of sulphate in this interaction demonstrated by binding studies with a series of lipid-linked oligosaccharides



High affinity binding of the leucocyte adhesion molecule L-selectin to 3'-sulphated Le-a and -Le-X oligosaccharides and the predominance of sulphate in this interaction demonstrated by binding studies with a series of lipid-linked oligosaccharides



Biochemical and Biophysical Research Communications 188(1): 244-251



The binding of the leucocyte adhesion molecule -selectin has been investigated toward several structurally defined lipid-linked oligosaccharides immobilized on silica gel chromatograms or plastic wells. In both assay system the 3'-sulphated Le-1/Le-x type tetrasaccharides were more strongly bound than 3'-sialyl analogues. A considerable binding was observed to the 3'-sulphated oligosaccharide backbone in the absence of fucose but not a 3'-sialyl analogue of fuco-oligosaccharide analogues lacking sulphate or sialic acid. Affinity for other sulphated saccharides: 3'-sulphoglucuronyl neolactotetraosyl ceramide and glycolipids with sulphate 3'-linked to terminal or sub-terminal galactose or N-acetylgalactosamine was detected in the chromatogram assay only. These studies, together with earlier reports that L-selectin binding to endothelium is inhibited by sulphatide, highlight the relative importance of sulphate in the adhesive specificity of this protein.

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Accession: 008770405

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PMID: 1384480


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