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
Green, P.J.; Tamatani, T.; Watanabe, T.; Miyasaka, M.; Hasegawa, A.; Kiso, M.; Yuen, C.T.; Stoll, M.S.; Feizi, T.
Biochemical and Biophysical Research Communications 188(1): 244-251
1992
ISSN/ISBN: 0006-291X PMID: 1384480 Document Number: 395056
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.