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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.

Abstract：

:The binding of the leucocyte adhesion molecule L-selectin has been investigated toward several structurally defined lipid-linked oligosaccharides immobilized on silica gel chromatograms or plastic wells. In both assay systems the 3'-sulphated Le(a)/Le(x) type tetrasaccharides [formula: see text] 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 to a 3'-sialyl analogue or 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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Green PJ,Tamatani T,Watanabe T,Miyasaka M,Hasegawa A,Kiso M,Yuen CT,Stoll MS,Feizi T

doi

10.1016/0006-291x(92)92376-9

subject

Has Abstract

pub_date

1992-10-15 00:00:00

pages

244-51

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(92)92376-9

journal_volume

188

pub_type

杂志文章

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