Csanaky G, Vass JA L-selectins revealed by immobilized analgue molecules on human peripheral blood lymphocytes Acta Biologica Hungarica44 (1993)
161-166
NCBI PubMed ID:7514330 Journal NLM ID:8404358 Publisher: Budapest : Akademiai Kiado Institutions: Department of Pathology, University Medical School, Pécs, Hungary
The lymphocyte-endothelial interaction is initiated by selection type adhesion molecules on the surface of the lymphocytes (L-selectins) and by their carbohydrate ligands (addressins) in the glycocalyx of the endothelial cells. Under experimental conditions they can be substituted by analogue sugars, such as polyphosphonomonoester core polysaccharide and fucoidin. In this study, the expression of phosphomannosyl and fucoidin receptors is demonstrated on lymphocytes from human peripheral blood by polyacrylamide immobilized analogues. Based on adhesion and sugar inhibitory experiments, authors suggest that lineage and probably species specific differences exist in the expression and activity of the selectins responsible for binding of the two analogue molecules.
Related record ID(s): 105606, 107859 NCBI Taxonomy refs (TaxIDs):36025 Reference(s) to other database(s): GTC:G62939PF, CCSD:43769, CBank-STR:13598 Show glycosyltransferases
There are 3 chemically distinct structures. Please, select:
Green PJ, Tamatani T, Watanabe T, Miyasaka M, Hasegawa A, Kiso M, Yuen CT, Stoll MS, Feizi T High affinity binding of the leucocyte adhesion molecule L-selectin to 3'-sulphated-Lea and -Lex oligosaccharides and the predominance of sulphate in this interaction demonstrated by binding studies with a series of lipid-linked oligosaccharides Biochemical and Biophysical Research Communications188 (1992)
244-251
NCBI PubMed ID:1384480 Journal NLM ID:0372516 Publisher: Academic Press Institutions: Glycoconjugates Section, MRC Clinical Research Centre, Harrow, Middlesex, U.K
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.
Related record ID(s): 100059, 107859 NCBI Taxonomy refs (TaxIDs):36025 Reference(s) to other database(s): GTC:G62939PF, CCSD:43769, CBank-STR:13598 Show glycosyltransferases
There are 3 chemically distinct structures. Please, select:
Yuen CT, Lawson AM, Chai W, Larkin M, Stoll MS, Stuart AC, Sullivan FX, Ahern TJ, Feizi T Novel sulfated ligands for the cell adhesion molecule E-selectin revealed by the neoglycolipid technology among O-linked oligosaccharides on an ovarian cystadenoma glycoprotein Biochemistry31 (1992)
9126-9131
NCBI PubMed ID:1382586 Journal NLM ID:0370623 Publisher: American Chemical Society Institutions: Glycoconjugates Section, MRC Clinical Research Centre, Harrow, Middlesex, U.K
E-selectin is the inducible adhesion protein on the surface of endothelial cells which has a crucial role in the initial stages of recruitment of leucocytes to sites of inflammation. In addition, it is almost certainly involved in tumor cell adhesion and metastasis. This report is concerned with identification of a new class of oligosaccharide ligand--sulfate-containing--for the human E-selectin molecule from among oligosaccharides on an ovarian cystadenoma glycoprotein. This has been achieved by application of the neoglycolipid technology to oligosaccharides released from the glycoprotein by mild alkaline beta-elimination. Oligosaccharides were conjugated to lipid, resolved by thin-layer chromatography, and tested for binding by Chinese hamster ovary cells which had been transfected to express the full-length E-selectin molecule. Several components with strong E-selectin binding activity were revealed among acidic oligosaccharides. The smallest among these was identified by liquid secondary ion mass spectrometric analysis of the neoglycolipid, in conjunction with methylation analysis of the purified oligosaccharide preparation as an equimolar mixture of the Le(a)- and Le(x)/SSEA-1-type fucotetrasaccharides sulfated at position 3 of outer galactose: [formula: see text] To our knowledge this is the first report of a sulfofucooligosaccharide ligand for E-selectin. The binding activity is substantially greater than those of lipid-linked Le(a) and Le(x)/SSEA-1 sequences and is at least equal to that of the 3'-sialyl-Le(x)/SSEA-1 glycolipid analogue.
Related record ID(s): 100059, 105606 NCBI Taxonomy refs (TaxIDs):36025 Reference(s) to other database(s): GTC:G62939PF, CCSD:43769, CBank-STR:13598 Show glycosyltransferases
There are 3 chemically distinct structures. Please, select:
Found 
report error
(later renamed to: Nakazawaea holstii; Pichia holstii)