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Glycobiology vol 3 no 6 pp. 633-641, 1993
© 1993

research-article

Structure—function studies on selectin carbohydrate ligands. Modifications to fucose, sialic acid and sulphate as a sialic acid replacement

Brian K. Brandley, Makoto Kiso2, Saeed Abbas, Pandarung Nikrad1, Om Srivasatava1, Carrol Foxall, Yuko Oda and Akira Hasegawa2

Glycomed, Inc., 860 Atlantic Avenue Alameda, CA 94501, USA
1Alberta Research Council, Edmonton, Alberta T6H 5X2, Canada
2Department of Bioorganic Chemistry, Gifu University Gifu, 501-11, Japan

The selectins are a family of carbohydrate-binding proteins that have been implicated in the initial interaction between leukocytes and the vascular endothelium. The three members of this family will bind to the sialyl-Lewisx epitope [Sia {alpha}2–3 Gal ß1–4 (Fuc {alpha}1–3) GlcNAc] and related oligosaccharides. In this report, we examine the molecular details of that recognition using synthesized carbohydrates with specific modifications on the sialyl-Lewisx epitope. E- and L-Selectin require hydroxyl groups at the 2, 3 and 4 positions of the fucose residue. P-Selectin, however, requires only the 3-position hydroxyl group, while tolerating removal of the oxygen at positions 2 or 4 of fucose residue. Modifications of the glycerol side chain or the N-acetyl group of the sialic acid have little effect on the binding of any of the selectins. All three selectins bind efficiently to an oligosaccharide with a sulphate replacement for the sialic acid [sulpho-Lewisx, or SO4-3Gal ß1–4 (Fuc {alpha}1–3) Glc-cer-amide]. For E-Selectin, binding to sulpho-Lewisx appears to be equivalent to binding to sialyl-Lewisx, while for L-and P-Selectin binding to the sulphated structure shows characteristics distinct from sialyl-Lewisx recognition. Taken together, these data indicate that, while all three selectins can recognize sialyl-Lewisx, E-, L- and P-Selectin each display distinct carbohydrate ligand preferences.

adhesion glycolipid inflammation lectin selectin


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