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Volume 271, Number 44, Issue of November 1, 1996 pp. 27213-27216
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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6-Sulfo Sialyl Le^x but Not 6-Sulfo Sialyl Le^x Expressed on the Cell Surface Supports L-selectin-mediated Adhesion

(Received for publication, July 25, 1996, and in revised form, August 15, 1996)

From the Glycobiology Program, La Jolla Cancer Research Center, The Burnham Institute, La Jolla, California 92037 and the ^§ Department of Chemistry, University of Alberta, Edmonton, Alberta, Canada T6G 2G2

In order to determine if a sulfated oligosaccharide on the cell surface can function as an L-selectin ligand, a novel approach for in vitro transfer of oligosaccharides was utilized (Srivastava, G., Kaun, K. J., Hindsgaul, O., and Palcic, M. M. (1992) J. Biol. Chem. 267, 22356-22361). CHO cells were incubated with synthetic 6-sulfo sialyl Le^x, NeuNAc23(sulfate-6)Gal14(Fuc13)GlcNAc or 6-sulfo sialyl Le^x, NeuNAc23Gal14[(Fuc13)sulfate6GlcNAc] oligosaccharide linked to C-6 of a fucose residue in GDP-fucose and a milk fucosyltransferase. The resultant CHO cells expressing 6-sulfo sialyl Le^x or 6-sulfo sialyl Le^x on their cell surface were tested for adhesion to E-selectin and L-selectin chimeric proteins coated on plates. The results indicate that 6-sulfo sialyl Le^x supports L-selectin-mediated adhesion much better than sialyl Le^x similarly tagged on the cell surface. In contrast, 6-sulfo sialyl Le^x containing a sulfate group on the N-acetylglucosamine residue did not support adhesion with either selectin. These combined results suggest that 6-sulfo sialyl Le^x is a much better ligand than sialyl Le^x oligosaccharide for L-selectin.

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