부산대학교 도서관

In order to determine if a sulfated oligosaccharide on the cell surface can function as an L-selectin ligand, a novel approach for in vitrotransfer 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 Lex, NeuNAcα2→3(sulfate-6)Galβ1→4(Fucα1→3)GlcNAc or 6-sulfo sialyl Lex, NeuNAcα2→3Galβ1→4[(Fucα1→3)sulfate→6GlcNAc] oligosaccharide linked to C-6 of a fucose residue in GDP-fucose and a milk fucosyltransferase. The resultant CHO cells expressing 6′-sulfo sialyl Lexor 6-sulfo sialyl Lexon 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 Lexsupports L-selectin-mediated adhesion much better than sialyl Lexsimilarly tagged on the cell surface. In contrast, 6-sulfo sialyl Lexcontaining a sulfate group on the N-acetylglucosamine residue did not support adhesion with either selectin. These combined results suggest that 6′-sulfo sialyl Lexis a much better ligand than sialyl Lexoligosaccharide for L-selectin.