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J. Biol. Chem., Vol. 259, Issue 20, 12536-12542, 10, 1984

A murine cytotoxic T lymphocyte cell line resistant to Vicia villosa lectin is deficient in UDP-GalNAc:beta-galactose beta 1,4-N- acetylgalactosaminyltransferase

A Conzelmann and S Kornfeld

We have reported the presence of N-acetylgalactosamine linked beta 1,4 to galactose on O-linked oligosaccharides of a cloned murine cytotoxic T cell line and the absence of these residues from the O-linked structures of a Vicia villosa lectin-resistant mutant line, VV6, derived from parental B6.1.SF.1 cells (Conzelmann, A., and Kornfeld, S. (1984) J. Biol. Chem. 259, 12528-12535). This study shows that B6.1.SF.1 cells contain an enzyme which transfers N-acetylgalactosamine from UDP-GalNAc onto the O-linked tetrasaccharides of human glycophorin A, giving rise to pentasaccharides which contain beta-glycosidically linked N-acetylgalactosamine. Desialylated glycophorin was inactive as an acceptor. The enzyme also transfers N-acetylgalactosamine to the N- linked oligosaccharides of the Tamm-Horsfall glycoprotein. This glycoprotein is known to contain N-linked oligosaccharides with beta- linked N-acetylgalactosamine residues which constitute the Sda blood group determinant. This N-acetylgalactosaminyltransferase could not be detected in VV6 cells which can account for the lack of beta-linked N- acetylgalactosamine residues on its O-linked oligosaccharides. The two cell lines have comparable levels of UDP-GalNAc:apomucin N- acetylgalactosaminyltransferase, demonstrating that the enzyme deficiency in VV6 cells is selective. Both cell lines have a similar glycolipid content, with the major component being asialo-GM1. Since this glycolipid contains N-acetylgalactosamine linked beta 1,4 to galactose, it would appear that the N-acetylgalactosyltransferase involved in the biosynthesis of glycolipids is different from the UDP- GalNAc:glycoprotein N-acetylgalactosaminyltransferase. An independently derived murine CTL line also contains the UDP-GalNAc:glycoprotein N- acetylgalactosaminyltransferase, suggesting that the expression of this enzyme is a common characteristic of this type of cell line.
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