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PMID: 6436236 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

The Journal of biological chemistry ·Vol. 259 ·No. 20 ·1984-10-25 ·Pages 12536-42

Conzelmann A, Kornfeld S

Abstract

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.

MeSH Terms
Animals Cell Line Drug Resistance Galactosyltransferases/deficiency,isolation & purification,metabolism Kinetics Lectins/pharmacology Mice N-Acetylgalactosaminyltransferases Plant Lectins Substrate Specificity T-Lymphocytes, Cytotoxic/enzymology,immunology
Chemicals
Lectins Plant Lectins Vicia lectins Galactosyltransferases N-Acetylgalactosaminyltransferases polypeptide N-acetylgalactosaminyltransferase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Conzelmann A
Kornfeld S
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1984-10-25
Pages
12536-42
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIGMS NIH HHS · 5T05GM02016 · United States
NCI NIH HHS · R01 CA 08759 · United States
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