PMID: 2116002Aug 1, 1990Paper

Cytologic assessment of nuclear and cytoplasmic O-linked N-acetylglucosamine distribution by using anti-streptococcal monoclonal antibodies

Proceedings of the National Academy of Sciences of the United States of America
J R TurnerN S Greenspan

Abstract

Recent studies have demonstrated the existence of single O-linked N-acetylglucosamine (O-GlcNAc) residues on cytoplasmic and nuclear glycoproteins. Labeled lectin and enzymatic techniques have been used to identify O-GlcNAc-bearing proteins, but no antibodies generally reactive with such O-linked GlcNAc moieties have been described. We have previously characterized monoclonal antibodies (mAbs) specific for the GlcNAc residues of streptococcal group A carbohydrate, which is composed of a polyrhamnose backbone with GlcNAc side chains. We now report that these mAbs recognize O-GlcNAc-bearing proteins. By immunofluorescence, the mAbs reacted strongly with the nuclear periphery and nucleoplasm of mammalian cells and stained the cytoplasm less intensely. The distribution was not consistent with labeling of the endoplasmic reticulum, Golgi complex, or plasma membrane. Furthermore, the staining pattern of a mutant cell line, which retains terminal GlcNAc residues on many N-linked glycans, was indistinguishable from that of wild-type cells. Nuclear and cytoplasmic staining were inhibited by free GlcNAc and were completely abolished by galactosylation of terminal GlcNAc residues. Indirect ELISA demonstrated GlcNAc- and galactosylation-in...Continue Reading

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