ArticleThe Journal of cell biology1998
GalNAc-alpha-O-benzyl inhibits NeuAcalpha2-3 glycosylation and blocks the intracellular transport of apical glycoproteins and mucus in differentiated HT-29 cells.
Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 99 citations in OpenAlex.
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- Bidirectional signals generated by Siglec-7 and its crucial ligand tri-sialylated T to escape of cancer cells from immune surveillance.iScience · 2024Article
- Identification of potential classes of glycoligands mediating dynamic endothelial adhesion of human tumor cells.Glycobiology · 2023Article
- Review
- Activation of the UPR sensor ATF6α is regulated by its redox-dependent dimerization and ER retention by ERp18.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Efficient inhibition of O-glycan biosynthesis using the hexosamine analog AcCell chemical biology · 2021Article
- Systematic analysis of the human tumor cell binding to human vs. murine E- and P-selectin under static vs. dynamic conditions.Glycobiology · 2020Article
- Article
- Thioglycosides Are Efficient Metabolic Decoys of Glycosylation that Reduce Selectin Dependent Leukocyte Adhesion.Cell chemical biology · 2018Article
- Sialylation regulates myofibroblast differentiation of human skin fibroblasts.Stem cell research & therapy · 2017Article
- Benzyl-2-Acetamido-2-Deoxy-α-d-Galactopyranoside Increases Human Immunodeficiency Virus Replication and Viral Outgrowth EfficacyFrontiers in immunology · 2017Article
- Simultaneous analyses of N-linked and O-linked glycans of ovarian cancer cells using solid-phase chemoenzymatic method.Clinical proteomics · 2017Article
- Core 2 Mucin-Type O-Glycan Is Related to EPEC and EHEC O157:H7 Adherence to Human Colon Carcinoma HT-29 Epithelial Cells.Digestive diseases and sciences · 2015Article
- Trafficking to the apical and basolateral membranes in polarized epithelial cells.Journal of the American Society of Nephrology : JASN · 2014Review
- Article
- Sialylation of N-linked glycans mediates apical delivery of endolyn in MDCK cells via a galectin-9-dependent mechanism.Molecular biology of the cell · 2012Article
- Core-glycosylated mucin-like repeats from MUC1 are an apical targeting signal.The Journal of biological chemistry · 2011Article
- Regulation of sialyl Lewis antigen expression in colon cancer cells by sialidase NEU4.The Journal of biological chemistry · 2011Article
- Dissecting the biological role of mucin-type O-glycosylation using RNA interference in Drosophila cell culture.The Journal of biological chemistry · 2010Article
- Steric shielding of surface epitopes and impaired immune recognition induced by the ebola virus glycoprotein.PLoS pathogens · 2010Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Exposure for 24 h of mucus-secreting HT-29 cells to the sugar analogue GalNAc-alpha-O-benzyl results in inhibition of Galbeta1-3GalNAc:alpha2,3-sialyltransferase, reduced mucin sialylation, and inhibition of their secretion (Huet, G., I. Kim, C. de Bolos, J.M. Loguidice, O. Moreau, B. Hémon, C. Richet, P. Delannoy, F.X. Real., and P. Degand. 1995. J. Cell Sci. 108:1275-1285). To determine the effects of prolonged inhibition of sialylation, differentiated HT-29 populations were grown under permanent exposure to GalNAc-alpha-O-benzyl. This results in not only inhibition of mucus secretion, but also in a dramatic swelling of the cells and the accumulation in intracytoplasmic vesicles of brush border-associated glycoproteins like dipeptidylpeptidase-IV, the mucin-like glycoprotein MUC1, and carcinoembryonic antigen which are no longer expressed at the apical membrane. The block occurs beyond the cis-Golgi as substantiated by endoglycosidase treatment and biosynthesis analysis. In contrast, the polarized expression of the basolateral glycoprotein GP 120 is not modified. Underlying these effects we found that (a) like in mucins, NeuAcalpha2-3Gal-R is expressed in the terminal position of the oligosaccharide species associated with the apical, but not the basolateral glycoproteins of the cells, and (b) treatment with GalNAc-alpha-O-benzyl results in an impairment of their sialylation. These effects are reversible upon removal of the drug. It is suggested that alpha2-3 sialylation is involved in apical targeting of brush border membrane glycoproteins and mucus secretion in HT-29 cells.
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