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Detailed O-glycomics of the Muc2 mucin from colon of wild-type, core 1- and core 3-transferase-deficient mice highlights differences compared with human MUC2.

Journal article
Authors Kristina A Thomsson
Jessica Holmén
Jonas Ångström
Malin E V Johansson
Lijun Xia
Gunnar C. Hansson
Published in Glycobiology
Volume 22
Issue 8
Pages 1128-39
ISSN 1460-2423
Publication year 2012
Published at Institute of Biomedicine
Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 1128-39
Language en
Keywords Amino Sugars, metabolism, Animals, Carbohydrate Sequence, Chromatography, Liquid, Colon, metabolism, Epitopes, Galactosyltransferases, physiology, Glycomics, Glycosylation, Humans, Intestinal Mucosa, cytology, metabolism, microbiology, Magnetic Resonance Spectroscopy, Metagenome, Mice, Mice, Inbred C57BL, Mice, Knockout, Molecular Sequence Data, Mucin-2, metabolism, N-Acetylglucosaminyltransferases, physiology, Polysaccharides, metabolism, Spectrometry, Mass, Electrospray Ionization
Subject categories Basic Medicine, Cell and Molecular Biology


The heavily O-glycosylated mucin MUC2 constitutes the major protein in the mucosal layer that acts as a physical barrier protecting the epithelial layer in the colon. In this study, Muc2 was purified from mucosal scrapings from the colon of wild-type (WT) mice, core 3 transferase knockout (C3Gnt(-/-)) mice and intestinal epithelial cell-specific core 1 knockout (IEC C1Galt1(-/-)) mice. The Muc2 O-glycans were released by reductive β-elimination and analyzed with liquid chromatography-mass spectrometry in the negative-ion mode. Muc2 from the distal colon of WT and C3Gnt(-/-) knockout mice carried a mixture of core 1- or core 2-type glycans, whereas Muc2 from IEC C1Galt1(-/-) mice carried highly sialylated core 3- and core 4-type glycans. A large portion of NeuAc in all mouse models was positioned on disialylated N-acetyllactosamine units, an epitope not reported on human colonic MUC2. Mass spectra and proton NMR spectroscopy revealed an abundant NeuAc linked to internally positioned N-acetylglucosamine on colonic murine Muc2, which also differs markedly from human MUC2. Our results highlight that murine colonic Muc2 O-glycosylation is substantially different from human MUC2, which could be one explanation for the different commensal microbiota of these two species.

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