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- Title
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.
- Authors
Thomsson, Kristina A; Holmén-Larsson, Jessica M; Ångström, Jonas; Johansson, Malin EV; Xia, Lijun; Hansson, Gunnar C
- Abstract
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.
- Subjects
MUCINS; GLYCOMICS; KNOCKOUT mice; LABORATORY mice; LIQUID chromatography-mass spectrometry; N-acetyllactosamine; COLON (Anatomy)
- Publication
Glycobiology, 2012, Vol 22, Issue 8, p1128
- ISSN
0959-6658
- Publication type
Article
- DOI
10.1093/glycob/cws083