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Intestinal Muc2 mucin O-glycosylation is affected by microbiota and regulated by differential expression of glycosyltranferases

Artikel i vetenskaplig tidskrift
Författare Liisa Arike
Jessica Holmén Larsson
Gunnar C. Hansson
Publicerad i Glycobiology
Volym 27
Nummer/häfte 4
Sidor 318-328
ISSN 0959-6658
Publiceringsår 2017
Publicerad vid Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi
Sidor 318-328
Språk en
Länkar dx.doi.org/10.1093/glycob/cww134
Ämnesord colon, mass spectrometry, mouse, mucus, small intestine, MOUSE STOMACH, HELICOBACTER-PYLORI, GENE-EXPRESSION, GUT MICROBIOTA, TRANSFERASE, MICE, METABOLISM, COLON, GLYCOSYLTRANSFERASE, FRACTIONATION, Biochemistry & Molecular Biology, ATES OF AMERICA, V105, P15064
Ämneskategorier Medicinska grundvetenskaper

Sammanfattning

Intestinal cells are covered by mucus. In the small intestine, a single unattached mucus is present whereas the colon has both an inner attached mucus layer and an outer loose mucus. The attached mucus of the colon is impenetrable to bacteria while the loose mucus acts as a habitat for commensal bacteria. In germ-free (GF) mice, small intestinal mucus is attached to the epithelium and the inner colon mucus is penetrable. O-glycosylation plays an important role in the host-microbiota interactions as the commensal bacteria use glycans as nutrient sources and attachment sites. While mucus protein composition is relatively homogenous along the intestine, its main component the Muc2 mucin shows regiospecific O-glycan patterns. We have now analyzed the glycosyltransferase relative concentrations in the epithelial cells along the intestine in GF and conventionally raised mice and compared this with the O-glycans formed. As Muc2 is the main O-glycosylated product in mucus, we made the simplified assumption that most of the glycosyltransferases found in the epithelial cells are involved in Muc2 O-glycan biosynthesis. The O-glycosyltransferase abundances along the intestine correlated well with the Muc2 O-glycan patterns. Some of the glycosyltransferases involved in the O-glycan elongation were decreased in GF mice, something that is in concordance with the observed shorter Muc2 O-glycans.

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