In situ characterization of O-linked glycans of Muc2 in mouse colon

Acta Histochem. 2012 Nov;114(7):723-32. doi: 10.1016/j.acthis.2011.12.009. Epub 2012 Jan 18.

Abstract

The characterization of mucus O-linked glycans in the proximal and distal mouse colon was performed by conventional histochemical methods and by lectin histochemistry in combination with enzymatic treatment (PNGase, α1,2 fucosidase, sialidase digestion), with and without prior desulfation. We demonstrated the presence of sialo- and sulfomucins in both the proximal and distal colon of the mouse. In the distal colon the sulfomucins were clearly prevalent, although there were always sialomucins with sialyl residues linked α2,6 to the subterminal galactose. Sialic acid was poorly O-acetylated, especially in the distal colon. The lectin binding pattern indicates a massive presence of fucose α1,2 linked to galactose in O-glycans and smaller quantities of fucose linked α1,6 to N-acetylglucosamine in the core of N-linked glycans. Lectin histochemistry also demonstrated the presence of glycosidic residues of N-acetylglucosamine, N-acetylgalactosamine, and galactose in oligosaccharide chains of highly sulfated mucins.

MeSH terms

  • Acetylglucosamine / metabolism
  • Animals
  • Carbohydrate Conformation
  • Colon / cytology
  • Colon / metabolism*
  • Fucose / metabolism
  • Galactose / metabolism
  • Glucose / metabolism
  • Goblet Cells / metabolism
  • Lectins / chemistry
  • Male
  • Mannose / metabolism
  • Mice / anatomy & histology*
  • Mice / metabolism
  • Mice, Inbred C57BL
  • Mucin-2 / metabolism*
  • Polysaccharides / metabolism*
  • Sialic Acids / metabolism
  • Staining and Labeling

Substances

  • Lectins
  • Muc2 protein, mouse
  • Mucin-2
  • Polysaccharides
  • Sialic Acids
  • Fucose
  • Glucose
  • Mannose
  • Acetylglucosamine
  • Galactose