Histochemical characterization of the sialic acid residues in mouse colon mucins

Mastrodonato, M; Mentino, D; Liquori, GE; Ferri, D

HERO ID

2902749

Reference Type

Journal Article

Year

2013

Language

English

PMID

23109168

HERO ID 2902749
In Press No
Year 2013
Title Histochemical characterization of the sialic acid residues in mouse colon mucins
Authors Mastrodonato, M; Mentino, D; Liquori, GE; Ferri, D
Journal Microscopy Research and Technique
Volume 76
Issue 2
Page Numbers 156-162
Abstract The mucins of colonic murine mucus are highly O-glycosilated sulfosialoglycoproteins. We have characterized the sialylation pattern of oligosaccharide chains of colonic murine mucins by conventional histochemical methods and by lectin histochemistry combined with chemical pretreatments and sialidase digestion. Oligosaccharide chains are strongly sulphated, with an increase of sulfation from the proximal toward the distal colon and a decrease of sialic acid expression and acetylation toward the distal colon. In the goblet cells of proximal colon, sialic acid bound α2,3 to Galβ1,3GalNAc subterminal dimers is diacetylated at C7,C8;C7,C9;C8,C9 or triacetylated at C7,8,9. In the distal colon, sialic acid-linked α2,3 to Galβ1,3GalNAc subterminal dimers shows reduced O-acetylation at C7 and/or C8, while acetyl substituents at C9 and at C4 are almost absent. Sialic acid is involved in different essential physiological functions; thus, alterations of its expression and acetylation in oligosaccharide chains of intestinal mucins are generally associated with diseases, such as ulcerative colitis and cancer. Mice may represent a suitable animal model to study alterations of oligosaccharidic chains in colonic mucins and lectin histochemistry combined with chemical pretreatments, and enzyme digestion may be a valuable tool for this study. Our present work may represent a landmark for further lectin histochemical studies to evaluate alterations of mouse colon mucins under different physiological, pathological, or experimental conditions, with possible translational value in humans.
Doi 10.1002/jemt.22146
Pmid 23109168
Is Certified Translation No
Dupe Override No
Is Public Yes
Language Text English