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The glycosylation of rat … - University of Gothenburg, Sweden Till startsida
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The glycosylation of rat intestinal Muc2 mucin varies between rat strains and the small and large intestine. A study of O-linked oligosaccharides by a mass spectrometric approach.

Journal article
Authors Niclas G. Karlsson
A Herrmann
Hasse Karlsson
Malin E V Johansson
I Carlstedt
Gunnar C. Hansson
Published in The Journal of biological chemistry
Volume 272
Issue 43
Pages 27025-34
ISSN 0021-9258
Publication year 1997
Published at Institute of Medical Biochemistry
Pages 27025-34
Language en
Keywords ABO Blood-Group System, chemistry, Animals, Carbohydrate Conformation, Carbohydrate Sequence, Chromatography, Gel, Epitopes, analysis, Gas Chromatography-Mass Spectrometry, methods, Glycopeptides, chemistry, isolation & purification, Glycosylation, Intestinal Mucosa, chemistry, metabolism, Intestine, Large, metabolism, Intestine, Small, metabolism, Molecular Sequence Data, Mucin-2, Mucins, biosynthesis, chemistry, metabolism, Neoplasm Proteins, chemistry, metabolism, Oligosaccharides, chemistry, isolation & purification, Organ Specificity, Rats, Sialic Acids, analysis
Subject categories Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)


The large glycosylated domains obtained from the rat intestinal mucin Muc2 were isolated from the large and small intestine of the inbred rat strains GOT-W and GOT-BW. The expression of the rat Muc2 in the large intestine was confirmed immunochemically and by Northern blotting. Released oligosaccharides were structurally characterized by gas chromatography-mass spectrometry (neutral and sialylated species) or by tandem mass spectrometry (sulfated species), and a total of 63 structures was assigned. The large intestinal oligosaccharides were found to be identical between the strains, while the small intestinal glycosylation differed. Until now, detailed structural analysis of oligosaccharides isolated from a single mucin core or mucin domain with different origin have not been performed, and the information of different mucin glycoforms has been limited to immunochemistry. Blood group A-determinants (GalNAcalpha1-3(Fucalpha1-2)Galbeta1-, and structures related to the blood group Sda/Cad-related epitope NeuAc/NeuGcalpha1-3(GalNAcbeta1-4)Galbeta1-, were found in GOT-BW small intestine, and also in both large intestines. Blood group H-determinants and NeuAc/NeuGcalpha1-3Galbeta1- were found in all samples. Core 1 (Galbeta1-3GalNAcalpha1-), core 2 (Galbeta1-3(GlcNAcbeta1-6)GalNAcalpha1-), core 3 (GlcNAcbeta1-3GalNAcalpha1-), and core 4 (GlcNAcbeta1-3(GlcNAcbeta1-6)GalNAcalpha1- were also found in all the samples. The large intestine were enriched in sulfated oligosaccharides and the small intestine contained higher amounts of sialylated species. Sulfation were found exclusively on C-6 of GlcNAc.

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