title: Glycosylation of the two O-glycosylated domains of human MUC2 mucin in patients transposed with artificial urinary bladders constructed from proximal colonic tissue.
abstract: Transposition of intestinal segments is frequently used for bladder reconstruction. Following transposition, bowel segments continue to produce mucus and a correlation between excessive mucus production and complications such as urinary tract infection or catheter blockage has been observed for a long time. However, no information is currently available on the change of mucin expression and glycosylation under these abnormal conditions. In this study, the variable number tandem repeat region and the irregular repeat domain of human MUC2 were isolated as two glycopeptide populations after reduction and trypsin digestion followed by gel chromatography from urine of patients transposed with urinary bladders. After alkaline borohydride treatment, the oligosaccharides released from the whole MUC2 mucin and the two glycosylated domains were investigated by nanoESI Q-TOF MS/MS (electrospray ionization quadrupole time-of-flight tandem mass spectrometry). More than 60 different glycans were identified, mainly based on sialylated core 3 structures. Some core 1, 2 and 4 oligosaccharides were also found. Most of the structures were acidic with NeuAc residues mainly alpha2-6 linked to the N-acetylgalactosaminitol and sulphate residues exclusively 3-linked to galactose. No expression of blood group A and B or Sda/Cad determinants was observed. Similar patterns of glycosylation were found in the tandem repeat region and the irregular repeat domain and the level of expression of the major oligosaccharides were in the same order of magnitude. The most interesting feature of this study was that sialyl-Tn antigen, which is considered as a tumour antigen, was the oligosaccharide most highly expressed. This result suggests that mucins from intestinal transposed segments are abnormally glycosylated.
authors.affiliation: Unité de Glycobiologie Structurale et Fonctionnelle, UMR CNRS/USTL 8576, IFR 147, Université des Sciences et Technologies de Lille, 59655, Villeneuve d'Ascq Cedex, France.
authors.forename: Catherine
authors.initials: C
authors.lastname: Robbe-Masselot
authors.forename: Annkatrin
authors.initials: A
authors.lastname: Herrmann
authors.forename: Ingemar
authors.initials: I
authors.lastname: Carlstedt
authors.forename: Jean-Claude
authors.initials: JC
authors.lastname: Michalski
authors.forename: Calliope
authors.initials: C
authors.lastname: Capon
mesh_terms: D000143:Acids / Q000737:chemistry; D001187:Artificial Organs; D002240:Carbohydrate Sequence; D002851:Chromatography, High Pressure Liquid; D003106:Colon / Q000378:metabolism* / Q000601:surgery; D006031:Glycosylation; D006801:Humans; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D009005:Monosaccharides / Q000737:chemistry / Q000378:metabolism; D055262:Mucin-2; D009077:Mucins / Q000737:chemistry* / Q000378:metabolism*; D009844:Oligosaccharides / Q000737:chemistry / Q000378:metabolism; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D001743:Urinary Bladder / Q000378:metabolism* / Q000601:surgery
chemical_list: D000143:Acids; C524625:MUC2 protein, human; D009005:Monosaccharides; D055262:Mucin-2; D009077:Mucins; D009844:Oligosaccharides; D021122:Protein Subunits