title: Secretion of fucosylated oligosaccharides related to the H antigen by human gastric cells.
abstract: Although the role of the blood group antigens in the gastrointestinal tract is not well understood, alterations in blood group-related antigens have been described in some pathological processes. Thus, the knowledge of their expression under normal conditions is of special interest. Those individuals expressing their ABO blood group in exocrine epithelia and secretions are called secretors. The aim of the present study was the localization of H antigen expression in the normal human gastric epithelial cells of non-O blood group individuals. For this, a monoclonal anti-H antibody was examined by immunocytochemical methods at both the light and electron microscopic levels. In combination with enzymatic and chemical treatments, the nature of the oligosaccharide chains containing the H antigen was characterized. The selected cases were four A secretors, three A nonsecretors, and three B non-secretors. The labeling of the anti-H antibody in the human stomach is described, irrespective of the blood group of the individuals. The staining was abolished when O-linked oligosaccharides were removed. Since commercially available anti-H antibodies usually also recognize other H-related antigens, the labeling of the antibody by H-related antigens cannot be dismissed. Our findings suggest the existence of H or H-related antigens in the O-linked oligosaccharides of the secretory granules of the surface, gastric pit, mucous neck, and transitional cells of the fundic mucosa, and in the intracellular canaliculi and tubulovesicular system of parietal cells. The H or H-related antigens were also localized in the apical membrane of all the cell types of the epithelial cells of the human fundic mucosa. The overall distribution of the H or H-related antigens in the stomach in non-O blood group individuals suggests the constitutive expression of an alpha(1,2)fucosyltransferase.
authors.affiliation: Department of Cell Biology and Morphological Sciences, School of Medicine and Dentistry, University of the Basque Country, Leioa, Vizcaya, Spain. gcpmacuj@lg.ehu.es
authors.forename: J F
authors.initials: JF
authors.lastname: Madrid
authors.forename: O
authors.initials: O
authors.lastname: Leis
authors.forename: L
authors.initials: L
authors.lastname: Díaz-Flores
authors.forename: F
authors.initials: F
authors.lastname: Hernández
mesh_terms: D000017:ABO Blood-Group System / Q000032:analysis*; D000581:Amidohydrolases; D019872:Chief Cells, Gastric / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D003594:Cytoplasmic Granules / Q000737:chemistry / Q000648:ultrastructure; D004847:Epithelial Cells / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D005643:Fucose; D005753:Gastric Mucosa / Q000166:cytology* / Q000276:immunology / Q000378:metabolism* / Q000648:ultrastructure; D006056:Golgi Apparatus / Q000737:chemistry / Q000648:ultrastructure; D006801:Humans; D007150:Immunohistochemistry; D009844:Oligosaccharides / Q000032:analysis / Q000378:metabolism*; D010295:Parietal Cells, Gastric / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
chemical_list: D000017:ABO Blood-Group System; D009844:Oligosaccharides; D005643:Fucose; D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase