title: Apical MUC1 expression revealed on the foveolar epithelium in H. pylori gastritis.
abstract: BACKGROUND
  The membrane mucin MUC1 is altered in its pattern of expression in cancer, and also in other pathological situations, including Helicobacter pylori gastritis. Here we investigate the basis for the loss of apical staining of the gastric foveolar epithelium in H. pylori gastritis.
  
  
  METHODS
  MUC1 was examined in the gastric antrum from cases of H. pylori gastritis and normal controls. We used tissue sections that were either treated or not treated with periodate to effect deglycosylation, and the monoclonal antibodies LICRLonM8, MUSE-11, CT2 and BC2.
  
  
  RESULTS
  We show that the epitopes on the TR domain of MUC1 are partially cryptic due to glycosylation and that MUC1 is present on the apical surface of the gastric foveolar epithelium of gastritis patients.
  
  
  CONCLUSIONS
  This observation suggests that there is no substantial loss of the mucin domain of MUC1 from the apical surface in gastritis, as suggested by others, but rather the H. pylori influences the glycosylation of MUC1. This paper highlights the issue of epitope specificity of monoclonal antibodies directed against disease-associated markers, specifically when they are glycoproteins, as is the case for many cancer markers.
authors: Department of Oncology, UCL Cancer Institute, London WCIE 6BT, UK.
authors: M
authors: M
authors: Rashid
authors: A S
authors: AS
authors: Teixeira
authors: U
authors: U
authors: Qureshi
authors: S P
authors: SP
authors: Pereira
authors: M R
authors: MR
authors: Novelli
authors: D M
authors: DM
authors: Swallow
mesh_terms: D005260:Female; D005753:Gastric Mucosa / Q000378:metabolism; D005756:Gastritis / Q000378:metabolism* / Q000382:microbiology; D006031:Glycosylation; D016481:Helicobacter Infections / Q000378:metabolism*; D016480:Helicobacter pylori; D006801:Humans; D008297:Male; D018396:Mucin-1 / Q000378:metabolism*; D011706:Pyloric Antrum / Q000378:metabolism*
chemical_list: D018396:Mucin-1