title: Spasmolytic polypeptide is a major antral peptide: distribution of the trefoil peptides human spasmolytic polypeptide and pS2 in the stomach.
abstract: BACKGROUND
  The regional differences in the distribution of the trefoil peptides pS2 and human spasmolytic polypeptide (hSP) within the stomach are not known. The aim of this study was to gain insight into these functionally obscure molecules by characterizing their distribution.
  
  
  METHODS
  Tissue from gastrectomy specimens removed for peptic ulceration was examined to chart the distribution of hSP and pS2, using immunohistochemistry and in situ hybridization to chart their messenger RNAs (mRNAs).
  
  
  RESULTS
  Colocalization of pS2 and hSP was noted in the gastric foveolar and surface epithelium throughout the stomach. In the gastric antrum and pylorus, an extremely strong hSP mRNA signal was present within pyloric-type glands; strong hSP immunostaining was also seen at this site and in mucous-neck cells. Neither pS2 mRNA nor pS2 peptide were shown within the deep portions of the pyloric glands. Within areas of intestinal metaplasia, a few goblet cells immunostained for pS2 and putative ulcer associated cell lineage was seen with a pattern of trefoil peptide localization similar to the ileum.
  
  
  CONCLUSIONS
  The detailed function of these trefoil peptides is unknown, but their distribution suggests involvement in repair-enhancing mechanisms. hSP may be an important antral peptide and both of these peptides may play a specific reparative role.
authors.affiliation: Imperial Cancer Research Fund/Royal College of Surgeons Histopathology Unit, London, England.
authors.forename: A M
authors.initials: AM
authors.lastname: Hanby
authors.forename: R
authors.initials: R
authors.lastname: Poulsom
authors.forename: S
authors.initials: S
authors.lastname: Singh
authors.forename: G
authors.initials: G
authors.lastname: Elia
authors.forename: R E
authors.initials: RE
authors.lastname: Jeffery
authors.forename: N A
authors.initials: NA
authors.lastname: Wright
mesh_terms: D004848:Epithelium / Q000737:chemistry; D006801:Humans; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D036341:Intercellular Signaling Peptides and Proteins; D009077:Mucins; D009124:Muscle Proteins; D009363:Neoplasm Proteins / Q000032:analysis* / Q000235:genetics; D009479:Neuropeptides; D010276:Parasympatholytics / Q000032:analysis*; D010455:Peptides / Q000032:analysis* / Q000235:genetics; D011506:Proteins; D011706:Pyloric Antrum / Q000737:chemistry*; D012333:RNA, Messenger / Q000032:analysis / Q000235:genetics; D013270:Stomach / Q000737:chemistry*; D000071163:Trefoil Factor-1; D000071164:Trefoil Factor-2; D000071165:Trefoil Factor-3; D025521:Tumor Suppressor Proteins
chemical_list: D036341:Intercellular Signaling Peptides and Proteins; D009077:Mucins; D009124:Muscle Proteins; D009363:Neoplasm Proteins; D009479:Neuropeptides; D010276:Parasympatholytics; D010455:Peptides; D011506:Proteins; D012333:RNA, Messenger; C051838:TFF1 protein, human; C099037:TFF3 protein, rat; C000604008:Tff2 protein, rat; D000071163:Trefoil Factor-1; D000071164:Trefoil Factor-2; D000071165:Trefoil Factor-3; D025521:Tumor Suppressor Proteins; C034407:pancreatic spasmolytic polypeptide