title: Expression of trefoil peptides pS2 and human spasmolytic polypeptide in gastric metaplasia at the margin of duodenal ulcers.
abstract: Duodenal ulcers are associated with gastric metaplasia in the duodenum, both at the ulcer margin and at more distant sites in the duodenal bulb. pS2 and human spasmolytic polypeptide (hSP) are secretory peptides expressed in gastric epithelial cells and in gastric metaplasia. As these peptides may be important in ulcer healing, this study investigated the possibility that the expression of pS2 and hSP is increased in gastric metaplasia at the margin of duodenal ulcers. Duodenal bulb biopsy specimens from 12 duodenal ulcer patients were assessed. Sections were immunostained with monoclonal antibodies for pS2 and hSP. Cytoplasmic stain intensities were measured by an image analysis system and expressed as integrated optical density (IOD) units, In situ hybridisation for pS2 and hSP mRNA was carried out on parallel sections. Duodenal sections were also stained with diatase periodic acid Schiff/alcian blue to localise areas of gastric metaplasia. pS2 antigen staining in the duodenum was restricted to surface epithelial cells, and hSP to acinar and ductular components of Brunner's gland. mRNA localisation corresponded to immunostaining cells. In gastric metaplasia, pS2 expression was greater at the ulcer margin than away from the ulcer, as judged by the intensity of antibody staining (mean IOD units (SEM), 20.6 (3.3) v 9.5 (3.0); p < 0.001). There was a trend towards greater hSP staining at the ulcer margin but this did not achieve statistical significance. These findings support the putative role of pS2 and possible hSP in mucosal healing and providy further evidence for an autocrine 'ulcer-gastric metaplasia-repair' loop involving these trefoil peptides.
authors.affiliation: Department of Medicine, St George's Hospital Medical School, London.
authors.forename: S
authors.initials: S
authors.lastname: Khulusi
authors.forename: A M
authors.initials: AM
authors.lastname: Hanby
authors.forename: J M
authors.initials: JM
authors.lastname: Marrero
authors.forename: P
authors.initials: P
authors.lastname: Patel
authors.forename: M A
authors.initials: MA
authors.lastname: Mendall
authors.forename: S
authors.initials: S
authors.lastname: Badve
authors.forename: R
authors.initials: R
authors.lastname: Poulsom
authors.forename: G
authors.initials: G
authors.lastname: Elia
authors.forename: N A
authors.initials: NA
authors.lastname: Wright
authors.forename: T C
authors.initials: TC
authors.lastname: Northfield
mesh_terms: D002011:Brunner Glands / Q000737:chemistry; D004381:Duodenal Ulcer / Q000473:pathology*; D004967:Estrogens / Q000032:analysis*; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins; D007413:Intestinal Mucosa / Q000737:chemistry / Q000502:physiology; D008679:Metaplasia; D009077:Mucins; D009124:Muscle Proteins; D009363:Neoplasm Proteins / Q000032:analysis*; D009479:Neuropeptides; D010276:Parasympatholytics / Q000032:analysis*; D010455:Peptides / Q000032:analysis*; D011506:Proteins; D012038:Regeneration; D013270:Stomach / Q000473:pathology*; D000071163:Trefoil Factor-1; D000071164:Trefoil Factor-2; D000071165:Trefoil Factor-3; D025521:Tumor Suppressor Proteins
chemical_list: D004967:Estrogens; D036341:Intercellular Signaling Peptides and Proteins; D009077:Mucins; D009124:Muscle Proteins; D009363:Neoplasm Proteins; D009479:Neuropeptides; D010276:Parasympatholytics; D010455:Peptides; D011506:Proteins; 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