title: Epithelial functions of the residual bowel after surgery for necrotising enterocolitis in human infants.
abstract: OBJECTIVE
  Information on epithelial functions of the residual small or colonic bowel after resection for necrotising enterocolitis (NEC) in human infants is scarce. Our aim is to evaluate epithelial functions in the intestinal resection margins of tissue obtained at bowel resection for acute NEC and consecutive stoma closure.
  
  
  METHODS
  Epithelial morphology, proliferation, and protein expression were (immuno)histochemically studied.
  
  
  RESULTS
  Acute NEC was associated with severe and mild epithelial damage varying from epithelial loss to fairly unaffected epithelium. Epithelial proliferation was increased both at acute NEC and at stoma closure. In acute NEC, lactase, glucose transporter-2 and -5 expression was down-regulated in severely affected epithelium, whereas sucrase-isomaltase and intestinal fatty acid binding protein expression was maintained. Goblet cells continued to express mucin 2 and trefoil factor 3, however, their numbers were decreased. Moreover, in acute NEC, Paneth cells were weakly lysozyme positive and were reduced in number. At stoma closure, expression of the above cell type-specific markers had completely been re-established.
  
  
  CONCLUSIONS
  Residual bowel after resection for acute NEC shows a disturbed epithelial proliferation/differentiation balance. Acute NEC was associated with downregulation of distinct enterocyte-specific proteins. Because of goblet cell and Paneth cell loss in acute NEC, mucosal barrier, and defense functions may be impaired.
authors.affiliation: Department of Pediatrics, Erasmus MC-Sophia Children's Hospital, The Netherlands.
authors.forename: Maaike W
authors.initials: MW
authors.lastname: Schaart
authors.forename: Adrianus C J M
authors.initials: AC
authors.lastname: de Bruijn
authors.forename: Deirdre M
authors.initials: DM
authors.lastname: Bouwman
authors.forename: Ronald R
authors.initials: RR
authors.lastname: de Krijger
authors.forename: Johannes B
authors.initials: JB
authors.lastname: van Goudoever
authors.forename: Dick
authors.initials: D
authors.lastname: Tibboel
authors.forename: Ingrid B
authors.initials: IB
authors.lastname: Renes
mesh_terms: D015415:Biomarkers / Q000378:metabolism; D049109:Cell Proliferation; D015536:Down-Regulation; D020345:Enterocolitis, Necrotizing / Q000378:metabolism / Q000473:pathology / Q000601:surgery*; D020895:Enterocytes / Q000378:metabolism* / Q000473:pathology; D004848:Epithelium / Q000378:metabolism* / Q000473:pathology; D050556:Fatty Acid-Binding Proteins / Q000378:metabolism; D015870:Gene Expression; D051273:Glucose Transporter Type 2 / Q000378:metabolism; D051296:Glucose Transporter Type 5 / Q000378:metabolism; D006801:Humans; D007223:Infant; D007413:Intestinal Mucosa / Q000378:metabolism* / Q000473:pathology; D043322:Lactase / Q000378:metabolism; D055262:Mucin-2 / Q000378:metabolism; D009113:Muramidase / Q000378:metabolism; D010455:Peptides / Q000378:metabolism; D013394:Sucrase-Isomaltase Complex / Q000378:metabolism; D000071165:Trefoil Factor-3
chemical_list: D015415:Biomarkers; D050556:Fatty Acid-Binding Proteins; D051273:Glucose Transporter Type 2; D051296:Glucose Transporter Type 5; D055262:Mucin-2; D010455:Peptides; C082495:TFF3 protein, human; D000071165:Trefoil Factor-3; D013394:Sucrase-Isomaltase Complex; D043322:Lactase; D009113:Muramidase