title: Three distinct messenger RNA distribution patterns in human jejunal enterocytes.
abstract: OBJECTIVE
  The importance of messenger RNA (mRNA) localization in human enterocytes is poorly understood. Previous studies from our laboratory have indicated that mRNAs are asymmetrically distributed in human intestinal epithelial cells, but in general colocalized with their encoded proteins. The aim of this study was to characterize, in human enterocytes, mRNA localization patterns of three genes with distinctly different functions.
  
  
  METHODS
  mRNA distribution was determined by in situ hybridization with digoxigenin-labeled RNA probes in tissue sections of human jejunum.
  
  
  RESULTS
  The mRNA for villin, a well-characterized microvillus cytoskeletal protein, was sorted to the basal region of the enterocyte. The mRNA for human sodium glucose cotransporter 1 was localized to the apical region, and the mRNA for human liver fatty acid-binding protein was distributed diffusely in the cytoplasm.
  
  
  CONCLUSIONS
  The three distinct mRNA distribution patterns suggest that active mRNA sorting mechanisms exist in human enterocytes. This study also reveals for the first time that dichotomies may occur between the distribution patterns of sorted mRNAs and their encoded proteins.
authors.affiliation: Department of Pediatrics, Floating Hospital for Children, Boston, Massachusetts, USA.
authors.forename: W
authors.initials: W
authors.lastname: Li
authors.forename: S D
authors.initials: SD
authors.lastname: Krasinski
authors.forename: M
authors.initials: M
authors.lastname: Verhave
authors.forename: R K
authors.initials: RK
authors.lastname: Montgomery
authors.forename: R J
authors.initials: RJ
authors.lastname: Grand
mesh_terms: D000328:Adult; D018938:Caco-2 Cells; D002352:Carrier Proteins / Q000235:genetics*; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D006367:HeLa Cells; D006801:Humans; D017403:In Situ Hybridization; D007583:Jejunum / Q000737:chemistry* / Q000166:cytology; D008562:Membrane Glycoproteins / Q000235:genetics*; D008840:Microfilament Proteins / Q000235:genetics*; D009004:Monosaccharide Transport Proteins / Q000235:genetics*; D018996:Myelin P2 Protein / Q000235:genetics*; D009363:Neoplasm Proteins; D012333:RNA, Messenger / Q000032:analysis*; D051269:Sodium-Glucose Transporter 1; D025521:Tumor Suppressor Proteins
chemical_list: D002352:Carrier Proteins; C107608:FABP7 protein, human; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D008562:Membrane Glycoproteins; D008840:Microfilament Proteins; D009004:Monosaccharide Transport Proteins; D018996:Myelin P2 Protein; D009363:Neoplasm Proteins; D012333:RNA, Messenger; C495674:SLC5A1 protein, human; D051269:Sodium-Glucose Transporter 1; D025521:Tumor Suppressor Proteins; C026615:villin