An enhancer activates the pig lactase phlorizin hydrolase promoter in intestinal cells

  • Troelsen J
  • Mitchelmore C
  • Olsen J
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Lactase phlorizin hydrolase is a small intestinal-specific brush border protein commonly used as a specific marker of differentiated enterocytes. A number of transcription factors involved in the enterocyte-specific expression of lactase phlorizin hydrolase have been identified. An upstream regulatory region, which we have named the 'LPH enhancer', located at position -894 to -798 in the porcine lactase phlorizin hydrolase gene, is necessary for high differentiation-dependent LPH expression in intestinal cells. The LPH enhancer was studied by mutation analysis, transfection experiments and electrophoretical mobility shift assays. The LPH enhancer is active in intestinal cells (Caco-2) and not in non-intestinal cells (HeLa). The LPH enhancer is only able to enhance expression when it is located in front of an intestinal-specific promoter such as the lactase phlorizin hydrolase promoter or the sucrase-isomaltase promoter. In front of an SV40-derived promoter the LPH enhancer has no stimulatory effect. In addition to the lack of promoter-promiscuity, the LPH enhancer is not a classical enhancer in the sense that it is not orientation-independent and it cannot function when located 3′ of a reporter gene. The LPH enhancer contains at least three cis-elements (at -894 to -880, -880 to -875 and -833 to -814) with functional importance for the LPH enhancer activity. © 2003 Elsevier Science B.V. All rights reserved.

Author-supplied keywords

  • Caco-2
  • Gene regulation
  • Small intestine
  • Sucrase-isomaltase
  • Transcription

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  • Jesper T. Troelsen

  • Cathy Mitchelmore

  • Jørgen Olsen

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