Identification of novel pancreas-specific regulatory sequences in the promoter region of human pancreatic secretory trypsin inhibitor gene

J Biol Chem. 1998 Dec 18;273(51):34413-21. doi: 10.1074/jbc.273.51.34413.

Abstract

The human pancreatic secretory trypsin inhibitor (PSTI) genes introduced into mice are specifically expressed in pancreas. The 1.0 kilobase pairs of PSTI 5'-flanking sequence directed preferential expression of a linked reporter chloramphenicol acetyltransferase, which was active in a PSTI-expressing pancreatic cell line (AR42j) but not in a PSTI-nonexpressing fibroblast cell line (XC). Two positively acting elements were found, Region I (-161/-116) and Region II (-103/-74), as defined by transfection and binding assays with AR42j cells. Region II is sufficient for the pancreas-specific expression, but the presence of both Regions I and II is needed for the maximum activity. Sequence studies also revealed that these two elements differ from the previously identified recognition sequence for pancreas transcription factor 1 (PTF1). When the same set of experiments was done with XC cells, one negatively acting element was identified, Region IV (-154/-137). Interestingly, Regions I and IV share a core sequence (-149/-139), CAATCAATAAC. These results suggest that this novel element regulates the human PSTI gene expression positively in pancreatic cells but negatively in nonpancreatic cells.

MeSH terms

  • Animals
  • Base Sequence
  • Cell Line
  • Cell Nucleus / metabolism
  • Chloramphenicol O-Acetyltransferase / genetics
  • Genes, Reporter
  • Humans
  • Male
  • Mice
  • Mice, Transgenic
  • Molecular Sequence Data
  • Organ Specificity
  • Pancreas / metabolism*
  • Promoter Regions, Genetic*
  • Rats
  • Recombinant Fusion Proteins / biosynthesis
  • Regulatory Sequences, Nucleic Acid
  • Transfection
  • Trypsin Inhibitor, Kazal Pancreatic / biosynthesis
  • Trypsin Inhibitor, Kazal Pancreatic / genetics*

Substances

  • Recombinant Fusion Proteins
  • Trypsin Inhibitor, Kazal Pancreatic
  • Chloramphenicol O-Acetyltransferase