Arginine decreases peroxisome proliferator-activated receptor-γ activity via c-Jun

Mol Cell Biochem. 2012 Mar;362(1-2):7-13. doi: 10.1007/s11010-011-1122-9. Epub 2011 Oct 26.

Abstract

We have previously shown in the post ischemic gut that enteral arginine enhanced injury and inflammation via c-Jun/AP-1 and abrogated peroxisome proliferator-activated receptor (PPAR) γ activity. In the current study, we investigated the mechanism by which arginine inhibited PPARγ in vitro in rat small bowel epithelial IEC-6 cells. Arginine repressed PPARγ transcriptional activity in a time and dose-dependent fashion. Furthermore, downregulation of PPARγ by arginine involved phosphorylation of c-Jun that occurred before to changes in PPARγ transcriptional activity. Silencing of c-Jun increased PPARγ beyond that of nonsilenced cells and was not mitigated by arginine. Using a series of blocking studies, we found no relationship between arginine and the ligand-dependent binding site of PPARγ. In conclusion, arginine decreased PPARγ transcriptional activity in small bowel intestinal epithelial cells. These changes are due, in part, to phosphorylation of c-Jun and may explain the deleterious effects of enteral arginine in the post ischemic gut.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Arginine / metabolism
  • Arginine / pharmacology*
  • Binding Sites
  • Cell Line
  • Epithelial Cells / metabolism
  • JNK Mitogen-Activated Protein Kinases / genetics
  • JNK Mitogen-Activated Protein Kinases / metabolism*
  • PPAR gamma / genetics*
  • PPAR gamma / metabolism*
  • Phosphorylation
  • RNA Interference
  • RNA, Small Interfering
  • Rats
  • Transcription, Genetic / drug effects*

Substances

  • PPAR gamma
  • RNA, Small Interfering
  • Arginine
  • JNK Mitogen-Activated Protein Kinases