Ligands of peroxisome proliferator-activated receptor-gamma induce apoptosis in AR42J cells

Pancreas. 2002 Mar;24(2):130-8. doi: 10.1097/00006676-200203000-00003.

Abstract

Introduction: Peroxisome proliferator-activated receptor-gamma (PPAR-gamma) is a ligand-activated transcription factor that controls growth, differentiation, and inflammation in different tissues. Roles of PPAR-gamma activation in pancreatic acinar cells are poorly characterized.

Aims: To examine the effects of PPAR-gamma activation on the induction of apoptosis in rat pancreatic AR42J cells.

Methodology: AR42J cells were treated with ligands of PPAR-gamma, and induction of apoptosis was evaluated by cell viability, DNA-fragmentation, and flow cytometry.

Results: Treatment of the cells with ligands of PPAR-gamma (15-deoxy-open triangle12,14-prostaglandin J2 or troglitazone) induced apoptosis in a dose-dependent manner. Troglitazone-induced apoptosis was not blocked by inhibitors of caspases (acetyl-DEVD-aldehyde and benzoyloxycarbonyl-VAD-fluoromethylketone). Troglitazone induced the expression of pancreatitis-associated protein-1 and clusterin mRNAs. Troglitazone activated c-Jun NH2-terminal kinase/stress-activated protein kinase, but inhibited the activation of extracellular signal-regulated kinases 1/2. Troglitazone did not activate NF-kappaB, suggesting a role of NF-kappaB-independent pathways. In AR42J cells and isolated pancreatic acini, PPAR-gamma gene and protein were detected. In addition, troglitazone increased the PPAR-dependent transcriptional activity, suggesting that PPAR-gamma is functional in AR42J cells.

Conclusion: These results indicate that activation of PPAR-gamma induces apoptosis in AR42J cells and imply that PPAR-gamma may be a potential therapeutic target of pancreatic inflammation, because of its anti-inflammatory effects in addition to its proapoptotic effects.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Chloromethyl Ketones / pharmacology
  • Animals
  • Annexin A5 / genetics
  • Antineoplastic Agents / pharmacology
  • Apoptosis / drug effects
  • Apoptosis / physiology*
  • Caspase Inhibitors
  • Cell Line
  • Chromans / pharmacology
  • Clusterin
  • Cysteine Proteinase Inhibitors / pharmacology
  • DNA-Binding Proteins / metabolism
  • Gene Expression / drug effects
  • Glycoproteins / genetics
  • I-kappa B Proteins*
  • Immunologic Factors / pharmacology*
  • Ligands
  • Mitogen-Activated Protein Kinase 1 / antagonists & inhibitors
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinase 8
  • Mitogen-Activated Protein Kinases / antagonists & inhibitors
  • Mitogen-Activated Protein Kinases / metabolism
  • Molecular Chaperones / genetics
  • NF-KappaB Inhibitor alpha
  • Oligopeptides / pharmacology
  • Pancreas / cytology*
  • Pancreatitis-Associated Proteins
  • Prostaglandin D2 / analogs & derivatives*
  • Prostaglandin D2 / pharmacology*
  • RNA, Messenger / metabolism
  • Rats
  • Receptors, Cytoplasmic and Nuclear / metabolism*
  • Thiazoles / pharmacology
  • Thiazolidinediones*
  • Transcription Factors / metabolism*
  • Troglitazone

Substances

  • 15-deoxy-delta(12,14)-prostaglandin J2
  • Amino Acid Chloromethyl Ketones
  • Annexin A5
  • Antineoplastic Agents
  • Caspase Inhibitors
  • Chromans
  • Clusterin
  • Cysteine Proteinase Inhibitors
  • DNA-Binding Proteins
  • Glycoproteins
  • I-kappa B Proteins
  • Immunologic Factors
  • Ligands
  • Molecular Chaperones
  • Nfkbia protein, rat
  • Oligopeptides
  • Pancreatitis-Associated Proteins
  • REG3A protein, human
  • RNA, Messenger
  • Receptors, Cytoplasmic and Nuclear
  • Thiazoles
  • Thiazolidinediones
  • Transcription Factors
  • aspartyl-glutamyl-valyl-aspartal
  • benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone
  • NF-KappaB Inhibitor alpha
  • Mitogen-Activated Protein Kinase 1
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinase 8
  • Mitogen-Activated Protein Kinases
  • Troglitazone
  • Prostaglandin D2