SIRT1 inhibits proliferation of pancreatic cancer cells expressing pancreatic adenocarcinoma up-regulated factor (PAUF), a novel oncogene, by suppression of β-catenin

Biochem Biophys Res Commun. 2012 Jun 29;423(2):270-5. doi: 10.1016/j.bbrc.2012.05.107. Epub 2012 May 26.

Abstract

Because we found in a recent study that pancreatic adenocarcinoma up-regulated factor (PAUF), a novel oncogene, induces a rapid proliferation of pancreatic cells by up-regulation of β-catenin, we postulated that β-catenin might be a target molecule for pancreatic cancer treatment. We thus speculated whether SIRT1, known to target β-catenin in a colon cancer model, suppresses β-catenin in those pancreatic cancer cells that express PAUF (Panc-PAUF). We further evaluated whether such suppression would lead to inhibition of the proliferation of these cells. The ectopic expression of either SIRT1 or resveratrol (an activator of SIRT1) suppressed levels of β-catenin protein and its transcriptional activity in Panc-PAUF cells. Conversely, suppression of SIRT1 expression by siRNA enhanced β-catenin expression and transcriptional activity. SIRT1 mutant analysis showed that nuclear localization of SIRT1 is not required for reduction of β-catenin. Treatment with MG132, a proteasomal inhibitor, restored β-catenin protein levels, suggesting that SIRT1-mediated degradation of β-catenin requires proteasomal activity. It was reported that inhibition of GSK-3β or Siah-1 stabilizes β-catenin in colon cancer cells, but suppression of GSK-3β or Siah-1 using siRNA in the presence of resveratrol instead diminished β-catenin protein levels in Panc-PAUF cells. This suggests that GSK-3β and Siah-1 are not involved in SIRT1-mediated degradation of β-catenin in the cells. Finally, activation of SIRT1 inhibited the proliferation of Panc-PAUF cells by down-regulation of cyclin-D1, a target molecule of β-catenin. These results suggest that SIRT1 activation may be a therapeutic strategy for treatment of pancreatic cancer cells that express PAUF via the down-regulation of β-catenin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line, Tumor
  • Cell Nucleus / metabolism
  • Cell Proliferation*
  • Cyclin D1 / genetics*
  • Gene Expression Regulation, Neoplastic*
  • HEK293 Cells
  • Humans
  • Intercellular Signaling Peptides and Proteins
  • Lectins / genetics*
  • Leupeptins / pharmacology
  • Oncogenes*
  • Pancreatic Neoplasms / genetics
  • Pancreatic Neoplasms / metabolism
  • Pancreatic Neoplasms / pathology*
  • Proteasome Endopeptidase Complex / metabolism
  • Proteolysis
  • Sirtuin 1 / genetics
  • Sirtuin 1 / physiology*
  • beta Catenin / metabolism*

Substances

  • CCND1 protein, human
  • Intercellular Signaling Peptides and Proteins
  • Lectins
  • Leupeptins
  • ZG16B protein, human
  • beta Catenin
  • Cyclin D1
  • Proteasome Endopeptidase Complex
  • SIRT1 protein, human
  • Sirtuin 1
  • benzyloxycarbonylleucyl-leucyl-leucine aldehyde