mda-7/IL-24 induces apoptosis in human HepG2 hepatoma cells by endoplasmic reticulum stress

Oncol Rep. 2008 Aug;20(2):437-42.

Abstract

mda-7/IL-24 shows tumor-suppressor activity in a broad spectrum of human cancer cells. However, the molecular mechanism by which mda-7/IL-24 induces apoptosis is not well understood and most likely involves different pathways depending on the tumor. We examined the apoptotic effect of the adenovirus-mediated mda-7/IL-24 (Ad.mda-7) on human HepG2 hepatoma cells. We found that blocking the endoplasmic reticulum (ER) stress inhibited apoptosis induced by Ad.mda-7 and down-regulated the expression of caspase-12, Bax and caspase-3. The treatment of subcutaneous tumor xenografts of HepG2 cells with Ad.mda-7 inhibited tumor growth and angiogenesis. As in the in vitro studies, we found that blocking ER stress prevented Ad.mda-7 from inducing apoptosis in liver cancer cells in vivo. Our studies suggest that Ad.mda-7 induces apoptosis of HepG2 cells mainly through activation of the ER stress pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenoviridae / genetics
  • Animals
  • Apoptosis*
  • Blotting, Western
  • Carcinoma, Hepatocellular / metabolism
  • Carcinoma, Hepatocellular / pathology*
  • Caspase 12 / metabolism
  • Caspase 3 / metabolism
  • Cell Differentiation
  • Cell Proliferation
  • Endoplasmic Reticulum / genetics
  • Endoplasmic Reticulum / metabolism*
  • Flow Cytometry
  • Genetic Therapy*
  • Humans
  • Interleukins / physiology*
  • Liver Neoplasms, Experimental / metabolism
  • Liver Neoplasms, Experimental / pathology*
  • Mice
  • Mice, Inbred BALB C
  • Mice, Nude
  • Neovascularization, Pathologic / prevention & control
  • Plasmids
  • bcl-2-Associated X Protein / metabolism

Substances

  • BAX protein, human
  • Interleukins
  • bcl-2-Associated X Protein
  • interleukin-24
  • CASP12 protein, human
  • Caspase 12
  • Caspase 3