EtBr-induced selective degradation of mitochondria occurs via autophagy

Oncol Rep. 2013 Sep;30(3):1201-8. doi: 10.3892/or.2013.2590. Epub 2013 Jul 4.

Abstract

Recent studies have implicated autophagy in numerous cellular responses to stress. During the establishment of human lung cancer cell lines without mitochondrial DNA, a significant depopulation of mitochondria occurred that was accompanied by the loss of the mitochondrial membrane potential. Notably, we observed autophagy in ethidium bromide (EtBr)-induced mitochondrial degradation. In the present study, we confirmed the involvement of autophagy in mitochondrial degradation after exposure to a low concentration of EtBr. Lung cancer cells undergoing mitochondrial autophagy exhibited a slower growth rate in vitro and in vivo. Furthermore, the degradation was mediated by the class III phosphatidylinositol 3-kinase (PI3K)-Beclin-1 complex. These findings indicate that autophagy is responsible for EtBr‑induced mitochondrial degradation via the PI3K‑Beclin-1 signaling pathway.

MeSH terms

  • Animals
  • Apoptosis Regulatory Proteins / metabolism
  • Autophagy / drug effects*
  • Beclin-1
  • Blotting, Western
  • Cell Movement / drug effects
  • Cell Proliferation / drug effects
  • Ethidium / toxicity*
  • Fluorescent Dyes / toxicity*
  • Humans
  • Lung Neoplasms / drug therapy
  • Lung Neoplasms / metabolism
  • Lung Neoplasms / pathology*
  • Membrane Potential, Mitochondrial / drug effects*
  • Membrane Proteins / metabolism
  • Mice
  • Mice, Inbred NOD
  • Mice, SCID
  • Microscopy, Confocal
  • Microscopy, Electron, Transmission
  • Mitochondria / drug effects*
  • Mitochondria / metabolism
  • Mitochondria / pathology*
  • Phosphatidylinositol 3-Kinases / metabolism
  • Signal Transduction / drug effects
  • Tumor Cells, Cultured
  • Xenograft Model Antitumor Assays

Substances

  • Apoptosis Regulatory Proteins
  • BECN1 protein, human
  • Beclin-1
  • Fluorescent Dyes
  • Membrane Proteins
  • Phosphatidylinositol 3-Kinases
  • Ethidium