K-ras(G12V) transformation leads to mitochondrial dysfunction and a metabolic switch from oxidative phosphorylation to glycolysis

Cell Res. 2012 Feb;22(2):399-412. doi: 10.1038/cr.2011.145. Epub 2011 Aug 30.

Abstract

Increased aerobic glycolysis and oxidative stress are important features of cancer cell metabolism, but the underlying biochemical and molecular mechanisms remain elusive. Using a tetracycline inducible model, we show that activation of K-ras(G12V) causes mitochondrial dysfunction, leading to decreased respiration, elevated glycolysis, and increased generation of reactive oxygen species. The K-RAS protein is associated with mitochondria, and induces a rapid suppression of respiratory chain complex-I and a decrease in mitochondrial transmembrane potential by affecting the cyclosporin-sensitive permeability transition pore. Furthermore, pre-induction of K-ras(G12V) expression in vitro to allow metabolic adaptation to high glycolytic metabolism enhances the ability of the transformed cells to form tumor in vivo. Our study suggests that induction of mitochondrial dysfunction is an important mechanism by which K-ras(G12V) causes metabolic changes and ROS stress in cancer cells, and promotes tumor development.

Publication types

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

MeSH terms

  • Animals
  • Cell Line
  • Cyclosporins / pharmacology
  • Doxycycline / pharmacology
  • Electron Transport Complex I / antagonists & inhibitors
  • Electron Transport Complex I / metabolism
  • Glycolysis*
  • HEK293 Cells
  • Humans
  • Membrane Potential, Mitochondrial
  • Mice
  • Mice, Nude
  • Mitochondria / metabolism*
  • Mitochondria / pathology
  • Oxidative Phosphorylation*
  • Reactive Oxygen Species / metabolism
  • ras Proteins / genetics
  • ras Proteins / metabolism*

Substances

  • Cyclosporins
  • Reactive Oxygen Species
  • ras Proteins
  • Electron Transport Complex I
  • Doxycycline