Fatty acid labeling from glutamine in hypoxia can be explained by isotope exchange without net reductive isocitrate dehydrogenase (IDH) flux

J Biol Chem. 2013 Oct 25;288(43):31363-9. doi: 10.1074/jbc.M113.502740. Epub 2013 Sep 12.

Abstract

Acetyl-CoA is an important anabolic precursor for lipid biosynthesis. In the conventional view of mammalian metabolism, acetyl-CoA is primarily derived by the oxidation of glucose-derived pyruvate in mitochondria. Recent studies have employed isotope tracers to show that in cancer cells grown in hypoxia or with defective mitochondria, a major fraction of acetyl-CoA is produced via another route, reductive carboxylation of glutamine-derived α-ketoglutarate (catalyzed by reverse flux through isocitrate dehydrogenase, IDH). Here, we employ a quantitative flux model to show that in hypoxia and in cells with defective mitochondria, oxidative IDH flux persists and may exceed the reductive flux. Therefore, IDH flux may not be a net contributor to acetyl-CoA production, although we cannot rule out net reductive IDH flux in some compartments. Instead of producing large amounts of net acetyl-CoA reductively, the cells adapt by reducing their demand for acetyl-CoA by importing rather than synthesizing fatty acids. Thus, fatty acid labeling from glutamine in hypoxia can be explained by spreading of label without net reductive IDH flux.

Keywords: Cancer; Hypoxia; Isotopic Tracers; Metabolism; Mitochondrial Metabolism.

MeSH terms

  • Acetyl Coenzyme A / metabolism
  • Cell Hypoxia
  • Cell Line, Tumor
  • Fatty Acids / chemistry
  • Fatty Acids / metabolism*
  • Glutamine / chemistry
  • Glutamine / metabolism*
  • Humans
  • Isocitrate Dehydrogenase / chemistry
  • Isocitrate Dehydrogenase / metabolism*
  • Ketoglutaric Acids / metabolism
  • Oxidation-Reduction

Substances

  • Fatty Acids
  • Ketoglutaric Acids
  • Glutamine
  • Acetyl Coenzyme A
  • Isocitrate Dehydrogenase