Enhanced sensitivity of protein kinase B/Akt to insulin in hypoxia is independent of HIF1alpha and promotes cell viability

Eur J Cell Biol. 2007 Jul;86(7):393-403. doi: 10.1016/j.ejcb.2007.04.006. Epub 2007 Jun 4.

Abstract

Maintenance of oxygen homeostasis is a key requirement to ensure normal mammalian cell growth and differentiation. Hypoxia arises when oxygen demand exceeds supply, and is a feature of multiple human diseases including stroke, cancer and renal fibrosis. We have investigated the effect of hypoxia on kidney cells, and observed that insulin-induced cell viability is increased in hypoxia. We have characterized the role of protein kinase B (PKB/Akt) in these cells as a potential mediator of this effect. PKB/Akt activity was increased by low oxygen concentrations in kidney cells, and insulin-stimulated activation of PKB/Akt was stronger, more rapid and more sustained in hypoxia. Reduction of HIF1alpha levels using antimycin-A or siRNA targeting HIF1alpha did not affect PKB/Akt activation in hypoxia. Pharmacologic stabilization of HIF1alpha independent of hypoxia did not increase insulin-stimulated PKB/Akt activation. Although increased insulin-stimulated cell viability was observed in hypoxia, no differences in the degree of insulin-stimulated glucose uptake were observed in L6 muscle cells in hypoxia compared to normoxia. Thus, PKB/Akt may regulate specific cellular responses to growth factors such as insulin under adverse conditions such as hypoxia.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing / metabolism
  • Animals
  • Antimycin A / pharmacology
  • Cell Hypoxia / drug effects
  • Cell Survival / drug effects
  • Cells, Cultured
  • Enzyme Activation / drug effects
  • Humans
  • Hypoxia-Inducible Factor 1, alpha Subunit / metabolism*
  • Insulin / pharmacology*
  • Membrane Proteins / metabolism
  • Mitochondria / drug effects
  • Mitochondria / metabolism
  • Phosphorylation / drug effects
  • Proto-Oncogene Proteins c-akt / metabolism*
  • Rats
  • Signal Transduction / drug effects
  • Thiolester Hydrolases
  • Time Factors

Substances

  • Adaptor Proteins, Signal Transducing
  • HIF1A protein, human
  • Hypoxia-Inducible Factor 1, alpha Subunit
  • Insulin
  • Membrane Proteins
  • Antimycin A
  • Proto-Oncogene Proteins c-akt
  • THEM4 protein, human
  • Thiolester Hydrolases