NAD(P)H oxidases regulate HIF-2alpha protein expression

J Biol Chem. 2007 Mar 16;282(11):8019-26. doi: 10.1074/jbc.M611569200. Epub 2007 Jan 2.

Abstract

Biallelic inactivation of the von Hippel-Lindau tumor suppressor gene (VHL) is linked to the development of hereditary and sporadic renal cell carcinoma (RCC). In the absence of VHL, the alpha subunits of heterodimeric hypoxia-inducible transcription factors (HIF-1alpha and HIF-2alpha) are stabilized. Reactive oxygen species, generated by NAD(P)H oxidases, are involved in signaling cascades of malignant growth. We show that in VHL-deficient cells p22phox, Nox4 protein levels and NADPH-dependent superoxide generation are increased. Reintroduction of VHL into the VHL-deficient cells down-regulates the expression of p22phox and NADPH-dependent superoxide generation. Inhibition of the 26 S proteasome in VHL-expressing cells increased p22phox protein levels, which correlated with an increase of NADPH-dependent superoxide generation. We also show that p22phox co-immunoprecipitates with VHL in vivo. Moreover, p22phox is a target of ubiquitination. Importantly, in VHL-deficient cells, diphenyleneiodonium chloride (DPI), an inhibitor of Nox oxidases, decreased the expression of HIF-2alpha. Down-regulation of Nox1, Nox4, and p22phox expression by small interfering RNA also decreased HIF-2alpha protein expression and inhibited Akt and 4E-BP1 phosphorylation, suggesting that a translational mechanism is involved in maintaining HIF-2alpha in VHL-deficient cells. Colony formation by RCC 786-O in soft agar was markedly inhibited by DPI. Moreover, DPI significantly inhibited RCC 786-O tumor formation in athymic mice. Collectively, the data demonstrate that VHL protein exerts its tumor suppressor action, at least partially, via inhibition of p22phox-based Nox4/Nox1 NADPH oxidase-dependent reactive oxygen species generation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Basic Helix-Loop-Helix Transcription Factors
  • Gene Expression Regulation*
  • Gene Expression Regulation, Enzymologic*
  • Humans
  • NADPH Oxidase 1
  • NADPH Oxidase 4
  • NADPH Oxidases / metabolism*
  • Onium Compounds / pharmacology
  • Phosphorylation
  • Proteasome Endopeptidase Complex / metabolism
  • Proteasome Inhibitors
  • Reactive Oxygen Species / metabolism
  • Superoxides / metabolism
  • Transcription Factors / biosynthesis*
  • Von Hippel-Lindau Tumor Suppressor Protein / metabolism

Substances

  • Basic Helix-Loop-Helix Transcription Factors
  • Onium Compounds
  • Proteasome Inhibitors
  • Reactive Oxygen Species
  • Transcription Factors
  • Superoxides
  • endothelial PAS domain-containing protein 1
  • diphenyleneiodonium
  • NADPH Oxidase 1
  • NADPH Oxidase 4
  • NADPH Oxidases
  • NOX1 protein, human
  • NOX4 protein, human
  • CYBA protein, human
  • Von Hippel-Lindau Tumor Suppressor Protein
  • Proteasome Endopeptidase Complex
  • ATP dependent 26S protease
  • VHL protein, human