Reduction of arsenic-induced cytotoxicity through Nrf2/HO-1 signaling in HepG2 cells

J Toxicol Sci. 2010 Jun;35(3):419-23. doi: 10.2131/jts.35.419.

Abstract

Our previous study indicated that Nrf2 is a key transcription factor in cellular defenses against inorganic arsenite (iAsIII). However, the role of heme oxygenase-1 (HO-1), which is regulated by Nrf2, in iAsIII-induced cytotoxicity is poorly understood. To address this issue, we examined the contribution of HO-1 to iAsIII-mediated Nrf2 activation and in protection against iAsIII cytotoxicity in HepG2 cells. Exposure of HepG2 cells to iAsIII (10 microM) caused persistent induction of HO-1 accompanied by prolonged Nrf2 activation, whereas siRNA-mediated knockdown of HO-1 decreased prolonged Nrf2 activation. Pretreatment with either HO-1 siRNA or HO inhibitor (tin protoporphyrin IX) significantly enhanced iAsIII-induced cytotoxicity. These results suggest that iAsIII-induced HO-1 appears, at least in part, to act as a positive feedback regulator of Nrf2 activation, thereby diminishing its cytotoxicity in HepG2 cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arsenites / toxicity*
  • Enzyme Induction / drug effects
  • Heme Oxygenase-1 / antagonists & inhibitors
  • Heme Oxygenase-1 / genetics
  • Heme Oxygenase-1 / metabolism
  • Heme Oxygenase-1 / physiology*
  • Hep G2 Cells
  • Humans
  • NF-E2-Related Factor 2 / metabolism
  • NF-E2-Related Factor 2 / physiology*
  • Protoporphyrins / pharmacology
  • RNA, Small Interfering / pharmacology
  • Signal Transduction / physiology*

Substances

  • Arsenites
  • NF-E2-Related Factor 2
  • Protoporphyrins
  • RNA, Small Interfering
  • protoporphyrin IX
  • HMOX1 protein, human
  • Heme Oxygenase-1
  • arsenite