Involvement of oxidative stress in hydroquinone-induced cytotoxicity in catalase-deficient Escherichia coli mutants

Masako Horita, Da Hong Wang, Ken Tsutsui, Kuniaki Sano, Noriyoshi Masuoka, Shohei Kira

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Hydroquinone is a benzene-derived metabolite. To clarify whether the reactive oxygen species (ROS) are involved in hydroquinone-induced cytotoxicity, we constructed transformants of Escherichia coli (E. coli) strains that express mammalian catalase gene derived from catalase mutant mice (Csb, Csc) and the wild-type (Csa) using a catalase-deficient E. coli UM255 as a recipient. Specific catalase activities of these tester strains were in order of Csa > Csc > Csb > UM255, and their susceptibility to hydrogen peroxide (H2O2) showed UM255 > Csb > Csc > Csa. We found that hydroquinone exposure reduced the survival of catalase-deficient E. coli mutants in a dose-dependent manner significantly, especially in the strains with lower catalase activities. Hydroquinone toxicity was also confirmed using zone of inhibition test, in which UM255 was the most susceptible, showing the largest zone of growth inhibition, followed by Csb, Csc and Csa. Furthermore, we found that hydroquinone-induced cell damage was inhibited by the pretreatment of catalase, ascorbic acid, dimethyl sulfoxide (DMSO), and ethylenediaminetetraacetic acid (EDTA), and augmented by superoxide dismutase (both CuZnSOD and MnSOD). The present results suggest that H2O2 is probably involved in hydroquinone-induced cytotoxicity in catalase-deficient E. coli mutants and catalase plays an important role in protection of the cells against hydroquinone toxicity.

Original languageEnglish
Pages (from-to)1035-1041
Number of pages7
JournalFree Radical Research
Volume39
Issue number10
DOIs
Publication statusPublished - Oct 2005

Keywords

  • Catalase
  • Catalase-deficient E. coli mutants
  • Hydrogen peroxide
  • Hydroquinone

ASJC Scopus subject areas

  • Biochemistry

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