Detoxification of methylmercury by hydrogen sulfide-producing enzyme in mammalian cells

Eiko Yoshida, Takashi Toyama, Yasuhiro Shinkai, Tomohiro Sawa, Takaaki Akaike, Yoshito Kumagai

Research output: Contribution to journalArticlepeer-review

46 Citations (Scopus)


Methylmercury (MeHg) covalently modifies cellular proteins through their SH groups, resulting in cytotoxicity. We report that cystathionine β-synthase (CBS), which catalyzes the production of hydrogen sulfide, contributes to cellular protection against MeHg. Pretreatment with NaHS or overexpression of CBS reduced MeHg cytotoxicity, whereas transfection with CBS small interfering RNA enhanced MeHg toxicity in human neuroblastoma SH-SY5Y cells. Bismethylmercury sulfide ((MeHg) 2S) was identified as a metabolite of MeHg in SH-SY5Y cells exposed to MeHg and in the livers of rats treated with MeHg. (MeHg) 2S had little chemical protein modification capability and little cytotoxicity compared with MeHg in vitro and in vivo.

Original languageEnglish
Pages (from-to)1633-1635
Number of pages3
JournalChemical Research in Toxicology
Issue number10
Publication statusPublished - 2011 Oct 17
Externally publishedYes

ASJC Scopus subject areas

  • Toxicology


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