Involvement of AAT transporters in methylmercury toxicity in Caenorhabditis elegans

Samuel W. Caito, Yaofang Zhang, Michael Aschner

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

Methylmercury (MeHg) is a potent neurotoxin that enters mammalian cells as a conjugate with l-cysteine through L-type large neutral amino acid transporter, LAT1, by a molecular mimicry mechanism by structurally resembling l-methionine. Caenorhabditis elegans (. C. elegans) has been increasingly used to study the neurotoxic effects of MeHg, but little is known about uptake and transport of MeHg in the worm. This study examined whether MeHg uptake through LAT1 is evolutionarily conserved in nematodes. MeHg toxicity in C. elegans was blocked by pre-treatment of worms with l-methionine, suggesting a role for amino acid transporters in MeHg transport. Knockdown of aat-1, aat-2, and aat-3, worm homologues to LAT1, increased the survival of C. elegans following MeHg treatment and significantly attenuated MeHg content following exposure. These results indicate that MeHg is transported in the worm by a conserved mechanism dependent on functioning amino acid transporters.

Original languageEnglish (US)
Pages (from-to)546-550
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume435
Issue number4
DOIs
StatePublished - Jun 14 2013
Externally publishedYes

Keywords

  • L-type large neutral amino acid transporter
  • Methylmercury
  • Molecular mimicry

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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