ArticleBiochemical and biophysical research communications2013
Involvement of AAT transporters in methylmercury toxicity in Caenorhabditis elegans.
Article in Biochemical and biophysical research communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Genetic factors in methylmercury-induced neurotoxicity: What have we learned fromAdvances in neurotoxicology · 2023Article
- The Modulatory Role of sti-1 in Methylmercury-Induced Toxicity in Caenorhabditis elegans.Neurotoxicity research · 2022Article
- Methylmercury-Induced Metabolic Alterations inToxics · 2021Article
- The Role of Human LRRK2 in Acute Methylmercury Toxicity in Caenorhabditis elegans.Neurochemical research · 2021Article
- Therapeutic Efficacy of the N,N' Bis-(2-Mercaptoethyl) Isophthalamide Chelator for Methylmercury Intoxication in Caenorhabditis elegans.Neurotoxicity research · 2020Article
- Drosophotoxicology: Elucidating Kinetic and Dynamic Pathways of Methylmercury Toxicity in a Drosophila Model.Frontiers in genetics · 2019Article
- Article
- C. elegans as a model in developmental neurotoxicology.Toxicology and applied pharmacology · 2018Review
- Cell Biology of the Mitochondrion.Genetics · 2017Review
- Guarana (Toxicology research · 2016Article
- Latent alterations in swimming behavior by developmental methylmercury exposure are modulated by the homolog of tyrosine hydroxylase in Caenorhabditis elegans.Neurotoxicology and teratologyArticle
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
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.
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Registered trials
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