Abstract
Selenoenzymes are required to prevent and reverse oxidative damage in the brain and neuroendocrine system, but these enzymes are vulnerable to irreversible inhibition by methylmercury (MeHg). Selenoenzyme inhibition appears likely to cause most if not all of the pathological effects of mercury toxicity. This biochemically based understanding seems to explain why certain tissues are affected by mercury, why the latency effect is unique to mercury poisoning, why selenium status is inversely related to mercury toxicity, why fetal exposures are so much more harmful than adult exposures, and why prenatal inhibition of selenoenzymes by high MeHg results in sustained loss of their activities.
Keywords
- Fetal Brain
- MeHg Exposure
- Mercury Toxicity
- Neuroendocrine Tissue
- High MeHg
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Asaduzzaman AM, Khan MAK, Schreckenbach G, Wang F. Computational studies of structural, electronic, spectroscopic and thermodynamic properties of methylmercury-amino acid complexes and their Se analogues. Inorg Chem. 2010;49:870–8.
Aschner M, Clarkson TW. Methyl mercury uptake across bovine brain capillary endothelial cells in vitro: the role of amino acids pharmacology and toxicology. Pharmacol Toxicol. 1989;64:293–7.
Bridges CC, Zalups RK. Transport of inorganic mercury and methylmercury in target tissues and organs. Toxicol Appl Pharmacol. 2005;204:274–308.
Budtz-Jørgensen E, Grandjean P, Weihe P. Separation of risks and benefits of seafood intake. Environ Health Perspect. 2007;115:323–7.
Carvalho CML, Chew E-H, Hashemy SI, Lu J, Holmgren A. Inhibition of the human thioredoxin system: a molecular mechanism of mercury toxicity. J Biol Chem. 2008;283(18):11913–23.
Clarkson TW, Magos L. The toxicology of mercury and its chemical compounds. Crit Rev Toxicol. 2006;36:609–62.
Dyrssen D, Wedborg M. The sulfur-mercury(II) system in natural waters. Water Air Soil Pollut. 1991;56:507–19.
Gromer S, Eubel JK, Lee BL, Jacob J. Human selenoproteins at a glance. Cell Mol Life Sci. 2005;62:2414–37.
Hoffmeyer RE, Singh SP, Doonan CJ, Ross AR, Hughes RJ, Pickering IJ, George GN. Molecular mimicry in mercury toxicology. Chem Res Toxicol. 2006;19:753–9.
Korbas M, O’Donoghue JL, Watson GE, Pickering IJ, Singh SP, Myers GJ, Clarkson TW, George GN. The chemical nature of mercury in human brain following poisoning or environmental exposure. Neuroscience. 2010;1:810–8.
Melnick JG, Yurkerwich K, Parkin GJ. On the chalcogenophilicity of mercury: evidence for a strong Hg–Se bond in [TmBut]HgSePh and its relevance to the toxicity of mercury. J Am Chem Soc. 2010;132:647–55.
Newland MC, Reed MN, LeBlanc A, Donlin WD. Brain and blood mercury and selenium after chronic and developmental exposure to methylmercury. Neurotoxicology. 2006;27:710–20.
Parizek J, Ostadalova I, Kalouskove J, Babicky A, Pavlik L, Bibr B. Effect of mercuric compounds on the maternal transmission of selenium in the pregnant and lactating. J Reprod Fertil. 1971;25:157–70.
Pinheiro MC, Muiller RC, Sarkis JE, Vieira JL, Oikawa T, Gomes MS, GuimaraÌfes GA, Do Nascimento JL, Silveira LC. Mercury and selenium concentrations in hair samples of women in fertile age from amazon riverside communities. Sci Total Environ. 2005;349(1–3):284–8.
Ralston NVC, Raymond LJ. Dietary selenium’s protective effects against methylmercury toxicity. Toxicology. 2010;278:112–23.
Ralston NVC, Ralston CR, Blackwell III JL, Raymond LJ. Dietary and tissue selenium in relation to methylmercury toxicity. Neurotoxicology. 2008;29:802–11.
Rayman M. The importance of selenium to human health. Lancet. 2000;356:233–41.
Reed MN, Banna KM, Donlin WD, Newland MC. Effects of gestational exposure to methylmercury and dietary selenium on reinforcement efficacy in adulthood. Neurotoxicol Teratol. 2008;30:29–37.
Schionning JD, Moller-Madsen BM. The effect of selenium on the localization of autometallographic mercury in dorsal root ganglia of rats. Virchows Arch B Cell Pathol Incl Mol Pathol. 1992;61:307–13.
Seppanen K, Soininen P, Salonen JT, Lotjonen S, Laatikainen R. Does mercury promote lipid peroxidation? An in vitro study concerning mercury, copper, and iron in peroxidation of low-density lipoprotein. Biol Trace Elem Res. 2004;101:117–32.
Stringari J, Nunes AKC, Franco JL, Bohrer D, Garcia SC, Dafre AL, Milatovic D, Souza DO, Rocha JBT, Aschner M, Farina M. Prenatal methylmercury exposure hampers glutathione antioxidant system ontogenesis and causes long-lasting oxidative stress in the mouse brain. Toxicol Appl Pharmacol. 2008;227:147–54.
Sugiura Y, Tamai Y, Tanaka H. Selenium protection against mercury toxicity: high binding affinity of methylmercury by selenium containing ligands in comparison with sulfur containing ligands. Bioinorg Chem. 1978;9:167–80.
Watanabe C, Yin K, Kasanuma Y, Satoh H. In utero exposure to methylmercury and selenium deficiency converge on the neurobehavioral outcome in mice. Neurotoxicol Teratol. 1999a;21:83–8.
Watanabe C, Yoshida K, Kasanuma Y, Kun Y, Satoh H. In utero methylmercury exposure differentially affects the activities of selenoenzymes in the fetal mouse brain. Environ Res. 1999b;80:208–14.
Wessjohann LA, Schneider A, Abbas M, Brandt W. Selenium in chemistry and biochemistry in comparison to sulfur. Biol Chem. 2007;388:997–1006.
Acknowledgments
This article was prepared by the University of North Dakota under award No. NA09NMF4520176 from National Oceanic and Atmospheric Administration, U.S. Department of Commerce. The statements, findings, conclusions, and recommendations are those of the authors and do not necessarily reflect the views of the funding agency.
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Ralston, N.V.C., Azenkeng, A., Raymond, L.J. (2012). Mercury-Dependent Inhibition of Selenoenzymes and Mercury Toxicity. In: Ceccatelli, S., Aschner, M. (eds) Methylmercury and Neurotoxicity. Current Topics in Neurotoxicity, vol 2. Springer, Boston, MA. https://doi.org/10.1007/978-1-4614-2383-6_5
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