21,425
Views
15
CrossRef citations to date
0
Altmetric
Original Articles

Severe elemental mercury poisoning managed with selenium and N-acetylcysteine administration

ORCID Icon, , &

References

  • Branco V, Godinho-Santos A, Gonçalves J, et al. Mitochondrial thioredoxin system as a primary target for mercury compounds. Toxicol Lett. 2014;Suppl:S57–S58, 229.
  • Branco V, Canario J, Lu J, et al. Mercury and selenium interaction in vivo: effects on thioredoxin reductase and glutathione peroxidase. Free Radical Biol Med. 2012;52:781–793.
  • Branco V, Lu J, Holmgren A, et al. Effect of mercury compounds over the redox state of thioredoxin 1 and 2 and its relation with glutathione levels and glutaredoxin activity in human neuroblastoma cells. Toxicol Lett. 2015;Suppl:s314.
  • Carvalho CML, Chew EH, Hashemy SI, et al. Inhibition of the human thioredoxin system: a molecular mechanism of mercury toxicity. J Biol Chem. 2008;283:11913–11923.
  • 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;9:167–180.
  • Spiller HA. Rethinking mercury: rethinking mercury: the role of selenium in the pathophysiology of mercury toxicity. Clin Toxicol. 2018:56.
  • Ralston NVC, Raymond LJ. Dietray selenium's protective effects against methylmercury toxicity. Toxicology. 2010;278:112–123.
  • Kosnett MJ. The role of chelation in the treatment of arsenic and mercury poisoning. J Med Toxicol. 2013;9:347–354.
  • Carvalho CML, Lu J, Zhang X, et al. Effects of selenite and chelating agents on mammalian thioredoxin reductase inhibited by mercury: implications for treatment of mercury poisoning. FASEB J. 2011;25:370–381.
  • Glaser V, Martins RP, Viera AJH, et al. Diphenyl diselenide administration enhances cortical mitochondrial number and activity by increasing hemeoxygenase type 1 content in a methylmercury-induced neurotoxicity mouse model. Mol Cell Biochem. 2014;390:1–9.
  • Mendelev N, Mehta SL, Idris H, et al. Selenite stimulates mitochondrial biogenesis signaling and enhances mitochondrial functional performance in Murine Hippocampal Neuronal Cells. PloS One. 2012;7:e47910.
  • Meinerz DF, de Paula MT, Comparsi B, et al. Protective effect of organoselenium compounds against methylmercury-induced oxidative stress in mouse brain mitochondrial-enriched fractions. Braz J Med Biol Res. 2011;44:1156–1163.
  • Dalla Corte CL, Soares FAA, Aschner M, et al. Diphenyl diselenide prevents methylmercury-induced mitochondrial dysfunction in rat liver slices. Tetrahedron. 2012;68:10437–10443.
  • Penglase S, Hamre K, Ellingsen S. Selenium prevents downregulation of antioxidant selenoprotein genes by methylmercury. Free Radical Biol Med. 2014;75:95–104.
  • Guerra I, Branco V, Rodrigues J, et al. Protective effects of selenium compounds in the toxicity of mercury over the thioredoxin system in neuroblastoma cells. Toxicol Lett. 2014;229:S101–S102.
  • Joshi D, Mittal DK, Shukla S, et al. Methylmercury toxicity: amelioration by selenium and water-soluble chelators as N-acetyl cysteine and dithiothreitol. Cell Biochem Funct. 2014;32:351–360.
  • Dutczak WJ, Ballatori N. Transport of glutathione-methylmercury across liver canalicular membranes on reduced glutathione carriers. J Biol Chem. 1994;269:9746–9751.
  • Tanaka-Kagawa T, Naganuma A, Imura N. Tubular excretion and reabsorption of mercury compounds in mouse kidney. J Pharmacol Exp Ther. 1993;264:776–782.
  • Wang H, Chen B, He M, et al. Selenocysteine against methylmercury cytotoxicity in HepG2 cells. Sci Rep. 2017;7:147. DOI:10.1038/s41598-017-00231-7
  • Koh AS, Simmon-Willis TA, Pritchard JB, et al. Identification of a mechanism by which the methylmercury antidotes N-acetylcyteine and dimercaptopropanesulfonate enhance urinary metal excretion: transport by the renal organic anion transporter-1. Mol Pharmacol. 2002;62:921–926.
  • Ballatori N, Lieberman MW, Wang W. N-acetylcysteine as an antidote in methylmercury poisoning. Environ Health Perspect. 1998;106:267–271.
  • Madejczyk MS, Aremu DA, Simmon-Willis TA, et al. Accelerated urinary excretion of methylmercury following administration of its antidote N-acetylcysteine requires Mrp2/Abcc2, the atypical multidrug resistant-associated protein. J Pharmacol Exp Ther. 2007;322:378–384.
  • Chen C, Yu H, Zhao J, et al. The roles of serum selenium and selenoproteins on mercury toxicity in environmental and occupational exposure. Environ Health Prespect. 2006;114:297–301.
  • García-Sevillano MA, Rodriguez-Moro G, Garcia-Barrera T, et al. Biological interactions between mercury and selenium in distribution and detoxification process in mice under controlled exposure. Effects of selenoprotein. Chem Biol Interact. 2015;229:82–90.
  • Li YF, Dong Z, Chen C, et al. Organic selenium supplementation increases mercury excretion and decreases oxidative damage in long-term mercury-exposed residents from Wanshan China. Environ Sci Technol. 2012;46:11313–11318.
  • Li X, Yin D, Chen Q, et al. Dietary selenium protects against redox-mediated immune suppression induced by methylmercury exposure. Food Chem Toxicol. 2014;72:169–177.
  • Hursh JB, Clarkson TW, Nowak TV, et al. Prediction of kidney mercury content by isotype techniques. Kidney Int. 1985;27:898–907.