ZFIN ID: ZDB-PUB-140730-22
Selenium prevents downregulation of antioxidant selenoprotein genes by methylmercury
Penglase, S., Hamre, K., Ellingsen, S.
Date: 2014
Source: Free radical biology & medicine   75: 95-104 (Journal)
Registered Authors: Ellingsen, Ståle
Keywords: Methylmercury, Selenium, Selenoprotein, Toxicity, Zebrafish
MeSH Terms:
  • Animals
  • Antioxidants/pharmacology*
  • Down-Regulation
  • Glutathione Peroxidase/genetics
  • Glutathione Peroxidase/metabolism
  • Iodide Peroxidase/genetics
  • Methionine Sulfoxide Reductases/genetics
  • Methylmercury Compounds/pharmacology*
  • Phosphotransferases/genetics
  • RNA, Messenger/biosynthesis*
  • Selenium/pharmacology*
  • Selenoproteins/genetics*
  • Thioredoxin-Disulfide Reductase/genetics
  • Water Pollutants, Chemical
  • Zebrafish
PubMed: 25064324 Full text @ Free Radic. Biol. Med.
ABSTRACT
Selenium (Se) is an essential nutrient required in Se-dependent proteins, termed selenoproteins. The selenoprotein family is small but diverse, and includes key proteins in antioxidant, redox signalling, thyroid hormone metabolism and protein folding pathways. Methylmercury (MeHg) is a toxic environmental contaminant that affects seafood safety. Selenium can reduced MeHg toxicity, but it is unclear how selenoproteins are affected in this interaction. In this study we explored how Se and MeHg interact to affect the mRNA expression of selenoprotein genes in whole zebrafish (Danio rerio) embryos. Embryos were obtained from adult zebrafish fed MeHg with or without elevated Se in a 2×2 factorial design. The embryo mRNA levels of 30 selenoprotein genes were then measured. These genes cover most of the selenoprotein families; including members of the glutathione peroxidase (GPX), thioredoxin reductase, iodothyronine deiodinase and methionine sulfoxide reductase families, along with selenophosphate synthetase 2, selenoprotein H, J-P, T, W, sep15, fep15 and fam213aa. GPX enzyme activity and larval locomotor activity were also measured. We found that around one quarter of the selenoprotein genes were downregulated by elevated MeHg. These downregulated genes were dominated by selenoproteins from antioxidant pathways that are also susceptible to Se deficiency induced downregulation. MeHg also decreased GPX activity and induced larval hypoactivity. Elevated Se partially prevented MeHg-induced disruption of selenoprotein gene mRNA levels, GPX activity and larval locomotor activity. Overall, the MeHg-induced downregulation and subsequent rescue by elevated Se levels of selenogenes regulated by Se status suggests that Se deficiency is a contributing factor to MeHg toxicity.
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