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Selenoprotein W is a glutathione-dependent antioxidant in vivo.

Abstract
The function of selenoprotein W (Se-W) was investigated by cloning the corresponding cDNA from mouse brain and expressing it in CHO cells and H1299 human lung cancer cells. Overexpression of Se-W markedly reduced the sensitivity of both cell lines to H2O2 cytotoxicity. The intracellular peroxide concentration of the transfected cells was lower than that of the parental cells in the absence or presence of extracellular H2O2. The resistance to oxidative stress conferred by Se-W was dependent on glutathione. Expression of Se-W mutants in which selenocysteine-13 or cysteine-37 was replaced by serine did not confer resistance to H2O2, implicating these residues in the antioxidant activity of Se-W in vivo.
AuthorsDae won Jeong, Tae Soo Kim, Youn Wook Chung, Byeong Jae Lee, Ick Young Kim
JournalFEBS letters (FEBS Lett) Vol. 517 Issue 1-3 Pg. 225-8 (Apr 24 2002) ISSN: 0014-5793 [Print] England
PMID12062442 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Antioxidants
  • DNA, Complementary
  • Peroxides
  • Proteins
  • SELENOW protein, human
  • Selenoprotein W
  • Selenoproteins
  • Selenocysteine
  • Hydrogen Peroxide
  • Glutathione
Topics
  • Animals
  • Antioxidants (metabolism)
  • CHO Cells (drug effects, metabolism)
  • Cloning, Molecular
  • Cricetinae
  • DNA, Complementary (genetics, isolation & purification)
  • Glutathione (metabolism)
  • Humans
  • Hydrogen Peroxide (toxicity)
  • Peroxides (analysis, metabolism)
  • Proteins (genetics, metabolism)
  • Selenocysteine (metabolism)
  • Selenoprotein W
  • Selenoproteins
  • Transfection
  • Tumor Cells, Cultured

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