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Aminoglycosides decrease glutathione peroxidase-1 activity by interfering with selenocysteine incorporation.

Diane E Handy1, Gaozhen Hang, John Scolaro

  • 1Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115, USA. dhandy@rics.bwh.harvard.edu

The Journal of Biological Chemistry
|December 16, 2005
PubMed
Summary
This summary is machine-generated.

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The aminoglycoside G418 affects glutathione peroxidase by promoting UGA codon read-through, leading to arginine substitution for selenocysteine and reduced enzyme activity.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Cellular glutathione peroxidase (GPx) is a crucial intracellular antioxidant enzyme.
  • GPx activity relies on a selenocysteine residue at its active site, requiring specific translational machinery for its incorporation.
  • Aminoglycoside antibiotics, like G418, are known to promote read-through of stop codons.

Purpose of the Study:

  • To investigate the impact of the aminoglycoside G418 on the expression and function of cellular glutathione peroxidase in mammalian cells.
  • To determine if G418 influences selenocysteine incorporation at the UGA codon within the GPx mRNA.
  • To elucidate the molecular mechanisms by which G418 affects GPx biosynthesis.

Main Methods:

  • Utilized a reporter construct with a selenocysteine incorporation element and a UGA codon to assess read-through.

Related Experiment Videos

  • Administered G418 to mammalian cells under varying selenium conditions.
  • Quantified GPx expression via immunoassay and enzyme activity assays.
  • Employed tandem mass spectrometry to identify amino acid substitutions at the UGA codon.

    • Main Results:

    • G418 enhanced UGA codon read-through, both in the presence and absence of selenium.
    • G418 treatment increased the levels of immunodetectable glutathione peroxidase.
    • Specific activity of glutathione peroxidase was decreased following G418 treatment.
    • Mass spectrometry revealed that G418 induced an l-arginine substitution for selenocysteine at the UGA codon.

    Conclusions:

    • G418 significantly affects glutathione peroxidase biosynthesis by promoting non-canonical read-through of the selenocysteine UGA codon.
    • This read-through results in the incorporation of arginine instead of selenocysteine, compromising the enzyme's antioxidant function.
    • G418 represents a novel modulator of selenocysteine incorporation and antioxidant enzyme activity.