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Selenium and the thioredoxin and glutaredoxin systems

M Björnstedt1, S Kumar, L Björkhem

  • 1Medical Nobel Institute for Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.

Biomedical and Environmental Sciences : BES
|October 7, 1997
PubMed
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The thioredoxin (Trx) system, including thioredoxin reductase (TR), efficiently reduces selenium compounds and influences cellular redox balance. Mammalian TR

Area of Science:

  • Biochemistry and Molecular Biology
  • Redox Biology
  • Selenium Metabolism

Background:

  • The thioredoxin (Trx) system, comprising Trx, thioredoxin reductase (TR), and NADPH, is crucial for DNA synthesis and protein redox regulation.
  • Selenium compounds, including selenite, selenodiglutathione (GS-Se-SG), and selenocystine, are substrates for the Trx system and mammalian TR.
  • Mammalian TR is homologous to glutathione reductase and contains a selenocysteine residue essential for its function.

Purpose of the Study:

  • To investigate the interactions between selenium compounds and the Trx system, particularly mammalian TR.
  • To elucidate the enzymatic mechanisms by which TR reduces selenium compounds and lipid hydroperoxides.
  • To explore the biological implications of selenocysteine in mammalian TR, including substrate specificity and cellular proliferation.

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Main Methods:

  • Enzymatic assays to determine the reduction of selenite, GS-Se-SG, selenocystine, and lipid hydroperoxides by Trx and TR.
  • Measurement of NADPH oxidation and kinetic parameters (Km, kcat) for TR-mediated reactions.
  • Analysis of the effects of selenium compounds and TR on transcription factor AP-1 DNA-binding and lipoxygenase activity.

Main Results:

  • Mammalian TR efficiently reduces selenocystine to selenocysteine with kinetics similar to its natural substrate, Trx-S2.
  • TR-mediated reduction of selenite and GS-Se-SG leads to selenide formation, causing significant NADPH oxidation.
  • TR directly reduces lipid hydroperoxides, a reaction enhanced by selenocysteine; selenide inhibits lipoxygenase activity.

Conclusions:

  • The Trx system and mammalian TR play significant roles in selenium metabolism and redox homeostasis.
  • The presence of selenocysteine in mammalian TR contributes to its broad substrate specificity and is vital for cell proliferation.
  • Selenium compounds can modulate cellular signaling pathways, including AP-1 DNA-binding and lipoxygenase activity.