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Thioredoxin and glutaredoxin regulate metabolism through different multiplex thiol switches.

M J López-Grueso1, R González-Ojeda2, R Requejo-Aguilar1

  • 1Dept. Biochemistry and Molecular Biology, University of Córdoba, Córdoba, Spain; Maimónides Biomedical Research Institute of Córdoba (IMIBIC), Córdoba, Spain.

Redox Biology
|January 15, 2019
PubMed
Summary

Thioredoxin (Trx) and Glutaredoxin (Grx) regulate metabolic thiol redox balance, impacting protein targets and cellular metabolism differently. Their downregulation reveals distinct metabolic shifts and highlights the sensitivity of cellular redox equilibrium.

Keywords:
GlycolysisNO synthaseRedox proteomeRedoxinsS-nitrosationThiol redox regulation

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Area of Science:

  • Cellular and Molecular Biology
  • Biochemistry
  • Redox Biology

Background:

  • Metabolic thiol redox regulation is crucial for cellular function.
  • Thioredoxin (Trx) and Glutaredoxin (Grx) are key players in maintaining redox homeostasis.
  • Understanding their specific roles and targets is essential for comprehending cellular responses to oxidative stress.

Purpose of the Study:

  • To define the roles of Trx and Grx in metabolic thiol redox regulation.
  • To identify specific protein and metabolite targets of Trx and Grx.
  • To investigate the metabolic consequences of Trx and Grx downregulation in a hepatocarcinoma cell model.

Main Methods:

  • Utilized the hepatocarcinoma-derived HepG2 cell line.
  • Employed overexpression of nitric oxide synthase (NOS3) to induce oxidative/nitrosative conditions.
  • Performed silencing of Grx1 or Trx1 (siRNA) to assess their impact on redox proteome and metabolism.

Main Results:

  • Silencing of Grx1 or Trx1 significantly altered the redox proteome, affecting cysteine oxidation states in glycolytic enzymes.
  • Identified novel Grx1 targets: Cys91 of peroxiredoxin-6 (PRDX6) and Cys153 of phosphoglycerate mutase-1 (PGAM1).
  • Observed distinct metabolic shifts: Trx1 silencing increased glycolysis and sphingolipid levels, while Grx1 silencing decreased glycolysis and promoted fatty acid synthesis.

Conclusions:

  • Trx and Grx possess both common and distinct protein cysteine redox targets.
  • Downregulation of Trx or Grx leads to markedly different metabolic outcomes, underscoring their specific regulatory functions.
  • Cellular redox equilibrium is highly sensitive to changes in redoxin levels, making metabolic responses difficult to predict.