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Oxidation-reduction or redox reactions involve the transfer of electrons from one molecule or atom to another. When an atom gains an electron, another atom must lose an electron, meaning oxidation and reduction must occur together. Since the redox occurs in pairs, the atom that gets oxidized is also called the reducing agent or reductant, and the atom that is reduced is also called the oxidizing agent or oxidant. A straightforward way to remember the definitions of oxidation and reduction is...
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Peroxiredoxin post-translational modifications by redox messengers.

Sylvie Riquier1, Jacques Breton1, Kahina Abbas1

  • 1Institut de Chimie des Substances Naturelles, UPR2301 CNRS, 91190 Gif-sur-yvette, France.

Redox Biology
|July 11, 2014
PubMed
Summary

Hydrogen sulfide (H2S) does not block hydrogen peroxide (H2O2)-induced modifications in 2-Cys peroxiredoxins (Prxs), unlike nitric oxide (NO). Prx2 is protected from peroxide-induced sulfinylation by NO, and Prx1 undergoes S-homocysteinylation.

Keywords:
CSE, cystathionine γ-lyaseCysteine oxidationDEA-NO, diethylamine NONOateDETA-NO, diethylenetriamine NONOateDMEM, Dulbecco’s modified Eagle’s mediumHcy, homocysteineHomocysteinylationHydrogen peroxideMacrophagesNitric oxidePeroxiredoxins

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Area of Science:

  • Biochemistry
  • Cellular Biology
  • Redox Signaling

Background:

  • Peroxiredoxins (Prxs) are crucial thiol peroxidases involved in hydroperoxide detoxification and regulating hydrogen peroxide (H2O2) signaling.
  • Mammalian 2-Cys Prxs (Prx1-4) utilize catalytic cysteines sensitive to reactive oxygen and nitrogen species, acting as redox switches.
  • Understanding how different reactive molecules modify Prxs is key to deciphering cellular redox homeostasis.

Purpose of the Study:

  • To investigate the distinct modifications of 2-Cys Prxs induced by hydrogen peroxide (H2O2), nitric oxide (NO), and hydrogen sulfide (H2S) in RAW264.7 macrophages.
  • To elucidate the differential effects of NO and H2S on H2O2-mediated Prx modifications, particularly sulfinylation.
  • To characterize the specific cysteine modifications on Prx1 and Prx2 under various redox conditions.

Main Methods:

  • Utilized mass spectrometry and immunoblotting to analyze 2-Cys Prx modifications.
  • Separated Prxs using one-dimensional and two-dimensional polyacrylamide gel electrophoresis (PAGE).
  • Exposed murine macrophage cell line RAW264.7 to H2O2, NO donors (Cys-SNO, DETA-NO), and IFN-γ/LPS stimulation.

Main Results:

  • Hydrogen sulfide (H2S) did not prevent H2O2-induced sulfinylation of 2-Cys Prxs.
  • Nitric oxide (NO) protected Prx2 against peroxide-induced sulfinylation, indicating differential regulation.
  • Exposure to NO resulted in an acidic form of Prx1, consistent with S-homocysteinylation of its peroxidatic cysteine.

Conclusions:

  • NO and H2S exhibit distinct regulatory roles in modulating 2-Cys Prx redox states.
  • Prx2 shows higher sensitivity to NO-mediated protection against oxidative stress.
  • S-homocysteinylation of Prx1 is a novel NO-induced modification impacting Prx function in macrophages.