Inhibition of erythrocyte's catalase, glutathione peroxidase or peroxiredoxin 2 - Impact on cytosol and membrane.

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  • Additional Information
    • Source:
      Publisher: Elsevier Country of Publication: United States NLM ID: 0372430 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1096-0384 (Electronic) Linking ISSN: 00039861 NLM ISO Abbreviation: Arch Biochem Biophys Subsets: MEDLINE
    • Publication Information:
      Publication: <2000- > : San Diego, CA : Elsevier
      Original Publication: New York, NY : Academic Press
    • Subject Terms:
      Antioxidants*/metabolism ; Peroxiredoxins*/metabolism; Catalase/metabolism ; Glutathione Peroxidase/metabolism ; Hydrogen Peroxide/metabolism ; Cytosol/metabolism ; Erythrocytes/metabolism ; Oxidative Stress ; Lipid Peroxidation ; Superoxide Dismutase/metabolism
    • Abstract:
      Catalase (CAT), glutathione peroxidase (GPx) and Prx2 (peroxiredoxin 2) are the main antioxidant enzymatic defenses of erythrocytes. They prevent and minimize oxidative injuries in red blood cell (RBC) components, which are continuously exposed to oxidative stress (OS). The crosstalk between CAT, GPx and Prx2 is still not fully disclosed, as well as why these typically cytoplasmic enzymes bind to the RBC membrane. Our aim was to understand the interplay between CAT, GPx and Prx2 in the erythrocyte's cytosol and membrane. Under specific (partial) inhibition of each enzyme and increasing H 2 O 2 -induced OS conditions, we evaluated the enzyme activities and amounts, the binding of CAT, GPx and Prx2 to RBC membrane, and biomarkers of OS, such as the reduced and oxidized glutathione levels, thiobarbituric acid reactive substances (TBARS) levels, membrane bound hemoglobin and total antioxidant status. Our results support the hypothesis that when high levels of H 2 O 2 get within the erythrocyte, CAT is the main player in the antioxidant protection of the cell, while Prx2 and GPx have a less striking role. Moreover, we found that CAT, appears to have more importance in the antioxidant protection of cytoplasm than of the membrane components, since when the activity of CAT is disturbed, GPx and Prx2 are both activated in the cytosol and mobilized to the membrane. In more severe OS conditions, the antioxidant activity of GPx is more significant at the membrane, as we found that GPx moves from the cytosol to the membrane, probably to protect it from lipid peroxidation.
      Competing Interests: Declaration of competing interest The authors report no declarations of interest.
      (Copyright © 2023 Elsevier Inc. All rights reserved.)
    • Contributed Indexing:
      Keywords: Catalase; Erythrocyte membrane; Glutathione peroxidase; Oxidative stress; Peroxiredoxin 2
    • Accession Number:
      EC 1.11.1.6 (Catalase)
      0 (Antioxidants)
      EC 1.11.1.9 (Glutathione Peroxidase)
      EC 1.11.1.15 (Peroxiredoxins)
      BBX060AN9V (Hydrogen Peroxide)
      EC 1.15.1.1 (Superoxide Dismutase)
    • Publication Date:
      Date Created: 20230314 Date Completed: 20230404 Latest Revision: 20230425
    • Publication Date:
      20231215
    • Accession Number:
      10.1016/j.abb.2023.109569
    • Accession Number:
      36918042