Literature DB >> 2824562

Human red cells scavenge extracellular hydrogen peroxide and inhibit formation of hypochlorous acid and hydroxyl radical.

C C Winterbourn1, A Stern.   

Abstract

The ability of intact human red cells to scavenge extracellularly generated H2O2 and O2-, and to prevent formation of hydroxyl radicals and hypochlorous acid has been examined. Red cells inhibited oxidation of ferrocytochrome c by H2O2. Cells treated with aminotriazole no longer inhibited, indicating that protection was almost entirely due to intracellular catalase. Contribution by the GSH system was slight, and apparent only with low H2O2 concentrations when catalase was inhibited by aminotriazole. The cells were about a quarter as efficient at inhibiting cytochrome c oxidation as an equivalent concentration of purified catalase. No inhibition of O2(-)-dependent reduction of ferricytochrome c or nitroblue tetrazolium was observed, although extracted red cell superoxide dismutase inhibited nitroblue tetrazolium reduction at one fortieth the concentration of that in the cells. Red cells efficiently inhibited deoxyribose oxidation by hydroxyl radicals generated from H2O2, O2- and Fe(EDTA), and myeloperoxidase-dependent oxidation of methionine to methionine sulfoxide by stimulated neutrophils. Most of the red cell inhibition of hydroxyl radical production, and all the inhibition of methionine oxidation, was prevented by blocking intracellular catalase with aminotriazole. Thus red cells are able to efficiently scavenge H2O2, but not O2-, produced in their environment, and to inhibit formation of hydroxyl radicals and hypochlorous acid. They may therefore have an important role in extracellular antioxidant defense.

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Year:  1987        PMID: 2824562      PMCID: PMC442408          DOI: 10.1172/JCI113230

Source DB:  PubMed          Journal:  J Clin Invest        ISSN: 0021-9738            Impact factor:   14.808


  24 in total

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6.  Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation.

Authors:  S J Weiss; R Klein; A Slivka; M Wei
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7.  Superoxide dismutase in extracellular fluids.

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8.  Oxidation of methionine by human polymorphonuclear leukocytes.

Authors:  M F Tsan; J W Chen
Journal:  J Clin Invest       Date:  1980-05       Impact factor: 14.808

9.  Oxidation of amino acids by human neutrophils.

Authors:  M F Tsan; R C Denison
Journal:  Inflammation       Date:  1981-12       Impact factor: 4.092

10.  Primaquine-mediated oxidative metabolism in the human red cell. Lack of dependence on oxyhemoglobin, H2O2 formation, or glutathione turnover.

Authors:  S N Kelman; S G Sullivan; A Stern
Journal:  Biochem Pharmacol       Date:  1982-07-15       Impact factor: 5.858

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  26 in total

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4.  Degradation of methyl and ethyl mercury into inorganic mercury by oxygen free radical-producing systems: involvement of hydroxyl radical.

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5.  Ontogeny of erythroid gene expression.

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Review 6.  Exercise, training and red blood cell turnover.

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8.  The effects of disruption of genes for peroxiredoxin-2, glutathione peroxidase-1, and catalase on erythrocyte oxidative metabolism.

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9.  Rickettsia rickettsii induces superoxide radical and superoxide dismutase in human endothelial cells.

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Review 10.  Redox modification of proteins as essential mediators of CNS autophagy and mitophagy.

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