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Neutrophil-mediated methemoglobin formation in the erythrocyte. The role of superoxide and hydrogen peroxide.

Abstract

Human neutrophils incubated with phorbol myristate acetate oxidized hemoglobin within the intact erythrocyte by a mechanism dependent on cell-cell contact but independent of phagocytosis. Spectrophotometric examination of the erythrocyte lysates revealed that the major component formed was methemoglobin along with small amounts of a species with spectral characteristics similar to choleglobin. Methemoglobin formation was directly related to the neutrophil concentration and the time of incubation. The addition of superoxide dismutase or catalase modestly inhibited the formation of methemoglobin, while a combination of the enzymes provided the most dramatic protection. Methemoglobin of hydroxyl radical or hypochlorous acid scavengers. Apparently, either O2.- or H2O2 alone was capable of mediating methemoglobin formation in the intact erythrocyte. Maintenance of the intraerythrocytic hemoglobin in its oxygenated state or its derivatization to carbon monoxyhemoglobin markedly inhibited methemoglobin formation. Blockade of the anion channels in the intact erythrocyte with sulfonated stilbenes inhibited O2.- but not H2O2 from oxidizing intracellular hemoglobin. It appears that neutrophil-derived O2.- and H2O2 can cross the erythrocyte membrane through the anion channel or diffuse directly into the intracellular space and react with oxyhemoglobin or deoxyhemoglobin to form a mixture of hemoglobin oxidation products within the intact cell.

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    Source

    The Journal of biological chemistry 257:6 1982 Mar 25 pg 2947-53

    MeSH

    Carbon Monoxide
    Cyanides
    Dithionite
    Erythrocytes
    Humans
    Hydrogen Peroxide
    Kinetics
    Methemoglobin
    Neutrophils
    Oxygen
    Oxygen Consumption
    Spectrophotometry
    Superoxides
    Tetradecanoylphorbol Acetate

    Pub Type(s)

    Journal Article
    Research Support, U.S. Gov't, P.H.S.

    Language

    eng

    PubMed ID

    6277918

    Citation

    Weiss, S J.. "Neutrophil-mediated Methemoglobin Formation in the Erythrocyte. the Role of Superoxide and Hydrogen Peroxide." The Journal of Biological Chemistry, vol. 257, no. 6, 1982, pp. 2947-53.
    Weiss SJ. Neutrophil-mediated methemoglobin formation in the erythrocyte. The role of superoxide and hydrogen peroxide. J Biol Chem. 1982;257(6):2947-53.
    Weiss, S. J. (1982). Neutrophil-mediated methemoglobin formation in the erythrocyte. The role of superoxide and hydrogen peroxide. The Journal of Biological Chemistry, 257(6), pp. 2947-53.
    Weiss SJ. Neutrophil-mediated Methemoglobin Formation in the Erythrocyte. the Role of Superoxide and Hydrogen Peroxide. J Biol Chem. 1982 Mar 25;257(6):2947-53. PubMed PMID: 6277918.
    * Article titles in AMA citation format should be in sentence-case
    TY - JOUR T1 - Neutrophil-mediated methemoglobin formation in the erythrocyte. The role of superoxide and hydrogen peroxide. A1 - Weiss,S J, PY - 1982/3/25/pubmed PY - 1982/3/25/medline PY - 1982/3/25/entrez SP - 2947 EP - 53 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 257 IS - 6 N2 - Human neutrophils incubated with phorbol myristate acetate oxidized hemoglobin within the intact erythrocyte by a mechanism dependent on cell-cell contact but independent of phagocytosis. Spectrophotometric examination of the erythrocyte lysates revealed that the major component formed was methemoglobin along with small amounts of a species with spectral characteristics similar to choleglobin. Methemoglobin formation was directly related to the neutrophil concentration and the time of incubation. The addition of superoxide dismutase or catalase modestly inhibited the formation of methemoglobin, while a combination of the enzymes provided the most dramatic protection. Methemoglobin of hydroxyl radical or hypochlorous acid scavengers. Apparently, either O2.- or H2O2 alone was capable of mediating methemoglobin formation in the intact erythrocyte. Maintenance of the intraerythrocytic hemoglobin in its oxygenated state or its derivatization to carbon monoxyhemoglobin markedly inhibited methemoglobin formation. Blockade of the anion channels in the intact erythrocyte with sulfonated stilbenes inhibited O2.- but not H2O2 from oxidizing intracellular hemoglobin. It appears that neutrophil-derived O2.- and H2O2 can cross the erythrocyte membrane through the anion channel or diffuse directly into the intracellular space and react with oxyhemoglobin or deoxyhemoglobin to form a mixture of hemoglobin oxidation products within the intact cell. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/6277918/Neutrophil_mediated_methemoglobin_formation_in_the_erythrocyte__The_role_of_superoxide_and_hydrogen_peroxide_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=6277918 DB - PRIME DP - Unbound Medicine ER -