Role of monochloramine in the oxidation of erythrocyte hemoglobin by stimulated neutrophils

M. B. Grisham, M. M. Jefferson, Edwin Thomas

Research output: Contribution to journalArticle

110 Citations (Scopus)

Abstract

Stimulation of the oxygen (O2) metabolism of isolated human neutrophilic leukocytes resulted in oxidation of hemoglobin of autologous erythrocytes without erythrocyte lysis. Hb oxidation could be accounted for by reduction of O2 to superoxide (O2-) by the neutrophils, dismutation of O2- to yield hydrogen peroxide (H2O2), myeloperoxidase-catalyzed oxidation of chloride (Cl-) by H2O2 to yield hypochlorous acid (HOCl), the reaction of HOCl with endogenous ammonia (NH4+) to yield monochloramine (NH2Cl), and the oxidative attack of NH2Cl on erythrocytes. NH2Cl was detected when HOCl reacted with the NH4+ and other substances released into the medium by neutrophils. The amount of NH4+ released was sufficient to form the amount of NH2Cl required for the observed Hb oxidation. Oxidation was increased by adding myeloperoxidase or NH4+ to increase NH2Cl formation. Due to the volatility of NH2Cl, Hb was oxidized when neutrophils and erythrocytes were incubated separately in a closed container. Oxidation was decreased by adding catalase to eliminate H2O2, dithiothreitol to reduce HOCl and NH2Cl, or taurine to react with HOCl or NH2Cl to yield taurine monochloramine. NH2Cl was up to 50 times more effective than H2O2, HOCl, or taurine monochloramine as an oxidant for erythrocyte Hb, whereas HOCl was up to 10 times more effective than NH2Cl as a lytic agent. NH2Cl contributes to oxidation of erythrocyte components by stimulated neutrophils and may contribute to other forms of neutrophil oxidative cytotoxicity.

Original languageEnglish (US)
Pages (from-to)6757-6765
Number of pages9
JournalJournal of Biological Chemistry
Volume259
Issue number11
StatePublished - 1984
Externally publishedYes

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Hypochlorous Acid
Hemoglobins
Neutrophils
Erythrocytes
Oxidation
Peroxidase
Volatilization
Dithiothreitol
Taurine
Cytotoxicity
chloramine
Ammonia
Oxidants
Metabolism
Superoxides
Catalase
Hydrogen Peroxide
Containers
Chlorides
Leukocytes

All Science Journal Classification (ASJC) codes

  • Biochemistry

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Role of monochloramine in the oxidation of erythrocyte hemoglobin by stimulated neutrophils. / Grisham, M. B.; Jefferson, M. M.; Thomas, Edwin.

In: Journal of Biological Chemistry, Vol. 259, No. 11, 1984, p. 6757-6765.

Research output: Contribution to journalArticle

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N2 - Stimulation of the oxygen (O2) metabolism of isolated human neutrophilic leukocytes resulted in oxidation of hemoglobin of autologous erythrocytes without erythrocyte lysis. Hb oxidation could be accounted for by reduction of O2 to superoxide (O2-) by the neutrophils, dismutation of O2- to yield hydrogen peroxide (H2O2), myeloperoxidase-catalyzed oxidation of chloride (Cl-) by H2O2 to yield hypochlorous acid (HOCl), the reaction of HOCl with endogenous ammonia (NH4+) to yield monochloramine (NH2Cl), and the oxidative attack of NH2Cl on erythrocytes. NH2Cl was detected when HOCl reacted with the NH4+ and other substances released into the medium by neutrophils. The amount of NH4+ released was sufficient to form the amount of NH2Cl required for the observed Hb oxidation. Oxidation was increased by adding myeloperoxidase or NH4+ to increase NH2Cl formation. Due to the volatility of NH2Cl, Hb was oxidized when neutrophils and erythrocytes were incubated separately in a closed container. Oxidation was decreased by adding catalase to eliminate H2O2, dithiothreitol to reduce HOCl and NH2Cl, or taurine to react with HOCl or NH2Cl to yield taurine monochloramine. NH2Cl was up to 50 times more effective than H2O2, HOCl, or taurine monochloramine as an oxidant for erythrocyte Hb, whereas HOCl was up to 10 times more effective than NH2Cl as a lytic agent. NH2Cl contributes to oxidation of erythrocyte components by stimulated neutrophils and may contribute to other forms of neutrophil oxidative cytotoxicity.

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