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Research Article Free access | 10.1172/JCI106507
Department of Biochemistry, University of Pittsburgh, School of Medicine, Pittsburgh, Pennsylvania 15213
Department of Medicine, University of Pittsburgh, School of Medicine, Pittsburgh, Pennsylvania 15213
Find articles by Vogt, M. in: JCI | PubMed | Google Scholar
Department of Biochemistry, University of Pittsburgh, School of Medicine, Pittsburgh, Pennsylvania 15213
Department of Medicine, University of Pittsburgh, School of Medicine, Pittsburgh, Pennsylvania 15213
Find articles by Thomas, C. in: JCI | PubMed | Google Scholar
Department of Biochemistry, University of Pittsburgh, School of Medicine, Pittsburgh, Pennsylvania 15213
Department of Medicine, University of Pittsburgh, School of Medicine, Pittsburgh, Pennsylvania 15213
Find articles by Vassallo, C. in: JCI | PubMed | Google Scholar
Department of Biochemistry, University of Pittsburgh, School of Medicine, Pittsburgh, Pennsylvania 15213
Department of Medicine, University of Pittsburgh, School of Medicine, Pittsburgh, Pennsylvania 15213
Find articles by Basford, R. in: JCI | PubMed | Google Scholar
Department of Biochemistry, University of Pittsburgh, School of Medicine, Pittsburgh, Pennsylvania 15213
Department of Medicine, University of Pittsburgh, School of Medicine, Pittsburgh, Pennsylvania 15213
Find articles by Gee, J. in: JCI | PubMed | Google Scholar
Published February 1, 1971 - More info
Phagocytosis by rabbit alveolar macrophages (AM) is accompanied by increases in O2 consumption, glucose oxidation, and H2O2 formation. Two aspects of the interrelations between these metabolic features of phagocytosis have been studied.
First, the following evidence indicates that glutathione, glutathione reductase, and peroxidase serve as a cytoplasmic shuttle between H2O2 and NADPH-dependent glucose oxidation: (a) AM contain 5.9 mμmoles of reduced glutathione per 106 cells and exhibit glutathione peroxidase and NADPH-specific glutathione reductase activity; (b) oxidized glutathione potentiates NADP stimulation of glucose oxidation; (c) an artificial H2O2-generating system stimulates glucose oxidation; (d) the cell penetrating thiol inhibitor, N-ethylmaleimide diminishes glucose oxidation. This effect largely depends on inhibition of the glutathione system rather than on inhibition of either H2O2 formation or enzymes directly subserving glucose oxidation.
Second, three potential H2O2-generating oxidases have been sought. No cyanide-insensitive NADH or NADPH oxidase activity could be detected. D-amino acid oxidase activity was 0.48 ±0.07 U/106 cells with D-alanine as substrate.