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The effect of bacteria and serum on superoxide production by granulocytes
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In this paper, the effect of bacteria and serum on O-dependent cytochrome c reduction by granulocytes is described, and it is shown that the reduction of extracellular cytochromychrome c was greatly diminished by superoxide dismutase, an enzyme catalyzing the conversion of superoxide to hydrogen peroxide and oxygen.Abstract:
A B S T R A C T We previously reported that granulocytes are able to produce superoxide (02-), a highly reactive compound formed by the one-electron reduction of oxygen. The demonstration of 02- production was based on the observation that the reduction of extracellular cytochrome c by granulocytes was greatly diminished by superoxide dismutase, an enzyme catalyzing the conversion of 02- to hydrogen peroxide and oxygen. In the present report, studies concerning the effect of bacteria and serum on O-dependent cytochrome c reduction by granulocytes are described. In the absence of bacteria, the 02-dependent reduction of extracellular cytochrome c by granulocytes under optimal assay conditions amounted to 9.2±2.8 SD nmol/3 X 106 cells/20 min. When bacteria (100 organisms/cell) were present, the 02-dependent cytochrome c reduction under otherwise similar conditions increased by a factor of nearly four (34.5+9.4). There was no effect of albumin or catalase on cytochrome c reduction, and boiled dismutase had only a small effect. Omission of granulocytes or substitution of live cells by cells killed by heat abolished 02-dependent cytochrome c reduction. Bacteria killed by autoclaving were almost as effective as live bacteria in stimulating granulocyte 02- production. Measurements of particle uptake and 02 uptake by granulocytes indicated that superoxide dismutase did not affect granulocyte metabolism nonspecifically, supporting the conclusion that the diminution of cytochrome c reduction in the presence of dismutase was due to the destruction of 02 by this enzyme. Stimulation of 02- production by bacteria was strongly dependent on the presence of serum in the incubationread more
Citations
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Oxygen-dependent microbial killing by phagocytes (second of two parts).
TL;DR: Since Metschnikoff's discovery, hundreds of scientists studying dozens of species have reported thousands of studies on these cells, perhaps the most widely recognized of which are those of the eminent English scientists.
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Involvement of superoxide anion generation in the hypersensitive response of potato tuber tissues to infection with an incompatible race of Phytophthora infestans and to the hyphal wall components
TL;DR: Results indicate that an O 2 − -generating system may be activated in potato tissues during the incompatible interaction induced by invading fungi or fungal wall components, and also that the generation of O 1 − may be involved during hypersensitive cell death as a trigger of the sequence of resistance reactions.
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Complement and immunoglobulins stimulate superoxide production by human leukocytes independently of phagocytosis.
TL;DR: Since enhanced O-2 production was stimulated by immune reactants in the absence of phagocytosis, the O-.2 generating system is very likely associated with the external plasma membrane of the polymorphonuclear leukocyte.
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The role of superoxide anion generation in phagocytic bactericidal activity. Studies with normal and chronic granulomatous disease leukocytes.
Richard B. Johnston,Bernard B. Keele,Hara P. Misra,J E Lehmeyer,L S Webb,R L Baehner,K.V. Rajagopalan +6 more
TL;DR: It would seem clear from these and other studies that the granulo cyte elaborates O2- as a concomitant of the respiratory burst that occurs with phagocytosis, and a requirement for .OH in thephagocytic bactericidal event might explain the apparent requirement for both O1- and H2O2 for such activity.
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Localization of NADH oxidase on the surface of human polymorphonuclear leukocytes by a new cytochemical method.
TL;DR: These findings, combined with oxygen consumption studies on resting and stimulated PMN in the presence or absence of NADH, indicate that NADH oxidase is a surface enzyme in human PMN, which is internalized duringphagocytosis and retains its peroxide-generating capacity within the phagocytic vacuole.
References
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Superoxide Dismutase AN ENZYMIC FUNCTION FOR ERYTHROCUPREIN (HEMOCUPREIN)
Joe M. McCord,Irwin Fridovich +1 more
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In Vitro Bactericidal Capacity of Human Polymorphonuclear Leukocytes: Diminished Activity in Chronic Granulomatous Disease of Childhood
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The c3-activator system: an alternate pathway of complement activation
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