scholarly journals Macrophage variants in oxygen metabolism.

1980 ◽  
Vol 152 (4) ◽  
pp. 808-822 ◽  
Author(s):  
G Damiani ◽  
C Kiyotaki ◽  
W Soeller ◽  
M Sasada ◽  
J Peisach ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Cytochrome C ◽  
Superoxide Anion ◽  
Oxygen Metabolism ◽  
Hexose Monophosphate ◽  
Phagocytic Cells ◽  
Form Complex ◽  
Hexose Monophosphate Shunt ◽  
Cytochrome C Reduction ◽  
Generate Superoxide Anion

Whereas phagocytic cells from normal individuals have the capacity to kill ingested bacteria and parasites, those from patients with several uncommon genetic deficiency diseases are known to be defective in bactericidal activity. Studies on neutrophils of these patients have revealed fundamental defects in their ability to reduce molecular oxygen and metabolize it to superoxide anion, hydrogen peroxide, and oxygen radicals. In the present experiments, we describe a clone of a continuous murine macrophage-like cell line, J774.16, that, upon appropriate stimulation, activates the hexose monophosphate shunt, and produces superoxide anion and hydrogen peroxide. With nitroblue tetrazolium to select against cells capable of being stimulated by phorbol myristate acetate to reduce the dye to polymer--formazan--which is toxic fot cells, we have selected for variants that are defective in oxygen metabolism. Four of these subclones have been characterized and found to be lacking in the ability (a) to generate superoxide anion, as measured by cytochrome c reduction; (b) to produce hydrogen peroxide, as measured by the ability to form complex I with cytochrome c peroxidase; and (c) to be stimulated to oxidize glucose via the hexose monophosphate shunt. These variants appear to represent a useful model for studying the molecular basis for macrophage cytocidal activity.

Detection of superoxide anion released extracellularly by endothelial cells using cytochrome c reduction, ESR, fluorescence and lucigenin-enhanced chemiluminescence techniques

2000 ◽  
Vol 29 (5) ◽  
pp. 388-396 ◽  
Author(s):  
Marie-Aline Barbacanne ◽  
Jean-Pierre Souchard ◽  
Benoit Darblade ◽  
Jean-Pierre Iliou ◽  
Françoise Nepveu ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Cytochrome C ◽  
Superoxide Anion ◽  
Enhanced Chemiluminescence ◽  
Cytochrome C Reduction

Release of oxygen products from lung macrophages by N-formyl peptides

1981 ◽  
Vol 50 (4) ◽  
pp. 736-740 ◽  
Author(s):  
A. Holian ◽  
R. P. Daniele
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Anion ◽  
Oxygen Metabolism ◽  
O2 Consumption ◽  
Extracellular Medium ◽  
Fourfold Increase ◽  
Pulmonary Macrophages ◽  
Hydrogen Peroxide Accumulation ◽  
Formyl Peptides

Incubation of guinea pig pulmonary macrophages with N-formylmethionylphenylalanine (FMP) resulted in 1) a rapid increase in O2 consumption and 2) an accumulation of superoxide anion and hydrogen peroxide in the extracellular medium. The accumulation of superoxide anion and hydrogen peroxide was completely prevented in the presence of superoxide dismutase and catalase, respectively. FMP-stimulated O2 consumption and superoxide anion and hydrogen peroxide accumulation were proportional to the macrophage concentration, showed similar dependence on FMP concentration, had nearly identical kinetics, and were partially abolished by antimycin A, an inhibitor of mitochondrial respiration. FMP also stimulated a three- to fourfold increase in hexose monophosphate shunt (HMS) activity. Catalase had no effect on the amount of glucose oxidized by the HMS, indicating that removal of hydrogen peroxide was without effect on the observed HMS activity. Since FMP is similar in structure to the oligopeptides of bacterial metabolism, its ability to stimulate the release of these microbiocidal products of oxygen metabolism may be important in vivo.

scholarly journals Rhodanese Rdl2 produces reactive sulfur species to scavenge hydroxyl radical and protect mitochondria

2021 ◽  
Author(s):  
Qingda Wang ◽  
Zhigang Chen ◽  
Xi Zhang ◽  
Yuping Xin ◽  
Yongzhen Xia ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Hydrogen Peroxide ◽  
Hydroxyl Radical ◽  
Superoxide Anion ◽  
Fenton Reaction ◽  
Aerobic Respiration ◽  
Oxygen Species ◽  
Sulfur Species ◽  
Ex Ante ◽  
Generate Superoxide Anion

During aerobic respiration, mitochondria generate superoxide anion (O2&middot−), hydrogen peroxide (H2O2), and hydroxyl radical (HO·), and these reactive oxygen species (ROS) are detrimental to mitochondria. Mitochondrial damage is linked to a broad spectrum of pathologies such as Alzheimer's disease, hemochromatosis, and diabetes. Mitochondria contain several enzymes for rapidly removing superoxide anion and hydrogen peroxide, but how they antagonize HO· is elusive, representing a loophole in the anti-ROS system. Herein, we discovered that Rhodanese 2 (Rdl2) is critical for maintaining the functionality and integrity of mitochondria under sub-lethal ROS stress in Saccharomyces cerevisiae. Rdl2 converts stable sulfur species (thiosulfate and dialkyl polysulfide) to reactive sulfane sulfur including persulfide that protects mitochondrial DNA via scavenging HO·. Surprisingly, hydrogen sulfide (H2S) promotes HO· production through stimulating the Fenton reaction, leading to increased DNA damage. Our study may reveal an ex-ante mean for antagonizing HO·, patching the loophole of the anti-ROS system in mitochondria.

scholarly journals Oxidative metabolic responses of rabbit pulmonary alveolar macrophages

Blood ◽  
1979 ◽  
Vol 53 (3) ◽  
pp. 486-491
Author(s):  
LA Boxer ◽  
G Ismail ◽  
JM Allen ◽  
RL Baehner
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Alveolar Macrophages ◽  
Cytochalasin B ◽  
Surface Membrane ◽  
Nitroblue Tetrazolium ◽  
Hexose Monophosphate ◽  
Hexose Monophosphate Shunt ◽  
Opsonized Zymosan ◽  
Ferricytochrome C

During phagocytosis of opsonized lipopolysaccharide-coated paraffin oil droplets, rabbit alveolar macrophages reduced nitroblue tetrazolium, which effect was in part inhibitable with the use of superoxide dismutase. Exposure of cytochalasin-B-treated rabbit alveolar macrophages to opsonized zymosan led to the generation of superoxide, as quantitated by ferricytochrome C reduction. It was found that nitroblue tetrazolium in the presence of ferricytochrome C could in turn serve as scavenger of superoxide during stimulation of cytochalasin-B-treated rabbit alveolar macrophages. Following challenge with either opsonized zymosan or the membrane perturbant digitonin, rabbit alveolar macrophages released hydrogen peroxide into the extracellular medium. Employment of the surface membrane stimulant phorbol myristrate acetate led to activation of the hexose monophosphate shunt, which activity could be further enhanced in the presence of superoxide dismutase or attenuated in the presence of catalase. These studies demonstrate that rabbit alveolar macrophages release superoxide and hydrogen peroxide during surface membrane perturbation. In turn, hydrogen peroxide generation can stimulate the hexose monophosphate shunt.

scholarly journals Oxidative metabolic responses of rabbit pulmonary alveolar macrophages

Blood ◽  
1979 ◽  
Vol 53 (3) ◽  
pp. 486-491 ◽  
Author(s):  
LA Boxer ◽  
G Ismail ◽  
JM Allen ◽  
RL Baehner
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Alveolar Macrophages ◽  
Cytochalasin B ◽  
Surface Membrane ◽  
Nitroblue Tetrazolium ◽  
Hexose Monophosphate ◽  
Hexose Monophosphate Shunt ◽  
Opsonized Zymosan ◽  
Ferricytochrome C

Abstract During phagocytosis of opsonized lipopolysaccharide-coated paraffin oil droplets, rabbit alveolar macrophages reduced nitroblue tetrazolium, which effect was in part inhibitable with the use of superoxide dismutase. Exposure of cytochalasin-B-treated rabbit alveolar macrophages to opsonized zymosan led to the generation of superoxide, as quantitated by ferricytochrome C reduction. It was found that nitroblue tetrazolium in the presence of ferricytochrome C could in turn serve as scavenger of superoxide during stimulation of cytochalasin-B-treated rabbit alveolar macrophages. Following challenge with either opsonized zymosan or the membrane perturbant digitonin, rabbit alveolar macrophages released hydrogen peroxide into the extracellular medium. Employment of the surface membrane stimulant phorbol myristrate acetate led to activation of the hexose monophosphate shunt, which activity could be further enhanced in the presence of superoxide dismutase or attenuated in the presence of catalase. These studies demonstrate that rabbit alveolar macrophages release superoxide and hydrogen peroxide during surface membrane perturbation. In turn, hydrogen peroxide generation can stimulate the hexose monophosphate shunt.

Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space

2001 ◽  
Vol 353 (2) ◽  
pp. 411-416 ◽  
Author(s):  
Derick HAN ◽  
Everett WILLIAMS ◽  
Enrique CADENAS
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Cytochrome C ◽  
Respiratory Chain ◽  
Superoxide Anion ◽  
Complex Iii ◽  
Spin Adduct ◽  
Intermembrane Space ◽  
Epr Signal ◽  
Mitochondrial Respiratory

It has been generally accepted that superoxide anion generated by the mitochondrial respiratory transport chain are vectorially released into the mitochondrial matrix, where they are converted to hydrogen peroxide through the catalytic action of Mn-superoxide dismutase. Release of superoxide anion into the intermembrane space is a controversial topic, partly unresolved by the reaction of superoxide anion with cytochrome c, which faces the intermembrane space and is present in this compartment at a high concentration. This study was aimed at assessing the topological site(s) of release of superoxide anion during respiratory chain activity. To address this issue, mitoplasts were prepared from isolated mitochondria by digitonin treatment to remove portions of the outer membrane along with portions of cytochrome c. EPR analysis in conjunction with spin traps of antimycin-supplemented mitoplasts revealed the formation of a spin adduct of superoxide anion. The EPR signal was (i) abrogated by superoxide dismutase, (ii) decreased competitively by exogenous ferricytochrome c and (iii) broadened by the membrane-impermeable spin-broadening agent chromium trioxalate. These results confirm the production and release of superoxide anion towards the cytosolic side of the inner mitochondrial membrane. In addition, co-treatment of mitoplasts with myxothiazol and antimycin A, resulting in an inhibition of the oxidation of ubiquinol to ubisemiquinone, abolished the EPR signal, thus suggesting that ubisemiquinone autoxidation at the outer site of the complex-III ubiquinone pool is a pathway for superoxide anion formation and subsequent release into the intermembrane space. The generation of superoxide anion towards the intermembrane space requires consideration of the mitochondrial steady-state values for superoxide anion and hydrogen peroxide, the decay pathways of these oxidants in this compartment and the implications of these processes for cytosolic events.

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