Nature of the oxygen species generated by xanthine oxidase involved in secretory histamine release from mast cells

1989 ◽  
Vol 67 (8) ◽  
pp. 397-403 ◽  
Author(s):  
I. Aravind Menon ◽  
Shaila Shirwadkar ◽  
Narendranath S. Ranadive
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Mast Cells ◽  
Xanthine Oxidase ◽  
Cell Lysis ◽  
Oxygen Species ◽  
Hydrogen Peroxide Production ◽  
Oxidase System ◽  
Beneficial Effects ◽  
Cellular Components

The present studies were carried out to characterize the nature of reactive oxygen species generated by the xanthine – xanthine oxidase system involved in the release of histamine by noncytotoxic and cytotoxic mechanisms. To distinguish secretory release from lytic release, mast cells were loaded with 51Cr and the release of 51Cr into the incubation medium was used as a measure of cell lysis. The secretory release of histamine was not inhibited by superoxide dismutase or catalase alone. However, together these agents inhibited the release. This suggests that the combination of superoxide and hydrogen peroxide can evoke secretory release. The lytic release of histamine, as monitored by concomitant release of 51Cr from mast cells at higher concentration of xanthine oxidase or longer periods of incubation, seems to be related to hydrogen peroxide production since catalase inhibited the cell lysis. Since it has been reported that exogenously added hydrogen peroxide at concentrations below 10 mM did not induce cell lysis, the lytic release, although hydrogen peroxide dependent, may not be due to its direct effect on the cell surface. The cell lysis observed in the xanthine – xanthine oxidase system seems to be brought about by a complex mechanism involving the interactions of hydrogen peroxide and superoxide with cellular components. These studies indicate that the beneficial effects of superoxide dismutase seen in biological systems may partly be due to inhibition of the secretory processes stimulated by superoxide.Key words: superoxide, hydrogen peroxide, mast cells, histamine, xanthine oxidase.

scholarly journals Cromoglycate and nedocromil enhanced the reactive oxygen species-dependent suppressions with, but not without, dexamethasone in ischaemic and histamine paw oedema of mice

1997 ◽  
Vol 6 (5-6) ◽  
pp. 369-374
Author(s):  
Y. Oyanagui
Keyword(s):  
Reactive Oxygen Species ◽  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Glucocorticoid Receptor ◽  
Low Dose ◽  
Natural Antioxidant ◽  
Target Cells ◽  
Oxygen Species ◽  
Paw Oedema ◽  
Β Carotene

Anti-inflammatory actions of two anti-allergic drugs, alone or with dexamethasone (Dex) were examined in two models, because inflammation is claimed to be important for allergic events, especially for asthma. Cromoglycate and nedocromil were tested in ischaemic- and histamineinduced paw oedema models of mice. These antiallergic drugs (1–100 mg/kg, i.p.) failed to suppress these oedemata, but enhanced the suppressions by a low dose of dexamethasone (0.1 mg/kg, s.c.) at 3–8 h after Dex injection. The mode of effects by anti-allergic drugs resembled that of a natural antioxidant (α-tocopherol, β-carotene etc.), and was different from that of an immunosuppressant like FK506. The enhancing potencies of the two anti-allergic drugs were similar at 6 h after Dex in both oedemata, and were diminished by superoxide dismutase (SOD) or catalase (i.p.). Cycloheximide completely abolished suppressions. Nedocromil, but not cromoglycate, inhibits inflammatory events. Therefore, there are common unknown actions by which the two anti-allergics enhance suppression by Dex. A possible mechanism of this action was supposed to enhance the superoxide and/or hydrogen peroxide-dependent glucocorticoid receptor (GR) signalling in the target cells.

scholarly journals Hemolysis and iodination of erythrocyte components by a myeloperoxidase- mediated system

Blood ◽  
1975 ◽  
Vol 45 (5) ◽  
pp. 699-707 ◽  
Author(s):  
SJ Klebanoff ◽  
RA Clark
Keyword(s):  
Superoxide Dismutase ◽  
Thyroid Hormones ◽  
Glucose Oxidase ◽  
Xanthine Oxidase ◽  
Combined Effect ◽  
Oxidase System ◽  
Generating System

Abstract Erythrocytes are hemolyzed by myeloperoxidase, an H2O2-generating system (glucose + glucose oxidase; hypoxanthine + xanthine oxidase) and an oxidizable cofactor (chloride, iodide, thyroxine, triiodothyronine). The combined effect of chloride and either iodide or the thyroid hormones is greater than additive. Myeloperoxidase can be replaced by lactoperoxidase in the iodide-, thyroxine and triiodothyronine- dependent, but not in the chloride-dependent, systems. Hemolysis is is inhibited by the peroxidase inhibitors, azide and cyanide, and by catalase and is stimulated by superoxide dismutase when the xanthine oxidase system is employed as the source of H2O2. Hemolysis by the iodide-dependent system is associated with the iodination of erythrocyte components.

scholarly journals NADPH Oxidase-Mediated Reactive Oxygen Species Production: Subcellular Localization and Reassessment of Its Role in Plant Defense

2009 ◽  
Vol 22 (7) ◽  
pp. 868-881 ◽  
Author(s):  
Jeannine Lherminier ◽  
Taline Elmayan ◽  
Jérôme Fromentin ◽  
Khadija Tantaoui Elaraqui ◽  
Simona Vesa ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Hydrogen Peroxide ◽  
Plasma Membrane ◽  
Nadph Oxidase ◽  
Subcellular Localization ◽  
Acquired Resistance ◽  
Reactive Oxygen ◽  
Oxygen Species ◽  
Wild Type ◽  
Hydrogen Peroxide Production

Chemiluminescence detection of reactive oxygen species (ROS) triggered in tobacco BY-2 cells by the fungal elicitor cryptogein was previously demonstrated to be abolished in cells transformed with an antisense construct of the plasma membrane NADPH oxidase, NtrbohD. Here, using electron microscopy, it has been confirmed that the first hydrogen peroxide production occurring a few minutes after challenge of tobacco cells with cryptogein is plasma membrane located and NtrbohD mediated. Furthermore, the presence of NtrbohD in detergent-resistant membrane fractions could be associated with the presence of NtrbohD-mediated hydrogen peroxide patches along the plasma membrane. Comparison of the subcellular localization of ROS in wild-type tobacco and in plants transformed with antisense constructs of NtrbohD revealed that this enzyme is also responsible for the hydrogen peroxide production occurring at the plasma membrane after infiltration of tobacco leaves with cryptogein. Finally, the reactivity of wild-type and transformed plants to the elicitor and their resistance against the pathogenic oomycete Phytophthora parasitica were examined. NtrbohD-mediated hydrogen peroxide production does not seem determinant for either hypersensitive response development or the establishment of acquired resistance but it is most likely involved in the signaling pathways associated with the protection of the plant cell.

Response of Antioxidant System in Leaves of Ginkgo biloba to Elevated CO2 and/or O3 and its Natural Recovery in an Urban Area

2013 ◽  
Vol 641-642 ◽  
pp. 18-21
Author(s):  
Jiang Yan Gao ◽  
Sheng Xu ◽  
Wei Chen ◽  
Xing Yuan He
Keyword(s):  
Oxidative Stress ◽  
Reactive Oxygen Species ◽  
Adverse Effect ◽  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Antioxidant System ◽  
Growing Season ◽  
Oxygen Species ◽  
Natural Recovery ◽  
Elevated O3

Changes of oxidative stress and antioxidant system were studied in leaves of Ginkgo biloba exposed to elevated CO2 and O3 fumigation (2006-2008), and released the gases fumigation for the natural recovery in open-top chambers (OTCs) during the growing season in 2009. Elevated CO2 had no significant effect on hydrogen peroxide (H2O2) and malondialdehyde (MDA) contents, and the activities of antioxidant enzymes in leaves of G. biloba during the gas fumigation in 2008. Elevated O3 increased significantly H2O2 and MDA contents, especially after 90 days of gas fumigation. The adverse effect or damage of elevated O3 on trees during the gas fumigation was also alleviated by the released-O3 exposure during the natural recovery. The antioxidative enzyme including superoxide dismutase (SOD), catalase (CAT) and ascorbate peroxidase (APX) activities showed higher levels under the natural recovery than under the gas fumigation, which may be a helpful response to scavenging reactive oxygen species (ROS). The results also indicated that future alleviating the emissions of CO2 and O3 would differentially affect the antioxidant system in plants.

Effect of Pyridone Carboxylic Acid Anti-microbials on the Generation of Reactive Oxygen Species In Vitro

1996 ◽  
Vol 24 (4) ◽  
pp. 345-351 ◽  
Author(s):  
H Akamatsu ◽  
Y Niwa ◽  
H Sasaki ◽  
Y Matoba ◽  
Y Asada ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Xanthine Oxidase ◽  
Reactive Oxygen ◽  
Human Neutrophils ◽  
Oxygen Species ◽  
Oxidase System ◽  
Superoxide Radical Anion ◽  
A Cell ◽  
Inflammatory Action

The effects of ofloxacin, ciprofloxacin and balofloxacin on the reactive oxygen species (ROS) levels generated by human neutrophils was examined in vitro; ROS generated in a cell-free, xanthine–xanthine oxidase system was also assessed. The species investigated were superoxide radical anion (O2−), hydrogen peroxide (H2O2) and hydroxyl radical (OH·). Both ofloxacin and ciprofloxacin markedly decreased the levels of O2−, H2O2 and OH· generated by human neutrophils. On the other hand, these drugs did not affect any of the ROS examined in the xanthine-xanthine oxidase system. Balofloxacin showed no significant effect on ROS generated by either system. The present study indicates that ofloxacin and ciprofloxacin may exert an anti-inflammatory action by reducing the potent ROS species excessively generated by neutrophils at the sites of inflammation.

scholarly journals Haemichrome formation from haemoglobin subunits by hydrogen peroxide

1978 ◽  
Vol 171 (2) ◽  
pp. 329-335 ◽  
Author(s):  
A Tomoda ◽  
K Sugimoto ◽  
M Suhara ◽  
M Takeshita ◽  
Y Yoneyama
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Glucose Oxidase ◽  
Xanthine Oxidase ◽  
Absorption Spectra ◽  
Human Haemoglobin ◽  
Kinetics Of

The effect of H2O2 on ferrous human haemoglobin subunits (alphash-, betash-, alphapmb- and betapmb-chains) was studied. These chains were easily transformed to haemichrome by the addition of H2O2 or H2O2-generating systems, including glucose oxidase (EC 1.1.3.4) AND XANTHINE OXIDASE (EC 1.2.3.2), and this was ascertained by e.p.r. measurements and by absorption spectra. The changes in these haemoglobin subunits were not inhibited by superoxide dismutase (EC 1.15.1.1), but were decreased by catalase (EC 1.11.1.6). The rate of oxidation of alphapmb-chains was higher than that of alphash-chains, and the rate of oxidation of betapmb-chains was higher than that of betash-chains. Haemichrome was demonstrated to be formed directly from these ferrous chains by the attack by H2O2, and this process did not involve formation of methaemoglobin. On the basis of these findings the kinetics of the reaction between the haemoglobin subunits and H2O2 was studied, and the pathological significance of H2O2 in disorders of erythrocytes such as thalassaemia was discussed.

Oxygen-derived free radicals, endothelium, and responsiveness of vascular smooth muscle

1986 ◽  
Vol 250 (5) ◽  
pp. H815-H821 ◽  
Author(s):  
G. M. Rubanyi ◽  
P. M. Vanhoutte
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Smooth Muscle ◽  
Free Radicals ◽  
Vascular Smooth Muscle ◽  
Xanthine Oxidase ◽  
Isometric Tension ◽  
Oxygen Derived Free Radicals ◽  
Major Shift ◽  
The Right

Experiments were designed to determine the role of oxygen-derived free radicals in modulating contractions of vascular smooth muscle and endothelium-mediated relaxations to acetylcholine. The effects of generating or scavenging these radicals were studied in rings of canine coronary arteries suspended for isometric tension recording. Xanthine oxidase plus xanthine caused relaxations, which were greater in rings with endothelium than in rings without endothelium; the relaxations were not affected by superoxide dismutase or mannitol, but could be prevented by catalase. Xanthine oxidase plus xanthine depressed endothelium-mediated relaxations to acetylcholine; this effect was prevented by superoxide dismutase, but was not affected by catalase or mannitol. Exogenous hydrogen peroxide induced catalase-sensitive relaxations, which were depressed by the removal of the endothelium. Superoxide dismutase evoked catalase-sensitive relaxations only in rings with endothelium. Endothelium-mediated relaxations to acetylcholine were slightly depressed by superoxide dismutase or catalase alone; the combination of the two enzymes or mannitol caused a major shift to the right of the concentration-response curve to acetylcholine. In rings without endothelium, relaxations caused by sodium nitroprusside were not affected by the scavengers (alone or in combination) but were augmented by xanthine oxidase plus xanthine. These data suggest that the endothelium-derived relaxing factor released by acetylcholine is not likely to be an oxygen-derived free radical; hydrogen peroxide has a direct inhibitory action on coronary arterial smooth muscle and triggers endothelium-dependent relaxations; and superoxide anions depress and hydroxyl radicals facilitate endothelium-dependent relaxations caused by activation of muscarinic receptors.

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