Novel Nitric Oxide and Superoxide Generation Inhibitors, Persenone A and B, from Avocado Fruit

2000 ◽  
Vol 48 (5) ◽  
pp. 1557-1563 ◽  
Author(s):  
Oe Kyung Kim ◽  
Akira Murakami ◽  
Yoshimasa Nakamura ◽  
Naohito Takeda ◽  
Hideo Yoshizumi ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Superoxide Generation ◽  
Avocado Fruit

scholarly journals Phosphorylation of Endothelial Nitric-oxide Synthase Regulates Superoxide Generation from the Enzyme

2008 ◽  
Vol 283 (40) ◽  
pp. 27038-27047 ◽  
Author(s):  
Chun-An Chen ◽  
Lawrence J. Druhan ◽  
Saradhadevi Varadharaj ◽  
Yeong-Renn Chen ◽  
Jay L. Zweier
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Endothelial Nitric Oxide Synthase ◽  
Superoxide Generation ◽  
Oxide Synthase ◽  
Endothelial Nitric Oxide

Inhibition by (−)-Persenone A-related Compounds of Nitric Oxide and Superoxide Generation from Inflammatory Leukocytes

2010 ◽  
Vol 74 (12) ◽  
pp. 2010E2-2010E2
Author(s):  
Oe Kyung KIM ◽  
Akira MURAKAMI ◽  
Yoshimasa NAKAMURA ◽  
Ha Won KIM ◽  
Hajime OHIGASHI
Keyword(s):  
Nitric Oxide ◽  
Superoxide Generation ◽  
Related Compounds ◽  
Inflammatory Leukocytes

Inhibition of nitric oxide formation and superoxide generation during reduction of LY83583 by neuronal nitric oxide synthase

1998 ◽  
Vol 360 (2-3) ◽  
pp. 213-218 ◽  
Author(s):  
Yoshito Kumagai ◽  
Kazumi Midorikawa ◽  
Yumi Nakai ◽  
Toshikazu Yoshikawa ◽  
Kazuki Kushida ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Neuronal Nitric Oxide Synthase ◽  
Oxide Formation ◽  
Superoxide Generation ◽  
Nitric Oxide Formation ◽  
Oxide Synthase

Inorganic nitrite attenuates NADPH oxidase-derived superoxide generation in activated macrophages via a nitric oxide-dependent mechanism

2015 ◽  
Vol 83 ◽  
pp. 159-166 ◽  
Author(s):  
Ting Yang ◽  
Maria Peleli ◽  
Christa Zollbrecht ◽  
Alessia Giulietti ◽  
Niccolo Terrando ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nadph Oxidase ◽  
Activated Macrophages ◽  
Superoxide Generation ◽  
Dependent Mechanism

scholarly journals Modulation of rat peripheral polymorphonuclear leukocyte response by nitric oxide and arginine

Blood ◽  
1994 ◽  
Vol 84 (8) ◽  
pp. 2741-2748 ◽  
Author(s):  
P Seth ◽  
R Kumari ◽  
M Dikshit ◽  
RC Srimal
Keyword(s):  
Nitric Oxide ◽  
Reactive Oxygen Species ◽  
Methylene Blue ◽  
Polymorphonuclear Leukocytes ◽  
Reactive Oxygen Species Generation ◽  
Oxygen Species ◽  
Superoxide Generation ◽  
No Donor ◽  
Radical Generation ◽  
Leukocyte Response

The effect of nitric oxide (NO) on the luminol-dependent chemiluminescence (LCL) response of rat polymorphonuclear leukocytes (PMNLs) was analyzed by using sodium nitroprusside (SNP), a NO donor, and L-arginine (L-arg), a NO precursor. A significant reduction in the LCL intensity was observed in presence of SNP (100 mumol/L) or L-arg (5 or 10 mmol/L) in arachidonic acid (AA) phorbol ester (PMA) and formyl- methionyl-leucyl-phenylalanine stimulated PMNLs. However, opsonized zymosan-induced LCL was not attenuated significantly. Reduction in hydroxyl radical and superoxide generation was also observed in SNP- or L-arg-pretreated cells. D-Arg (10 mmol/L) pretreatment did not inhibit PMNLs' LCL response. Furthermore, methylene blue (5 mumol/L) and L-NG- mono methyl-L-arginine (100 or 300 mumol/L) significantly attenuated the LCL response, as induced by various agonists. Cyclic GMP did not alter the reactive oxygen species generation from rat PMNLs. In addition, AA-induced release of myeloperoxidase, a marker of azurophilic granules, was found to be enhanced in L-arg- (10 mmol/L) pretreated PMNLs. The results suggest that NO inhibits free radical generation from rat PMNLs.

Abstract 1396: Mitigation Of Cardiac Injury By Sulfaphenazole, A CYP2C9 Inhibitor Through Involvement Of Inducible Nitric Oxide Synthase (iNOS) in Post-ischemic Heart

Circulation ◽  
2007 ◽  
Vol 116 (suppl_16) ◽  
Author(s):  
Mahmood Khan ◽  
Iyyapu K Mohan ◽  
Damodhar Kumbala ◽  
Vijay K Kutala ◽  
Periannan Kuppusamy
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Infarct Size ◽  
Ischemia Reperfusion ◽  
Left Ventricular ◽  
Control Group ◽  
Myocardial Tissue ◽  
Cytochrome P450 Enzymes ◽  
Superoxide Generation ◽  
Oxide Synthase

Cytochrome P450 enzymes play a significant role in ischemia-reperfusion (I/R) injury. Sulfaphenazole (SFZ), a potent CYP2C9 inhibitor, is known to reduce I/R injury. However, the mechanism of its cardioprotective effects and the role of nitric oxide (NO) is not clear. Objective : Reactive oxygen species (ROS) and reactive nitrogen species (RNS) are important mediators of I/R injury. The objective of this study was to determine how SFZ treatment modulates myocardial tissue oxygenation (pO 2 ) and RNS generation in vivo . Methods: Myocardial infarction was induced in rats by ligating the left anterior descending coronary artery (LAD) for 30 min, followed by 24 h of reperfusion. The study was divided into 4 groups: Untreated I/R control, SFZ, L-NAME, and SFZ+L-NAME. L-NAME (100 mg/kg/day), a nitric oxide synthase inhibitor, was given orally for 3 days prior to LAD ligation. SFZ (1.5 mg/kg, ip) was injected 30 min prior to LAD ligation. Oxygen-sensing crystals were implanted into the LV wall and the rat was placed in an L-band (1.2 GHz) electron paramagnetic resonance (EPR) spectrometer for measurement of myocardial tissue pO 2 during I/R injury. Hemodynamic data was collected with a microtip catheter. Infarct size was measured after 24 h of reperfusion. Superoxide generation was determined by dihydroethidium fluorescence imaging. Immunohistological staining was performed for nitrotyrosine and iNOS. Results: After LAD ligation, pO 2 decreased from 18 mmHg baseline to <2 mmHg. At reperfusion, there was a significant myocardial hyperoxygenation in SFZ-treated rats compared to control group (45.0±1.3 vs. 34.0±2.0 mmHg, P<0.05). In L-NAME and L-NAME+SFZ-treated rats, there was a significant reduction in pO 2 (24.0±1.6 and 26.0±2.3 mmHg, respectively). Compared to control, SFZ treatment significantly improved the left ventricular developed pressure (94.0±4.7 vs. 69.0±6.5 mmHg, P<0.05), decreased infarct size % (35.0±4.2 vs. 16.0±2.5, P<0.05), decreased superoxide generation and nitrotyrosine production. Conclusions: These findings demonstrate that SFZ may provide potent cardioprotection by attenuating post-ischemic ROS and RNS generation, and could serve as an attractive adjuvant therapy in the clinical setting of myocardial I/R injury.

Generation of superoxide in cardiomyocytes during ischemia before reperfusion

1999 ◽  
Vol 277 (6) ◽  
pp. H2240-H2246 ◽  
Author(s):  
Lance B. Becker ◽  
Terry L. vanden Hoek ◽  
Zuo-Hui Shao ◽  
Chang-Qing Li ◽  
Paul T. Schumacker
Keyword(s):  
Nitric Oxide ◽  
Superoxide Dismutase ◽  
Electron Transport Chain ◽  
Redox State ◽  
Oxidase Inhibitor ◽  
Mitochondrial Electron Transport Chain ◽  
Superoxide Generation ◽  
Transport Chain ◽  
Oxide Synthase ◽  
Cu And Zn

Although a burst of oxidants has been well described with reperfusion, less is known about the oxidants generated by the highly reduced redox state and low O2 of ischemia. This study aimed to further identify the species and source of these oxidants. Cardiomyocytes were exposed to 1 h of simulated ischemia while oxidant generation was assessed by intracellular dihydroethidine (DHE) oxidation. Ischemia increased DHE oxidation significantly (0.7 ± 0.1 to 2.3 ± 0.3) after 1 h. Myxothiazol (mitochondrial site III inhibitor) attenuated oxidation to 1.3 ± 0.1, as did the site I inhibitors rotenone (1.0 ± 0.1), amytal (1.1 ± 0.1), and the flavoprotein oxidase inhibitor diphenyleneiodonium (0.9 ± 0.1). By contrast, the site IV inhibitor cyanide, as well as inhibitors of xanthine oxidase (allopurinol), nitric oxide synthase (nitro-l-arginine methyl ester), and NADPH oxidase (apocynin), had no effect. Finally, DHE oxidation increased with Cu- and Zn-containing superoxide dismutase (SOD) inhibition using diethyldithiocarbamate (2.7 ± 0.1) and decreased with exogenous SOD (1.1 ± 0.1). We conclude that significant superoxide generation occurs during ischemia before reperfusion from the ubisemiquinone site of the mitochondrial electron transport chain.

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