NO accounts completely for the oxygenated nitrogen species generated by enzymic <scp>l</scp>-arginine oxygenation

Mülsch, Alexander; Vanin, Anatoly F.; Mordvintcev, Peter I.; Hauschildt, Sunna; Busse, Rudi

doi:10.1042/bj2880597

Cited by 74 publications

(25 citation statements)

References 45 publications

(58 reference statements)

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“…In addition to the oxyhemoglobin assay, the formation of NO was assessed by trapping NO as a paramagnetic Fe-(DETC) 2 -NO complex followed by detection by EPR spectroscopy [32,44]. The two methods led to identical conclusions (data not shown).…”

Section: Oxidation Of Gua 1-17 and Nohg 18-30 To No Catalyzed By Wt Amentioning

confidence: 93%

“…In some assays, the levels of NO formation were measured by EPR spectroscopy following the formation of the paramagnetic nitrosyl-(diethyldithiocarbamato)-iron(II) complex (Fe II (DETC) 2 -NO) following a previously described protocol [32,44]. The EPR spectra were recorded at 100 ± 5 K with the following instrument settings: modulation frequency 100 kHz, modulation amplitude 1 mT, time constant 0.04 s, field sweep 400 mT, microwave power 20 mW, sampling time 41 ms, and four scans.…”

Section: Detection Of No Formationmentioning

confidence: 99%

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Comparison of wild type neuronal nitric oxide synthase and its Tyr588Phe mutant towards various l-arginine analogues

Giroud

Moreau

Sagami

et al. 2010

Journal of Inorganic Biochemistry

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Section: Oxidation Of Gua 1-17 and Nohg 18-30 To No Catalyzed By Wt Amentioning

confidence: 93%

Section: Detection Of No Formationmentioning

confidence: 99%

Comparison of wild type neuronal nitric oxide synthase and its Tyr588Phe mutant towards various l-arginine analogues

Giroud

Moreau

Sagami

et al. 2010

Journal of Inorganic Biochemistry

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“…Scans were traced with 2.85 G modulation amplitude, 340 G sweep width, and 3356 G central field as described [34,35]. Analysis of NO content was performed with double integration of the NO signal as described previously [34][35][36]. NO content of the samples were expressed in arbitrary units as this method enables a semi-quantitative assessment of NO content in biological samples (see for review Csonka et al [37]).…”

Section: Antibodies and Materialsmentioning

confidence: 99%

“…Electron spin resonance spectra were recorded with a Bruker ECS106 (Rheinstetten, Germany) spectrometer operating at X band with 100 kHz modulation frequency at a temperature of 160 K, using 10 mW microwave power to avoid saturation. Scans were traced with 2.85 G modulation amplitude, 340 G sweep width, and 3356 G central field as described [34,35]. Analysis of NO content was performed with double integration of the NO signal as described previously [34][35][36].…”

Section: Antibodies and Materialsmentioning

confidence: 99%

Nitric oxide synthetic pathway and cGMP levels are altered in red blood cells from end-stage renal disease patients

et al. 2016

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Red blood cells (RBCs) enzymatically produce nitric oxide (NO) by a functional RBC-nitric oxide synthase (RBC-NOS). NO is a vascular key regulatory molecule. In RBCs its generation is complex and influenced by several factors, including insulin, acetylcholine, and calcium. NO availability is reduced in end-stage renal disease (ESRD) and associated with endothelial dysfunction. We previously demonstrated that, through increased phosphatidylserine membrane exposure, ESRD-RBCs augmented their adhesion to human cultured endothelium, in which NO bioavailability decreased. Since RBC-NOS-dependent NO production in ESRD is unknown, this study aimed to investigate RBC-NOS levels/activation, NO production/bioavailability in RBCs from healthy control subjects (C, N = 18) and ESRD patients (N = 27). Although RBC-NOS expression was lower in ESRDRBCs, NO, cyclic guanosine monophosphate (cGMP), RBC-NOS Serine1177 phosphorylation level and eNOS/ Calmodulin (CaM)/Heat Shock Protein-90 (HSP90) interaction levels were higher in ESRD-RBCs, indicating increased enzyme activation. Conversely, following RBCs stimulation with insulin or ionomycin, NO and cGMP levels were significantly lower in ESRD-than in C-RBCs, suggesting that uremia might reduce the RBC-NOS response to further stimuli. Additionally, the activity of multidrug-resistance-associated protein-4 (MRP4; cGMPmembrane transporter) was significantly lower in ESRDRBCs, suggesting a possible compromised efflux of cGMP across the ESRD-RBCs membrane. This study for the first time showed highest basal RBC-NOS activation in ESRDRBCs, possibly to reduce the negative impact of decreased NOS expression. It is further conceivable that high NO production only partially affects cell function of ESRDRBCs maybe because in vivo they are unable to respond to physiologic stimuli, such as calcium and/or insulin.Keywords End-stage renal disease Á Red blood cells Á Nitric oxide Á cGMP Á Nitric oxide synthase Mario Bonomini, and Assunta Pandolfi have contributed equally to the study.Electronic supplementary material The online version of this article

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“…NO has been shown to derive in animal tissues solely from guanidino nitrogens of L-arginine and to account completely for the oxygenated nitrogen species generated from these N atoms [84,99]. Things could be more complicated under some particular physiopathological situations, due to the existence of a substantial intermediate nitrite pool (see below).…”

Section: Possible Artefacts In the Use Of Iron-dithiocarbamate Complementioning

confidence: 99%

Contribution of spin-trapping EPR techniques for the measurement of NO production in biological systems

Henry¹,

Guissani²

2000

Analusis

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In this overview of NO spin-trapping methods, we have pointed out their main advantages over frozen solution EPR spectroscopy detection of nitrosylated metalloproteins: improved sensitivity, potential specificity and time-resolution. A few simple ideas concerning EPR methodology have been recalled. Examples of possible artefacts, sometimes unexpected, which can easily be encountered in any analytical methods have been described. New methodological developments have also been mentioned.

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NO accounts completely for the oxygenated nitrogen species generated by enzymic l-arginine oxygenation

Abstract: We have assessed the stoichiometry of the nitric oxide (NO) synthase reaction by using a novel e.p.r. technique. NO generated by crude and partially purified NO

Cited by 74 publications

References 45 publications

Comparison of wild type neuronal nitric oxide synthase and its Tyr588Phe mutant towards various l-arginine analogues

Comparison of wild type neuronal nitric oxide synthase and its Tyr588Phe mutant towards various l-arginine analogues

Nitric oxide synthetic pathway and cGMP levels are altered in red blood cells from end-stage renal disease patients

Contribution of spin-trapping EPR techniques for the measurement of NO production in biological systems

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