Butler et al. reply

Butler, Annemarie; Flitney, F.W.; Williams, Dyfri

doi:10.1016/s0165-6147(00)89056-2

Cited by 27 publications

(30 citation statements)

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“…However, the mechanism of S-nitrosothiol formation in vivo is uncertain (23). The direct reaction of NO with a thiol does not produce RSNOs (30), although intermediates formed during NO oxidation can nitrosate thiols (30) and might be produced by the selective concentration of NO and O 2 within phospholipid bilayers (31). Other possible routes to RSNOs include the reaction of NO with a thiyl radical (16) and reaction of thiols with dinitrosyl iron complexes or by the reaction of ONOO Ϫ with thiols (32).…”

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confidence: 99%

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Persistent S-Nitrosation of Complex I and Other Mitochondrial Membrane Proteins by S-Nitrosothiols but Not Nitric Oxide or Peroxynitrite

Dahm

Moore

Murphy

2006

Journal of Biological Chemistry

189

142

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S-Nitrosation of mitochondrial proteins has been proposed to contribute to the pathophysiological interactions of nitric oxide (NO) and its derivatives with mitochondria but has not been shown directly. Furthermore, little is known about the mechanism of formation or the fate of these putative S-nitrosothiols. Here we have determined whether mitochondrial membrane protein thiols can be S-nitrosated on exposure to free NO from 3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene (DETA-NONOate) by interaction with S-nitrosoglutathione or S-nitroso-N-acetylpenicillamine (SNAP) and by the NO derivative peroxynitrite. S-Nitrosation of protein thiols was measured directly by chemiluminescence detection. S-Nitrosoglutathione and S-nitroso-N-acetylpenicillamine led to extensive protein thiol oxidation, with about 30% of the modified protein thiols persistently S-nitrosated. In contrast, there was no protein thiol oxidation or S-nitrosation on exposure to 3,3-bis (aminoethyl)-1-hydroxy-2-oxo-1-triazene. Peroxynitrite extensively oxidized protein thiols but produced negligible amounts of S-nitrosothiols. Therefore, mitochondrial membrane protein thiols are S-nitrosated by preformed S-nitrosothiols but not by NO or by peroxynitrite. These S-nitrosated protein thiols were readily reduced by glutathione, so S-nitrosation will only persist when the mitochondrial glutathione pool is oxidized. Respiratory chain complex I was S-nitrosated by S-nitrosothiols, consistent with it being an important target for S-nitrosation during nitrosative stress. The S-nitrosation of complex I correlated with a significant loss of activity that was reversed by thiol reductants. S-Nitrosation was also associated with increased superoxide production from complex I. These findings point to a significant role for complex I S-nitrosation and consequent dysfunction during nitrosative stress in disorders such as Parkinson disease and sepsis.

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confidence: 99%

“…One important reaction of RSNOs is transnitrosation, by which a nitrosonium (NO ϩ ) is transferred to another thiol (30). This is likely to be of particular importance for GSH, the predominant low molecular weight thiol in cells, which can form S-nitrosoglutathione (GSNO) and transfer the NO ϩ onto protein thiols.…”

mentioning

confidence: 99%

Persistent S-Nitrosation of Complex I and Other Mitochondrial Membrane Proteins by S-Nitrosothiols but Not Nitric Oxide or Peroxynitrite

Dahm

Moore

Murphy

2006

Journal of Biological Chemistry

189

142

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“…[13] 0.69 ± 0.05 ± 0.05 CLEO (1991) [14] CLEOII (1993) [15] 0.76 ± 0.01 ± 0.04 CLEOII (1995) [16] 0.163 ± 0.031 ± 0.011 E687 (1995) [17] 0.69 ± 0.03 ± 0.03 E687 (1996) [18] 0.160 ± 0.018 ± 0.004 BESII (2004) [19] 0.78 ± 0.04 ± 0. …”

Section: Methodsmentioning

confidence: 99%

Charm semileptonic decays.

Oyanguren¹

2012

Proceedings of the XIth International Conference on Heavy Quarks and Leptons — PoS(HQL 2012)

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“…9), which is definitely different from other treatments. Oxygen-rich conditions in the arterial blood prevented decreases in plasma NO 2 Ϫ , suggesting that the decrease in NO 2 Ϫ concentration cannot be due to NO 3 Ϫ oxidation by oxyhemoglobin 43,44) ; only oxygen-rich conditions or hyperoxygenation attenuated the disappearance of NO 2 Ϫ from plasma.…”

Section: )mentioning

confidence: 96%

Different Disappearance Rates of Plasma Nitrite (NO2-) Contribute to Apparent Steady-State Arterio-Venous Differences in Anesthetized Animals

Ishibashi

Nishizawa

Nakamoto-Nomura

et al. 2011

Biological & Pharmaceutical Bulletin

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) is not only an oxidative product of nitric oxide (NO), but also serves as an indicator of endothelial nitric oxide synthase activity and as a circulating reservoir of NO bioactivity in the circulatory system. [1][2][3] The indicator status is supported by observations that approximately 70-90% of circulating plasma NO 2 Ϫ levels derive from NO produced by endothelial nitric oxide synthase. 4,5) The reservoir activity is widely accepted (see reviews [1][2][3] ) as is maintained when NO 2 Ϫ reacts with deoxygenated hemoglobin (Hb) in red blood cells (RBCs) to form NO and methemoglobin (metHb), leading to biological responses including vasodilation.2,6,7) Therefore, precise evaluation of NO 2 Ϫ plasma levels, including detailed kinetic knowledge, is required for further understanding of NO 2 Ϫ biology in the circulation. However, only limited kinetic data [8][9][10] are presently available, and many problems of NO 2 Ϫ biology await resolution.For example, it is still controversial whether arterio-venous (A-V) differences in plasma NO 2 Ϫ levels actually exist. 10-16)The A-V difference may reflect consumption of NO 2 Ϫ to form NO during peripheral circulation for preservation of blood flow at lower oxygen tension.12) Although we have previously reported a small but significant A-V difference under steadystate conditions, 10,14,17) these observations are complicated by a report that, in isolated blood, uptake of NO 2 Ϫ by RBCs is faster in venous blood than in arterial blood, 15) a scenario that may cause artificial apparent A-V differences when arterial and venous blood samples are treated after some delay. If this situation is indeed the case, our previous work reporting kinetic parameters 10) should also be re-evaluated. It is also unclear whether plasma NO 2 Ϫ levels reflect in vivo changes in NO 2 Ϫ levels. 10,12,18) Exogenously administered NO 2 Ϫ or NO resulted in a large A-V difference in plasma NO 2 Ϫ , with arterial blood preferentially reflecting the changes, 10,14,17) presumably due to greater contributions by RBCs or tissue as a buffering compartment under a state of lower oxygenation. A possible difference in the uptake rate of RBCs could not be large enough to explain such a large A-V difference, and contributions of tissue factors would be a great concern. 18,19) The emerging role of tissue as a reservoir of NO bioactivity via NO 2 Ϫ should be taken into consideration; some reports indicate that plasma NO 2 Ϫ levels may not accurately reflect increases in NO or NO 2 Ϫ levels in biological systems. 3,20,21) However, no alternative measures exist for assessing NO bioactivity in easily accessible biomaterials (such as blood). Therefore, the aim of this study was to estimate the steady-state concentration of plasma NO 2 Ϫ in order to evaluate whether the putative A-V difference actually exists. We also re-evaluated the pertinent kinetic features in vivo, considering uptake by RBC and tissue factors. MATERIALS AND METHODSJapanese white rabbits weighing 2.4-3.5 kg were anesthetized with intravenous sodium...

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Butler et al. reply

Cited by 27 publications

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Persistent S-Nitrosation of Complex I and Other Mitochondrial Membrane Proteins by S-Nitrosothiols but Not Nitric Oxide or Peroxynitrite

Persistent S-Nitrosation of Complex I and Other Mitochondrial Membrane Proteins by S-Nitrosothiols but Not Nitric Oxide or Peroxynitrite

Charm semileptonic decays.

Different Disappearance Rates of Plasma Nitrite (NO2-) Contribute to Apparent Steady-State Arterio-Venous Differences in Anesthetized Animals

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