Peroxynitrite and hydrogen peroxide elicit similar cellular stress responses mediated by the Ccp1 sensor protein

Martins, Dorival; Bakas, Iolie; McIntosh, Kelly; English, Ann M.

doi:10.1016/j.freeradbiomed.2015.04.010

Cited by 5 publications

(3 citation statements)

References 75 publications

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“…The hypothesis presented in Equation 10 was actually inspired by the peroxynitrite redox reactions with divalent lowmolecular weight metal complexes (43,44) and hemeproteins (42,(45)(46)(47). According to Radi and co-workers (18) the antioxidant effects of iron and manganese metalloporphyrin complexes on peroxynitrite depend precisely on the two-electron redox reaction of their divalent states (48,49).…”

Section: Peroxynitrite Reacts With the Labile Iron Poolmentioning

confidence: 99%

The labile iron pool attenuates peroxynitrite-dependent damage and can no longer be considered solely a pro-oxidative cellular iron source

Damasceno

Condeles

Lopes

et al. 2018

Journal of Biological Chemistry

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The ubiquitous cellular labile iron pool (LIP) is often associated with the production of the highly reactive hydroxyl radical, which forms through a redox reaction with hydrogen peroxide. Peroxynitrite is a biologically relevant peroxide produced by the recombination of nitric oxide and superoxide. It is a strong oxidant that may be involved in multiple pathological conditions, but whether and how it interacts with the LIP are unclear. Here, using fluorescence spectroscopy, we investigated the interaction between the LIP and peroxynitrite by monitoring peroxynitrite-dependent accumulation of nitrosated and oxidized fluorescent intracellular indicators. We found that, in murine macrophages, removal of the LIP with membrane-permeable iron chelators sustainably accelerates the peroxynitrite-dependent oxidation and nitrosation of these indicators. These observations could not be reproduced in cell-free assays, indicating that the chelator-enhancing effect on peroxynitrite-dependent modifications of the indicators depended on cell constituents, presumably including LIP, that react with these chelators. Moreover, neither free nor ferrous-complexed chelators stimulated intracellular or extracellular oxidative and nitrosative chemistries. On the basis of these results, LIP appears to be a relevant and competitive cellular target of peroxynitrite or its derived oxidants, and thereby it reduces oxidative processes, an observation that may change the conventional notion that the LIP is simply a cellular source of pro-oxidant iron.

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Section: Peroxynitrite Reacts With the Labile Iron Poolmentioning

confidence: 99%

The labile iron pool attenuates peroxynitrite-dependent damage and can no longer be considered solely a pro-oxidative cellular iron source

Damasceno

Condeles

Lopes

et al. 2018

Journal of Biological Chemistry

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“…Reports suggest that the high reactivity of ONOOH towards Ccp1 inhibits signaling. So it is assumed that H 2 O 2 and ONOO(H) can elicit a similar antioxidant response when reacting with the sensor Ccp1 [18,68].…”

Section: Cytochrome C Peroxidase (Ccp1)mentioning

confidence: 99%

Enzymatic and Non-Enzymatic Response during Nitrosative Stress in Escherichia coli

Nath

Sengupta

Bhattacharjee

2022

Postępy Mikrobiologii - Advancements of Microbiology

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Nitrosative stress is an adverse physiological condition mediated by an excessive level of reactive nitrogen species (RNS). RNS react with the different macromolecules in vivo and result in the inactivation of these molecules. But the mechanism to counteract the effect of nitrosative stress is poorly understood. Escherichia coli is one of the best understood and well-studied microorganism. Although several studies have been reported on Escherichia coli to characterize the effect of various stress response but fewer works are there to see the effect of nitrosative stress. Escherichia coli encounter numerous stresses during its growth, survival, and infection. They respond to various stress conditions by activating common regulator proteins and thiols. These stress conditions result in the accumulation of these regulator proteins and thiols that allow cells to adjust to specific stress situations, conferring stress tolerance and survival. In this review, different enzymatic and non-enzymatic mechanisms to counteract the effect of nitrosative stress in Escherichia coli have been discussed and a hypothesis for the working mechanism of hybrid cluster protein that helps to combat nitrosative stress has been proposed. Here, we have tried to give a clear scenario about the mode of action of stress-responsive elements present in Escherichia coli.

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“…cerevisiae was chosen as the model for the present study because this yeast expresses eight TP members (five Prx and three GPx) and viable strains lacking specific TPs, and all eight isoforms are available [13]. Additionally, S. cerevisiae also expresses a cytochrome c peroxidase (Ccp1), which has been shown to react rapidly with peroxynitrite [14].…”

Section: The Competition Assaymentioning

confidence: 99%

Thiol Peroxidases as Major Regulators of Intracellular Levels of Peroxynitrite in Live Saccharomyces cerevisiae Cells

et al. 2020

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Thiol peroxidases (TP) are ubiquitous and abundant antioxidant proteins of the peroxiredoxin and glutathione peroxidase families that can catalytically and rapidly reduce biologically relevant peroxides, such as hydrogen peroxide and peroxynitrite. However, the TP catalytic cycle is complex, depending on multiple redox reactions and partners, and is subjected to branching and competition points that may limit their peroxide reductase activity in vivo. The goals of the present study were to demonstrate peroxynitrite reductase activity of TP members in live cells in real time and to evaluate its catalytic characteristics. To these ends, we developed a simple fluorescence assay using coumarin boronic acid (CBA), exploiting that fact that TP and CBA compete for peroxynitrite, with the expectation that higher TP peroxynitrite reductase activity will lower the CBA oxidation. TP peroxynitrite reductase activity was evaluated by comparing CBA oxidation in live wild type and genetically modified Δ8 (TP-deficient strain) and Δ8+TSA1 (Δ8 strain that expresses only one TP member, the TSA1 gene) Saccharomyces cerevisiae strains. The results showed that CBA oxidation decreased with cell density and increased with increasing peroxynitrite availability. Additionally, the rate of CBA oxidation decreased in the order Δ8 > Δ8+TSA1 > WT strains both in control and glycerol-adapted (expressing higher TP levels) cells, showing that the CBA competition assay could reliably detect peroxynitrite in real time in live cells, comparing CBA oxidation in strains with reduced and increased TP expression. Finally, there were no signs of compromised TP peroxynitrite reductase activity during experimental runs, even at the highest peroxynitrite levels tested. Altogether, the results show that TP is a major component in the defense of yeast against peroxynitrite insults under basal and increasing stressful conditions.

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Peroxynitrite and hydrogen peroxide elicit similar cellular stress responses mediated by the Ccp1 sensor protein

Cited by 5 publications

References 75 publications

The labile iron pool attenuates peroxynitrite-dependent damage and can no longer be considered solely a pro-oxidative cellular iron source

The labile iron pool attenuates peroxynitrite-dependent damage and can no longer be considered solely a pro-oxidative cellular iron source

Enzymatic and Non-Enzymatic Response during Nitrosative Stress in Escherichia coli

Thiol Peroxidases as Major Regulators of Intracellular Levels of Peroxynitrite in Live Saccharomyces cerevisiae Cells

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