Mitochondrial 1-Cys-peroxiredoxin/thioredoxin system protects manganese-containing superoxide dismutase (Mn-SOD) against inactivation by peroxynitrite in Saccharomyces cerevisiae

Pedrajas, José Rafael; Carreras, Alfonso; Valderrama, Raquel; Barroso, Juan B.

doi:10.1016/j.niox.2010.06.004

Cited by 13 publications

(6 citation statements)

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“…Of note, expression levels of other endothelial ROS and reactive nitrogen species detoxification systems, including catalase and the thioredoxin system, were unaffected by transient knockdown of Sirt3. Therefore, a thioredoxin-mediated transcriptional induction of SOD2, as reported in yeast and primary human lung microvascular endothelial cells [ 11 , 39 ] appears unlikely. Assessment of endothelial nitric oxide synthase (eNOS) uncovered a decreased phosphorylation of Thr495 as well as an increased coupling following transient knockdown of Sirt3, equivalent to an increased enzymatic activity [ 43 , 52 ].…”

Section: Discussionmentioning

confidence: 99%

Mild endothelial dysfunction in Sirt3 knockout mice fed a high-cholesterol diet: protective role of a novel C/EBP-β-dependent feedback regulation of SOD2

et al. 2016

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Sirtuin 3 (Sirt3) is an NAD+-dependent mitochondrial deacetylase associated with superoxide dismutase 2 (SOD2)-mediated protection from oxidative stress. We have reported accelerated weight gain and impaired metabolic flexibility in atherosclerotic Sirt3−/− mice. Oxidative stress is a hallmark of endothelial dysfunction. Yet, the role of Sirt3 in this context remains unknown. Thus, we aimed to unravel the effects of endogenous Sirt3 on endothelial function and oxidative stress. Knockdown of Sirt3 in human aortic endothelial cells (HAEC) increased intracellular mitochondrial superoxide accumulation, as assessed by electron spin resonance spectroscopy and fluorescence imaging. Endothelium-dependent relaxation of aortic rings from Sirt3−/− mice exposed to a normal diet did not differ from wild-type controls. However, following 12 weeks of high-cholesterol diet and increasing oxidative stress, endothelial function of Sirt3−/− mice was mildly impaired compared with wild-type controls. Relaxation was restored upon enhanced superoxide scavenging using pegylated superoxide dismutase. Knockdown of Sirt3 in cultured HAEC diminished SOD2 specific activity, which was compensated for by a CCAAT/enhancer binding protein beta (C/EBP-β)-dependent transcriptional induction of SOD2. Abrogation of this feedback regulation by simultaneous knockdown of C/EBP-β and Sirt3 exacerbated mitochondrial superoxide accumulation and culminated into endothelial cell death upon prolonged culture. Taken together, Sirt3 deficiency induces a mild, superoxide-dependent endothelial dysfunction in mice fed a high-cholesterol diet. In cultured endothelial cells, a novel C/EBP-β-dependent rescue mechanism maintains net SOD2 activity upon transient knockdown of Sirt3.Electronic supplementary materialThe online version of this article (doi:10.1007/s00395-016-0552-7) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Mild endothelial dysfunction in Sirt3 knockout mice fed a high-cholesterol diet: protective role of a novel C/EBP-β-dependent feedback regulation of SOD2

et al. 2016

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“…Peroxiredoxins (PRXs) are antioxidant enzymes that use redox-active cysteines to reduce peroxide by employing the reducing potential of a variety of thiols [21]. Additionally, the mitochondrial peroxiredoxin/ thioredoxin system protects MnSod against inactivation by peroxynitrite, which is primarily generated by the reaction of the superoxide anion and NO [22]. The mycelial phase has been reported to have a more aerobic metabolism compared to the yeast phase, as demonstrated by transcriptional analysis [5].…”

Section: Discussionmentioning

confidence: 99%

A quantitative view of the morphological phases of Paracoccidioides brasiliensis using proteomics

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Borges

Magalhães

et al. 2011

Journal of Proteomics

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“…In plants, S- nitrosylation inhibits the peroxidase activity of PrxII E ( Romero-Puertas et al, 2007 ) and PrxII F ( Camejo et al, 2015 ). Interestingly, some members of Prx family posses ONOO - reductase activity ( Bryk et al, 2000 ; Romero-Puertas et al, 2007 ; Pedrajas et al, 2010 ) and therefore could protect against ONOO - -mediated oxidative and nitrosative stresses. In plants, PrxII E is S- nitrosylated during hypersensitive response ( Romero-Puertas et al, 2008 ) and this modification inhibits its peroxynitrite reductase activity promoting tyrosine nitration ( Romero-Puertas et al, 2007 ).…”

Section: S -Nitrosylation Controls Onoo - mentioning

confidence: 99%

Antioxidant Systems are Regulated by Nitric Oxide-Mediated Post-translational Modifications (NO-PTMs)

et al. 2016

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Nitric oxide (NO) is a biological messenger that orchestrates a plethora of plant functions, mainly through post-translational modifications (PTMs) such as S-nitrosylation or tyrosine nitration. In plants, hundreds of proteins have been identified as potential targets of these NO-PTMs under physiological and stress conditions indicating the relevance of NO in plant-signaling mechanisms. Among these NO protein targets, there are different antioxidant enzymes involved in the control of reactive oxygen species (ROS), such as H2O2, which is also a signal molecule. This highlights the close relationship between ROS/NO signaling pathways. The major plant antioxidant enzymes, including catalase, superoxide dismutases (SODs) peroxiredoxins (Prx) and all the enzymatic components of the ascorbate-glutathione (Asa-GSH) cycle, have been shown to be modulated to different degrees by NO-PTMs. This mini-review will update the recent knowledge concerning the interaction of NO with these antioxidant enzymes, with a special focus on the components of the Asa-GSH cycle and their physiological relevance.

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Mitochondrial 1-Cys-peroxiredoxin/thioredoxin system protects manganese-containing superoxide dismutase (Mn-SOD) against inactivation by peroxynitrite in Saccharomyces cerevisiae

Cited by 13 publications

References 70 publications

Mild endothelial dysfunction in Sirt3 knockout mice fed a high-cholesterol diet: protective role of a novel C/EBP-β-dependent feedback regulation of SOD2

Mild endothelial dysfunction in Sirt3 knockout mice fed a high-cholesterol diet: protective role of a novel C/EBP-β-dependent feedback regulation of SOD2

A quantitative view of the morphological phases of Paracoccidioides brasiliensis using proteomics

Antioxidant Systems are Regulated by Nitric Oxide-Mediated Post-translational Modifications (NO-PTMs)

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