Protein
            <i>S</i>
            -Nitrosylation and Cardioprotection

Sun, Junhui; Murphy, Elizabeth

doi:10.1161/circresaha.109.209452

Cited by 181 publications

(226 citation statements)

References 160 publications

(212 reference statements)

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“…Actually, in addition to activating cyclic guanosine monophosphate/protein kinase G-dependent signaling pathways, NO • and RNS can modify sulfhydryl residues of protein through Snitrosylation (SNO), which has emerged as an important post-translational protein modification [11,24,40,56,57]. Nitrosylation has been proposed to be important in the preconditioning cardioprotection, also modifying mitochondrial proteins and limiting oxidative stress [6,36,56,57].…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…Nitrosylation has been proposed to be important in the preconditioning cardioprotection, also modifying mitochondrial proteins and limiting oxidative stress [6,36,56,57]. Although PostC requires NO • [28,29,33,49,52], nitrosylation has not been studied under this condition [56]. Yet, the studies on nitration of proteins with 3-nitrotyrosine (3-NT) concentration (a marker for ONOO -formation) achieved contradictory results: while Kupai et al [32] reported that PostC increases cardiac 3-NT after 5-min of reperfusion, Iliodromitis et al [28] observed that PostC reduces myocardial and circulating levels of 3-NT after 10-min of reperfusion.…”

Section: Introductionmentioning

confidence: 99%

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Post-ischemic early acidosis in cardiac postconditioning modifies the activity of antioxidant enzymes, reduces nitration, and favors protein S-nitrosylation

Penna

Perrelli

Tullio

et al. 2011

Pflugers Arch - Eur J Physiol

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Postconditioning (PostC) modifies early post-ischemic pH, redox-environment and activity of enzymes. We hypothesized that early acidosis in PostC may affect superoxide-dismutase (SOD) and catalase(CAT) activities, may reduce 3-nitrotyrosine(3-NT)-and may increase S-nitrosylated (SNO)-protein levels, thus deploying its protective effects. To verify this hypothesis, we studied early (7 th min) and late (120 th min) phases of reperfusion a) endogenous-SOD and -CAT activities, and b) 3-NT-and SNO-protein levels. Isolated rat hearts underwent 30-min ischemia/120-min reperfusion(I/R) or PostC (5 cycles of 10-s I/R at the beginning of 120-min reperfusion) either with or without exogenous-CAT or -SOD infused during the initial 3-min of reperfusion. The effects of early reperfusion with acidic-buffer(AB, pH 6.8) on endogenous antioxidant-enzymes were also tested. Pressure, infarct-size and lactate-dehydrogenase release were also measured. At the 7 th min, PostC induced a significant decrease in SOD-activity with no major change in both Mn-and Cu/Zn-SOD levels, and in CAT-activity and level. PostC also reduced 3-NT and increased SNO levels. Exogenous-SOD, but not -CAT abolished PostCcardioprotection. In late reperfusion(120-min), I/R increased SOD-activity, but decreased CATactivity and Cu/Zn-SOD levels; these effects were reversed by PostC; 3-NT was not affected, but SNO was increased by PostC. AB reproduced PostC effects on antioxidant-enzymes.Conclusions: PostC downregulates endogenous-SOD and preserves -CAT activity, thus increasing SNO and reducing 3-NT levels. These effects are triggered by early post-ischemic acidosis. Yet acidosis-induced SOD-downregulation may limit denitrosylation; thus contributing to PostC-triggering. Hence, exogenous-SOD, but not -CAT, interferes with PostC-triggering.Persistent SOD-downregulation and SNO-increase may contribute to PostC and AB beneficial effects.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Post-ischemic early acidosis in cardiac postconditioning modifies the activity of antioxidant enzymes, reduces nitration, and favors protein S-nitrosylation

Penna

Perrelli

Tullio

et al. 2011

Pflugers Arch - Eur J Physiol

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“…One concept is that S-nitrosylation prevents over-oxidation of important cysteinyl residues during ischemia and reperfusion. This protective S-nitrosylation comes at the expense of inhibiting these thiol-dependent enzymes, but this is reversible and eventually the activity can recover, whereas over-oxidation causes permanent inactivation [6]. But to reiterate the considerations above, S-nitrosylation is anticipated to yield disulfides, which have been observed in isolated hearts after nitrosative stress [77].…”

Section: Further Considerations Of the Stability Of Protein S-nitrosomentioning

confidence: 99%

“…The putative roles for protein Snitrosothiols within the cardiovascular systems is vast with over 1000 proposed targets in the heart alone [5]. Many reviews ascribe S-nitrosothiols as end-effectors of NO signalling that contribute to homeostasis during health [6][7][8], with dysregulation of these processes contributing to disease pathogenesis. For example, hyper-or hypo-S-nitrosylation contributes to a range cardiovascular disease including type 1 and 2 diabetes [9], atherosclerosis [10], cardiac ischemic injury [11], hypertrophy [12] and sepsis [13].…”

Section: Introductionmentioning

confidence: 99%

How widespread is stable protein S-nitrosylation as an end-effector of protein regulation?

Wolhuter

Eaton

2017

Free Radical Biology and Medicine

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Over the last 25 years protein S-nitrosylation, also known more correctly as S-nitrosation, has been progressively implicated in virtually every nitric oxide-regulated process within the cardiovascular system. The current, widely-held paradigm is that S-nitrosylation plays an equivalent role as phosphorylation, providing a stable and controllable post-translational modification that directly regulates end-effector target proteins to elicit biological responses. However, this concept largely ignores the intrinsic instability of the nitrosothiol bond, which rapidly reacts with typically abundant thiol-containing molecules to generate more stable disulfide bonds. These protein disulfides, formed via a nitrosothiol intermediate redox state, are rationally anticipated to be the predominant endeffector modification that mediates functional alterations when cells encounter nitrosative stimuli. In this review we present evidence and explain our reasoning for arriving at this conclusion that may be controversial to some researchers in the field.

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Extremely low frequency electromagnetic field (ELF‐EMF) reduces oxidative stress and improves functional and psychological status in ischemic stroke patients

Cichoń

Bijak

Miller

et al. 2017

Bioelectromagnetics

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As a result of ischaemia/reperfusion, massive generation of reactive oxygen species occurs, followed by decreased activity of antioxidant enzymes. Extremely low frequency electromagnetic fields (ELF-EMF) can modulate oxidative stress, but there are no clinical antioxidant studies in brain stroke patients. The aim of our study was to investigate the effect of ELF-EMF on clinical and antioxidant status in post-stroke patients. Fifty-seven patients were divided into two groups: ELF-EMF and non-ELF-EMF. Both groups underwent the same 4-week rehabilitation program. Additionally, the ELF-EMF group was exposed to an ELF-EMF field of 40 Hz, 7 mT for 15 min/day for 4 weeks (5 days a week). The activity of catalase and superoxide dismutase was measured in hemolysates, and total antioxidant status (TAS) determined in plasma. Functional status was assessed before and after the series of treatments using Activities of Daily Living (ADL), Mini-Mental State Examination (MMSE), and Geriatric Depression Scale (GDS). Applied ELF-EMF significantly increased enzymatic antioxidant activity; however, TAS levels did not change in either group. Results show that ELF-EMF induced a significant improvement in functional (ADL) and mental (MMSE, GDS) status. Clinical parameters had positive correlation with the level of enzymatic antioxidant protection. Bioelectromagnetics. 38:386-396, 2017. © 2017 Wiley Periodicals, Inc.

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Protein S -Nitrosylation and Cardioprotection

Cited by 181 publications

References 160 publications

Post-ischemic early acidosis in cardiac postconditioning modifies the activity of antioxidant enzymes, reduces nitration, and favors protein S-nitrosylation

Post-ischemic early acidosis in cardiac postconditioning modifies the activity of antioxidant enzymes, reduces nitration, and favors protein S-nitrosylation

How widespread is stable protein S-nitrosylation as an end-effector of protein regulation?

Extremely low frequency electromagnetic field (ELF‐EMF) reduces oxidative stress and improves functional and psychological status in ischemic stroke patients

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