Characterization of human triosephosphate isomerase S-nitrosylation

Romero, Jorge M.; Carrizo, M.E.; Curtino, Juan A.

doi:10.1016/j.niox.2018.04.004

Cited by 9 publications

(9 citation statements)

References 43 publications

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“…In the absence of Nrx, four cysteinyl residues were found to be more reduced: Cys67 (38.9%, p value 0.0385), Cys87 (29.4%, p value 0.0245), Cys127 (42.1%, p value 0.0125), and Cys218 (38.7%, p value 0.0479). The S-nitrosylation of the latter Cys218 residue has been reported to lead to a reduction in the activity of the human protein by 30% [29]. The glutathionylation of the human enzyme has been described in stressed T-lymphocytes [26].…”

Section: Resultsmentioning

confidence: 99%

Nucleoredoxin‐Dependent Targets and Processes in Neuronal Cells

Urbainsky

Nölker

Imber

et al. 2018

Oxidative Medicine and Cellular Longevity

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Nucleoredoxin (Nrx) is an oxidoreductase of the thioredoxin family of proteins. It was shown to act as a signal transducer in some pathways; however, so far, no comprehensive analysis of its regulated substrates and functions was available. Here, we used a combination of two different strategies to fill this gap. First, we analyzed the thiol-redox state of the proteome of SH-SY5Y neuroblastoma cells depleted of Nrx compared to control cells using a differential thiol-labeling technique and quantitative mass spectrometry. 171 proteins were identified with an altered redox state; 161 of these were more reduced in the absence of Nrx. This suggests functions of Nrx in the oxidation of protein thiols. Second, we utilized the active site mutant Cys208Ser of Nrx, which stabilizes a mixed disulfide intermediate with its substrates and therefore trapped interacting proteins from the mouse brain (identifying 1710 proteins) and neuronal cell culture extracts (identifying 609 proteins). Profiling of the affected biological processes and molecular functions in cells of neuronal origin suggests numerous functions of Nrx in the redox regulation of metabolic pathways, cellular morphology, and signal transduction. These results characterize Nrx as a cellular oxidase that itself may be oxidized by the formation of disulfide relays with peroxiredoxins.

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Section: Resultsmentioning

confidence: 99%

Nucleoredoxin‐Dependent Targets and Processes in Neuronal Cells

Urbainsky

Nölker

Imber

et al. 2018

Oxidative Medicine and Cellular Longevity

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“…Similarly, surface exposure of Cys 42 and Cys 218 could be seen, while Cys 67 appears buried at the interface of the hTPI homodimer. A previous report suggested that Cys 67 was more solvent accessible than Cys 42 or Cys 218 ; however, the same study identified Cys 218 as the only site of SNO modification (68). Quantitation of redox-modified sites in other proteins with known structure will further enable confirmation of the structural constraints for reversible and irreversible Cys redox PTMs.…”

Section: Discussionmentioning

confidence: 89%

A Global Profile of Reversible and Irreversible Cysteine Redox Post-Translational Modifications During Myocardial Ischemia/Reperfusion Injury and Antioxidant Intervention

Rookyard

Paulech

Thyssen

et al. 2021

Antioxidants & Redox Signaling

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Aims: Cysteine (Cys) is a major target for redox post-translational modifications (PTMs) that occur in response to changes in the cellular redox environment. We describe multiplexed, peptide-based enrichment and quantitative mass spectrometry (MS) applied to globally profile reversible redox Cys PTM in rat hearts during ischemia/ reperfusion (I/R) in the presence or absence of an aminothiol antioxidant, N-2-mercaptopropionylglycine (MPG). Parallel fractionation also allowed identification of irreversibly oxidized Cys peptides (Cys-SO 2 H/SO 3 H). Results: We identified 4505 reversibly oxidized Cys peptides of which 1372 were significantly regulated by ischemia and/or I/R. An additional 219 peptides (247 sites) contained Cys-SO 2 H/Cys-SO 3 H modifications, and these were predominantly identified from hearts subjected to I/R (n = 168 peptides). Parallel reaction monitoring MS (PRM-MS) enabled relative quantitation of 34 irreversibly oxidized Cys peptides. MPG attenuated a large cluster of I/R-associated reversibly oxidized Cys peptides and irreversible Cys oxidation to less than nonischemic controls (n = 24 and 34 peptides, respectively). PRM-MS showed that Cys sites oxidized during ischemia and/or I/R and ''protected'' by MPG were largely mitochondrial, and were associated with antioxidant functions (peroxiredoxins 5 and 6) and metabolic processes, including glycolysis. Metabolomics revealed I/R induced changes in glycolytic intermediates that were reversed in the presence of MPG, which were consistent with irreversible PTM of triose phosphate isomerase and glyceraldehyde-3-phosphate dehydrogenase (GAPDH), altered GAPDH enzyme activity, and reduced I/R glycolytic payoff as evidenced by adenosine triphosphate and NADH levels. Innovation: Novel enrichment and PRM-MS approaches developed here enabled large-scale relative quantitation of Cys redox sites modified by reversible and irreversible PTM during I/R and antioxidant remediation. Conclusions: Cys sites identified here are targets of reactive oxygen species that can contribute to protein dysfunction and the pathogenesis of I/R. Antioxid. Redox Signal. 34,

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“…For instance, ALDOA affects fructose 1,6-diphosphate conversion levels and its S-nitrosylation modification was noted to induce dysregulation of the glycolytic pathway and adenosine triphosphate (ATP) depletion . TPI acts as a critical part in the catalysis of dihydroxyacetone phosphate to glyceraldehyde-3 phosphate, and the report has revealed that the V max of this catalytic reaction could be depressed by 30% once the TPI was S-nitrosylated . PGK is an enzyme that drives the first energy-producing reaction (ATP synthesis) in the glycolysis process.…”

Section: Resultsmentioning

confidence: 99%

“…35 TPI acts as a critical part in the catalysis of dihydroxyacetone phosphate to glyceraldehyde-3 phosphate, and the report has revealed that the V max of this catalytic reaction could be depressed by 30% once the TPI was S-nitrosylated. 36 PGK is an enzyme that drives the first energy-producing reaction (ATP synthesis) in the glycolysis process. Similar to our result, Liu et al 21 also identified a higher S-nitrosylation level of PGK in PSE meat as compared with normal meat.…”

Section: Journal Of Agricultural and Food Chemistrymentioning

confidence: 99%

Modification-Specific Proteomic Analysis Reveals Cysteine S-Nitrosylation Mediated the Effect of Preslaughter Transport Stress on Pork Quality Development

Ma,

Zhang,

Zhang

et al. 2023

J. Agric. Food Chem.

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Characterization of human triosephosphate isomerase S-nitrosylation

Cited by 9 publications

References 43 publications

Nucleoredoxin‐Dependent Targets and Processes in Neuronal Cells

Nucleoredoxin‐Dependent Targets and Processes in Neuronal Cells

A Global Profile of Reversible and Irreversible Cysteine Redox Post-Translational Modifications During Myocardial Ischemia/Reperfusion Injury and Antioxidant Intervention

Modification-Specific Proteomic Analysis Reveals Cysteine S-Nitrosylation Mediated the Effect of Preslaughter Transport Stress on Pork Quality Development

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