Measurement of Peroxiredoxin Activity

Nelson, Kimberly; Parsonage, Derek

doi:10.1002/0471140856.tx0710s49

Cited by 58 publications

(63 citation statements)

References 66 publications

(105 reference statements)

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“…Glutathione peroxidase (GPx), superoxide dismutase (SOD), thioredoxin reductase (TRX), glutathione reductase (GSR), and catalase (CAT) enzyme activities were determined by using commercially available kits from Biovision according to the manufacturer’s instructions. Peroxiredoxin (PRX) enzyme activity was assayed by coupling its activity to oxidation of NADPH via thioredoxin reductases (Nelson and Parsonage, 2011). …”

Section: Methodsmentioning

confidence: 99%

Glutamate Dehydrogenase 1 Signals through Antioxidant Glutathione Peroxidase 1 to Regulate Redox Homeostasis and Tumor Growth

et al. 2015

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SUMMARY How mitochondrial glutaminolysis contributes to redox homeostasis in cancer cells remains unclear. Here we report that the mitochondrial enzyme glutamate dehydrogenase 1 (GDH1) is commonly upregulated in human cancers. GDH1 is important for redox homeostasis in cancer cells by controlling the intracellular levels of its product alpha-ketoglutarate (α-KG) and subsequent metabolite fumarate. Mechanistically, fumarate binds to and activates a ROS scavenging enzyme glutathione peroxidase 1 (GPx1). Targeting GDH1 by shRNA or a small molecule inhibitor R162 resulted in imbalanced redox homeostasis, leading to attenuated cancer cell proliferation and tumor growth.

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Section: Methodsmentioning

confidence: 99%

Glutamate Dehydrogenase 1 Signals through Antioxidant Glutathione Peroxidase 1 to Regulate Redox Homeostasis and Tumor Growth

et al. 2015

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“…Determination of Peroxidase Activity-Peroxidase activity was measured based on a previously reported method (27) and as follows. Untreated or nitrosylated Prx1 (10 M) diluted in 25 mM potassium phosphate, 1 mM EDTA, pH 7.0, was incubated with the Trx system (5 M Trx, 0.1 M TrxR, and 450 M NADPH) and 500 M H 2 O 2 at 37°C for 10 min.…”

Section: Analysis Of Modifications Of Prx1 Bymentioning

confidence: 99%

Multilevel Regulation of 2-Cys Peroxiredoxin Reaction Cycle by S-Nitrosylation

Engelman

Weisman-Shomer

Ziv

et al. 2013

Journal of Biological Chemistry

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Background: S-Nitrosylation may regulate 2-Cys peroxiredoxin systems to affect cellular metabolism of hydrogen peroxide. Results: Nitrosylation impeded the peroxiredoxin-1 catalytic cycle by directly inhibiting the activity of peroxiredoxin-1 and by interfering with the recycling of oxidized peroxiredoxin-1 by the thioredoxin system. Conclusion: Nitrosylation exerts multilevel control of the thioredoxin-peroxiredoxin system. Significance: Through its multiple effects on the thioredoxin-peroxiredoxin system, nitrosylation may influence cellular redox homeostasis.

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“…=========== Table 1 glutathione-S-transferase (GST), catalase, superoxide-dismutases (SODs), and peroxiredoxins (PRDxs) was measured through ELISA or the horseradishperoxidase (HRP) method (9). GPx activity was found to be significantly reduced in PD patients, as indicated by one-way ANOVA (group effect, F 2, 36 =44.1, p<0.001).…”

Section: Resultsmentioning

confidence: 96%

“…Finally, peroxirredoxin activity was measured following the HRP method, based on measurement of peroxide-dependent peroxiredoxin activity with hydrogen peroxide using horseradish peroxidase competition assay (9).…”

Section: Tibbling-link Indexmentioning

confidence: 99%

Does the Cerebrospinal Fluid Reflect Altered Redox State But Not Neurotrophic Support Loss in Parkinson's Disease?

PablosAngel

García-MorenoJosé-Manuel

FernándezEmilio

2015

Antioxidants & Redox Signaling

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Alteration in neurotrophic factors support and antioxidant defenses in the central nervous system (CNS) along with deficit of ferritin have been associated with idiopathic Parkinson's disease (PD). The objectives were to analyze in the cerebrospinal fluid (CSF) of patients with PD and controls the following: (i) the levels of the neuroprotectant factors glial cell line-derived neurotrophic factor, persephin, neurturin, and brain-derived neurotrophic factor, (ii) the levels of transforming growth factor-β1 (TGFβ1) and transforming growth factor-β2 (TGFβ2), proinflammatory factors, (iii) the activity of the antioxidant enzymes glutathione peroxidase (GPx), glutathione reductase (GR), glutathione-S-transferase (GST), catalase, superoxide dismutases (SODs), and peroxiredoxins (PRDxs), and (iv) ferritin levels. The study revealed that, among neurotrophic factors, only TGFβ1 levels were found to be enhanced in patients with PD (early, p < 0.05; advanced, p < 0.02). Regarding antioxidant enzymes, the activity of GPx, catalase, and PRDxs, all hydrogen peroxide scavengers, was found to be significantly reduced in patients (GPx, p < 0.001; catalase, p < 0.01; PRDxs, p < 0.01, one-way analysis of variance). Finally, ferritin content in CSF was significantly diminished over time in patients (early, p < 0.01, -49%; advanced, p < 0.001, -80.7%). Our observations lead to the hypothesis that parkinsonian patients suffer from a serious disturbance of redox state in the CNS, as evaluated through the CSF, characterized by reduced hydrogen peroxide scavenging and iron storage.

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Measurement of Peroxiredoxin Activity

Cited by 58 publications

References 66 publications

Glutamate Dehydrogenase 1 Signals through Antioxidant Glutathione Peroxidase 1 to Regulate Redox Homeostasis and Tumor Growth

Glutamate Dehydrogenase 1 Signals through Antioxidant Glutathione Peroxidase 1 to Regulate Redox Homeostasis and Tumor Growth

Multilevel Regulation of 2-Cys Peroxiredoxin Reaction Cycle by S-Nitrosylation

Does the Cerebrospinal Fluid Reflect Altered Redox State But Not Neurotrophic Support Loss in Parkinson's Disease?

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