Peroxiredoxins as biomarkers of oxidative stress

Poynton, Rebecca A.; Hampton, Mark B.

doi:10.1016/j.bbagen.2013.08.001

Cited by 152 publications

(124 citation statements)

References 66 publications

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“…It has been reported that Prxs may act as a housekeeping-type gene to regulate the intracellular ROS level because its expression can be found in all stages of the bee life cycle (Wang et al 2008). In addition, the accumulation of oxidized Prxs may indicate the disruption of cellular redox homeostasis (Poynton and Hampton 2014). Q-PCR analysis showed that AccTpx4 was expressed throughout the life cycle of bees (Fig.…”

Section: Discussionmentioning

confidence: 97%

A novel 1-Cys thioredoxin peroxidase gene in Apis cerana cerana: characterization of AccTpx4 and its role in oxidative stresses

Huaxia

Wang

Yan

et al. 2015

Cell Stress and Chaperones

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Thioredoxin peroxidase (Tpx), also named peroxiredoxin (Prx), is an important peroxidase that can protect organisms against stressful environments. AccTpx4, a 1-Cys thioredoxin peroxidase gene from the Chinese honey bee Apis cerana cerana, was cloned and characterized. The AccTpx4 gene encodes a protein that is predicted to contain the conserved PVCTTE motif from 1-Cys peroxiredoxin. Quantitative real-time PCR (Q-PCR) and Western blotting revealed that AccTpx4 was induced by various oxidative stresses, such as cold, heat, insecticides, H 2 O 2 , and HgCl 2 . The in vivo peroxidase activity assay showed that recombinant AccTpx4 protein could efficiently degrade H 2 O 2 in the presence of DL-dithiothreitol (DTT). In addition, disc fusion assays revealed that AccTpx4 could function to protect cells against oxidative stresses. These results indicate that AccTpx4 plays an important role in oxidative stress responses and may contribute to the conservation of honeybees.

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Section: Discussionmentioning

confidence: 97%

A novel 1-Cys thioredoxin peroxidase gene in Apis cerana cerana: characterization of AccTpx4 and its role in oxidative stresses

Huaxia

Wang

Yan

et al. 2015

Cell Stress and Chaperones

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“…95 Peroxidasin Homolog (PXDN) and Peroxiredoxin 2 (PRDX2) may play an important role in eliminating peroxides generated during metabolism. 96,97 Apparently, low levels of ROS (such as peroxides) may be required for the pluripotency of ESCs. This finding confirms the proposed hypothesis that intact eicosanoids are required for ESC pluripotency, and that the oxidation of eicosanoids by ROS initiates ESC differentiation.…”

Section: Lessons From Transcriptome Studies; Lipid Metabolic and Hydrmentioning

confidence: 99%

Unique Metabolic Features of Stem Cells, Cardiomyocytes, and Their Progenitors

Gaspar

Doss

Hengstler³

et al. 2014

Circulation Research

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“…Dimeric Prdx1, Prdx2, Prdx3, and Prdx4 are typical 2-Cys Prdxs in which the peroxidatic thiol reacts with H 2 O 2 to form a sulfenic acid, which is then "attacked" by a resolving cysteine on the other monomer in the functional pair. The resulting Prdx disulfide dimer is reduced by the disulfide reductase thioredoxin (Trx) to regenerate reduced Prdx proteins capable of decomposing another molecule of H 2 O 2 (26). When the Trx reduces the oxidized Prdx, it does so at the expense of becoming oxidized itself via a thiol disulfide-exchange reaction.…”

mentioning

confidence: 99%

Oxidant-induced Interprotein Disulfide Formation in Cardiac Protein DJ-1 Occurs via an Interaction with Peroxiredoxin 2

Fernandez-Caggiano

Schröder

Cho

et al. 2016

Journal of Biological Chemistry

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The role and responses of the dimeric DJ-1 protein to cardiac oxidative stress is incompletely understood. H 2 O 2 induces a 50-kDa DJ-1 interprotein homodimer disulfide, known to form between Cys-53 on each subunit. A trimeric 75-kDa DJ-1 complex that mass spectrometry shows contained 2-Cys peroxiredoxin also formed and precedes the appearance of the disulfide dimer. These observations may represent peroxiredoxin sensing and transducing the oxidant signal to DJ-1. The dimeric disulfide DJ-1 complex was stabilized by auranofin, suggesting that thioredoxin recycles it in cells. Higher concentrations of H 2 O 2 concomitantly induce DJ-1 Cys-106 hyperoxidation (sulfination or sulfonation) in myocytes, perfused heart, or HEK cells. An oxidation-resistant C53A DJ-1 shows potentiated H 2 O 2 -induced Cys-106 hyperoxidation. DJ-1 also forms multiple disulfides with unknown target proteins during H 2 O 2 treatment, the formation of which is also potentiated in cells expressing the C53A mutant. This suggests that the intersubunit disulfide induces a conformational change that limits Cys-106 forming heterodisulfide protein complexes or from hyperoxidizing. High concentrations of H 2 O 2 also induce cell death, with DJ-1 Cys-106 sulfonation appearing causal in these events, as expression of C53A DJ-1 enhanced both Cys-106 sulfonation and cell death. Nonetheless, expression of the DJ-1 C106A mutant, which fully prevents hyperoxidation, also showed exacerbated cell death responses to H 2 O 2 . A rational explanation for these findings is that DJ-1 Cys-106 forms disulfides with target proteins to limit oxidantinduced cell death. However, when Cys-106 is hyperoxidized, formation of these potentially protective heterodimeric disulfide complexes is limited, and so cell death is exacerbated.

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Peroxiredoxins as biomarkers of oxidative stress

Cited by 152 publications

References 66 publications

A novel 1-Cys thioredoxin peroxidase gene in Apis cerana cerana: characterization of AccTpx4 and its role in oxidative stresses

A novel 1-Cys thioredoxin peroxidase gene in Apis cerana cerana: characterization of AccTpx4 and its role in oxidative stresses

Unique Metabolic Features of Stem Cells, Cardiomyocytes, and Their Progenitors

Oxidant-induced Interprotein Disulfide Formation in Cardiac Protein DJ-1 Occurs via an Interaction with Peroxiredoxin 2

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