Peroxiredoxin, a Novel Family of Peroxidases

Rhee, Sue Goo; Kang, Sang Won; Chang, Tong‐Shin; Jeong, Woojin; Kim, Kanghwa

doi:10.1080/15216540252774748

Cited by 569 publications

(474 citation statements)

References 33 publications

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“…Mammalian PRDXs are divided into three categories based on their number of conserved Cys residues and catalytic mechanism: 2‐Cys PRDXs (PRDX1–4), atypical 2‐Cys PRDX (PRDX5) and 1‐Cys PRDX (Prx6) 5. All PRDXs contain a thioredoxin fold with a few additional secondary structure elements present as insertions 5.…”

Section: Structure Functions Of Prdx1 and Its Role In Ros‐dependent mentioning

confidence: 99%

“…All PRDXs contain a thioredoxin fold with a few additional secondary structure elements present as insertions 5. PRDX1 contains a conserved Cys 52 at the N‐terminal and a conserved Cys 173 at the C‐terminal 7.…”

Section: Structure Functions Of Prdx1 and Its Role In Ros‐dependent mentioning

confidence: 99%

“…The net emission of ROS depends upon the balance between free radical production (pro‐oxidative process) and its elimination by antioxidants (antioxidant defense process) 4. Peroxiredoxins (PRDXs), a family of this kind of antioxidants, are classified on the basis of having either one (1‐Cys) or two (2‐Cys) conserved cysteine residues 5. PRDX1 is a member of the 2‐Cys PRDXs subfamily and is present mainly in the cytosol 6.…”

Section: Introductionmentioning

confidence: 99%

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Peroxiredoxin 1 – an antioxidant enzyme in cancer

Ding

Fan

2016

J Cellular Molecular Medi

152

116

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Peroxiredoxins (PRDXs), a ubiquitous family of redox‐regulating proteins, are reported of potential to eliminate various reactive oxygen species (ROS). As a major member of the antioxidant enzymes, PRDX1 can become easily over‐oxidized on its catalytically active cysteine induced by a variety of stimuli in vitro and in vivo. In nucleus, oligomeric PRDX1 directly associates with p53 or transcription factors such as c‐Myc, NF‐κB and AR, and thus affects their bioactivities upon gene regulation, which in turn induces or suppresses cell death. Additionally, PRDX1 in cytoplasm has anti‐apoptotic potential through direct or indirect interactions with several ROS‐dependent (redox regulation) effectors, including ASK1, p66Shc, GSTpi/JNK and c‐Abl kinase. PRDX1 is proven to be a versatile molecule regulating cell growth, differentiation and apoptosis. Recent studies have found that PRDX1 and/or PRDX1‐regulated ROS‐dependent signalling pathways play an important role in the progression and metastasis of human tumours, particularly in breast, oesophageal and lung cancers. In this paper, we review the structure, effector functions of PRDX1, its role in cancer and the pivotal role of ROS in anticancer treatment.

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Section: Structure Functions Of Prdx1 and Its Role In Ros‐dependent mentioning

confidence: 99%

Section: Structure Functions Of Prdx1 and Its Role In Ros‐dependent mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Peroxiredoxin 1 – an antioxidant enzyme in cancer

Ding

Fan

2016

J Cellular Molecular Medi

152

116

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“…By contrast, 1-cys peroxiredoxin (1-cysPrx or Prx VI) † has a single conserved cysteine (5) and does not use thioredoxin as reductant (5, 6). This peroxiredoxin is expressed in all tissues but at particularly high levels in brain, eye, testes, and lung (2,7,8). Expression of 1-cysPrx protein or mRNA is decreased in a mouse that is susceptible to experimental atherosclerosis (9) and is elevated in brains of patients with Parkinsonian dementia (10), sporadic Creutzfeldt-Jacob disease (11), and Pick disease (12), in lungs from newborns (13), in malignant mesothelioma (14), in the healing edge of skin wounds (15), and in experimental cellular premature senescence (16).…”

mentioning

confidence: 99%

“…P eroxiredoxins are a superfamily of nonheme and nonselenium peroxidases that are widely distributed throughout all phyla (1)(2)(3)(4). Of the six mammalian peroxiredoxins, five (Prx I-V) contain two conserved cysteines that participate in intramolecular disulfide͞sulfhydryl redox cycling with thioredoxin resulting in reduction of H 2 O 2 and organic hydroperoxides into corresponding alcohols (2).…”

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confidence: 99%

Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with πGST

Manevich

Feinstein

Fisher

2004

Proc. Natl. Acad. Sci. U.S.A.

320

263

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1-cys peroxiredoxin (1-cysPrx), a member of the peroxiredoxin superfamily, can protect cells against membrane oxidation through glutathione (GSH)-dependent reduction of phospholipid hydroperoxides to corresponding alcohols. However, purified native or recombinant enzyme in vitro generally lacks GSH peroxidase (GPx) activity because of oxidation of its single conserved cysteine. Reduction of the resultant oxidized cysteine is difficult because of its protected location within the homodimer formed by the oxidized protein monomers. Partial purification of 1-cysPrx from bovine lung revealed the presence of GST in an active preparation, while purification to homogeneity yielded enzyme that inactivated with time. We show that heterodimerization of 1-cysPrx with GSH-saturated GST results in glutathionylation of the oxidized cysteine in 1-cysPrx followed by subsequent spontaneous reduction of the mixed disulfide and restoration of enzymatic activity. Maximum activation of 1-cysPrx occurred with a 1:1 molar ratio of GSH-saturated GST and a 2:1 molar ratio of GSH to 1-cysPrx. Liposome-mediated delivery of oxidized recombinant enzyme into NCI-H441 cells that lack 1-cysPrx but express GST resulted in 1-cysPrx activation, whereas activation in MCF7 cells required co-delivery of GST. Our data indicate a physiological mechanism for glutathionylation of the oxidized catalytic cysteine of 1-cysPrx by its heterodimerization with GST followed by its GSH-mediated reduction and enzyme activation. P eroxiredoxins are a superfamily of nonheme and nonselenium peroxidases that are widely distributed throughout all phyla (1-4). Of the six mammalian peroxiredoxins, five (Prx I-V) contain two conserved cysteines that participate in intramolecular disulfide͞sulfhydryl redox cycling with thioredoxin resulting in reduction of H 2 O 2 and organic hydroperoxides into corresponding alcohols (2). By contrast, 1-cys peroxiredoxin (1-cysPrx or Prx VI) † has a single conserved cysteine (5) and does not use thioredoxin as reductant (5, 6). This peroxiredoxin is expressed in all tissues but at particularly high levels in brain, eye, testes, and lung (2,7,8). Expression of 1-cysPrx protein or mRNA is decreased in a mouse that is susceptible to experimental atherosclerosis (9) and is elevated in brains of patients with Parkinsonian dementia (10), sporadic Creutzfeldt-Jacob disease (11), and Pick disease (12), in lungs from newborns (13), in malignant mesothelioma (14), in the healing edge of skin wounds (15), and in experimental cellular premature senescence (16). 1-cysPrx can reduce phospholipid and other hydroperoxides (6) and protects against cellular membrane damage (17, 18). This enzyme has phospholipase A 2 activity (19), participates in the activation of neutrophil NADPH oxidase through its interaction with p67 phox (20), and prevent methemoglobin formation in erythrocyte hemolysates (21).1-cysPrx catalysis results in the peroxide-mediated oxidation of its Cys-47 to sulfenic acid as deduced from 1-cysPrx crystallization (22). Reduction of the sul...

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Control of Primary Metabolism in Plants

Plaxton¹,

McManus²

2006

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Evaluation of the transcriptome and genome to inform the study of metabolic control in plants OLIVER THIMM, OLIVER E. BLÄSING, BJORN USADEL and YVES GIBON 2.3.3 Mitochondrial and chloroplast proteomes 2.3.4 Other subcellular proteomes 2.3.5 A stamp of authenticity for the subcellular protein postcode? 2.4 Quantitative analyses of the proteome 2.4.1 Examples of quantitative proteomics 2.4.2 The use of high-throughput measurements of enzyme activity as a proxy for quantitative proteomics 2.5 The use of proteomics to investigate post-translational modification of proteins 2.5.1 Systematic identification of phosphorylated proteins 2.5.2 Systematic identification of protein redox modifications 2.6 The use of proteomics to investigate protein-protein interactions 2.7 Future perspectives References

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Peroxiredoxin, a Novel Family of Peroxidases

Cited by 569 publications

References 33 publications

Peroxiredoxin 1 – an antioxidant enzyme in cancer

Peroxiredoxin 1 – an antioxidant enzyme in cancer

Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with πGST

Control of Primary Metabolism in Plants

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