• Journal of Trauma and Injury
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• v.19 no.2
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• pp.105-112
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• 2006

Purpose: Many stresses produce reactive oxygen species and bring about mechanism of antioxidant reaction. Cytokine and a neurotransmitter through the cell membrane, as well as signal transduction through the cell membrane, are used for various pathological condition of the brain, such as neurodegenerative disease. There are several antioxidant enzymes in cells (superoxcide dismutase, glutathion peroxidasae, peroxiredoxin catalase, etc.) Methods: This study used single- or double-label immunohistochemical techniques to analyze mouse spinal neuron cells expressing Prx I and Prx III after acute mobilization stress. Results: Prx I was observed in dendritic cell of the gray matter of the spinal cord, and Prx III was observed in the cytoplasm of the GM of the spinal cord. Conclusion: The results of this study will help to explain differences of expression in the distributions of the peroxiredoxin enzymes of the spinal cord.

• BMB Reports
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• v.50 no.8
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• pp.391-392
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• 2017

Overexpression of mammalian 2-Cys peroxiredoxin (Prx) enzymes is observed in most cancer tissues. Nevertheless, their specific roles in colorectal cancer (CRC) progression has yet to be fully elucidated. Here, a novel molecular mechanism by which PrxII/Tankyrase (TNKS) interaction mediates survival of adenomatous polyposis coli (APC)-mutant CRC cells was explored. In mice with an inactivating APC mutation, a model of spontaneous intestinal tumorigenesis, deletion of PrxII reduced intestinal adenomatous polyposis and thereby increased survival. In APC-mutant human CRC cells, PrxII depletion hindered PARP-dependent Axin1 degradation through TNKS inactivation. $H_2O_2-sensitive$ Cys residues in the zinc-binding domain of TNKS1 was found to be crucial for PARsylation activity. Mechanistically, direct binding of PrxII to ARC4/5 domains of TNKS conferred vital redox protection against oxidative inactivation. As a proof-of-concept experiment, a chemical compound targeting PrxII inhibited the growth of tumors xenografted with APC-mutation-positive CRC cells. Collectively, the results provide evidence revealing a novel redox mechanism for regulating TNKS activity such that physical interaction between PrxII and TNKS promoted survival of APC-mutant colorectal cancer cells by PrxII-dependent antioxidant shielding.

• Biomedical Science Letters
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• v.14 no.4
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• pp.263-267
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• 2008

Photodynamic therapy (PDT) is a treatment utilizing the generation of singlet oxygen and other reactive oxygen species (ROS), which selectively accumulate in target cells. Peroxiredoxin (prx) plays an important role in eliminating peroxides generated during metabolism. Prx exert protective antioxidant role in cells though peroxidase activity. The aim of present work is to investigate the cytotoxicity of photofrin-mediated PDT in prx IV-transfectant AMC-HN3 cell lines. We confirmed that PDT has an effect on ROS generation in prx IV-induced cell lines. Treatment of PDT in prx IV-HN3 cell lines inhibits cytotoxic effects. Prx IV-induced HN3 cell lines resists in cell death during PDT. Also, prx IV-HN3 cell lines treated PDT inhibited ROS generation in contrast with vector control. We indicated that prx IV-induced AMC-HN3 cell lines have a function as inhibitors during PDT.

• Parasites, Hosts and Diseases
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• v.39 no.2
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• pp.133-141
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• 2001

A cDNA of 1.1 kb comprising the gene encoding the peroxiredoxin of Toxo-plasma gondii(TgPrx) has been cloned. The open reading frame of 591 Up was translated into a protein of 196 amino acids with a molecular mass of 25 kDa. Conserved 2 cysteine domains of Phe-Val-Cys-Pro and Glu-Val-Cys-Pro indicated TgPrx belonged to 2-Cys Prx families. TgPrx showed the highest homology with that of Arabidopsis thaliana by 53.9% followed by Entamoeba histolytica with 39.5% by the amino acid sequence alignment. Polyclonal antibody against recombinant TgPrx detected 25 kDa band in T. gondii without binding to host cell proteins TgPrx was located in the cytoplasm of T. gondii extracellularly or intracellularly by immunofluorescence assay. The expression of TgPrx was increased as early as 30 min after the treatment with artemisinin in the intracellular stage, while no changes in those of host Prx I and TgSOD. This result implies that TgPrx may function as an antioxidant protecting the cell from the attack of reactive oxygen intermediates. It is also suggested that TgPrx is a possible target of chemotherapy.

• Molecules and Cells
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• v.28 no.6
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• pp.583-588
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• 2009

The peroxiredoxin family of peroxidase has six mammalian members (Prx 1-6). Considering their frequent up-regulation in cancer cells, Prxs may contribute to cancer cells' survival in face of oxidative stress. Here, we show that Prx 6 promotes the invasiveness of lung cancer cells, accompanied by an increase in the activity of phosphoinositide 3-kinase (PI3K), the phosphorylation of p38 kinase and Akt, and the protein levels of uPA. Functional studies reveal that these components support Prx 6-induced invasion in the sequence p38 kinase/PI3K, Akt, and uPA. The findings provide a new understanding of the action of Prx 6 in cancer.

• BMB Reports
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• v.43 no.3
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• pp.170-175
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• 2010

Chaperone;Glutathione peroxidase;Peroxiredoxin;Schizosaccharomyces pombe;Thioredoxin peroxidase;To investigate the differences in the functional roles of peroxiredoxins (Prxs) and glutathione peroxidase (GPx) of Schizosaccharomyces pombe, we examined the peroxidase and molecular chaperone properties of the recombinant proteins. TPx (thioredoxin peroxidase) exhibited a capacity for peroxide reduction with the thioredoxin system. GPx also showed thioreoxin-dependent peroxidase activity rather than GPx activity. The peroxidase activity of BCP (bacterioferritin comigratory protein) was similar to that of TPx. However, peroxidase activity was not observed for PMP20 (peroxisomal membrane protein 20). TPx, PMP20, and GPx inhibited thermal aggregation of citrate synthase at 43$^{\circ}C$, but BCP failed to inhibit the aggregation. The chaperone activities of PMP20 and GPx were weaker than that of TPx. The peroxidase and chaperone properties of TPx, BCP, and GPx of the fission yeast are similar to those of Saccharomyces cerevisiae. The fission yeast PMP20 without thioredoxin-dependent peroxidase activity may act as a molecular chaperone.

• BMB Reports
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• v.33 no.6
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• pp.514-518
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• 2000

Two open reading frames of Haemophilus influenzae, HI0572 and HI0751, showing homology to a yeast thioredoxin peroxidase II (TPx II) and an E. coli thiol peroxidase $P_{20}$, respectively, were cloned and expressed in E. coli, and then the proteins were subsequently purified and characterized. HI0751 protein showed the thioredoxin (Trx)-dependent peroxidase activity, whereas HI0572 protein showed glutathione-dependent peroxidase. The HI0572 is the first peroxiredoxin with glutathione peroxidase activity rather than thioredoxin peroxidase. Purified HI0572 and HI0751 proteins protected specifically the inactivation of glutamine synthetase by metal catalyzed oxidation (MCO) systems composed of $Fe^{3+}$, $O_2$ and mercaptans such as dithiothreitol, ${\beta}-mercaptoethanol$ and glutathione (GSH). Unlike the HI0751 protein, the HI0572 protein was more effective in protecting glutamine synthetase from inactivation by the $GSH/Fe^{3+}/O_2$ system. It seems that these unique properties of the HI0572 protein are due to the structure containing a glutaredoxin domain at it's C-terminal in addition to a peroxiredoxin domain.

• Biomolecules & Therapeutics
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• v.30 no.4
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• pp.334-339
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• 2022

Peroxiredoxin 6 (PRDX6) is a bifunctional protein with both glutathione peroxidase and calcium-independent phospholipase activity. Recently, we reported that PRDX6 plays an important role in dopaminergic neurodegeneration in Parkinson's disease. However, the relationship between PRDX6 function and emotional behavior remains elusive. In the present study, we examined depression- and anxiety-like behaviors in PRDX6-overexpressing transgenic (PRDX6-Tg) mice using the forced swim test, tail suspension test, open field paradigm, and elevated plus-maze. PRDX6-Tg mice exhibited depression-like behaviors and low anxiety. In particular, female PRDX6-Tg mice exhibited anxiolytic behavior in the open field test. Furthermore, the serotonin content in the cortex and 5-hydroxytryptophan-induced head twitch response were both reduced in PRDX6-Tg mice. Interestingly, levels of dopa decarboxylase expression in the cortex were decreased in male PRDX6-Tg mice but not in female mice. Our findings provide novel insights into the role of PRDX6 in 5-HT synthesis and suggest that PRDX6 overexpression can induce depression-like behaviors via downregulation of the serotonergic neuronal system.

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2003.10a
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• pp.80-84
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• 2003

The thioredoxin peroxidase (TPx) is an antioxidant member of the peroxiredoxin family of enzymes. The TPx enzyme system has been implicated in the elimination of hydrogen peroxide and hydroxyl radicals generated during cellular processes. Such reactive molecules have been shown to cause damage to all major classes of biological macromolecules, including lipid, protein and DNA. Compared to mammalian peroxiredoxin genes, little is known about the insect TPx. (omitted)

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2003.10a
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• pp.130-133
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• 2003

Peroxiredoxins are a family of antioxidant proteins ubiquitously found in all living organisms. A type of peroxidase enzyme, named thioredoxin peroxidase (TPx), that reduces $H_2O$$_2$ with the use of electrons from thioredoxin and contains two essential cysteines was identified in a wide variety of organisms ranging from prokaryotes to mammals. TPx homologs, termed peroxiredoxin (Prx), have also been identified and include several proteins, designated 1-Cys Prx, that contain only one conserved cysteine. (omitted)