• Title/Summary/Keyword: Peroxiredoxin 3

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Change of Peroxiredoxin-5 Expression by Curcumin Treatment in Cerebral Ischemia (허혈성 대뇌손상시 curcumin 투여에 의한 peroxiredoxin-5 발현의 변화)

  • Gim, Sang-Ah;Koh, Phil-Ok
    • Journal of agriculture & life science
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    • v.50 no.3
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    • pp.129-139
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    • 2016
  • Curcumin plays a protective role in brain injury through its anti-oxidant and anti-inflammatory activities. Moreover, peroxiredoxin-5 exerts a protective effect against oxidative stress. The aim of this study was to investigate whether curcumin modulated the peroxiredoxin-5 expression in focal cerebral ischemic animal model. Middle cerebral artery occlusion(MCAO) was performed to induce cerebral ischemic injury in rats. Adult male rats were injected intraperitoneally with vehicle or curcumin(50mg/kg B.W.) 1 h after MCAO and cerebral cortex tissues were collected 24 h after MCAO. Photographs of hematoxylin and eosin staining showed that MCAO induced necrotic changes with scalloped shrunken form and apoptotic changes with nuclear chromatin condensations. However, curcumin treatment attenuated MCAO-induced histopathological changes. Moreover, this study clearly showed that peroxiredoxin-5 expression was decreased in MCAO operated animal with vehicle using a proteomics approach. However, this decrease in peroxiredoxin-5 expression was attenuated by curcumin treatment. Reverse-transcription PCR and Western blot analyses confirmed that curcumin treatment alleviated the MCAO injury-induced decrease in peroxiredoxin-5 expression(p<0.05). These results demonstrated that curcumin regulates peroxiredoxin-5 expression in MCAO animal model. In conclusion, our findings suggest that curcumin exerts a neuroprotective effect in cerebral ischemia by attenuating the MCAO-induced decrease in peroxiredoxin-5 expression.

Anti-effects of Photodynamic Therapy in Peroxiredoxin IV-induced AMC-HN3 Cell Lines

  • Ahn, Jin-Chul;Kang, Jung-Wook;Kim, Dae-Sik;Hong, Seong-No
    • 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.

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Peroxiredoxin 6 Promotes Lung Cancer Cell Invasion by Inducing Urokinase-Type Plasminogen Activator via p38 Kinase, Phosphoinositide 3-Kinase, and Akt

  • Lee, Seung Bum;Ho, Jin-Nyoung;Yoon, Sung Hwan;Kang, Ga Young;Hwang, Sang-Gu;Um, Hong-Duck
    • 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.

Distinct functional roles of peroxiredoxin isozymes and glutathione peroxidase from fission yeast, Schizosaccharomyces pombe

  • Kim, Ji-Sun;Bang, Mi-Ae;Lee, Song-Mi;Chae, Ho-Zoon;Kim, Kang-Hwa
    • 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.

Characterization of Haemophilus influenzae Peroxiredoxins

  • Hwang, Young-Sun;Chae, Ho-Zoon;Kim, Kang-Hwa
    • 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.

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The Effects of Peroxiredoxin III on Human HeLa Cell Proliferation

  • Choi, Soonyoung;Kang, Sangwon
    • IMMUNE NETWORK
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    • v.3 no.4
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    • pp.276-280
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    • 2003
  • Background: Peroxidases (Prx) of the peroxiredoxin family reduce hydrogen peroxide and alkyl hydroperoxides to water and alcohol respectively. Hydrogen peroxide is implicated as an intracellular messenger in various cellular responses such as proliferation and differentiation. And Prx I activity is regulated by Cdc-2 mediated phosphorylation. This work was undertaken to investigate the proliferation role of peroxiredoxin III as a member of Prx family in Prx III overexpressed HeLa cell line. Methods: To provide further evidence of proliferation, we selected Prx III stably expressed HeLa Tet-off cell lines. Cell proliferation was examined by using proliferation reagent WST-1 in the presence or absence of doxycycline. Prx III, 2-cys Prx enzymes exist as homodimer. The activation of Prx III heterodimer with induced and endogenous Prx III was examined by immunoprecipitation. Results: Immunoprecipitation analysis of the induced and endogenous Prx III with anti-myc showed that the induced wild type (WT) and dominant negative (DN) Prx III from HeLa Prx III Tet-off stable cell heterodimerized with endogenous Prx III each other. And the expression level of induced Prx III was examined after addition of doxycycline. By 72 hr, the expression level of induced Prx III was diminished gradually and the half-life of the induced wild type Prx III was approximately 17 hr. The proliferation experiment demonstrated that the relative proliferation value of induced and endogenous WT Prx III stable cell has no changes but the DN Prx III induced HeLa Tet-off stable cells were lower than endogenous Prx III. Conclusion: In conclusion, the HeLa dominant negative Prx III Tet-off stable cells were decreased the proliferation.

Peroxiredoxin 3 Has Important Roles on Arsenic Trioxide Induced Apoptosis in Human Acute Promyelocytic Leukemia Cell Line via Hyperoxidation of Mitochondrial Specific Reactive Oxygen Species

  • Mun, Yeung-Chul;Ahn, Jee Young;Yoo, Eun Sun;Lee, Kyoung Eun;Nam, Eun Mi;Huh, Jungwon;Woo, Hyun Ae;Rhee, Sue Goo;Seong, Chu Myong
    • Molecules and Cells
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    • v.43 no.9
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    • pp.813-820
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    • 2020
  • NB4 cell, the human acute promyelocytic leukemia (APL) cell line, was treated with various concentrations of arsenic trioxide (ATO) to induce apoptosis, measured by staining with 7-amino-actinomycin D (7-AAD) by flow cytometry. 2', 7'-dichlorodihydro-fluorescein-diacetate (DCF-DA) and MitoSOX™ Red mitochondrial superoxide indicator were used to detect intracellular and mitochondrial reactive oxygen species (ROS). The steady-state level of SO2 (Cysteine sulfinic acid, Cys-SO2H) form for peroxiredoxin 3 (PRX3) was measured by a western blot. To evaluate the effect of sulfiredoxin 1 depletion, NB4 cells were transfected with small interfering RNA and analyzed for their influence on ROS, redox enzymes, and apoptosis. The mitochondrial ROS of NB4 cells significantly increased after ATO treatment. NB4 cell apoptosis after ATO treatment increased in a time-dependent manner. Increased SO2 form and dimeric PRX3 were observed as a hyperoxidation reaction in NB4 cells post-ATO treatment, in concordance with mitochondrial ROS accumulation. Sulfiredoxin 1 expression is downregulated by small interfering RNA transfection, which potentiated mitochondrial ROS generation and cell growth arrest in ATO-treated NB4 cells. Our results indicate that ATO-induced ROS generation in APL cell mitochondria is attributable to PRX3 hyperoxidation as well as dimerized PRX3 accumulation, subsequently triggering apoptosis. The downregulation of sulfiredoxin 1 could amplify apoptosis in ATO-treated APL cells.

Plasma Nuclear Factor Kappa B and Serum Peroxiredoxin 3 in Early Diagnosis of Hepatocellular Carcinoma

  • Ismail, Saber;Mayah, Wael;Battia, Hassan El;Gaballah, Hanaa;Jiman-Fatani, Asif;Hamouda, Hala;Afifi, Mohamed A.;Elmashad, Nehal;Saadany, Sherif El
    • Asian Pacific Journal of Cancer Prevention
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    • v.16 no.4
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    • pp.1657-1663
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    • 2015
  • Background: Early diagnosis of hepatocellular carcinoma (HCC) is the most important step in successful treatment. However, it is usually rare due to the lack of a highly sensitive specific biomarker so that the HCC is usually fatal within few months after diagnosis. The aim of this work was to study the role of plasma nuclear factor kappa B (NF-${\kappa}B$) and serum peroxiredoxin 3 (PRDX3) as diagnostic biomarkers for early detection of HCC in a high-risk population. Materials and Methods: Plasma nuclear factor kappa B level (NF-${\kappa}B$) and serum peroxiredoxin 3 (PRDX3) levels were measured using enzyme linked immunosorbent assay (ELISA), in addition to alpha-fetoprotein (AFP) in 72 cirrhotic patients, 64 patients with HCC and 29 healthy controls. Results: NF-${\kappa}B$ and PRDX3 were significantly elevated in the HCC group in relation to the others. Higher area under curve (AUC) of 0.854 (for PRDX3) and 0.825 (for NF-${\kappa}B$) with sensitivity of 86.3% and 84.4% and specificity of 75.8% and 75.4% respectively, were found compared to AUC of alpha-fetoprotein (AFP) (0.65) with sensitivity of 72.4% and specificity of 64.3%. Conclusions: NF-${\kappa}B$ and PRDX3 may serve as early and sensitive biomarkers for early detection of HCC facilitating improved management. The role of nuclear factor kappa B (NF-${\kappa}B$) as a target for treatment of liver fibrosis and HCC must be widely evaluated.

Classification of Peroxiredoxin Subfamilies Using Regular Expressions

  • Chon, Jae Kyung;Choi, Jongkeun;Kim, Sang Soo;Shin, Whanchul
    • Genomics & Informatics
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    • v.3 no.2
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    • pp.55-60
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    • 2005
  • Peroxiredoxins (Prx's) are a superfamily of peroxidases that are ubiquitous in all super-kingdoms. Previous biochemical and structural studies have suggested that Prx's could be divided into five subfamilies (1-Cys, Typical 2-Cys, Atypical 2-Cys C-, L- and R- types). In this work, we have developed a set of regular expression patterns describing subfamily-specific spatial constraints of the key catalytic residues. Using these patterns, 1,016 Prx's available in public databases were classified into the five subfamilies. Our method performed well for most of the types except for Atypical 2 Cys R type.

Artificial Oxidation of Cysteine Residues in Peroxiredoxin 6 Detected by Twodimensional Gel Electrophoresis and Capillary Liquid Chromatography-Electrospray Mass Spectrometry

  • Kimata, Junko;Shigeri, Yasushi;Yoshida, Yasukazu;Niki, Etsuo;Kinumi, Tomoya
    • Mass Spectrometry Letters
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    • v.3 no.1
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    • pp.10-14
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    • 2012
  • Artificially oxidized cysteine residues in peroxiredoxin 6 (Prx6) were detected by electrospray interface capillary liquid chromatography-linear ion trap mass spectrometry after the preparation of two-dimensional gel electrophoresis (2D-GE). We used Prx6 as a model protein because it possesses only two cysteine residues at the 47th and 91st positions. The spot of Prx6 on 2D-GE undergoes a basic (isoelectric point, pI 6.6) to acidic (pI 6.2) shift by exposure to peroxide due to selective overoxidation of the active-site cysteine Cys-47 but not of Cys-91. However, we detected a tryptic peptide containing cysteine sulfonic acid at the 47th position from the basic spot and a peptide containing both oxidized Cys-47 and oxidized Cys-91 from the acidic spot of Prx6 after the separation by 2D-GE. We prepared two types of oxidized Prx6s: carrying oxidized Cys-47 (single oxidized Prx6), and other carrying both oxidized Cys-47 and Cys-91 (double oxidized Prx6). Using these oxidized Prx6s, the single oxidized Prx6 and double oxidized Prx6 migrated to pIs at 6.2 and 5.9, respectively. These results suggest that oxidized Cys-47 from the basic spot and oxidized Cys-91 from the acidic spot are generated by artificial oxidation during sample handling processes after isoelectric focusing of 2D-GE. Therefore, it is important to make sure of the origin of cysteine oxidation, if it is physiological or artificial, when an oxidized cysteine residue(s) is identified.