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Volumn 81, Issue , 2015, Pages 58-68

Glutathione peroxidase 8 is transcriptionally regulated by HIFα and modulates growth factor signaling in HeLa cells

Author keywords

Endoplasmic reticulum; Free radicals; GPx8; Hydroperoxide; Hypoxia; Receptor tyrosine kinase; Redox Signaling

Indexed keywords

FIBROBLAST GROWTH FACTOR; GLUTATHIONE PEROXIDASE 8; HYPOXIA INDUCIBLE FACTOR; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 2ALPHA; HYPOXIA INDUCIBLE FACTOR PROLINE DIOXYGENASE; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; OXIDOREDUCTASE; PROTEIN KINASE B; SMALL INTERFERING RNA; STABILIZING AGENT; UNCLASSIFIED DRUG; 2,2' BIPYRIDINE; BASIC HELIX LOOP HELIX TRANSCRIPTION FACTOR; DIETHYL SUCCINATE; ENDOTHELIAL PAS DOMAIN-CONTAINING PROTEIN 1; GPX8 PROTEIN, HUMAN; HIF1A PROTEIN, HUMAN; HYBRID PROTEIN; INSULIN; LUCIFERASE; MAPK1 PROTEIN, HUMAN; PEROXIDASE; SUCCINIC ACID DERIVATIVE;

EID: 84923354606     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2014.12.020     Document Type: Article
Times cited : (27)

References (53)
  • 1
    • 33745631769 scopus 로고    scopus 로고
    • 2, a necessary evil for cell signaling
    • 2, a necessary evil for cell signaling Science 312 2006 1882 1883
    • (2006) Science , vol.312 , pp. 1882-1883
    • Rhee, S.G.1
  • 2
    • 75749136883 scopus 로고    scopus 로고
    • Signaling functions of reactive oxygen species
    • H.J. Forman, M. Maiorino, and F. Ursini Signaling functions of reactive oxygen species Biochemistry 49 2010 835 842
    • (2010) Biochemistry , vol.49 , pp. 835-842
    • Forman, H.J.1    Maiorino, M.2    Ursini, F.3
  • 3
    • 79954504166 scopus 로고    scopus 로고
    • Basic principles and emerging concepts in the redox control of transcription factors
    • R. Brigelius-Flohé, and L. Flohé Basic principles and emerging concepts in the redox control of transcription factors Antioxid. Redox Signaling 15 2011 2335 2381
    • (2011) Antioxid. Redox Signaling , vol.15 , pp. 2335-2381
    • Brigelius-Flohé, R.1    Flohé, L.2
  • 4
    • 77956207316 scopus 로고    scopus 로고
    • Changing paradigms in thiology from antioxidant defense toward redox regulation
    • L. Flohé Changing paradigms in thiology from antioxidant defense toward redox regulation Methods Enzymol. 473 2010 1 39
    • (2010) Methods Enzymol. , vol.473 , pp. 1-39
    • Flohé, L.1
  • 7
    • 72649102227 scopus 로고    scopus 로고
    • Catalytic mechanisms and specificities of glutathione peroxidases: Variations of a basic scheme
    • S. Toppo, L. Flohé, F. Ursini, S. Vanin, and M. Maiorino Catalytic mechanisms and specificities of glutathione peroxidases: variations of a basic scheme Biochim. Biophys. Acta 1790 2009 1486 1500
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 1486-1500
    • Toppo, S.1    Flohé, L.2    Ursini, F.3    Vanin, S.4    Maiorino, M.5
  • 8
    • 0025060737 scopus 로고
    • Protective action of phospholipid hydroperoxide glutathione peroxidase against membrane-damaging lipid peroxidation: In situ reduction of phospholipid and cholesterol hydroperoxides
    • J.P. Thomas, M. Maiorino, F. Ursini, and A.W. Girotti Protective action of phospholipid hydroperoxide glutathione peroxidase against membrane-damaging lipid peroxidation: in situ reduction of phospholipid and cholesterol hydroperoxides J. Biol. Chem. 265 1990 454 461
    • (1990) J. Biol. Chem. , vol.265 , pp. 454-461
    • Thomas, J.P.1    Maiorino, M.2    Ursini, F.3    Girotti, A.W.4
  • 14
    • 6344270258 scopus 로고    scopus 로고
    • Identification of a novel putative non-selenocysteine containing phospholipid hydroperoxide glutathione peroxidase (NPGPx) essential for alleviating oxidative stress generated from polyunsaturated fatty acids in breast cancer cells
    • A. Utomo, X. Jiang, S. Furuta, J. Yun, D.S. Levin, Y.C.J. Wang, K.V. Desai, J.E. Green, P.L. Chen, and W.H. Lee Identification of a novel putative non-selenocysteine containing phospholipid hydroperoxide glutathione peroxidase (NPGPx) essential for alleviating oxidative stress generated from polyunsaturated fatty acids in breast cancer cells J. Biol. Chem. 279 2004 43522 43529
    • (2004) J. Biol. Chem. , vol.279 , pp. 43522-43529
    • Utomo, A.1    Jiang, X.2    Furuta, S.3    Yun, J.4    Levin, D.S.5    Wang, Y.C.J.6    Desai, K.V.7    Green, J.E.8    Chen, P.L.9    Lee, W.H.10
  • 16
    • 0036021259 scopus 로고    scopus 로고
    • GPX5 is present in the mouse caput and cauda epididymidis lumen at three different locations
    • H. Rejraji, P. Vernet, and J.R. Drevet GPX5 is present in the mouse caput and cauda epididymidis lumen at three different locations Mol. Reprod. Dev. 63 2002 96 103
    • (2002) Mol. Reprod. Dev. , vol.63 , pp. 96-103
    • Rejraji, H.1    Vernet, P.2    Drevet, J.R.3
  • 17
    • 46449103532 scopus 로고    scopus 로고
    • Evolutionary and structural insights into the multifaceted glutathione peroxidase (Gpx) superfamily
    • S. Toppo, S. Vanin, V. Bosello, and S.C.E. Tosatto Evolutionary and structural insights into the multifaceted glutathione peroxidase (Gpx) superfamily Antioxid. Redox Signaling 10 2008 1501 1513
    • (2008) Antioxid. Redox Signaling , vol.10 , pp. 1501-1513
    • Toppo, S.1    Vanin, S.2    Bosello, V.3    Tosatto, S.C.E.4
  • 19
    • 79960191503 scopus 로고    scopus 로고
    • Cysteine mutant of mammalian GPx4 rescues cell death induced by disruption of the wild-type selenoenzyme
    • A.M. Mannes, A. Seiler, V. Bosello, M. Maiorino, and M. Conrad Cysteine mutant of mammalian GPx4 rescues cell death induced by disruption of the wild-type selenoenzyme FASEB J. 25 2011 2135 2144
    • (2011) FASEB J. , vol.25 , pp. 2135-2144
    • Mannes, A.M.1    Seiler, A.2    Bosello, V.3    Maiorino, M.4    Conrad, M.5
  • 21
    • 84887465759 scopus 로고    scopus 로고
    • Glutathione peroxidase 7 utilizes hydrogen peroxide generated by ero1α to promote oxidative protein folding
    • L. Wang, L. Zhang, Y. Niu, R. Sitia, and C.C. Wang Glutathione peroxidase 7 utilizes hydrogen peroxide generated by ero1α to promote oxidative protein folding Antioxid. Redox Signaling 20 2014 545 556
    • (2014) Antioxid. Redox Signaling , vol.20 , pp. 545-556
    • Wang, L.1    Zhang, L.2    Niu, Y.3    Sitia, R.4    Wang, C.C.5
  • 24
    • 58249084836 scopus 로고    scopus 로고
    • DNA hypermethylation regulates the expression of members of the Mu-class glutathione S-transferases and glutathione peroxidases in Barretts adenocarcinoma
    • D.F. Peng, M. Razvi, H. Chen, K. Washington, A. Roessner, R. Schneider-Stock, and W. El-Rifai DNA hypermethylation regulates the expression of members of the Mu-class glutathione S-transferases and glutathione peroxidases in Barretts adenocarcinoma Gut 58 2009 5 15
    • (2009) Gut , vol.58 , pp. 5-15
    • Peng, D.F.1    Razvi, M.2    Chen, H.3    Washington, K.4    Roessner, A.5    Schneider-Stock, R.6    El-Rifai, W.7
  • 28
    • 84857918033 scopus 로고    scopus 로고
    • Transcriptomic and proteomic profiling of KEAP1 disrupted and sulforaphane-treated human breast epithelial cells reveals common expression profiles
    • A.S. Agyeman, R. Chaerkady, P.G. Shaw, N.E. Davidson, K. Visvanathan, A. Pandey, and T.W. Kensler Transcriptomic and proteomic profiling of KEAP1 disrupted and sulforaphane-treated human breast epithelial cells reveals common expression profiles Breast Cancer Res. Treat. 132 2012 175 187
    • (2012) Breast Cancer Res. Treat. , vol.132 , pp. 175-187
    • Agyeman, A.S.1    Chaerkady, R.2    Shaw, P.G.3    Davidson, N.E.4    Visvanathan, K.5    Pandey, A.6    Kensler, T.W.7
  • 29
    • 3042621447 scopus 로고    scopus 로고
    • Determinants of human plasma glutathione peroxidase (GPx-3) expression
    • C. Bierl, B. Voetsch, R.C. Jin, D.E. Handy, and J. Loscalzo Determinants of human plasma glutathione peroxidase (GPx-3) expression J. Biol. Chem. 279 2004 26839 26845
    • (2004) J. Biol. Chem. , vol.279 , pp. 26839-26845
    • Bierl, C.1    Voetsch, B.2    Jin, R.C.3    Handy, D.E.4    Loscalzo, J.5
  • 31
    • 35448995703 scopus 로고    scopus 로고
    • Transcription of mammalian cytochrome c oxidase subunit IV 2 is controlled by a novel conserved oxygen responsive element
    • M. Hüttemann, I. Lee, J. Liu, and L.I. Grossman Transcription of mammalian cytochrome c oxidase subunit IV 2 is controlled by a novel conserved oxygen responsive element FEBS J. 274 2007 5737 5748
    • (2007) FEBS J. , vol.274 , pp. 5737-5748
    • Hüttemann, M.1    Lee, I.2    Liu, J.3    Grossman, L.I.4
  • 32
    • 76349095132 scopus 로고    scopus 로고
    • Defining the role of hypoxia-inducible factor 1 in cancer biology and therapeutics
    • G.L. Semenza Defining the role of hypoxia-inducible factor 1 in cancer biology and therapeutics Oncogene 29 2010 625 634
    • (2010) Oncogene , vol.29 , pp. 625-634
    • Semenza, G.L.1
  • 33
    • 9444283176 scopus 로고    scopus 로고
    • Differentiating the functional role of hypoxia-inducible factor (HIF)-1alpha and HIF-2alpha (EPAS-1) by the use of RNA interference: Erythropoietin is a HIF-2alpha target gene in Hep3B and Kelly cells
    • C. Warnecke, Z. Zaborowska, J. Kurreck, V.A. Erdmann, U. Frei, M. Wiesener, and K.-U. Eckardt Differentiating the functional role of hypoxia-inducible factor (HIF)-1alpha and HIF-2alpha (EPAS-1) by the use of RNA interference: erythropoietin is a HIF-2alpha target gene in Hep3B and Kelly cells FASEB J. 18 2004 1462 1464
    • (2004) FASEB J. , vol.18 , pp. 1462-1464
    • Warnecke, C.1    Zaborowska, Z.2    Kurreck, J.3    Erdmann, V.A.4    Frei, U.5    Wiesener, M.6    Eckardt, K.-U.7
  • 34
    • 0141706719 scopus 로고    scopus 로고
    • Distinct promoters determine alternative transcription of gpx-4 into phospholipid-hydroperoxide glutathione peroxidase variants
    • M. Maiorino, M. Scapin, F. Ursini, M. Biasolo, V. Bosello, and L. Flohé Distinct promoters determine alternative transcription of gpx-4 into phospholipid-hydroperoxide glutathione peroxidase variants J. Biol. Chem. 278 2003 34286 34290
    • (2003) J. Biol. Chem. , vol.278 , pp. 34286-34290
    • Maiorino, M.1    Scapin, M.2    Ursini, F.3    Biasolo, M.4    Bosello, V.5    Flohé, L.6
  • 35
    • 0032891708 scopus 로고    scopus 로고
    • Induction and nuclear translocation of hypoxia-inducible factor-1 (HIF-1): Heterodimerization with ARNT is not necessary for nuclear accumulation of HIF-1alpha
    • D. Chilov, G. Camenisch, I. Kvietikova, U. Ziegler, M. Gassmann, and R.H. Wenger Induction and nuclear translocation of hypoxia-inducible factor-1 (HIF-1): heterodimerization with ARNT is not necessary for nuclear accumulation of HIF-1alpha J. Cell Sci. 112 1999 1203 1212
    • (1999) J. Cell Sci. , vol.112 , pp. 1203-1212
    • Chilov, D.1    Camenisch, G.2    Kvietikova, I.3    Ziegler, U.4    Gassmann, M.5    Wenger, R.H.6
  • 36
    • 84923379742 scopus 로고    scopus 로고
    • Bioinformatic prediction and experimental validation of transcription factors for glutathione peroxidases
    • K. Meyer Bioinformatic prediction and experimental validation of transcription factors for glutathione peroxidases Toppo, S.; Maiorino, M., supervisors 2010 1 61
    • (2010) Toppo, S.; Maiorino, M., Supervisors , pp. 1-61
    • Meyer, K.1
  • 37
    • 0027138262 scopus 로고
    • Novel inhibitors of prolyl 4-hydroxylase. 5. The intriguing structure-activity relationships seen with 2,2′-bipyridine and its 5,5′-dicarboxylic acid derivatives
    • N.J. Hales, and J.F. Beattie Novel inhibitors of prolyl 4-hydroxylase. 5. The intriguing structure-activity relationships seen with 2,2′-bipyridine and its 5,5′-dicarboxylic acid derivatives J. Med. Chem. 36 1993 3853 3858
    • (1993) J. Med. Chem. , vol.36 , pp. 3853-3858
    • Hales, N.J.1    Beattie, J.F.2
  • 38
    • 33947520506 scopus 로고    scopus 로고
    • Inhibition of HIF hydroxylases by citric acid cycle intermediates: Possible links between cell metabolism and stabilization of HIF
    • P. Koivunen, M. Hirsilä, A.M. Remes, I.E. Hassinen, K.I. Kivirikko, and J. Myllyharju Inhibition of HIF hydroxylases by citric acid cycle intermediates: possible links between cell metabolism and stabilization of HIF J. Biol. Chem. 282 2006 4524 4532
    • (2006) J. Biol. Chem. , vol.282 , pp. 4524-4532
    • Koivunen, P.1    Hirsilä, M.2    Remes, A.M.3    Hassinen, I.E.4    Kivirikko, K.I.5    Myllyharju, J.6
  • 39
    • 60549083256 scopus 로고    scopus 로고
    • Regulation of cancer cell metabolism by hypoxia-inducible factor 1
    • G.L. Semenza Regulation of cancer cell metabolism by hypoxia-inducible factor 1 Semin. Cancer Biol. 19 2009 12 16
    • (2009) Semin. Cancer Biol. , vol.19 , pp. 12-16
    • Semenza, G.L.1
  • 40
    • 46249108461 scopus 로고    scopus 로고
    • Regulation of ROS signal transduction by NADPH oxidase 4 localization
    • K. Chen, M.T. Kirber, H. Xiao, Y. Yang, and J.F. Keaney Regulation of ROS signal transduction by NADPH oxidase 4 localization J. Cell Biol. 181 2008 1129 1139
    • (2008) J. Cell Biol. , vol.181 , pp. 1129-1139
    • Chen, K.1    Kirber, M.T.2    Xiao, H.3    Yang, Y.4    Keaney, J.F.5
  • 41
    • 84865429409 scopus 로고    scopus 로고
    • Passing the baton: The HIF switch
    • M.Y. Koh, and G. Powis Passing the baton: the HIF switch Trends Biochem. Sci. 37 2012 364 372
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 364-372
    • Koh, M.Y.1    Powis, G.2
  • 42
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • A. Salmeen, J.N. Andersen, M.P. Myers, T.C. Meng, J.A. Hinks, N.K. Tonks, and D. Barford Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate Nature 423 2003 769 773
    • (2003) Nature , vol.423 , pp. 769-773
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Meng, T.C.4    Hinks, J.A.5    Tonks, N.K.6    Barford, D.7
  • 43
    • 0026584285 scopus 로고
    • The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence
    • J.V. Frangioni, P.H. Beahm, V. Shifrin, C.A. Jost, and B.G. Neel The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence Cell 68 1992 545 560
    • (1992) Cell , vol.68 , pp. 545-560
    • Frangioni, J.V.1    Beahm, P.H.2    Shifrin, V.3    Jost, C.A.4    Neel, B.G.5
  • 44
    • 84872770077 scopus 로고    scopus 로고
    • PTP1B and TCPTP - Nonredundant phosphatases in insulin signaling and glucose homeostasis
    • T. Tiganis PTP1B and TCPTP - nonredundant phosphatases in insulin signaling and glucose homeostasis FEBS J. 280 2013 445 458
    • (2013) FEBS J. , vol.280 , pp. 445-458
    • Tiganis, T.1
  • 46
    • 34548572037 scopus 로고    scopus 로고
    • Glutathione peroxidase 3, deleted or methylated in prostate cancer, suppresses prostate cancer growth and metastasis
    • Y.P. Yu, G. Yu, G. Tseng, K. Cieply, J. Nelson, M. Defrances, R. Zarnegar, G. Michalopoulos, and J.-H. Luo Glutathione peroxidase 3, deleted or methylated in prostate cancer, suppresses prostate cancer growth and metastasis Cancer Res. 67 2007 8043 8050
    • (2007) Cancer Res. , vol.67 , pp. 8043-8050
    • Yu, Y.P.1    Yu, G.2    Tseng, G.3    Cieply, K.4    Nelson, J.5    Defrances, M.6    Zarnegar, R.7    Michalopoulos, G.8    Luo, J.-H.9
  • 48
    • 84871322482 scopus 로고    scopus 로고
    • Glutathione peroxidase overexpression causes aberrant ERK activation in neonatal mouse cortex after hypoxic preconditioning
    • D. Autheman, R.A. Sheldon, N. Chaudhuri, S. Arx, von, C. Siegenthaler, D.M. Ferriero, and S. Christen Glutathione peroxidase overexpression causes aberrant ERK activation in neonatal mouse cortex after hypoxic preconditioning Pediatr. Res. 72 2012 568 575
    • (2012) Pediatr. Res. , vol.72 , pp. 568-575
    • Autheman, D.1    Sheldon, R.A.2    Chaudhuri, N.3    Von, A.S.4    Siegenthaler, C.5    Ferriero, D.M.6    Christen, S.7
  • 49
    • 34548803430 scopus 로고    scopus 로고
    • Translational up-regulation of the EGFR by tumor hypoxia provides a nonmutational explanation for its overexpression in human cancer
    • A. Franovic, L. Gunaratnam, K. Smith, I. Robert, D. Patten, and S. Lee Translational up-regulation of the EGFR by tumor hypoxia provides a nonmutational explanation for its overexpression in human cancer Proc. Natl. Acad. Sci. USA 104 2007 13092 13097
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 13092-13097
    • Franovic, A.1    Gunaratnam, L.2    Smith, K.3    Robert, I.4    Patten, D.5    Lee, S.6
  • 52
    • 13144275217 scopus 로고    scopus 로고
    • Dynamic balancing of the dual nature of HIF-1alpha for cell survival
    • M. Koshiji, and L.E. Huang Dynamic balancing of the dual nature of HIF-1alpha for cell survival Cell Cycle 3 2004 853 854
    • (2004) Cell Cycle , vol.3 , pp. 853-854
    • Koshiji, M.1    Huang, L.E.2
  • 53
    • 0037517089 scopus 로고    scopus 로고
    • The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1 Lα
    • B. Gess, K.H. Hofbauer, R.H. Wenger, C. Lohaus, H.E. Meyer, and A. Kurtz The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1 Lα Eur. J. Biochem. 270 2003 2228 2235
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2228-2235
    • Gess, B.1    Hofbauer, K.H.2    Wenger, R.H.3    Lohaus, C.4    Meyer, H.E.5    Kurtz, A.6


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