메뉴 건너뛰기




Volumn 5, Issue 12, 2010, Pages 1-11

Nuclear shield: A multi-enzyme task-force for nucleus protection

Author keywords

[No Author keywords available]

Indexed keywords

CATALASE; GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE; NUCLEAR PROTEIN; ANTIOXIDANT; CATION;

EID: 78650744699     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0014125     Document Type: Article
Times cited : (17)

References (53)
  • 1
    • 0019842267 scopus 로고
    • The nuclear envelope and the architecture of the nuclear periphery
    • Franke W W, Scheer U, Krohne G, Jarasch E-D (1981) The nuclear envelope and the architecture of the nuclear periphery. J Cell Biol 91: 39-50.
    • (1981) J Cell Biol , vol.91 , pp. 39-50
    • Franke, W.W.1    Scheer, U.2    Krohne, G.3    Jarasch, E.-D.4
  • 2
    • 0033643459 scopus 로고    scopus 로고
    • Antioxidant regulation of genes encoding enzymes that detoxify xenobiotics and carcinogens
    • Dhakshinamoorthy S, Long DJ, 2nd, Jaiswal AK (2000) Antioxidant regulation of genes encoding enzymes that detoxify xenobiotics and carcinogens. Curr Top Cell Regul 36: 201-216.
    • (2000) Curr Top Cell Regul , vol.36 , pp. 201-216
    • Dhakshinamoorthy, S.1    Long, D.J.2    Jaiswal, A.K.3
  • 3
    • 7744235173 scopus 로고    scopus 로고
    • Cellular and subcellular localization of heme oxygenase-2 in monkey retina
    • Ma N, Ding X, Doi M, Izumi N, Semba R (2004) Cellular and subcellular localization of heme oxygenase-2 in monkey retina. J Neurocytol 33: 407-415.
    • (2004) J Neurocytol , vol.33 , pp. 407-415
    • Ma, N.1    Ding, X.2    Doi, M.3    Izumi, N.4    Semba, R.5
  • 4
    • 33751094332 scopus 로고    scopus 로고
    • HO-2 provides endogenous protection against oxidative stress and apoptosis caused by TNF-alpha in cerebral vascular endothelial cells
    • Basuroy S, Bhattacharya S, Tcheranova D, Qu Y, Regan RF, et al. (2006) HO-2 provides endogenous protection against oxidative stress and apoptosis caused by TNF-alpha in cerebral vascular endothelial cells. Am J Physiol Cell Physiol 291: C897-C908.
    • (2006) Am J Physiol Cell Physiol , vol.291 , pp. 897-908
    • Basuroy, S.1    Bhattacharya, S.2    Tcheranova, D.3    Qu, Y.4    Regan, R.F.5
  • 5
    • 55549089967 scopus 로고    scopus 로고
    • Human DNA polymerase iota protects cells against oxidative stress
    • Petta TB, Nakajima S, Zlatanou A, Despras E, Sarasin A, et al. (2008) Human DNA polymerase iota protects cells against oxidative stress. EMBO J 27: 2883-2895.
    • (2008) EMBO J , vol.27 , pp. 2883-2895
    • Petta, T.B.1    Nakajima, S.2    Zlatanou, A.3    Despras, E.4    Sarasin, A.5
  • 6
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evolution of glutathione transferases: Implications for classification of non- mammalian members of an ancient enzyme superfamily
    • Sheehan D, Meade G, Foley VM, Dowd CA (2001) Structure, function and evolution of glutathione transferases: implications for classification of non- mammalian members of an ancient enzyme superfamily. Biochem J 360: 1-16.
    • (2001) Biochem J , vol.360 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.A.4
  • 7
    • 34250355613 scopus 로고    scopus 로고
    • Glutathione transferases sequester toxic dinitrosyl-iron complexes in cells
    • Pedersen JZ, De Maria F, Turella P, Federici G, Mattei M, et al. (2007) Glutathione transferases sequester toxic dinitrosyl-iron complexes in cells. J Biol Chem 282: 6364-6371.
    • (2007) J Biol Chem , vol.282 , pp. 6364-6371
    • Pedersen, J.Z.1    de Maria, F.2    Turella, P.3    Federici, G.4    Mattei, M.5
  • 8
  • 9
    • 53449101213 scopus 로고    scopus 로고
    • Molecular mechanisms of natural products in chemoprevention: Induction of cytoprotective enzymes by Nrf2
    • Eggler AL, Gay KA, Mesecar AD (2008) Molecular mechanisms of natural products in chemoprevention: induction of cytoprotective enzymes by Nrf2. Mol Nutr Food Res 52: S84-S94.
    • (2008) Mol Nutr Food Res , vol.52 , pp. 84-94
    • Eggler, A.L.1    Gay, K.A.2    Mesecar, A.D.3
  • 10
  • 12
    • 0024513273 scopus 로고
    • Immunohistochem- ical localization of human liver glutathione S-transferase (GST) isozymes with special reference to polymorphic GST1
    • Abei M, Harada S, Tanaka N, McNeil M, Osuga T (1989) Immunohistochem- ical localization of human liver glutathione S-transferase (GST) isozymes with special reference to polymorphic GST1. Biochim Biophys Acta 995: 279-284.
    • (1989) Biochim Biophys Acta , vol.995 , pp. 279-284
    • Abei, M.1    Harada, S.2    Tanaka, N.3    McNeil, M.4    Osuga, T.5
  • 14
    • 0028839833 scopus 로고
    • The content of glutathione and glutathione S-transferases and the glutathione peroxidase activity in rat liver nuclei determined by a non-aqueous technique of cell fractionation
    • Soboll S, Gruendel S, Harris J, Kolb-Bachofen V, Ketterer B, et al. (1995) The content of glutathione and glutathione S-transferases and the glutathione peroxidase activity in rat liver nuclei determined by a non-aqueous technique of cell fractionation. Biochem J 311: 889-894.
    • (1995) Biochem J , vol.311 , pp. 889-894
    • Soboll, S.1    Gruendel, S.2    Harris, J.3    Kolb-Bachofen, V.4    Ketterer, B.5
  • 15
    • 34250314965 scopus 로고    scopus 로고
    • Electrostatic association of glutathione transferase to the nuclear membrane
    • Stella L, Pallottini V, Moreno S, Leoni S, De Maria F, et al. (2007) Electrostatic association of glutathione transferase to the nuclear membrane. J Biol Chem 282: 6372-6379.
    • (2007) J Biol Chem , vol.282 , pp. 6372-6379
    • Stella, L.1    Pallottini, V.2    Moreno, S.3    Leoni, S.4    de Maria, F.5
  • 20
    • 0016772784 scopus 로고
    • Relationship between in vivo degradative rates and isoelectric points of proteins
    • Dice JF, Godberg AL (1975) Relationship between in vivo degradative rates and isoelectric points of proteins. Proc Natl Acad Sci USA 72: 3893-3897.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 3893-3897
    • Dice, J.F.1    Godberg, A.L.2
  • 21
    • 0037086447 scopus 로고    scopus 로고
    • Addressing protein localization within the nucleus
    • Bickmore W A, Sutherland H G E (2002) Addressing protein localization within the nucleus. EMBO J 21: 1248-1254.
    • (2002) EMBO J , vol.21 , pp. 1248-1254
    • Bickmore, W.A.1    Sutherland, H.G.E.2
  • 22
    • 0032524233 scopus 로고    scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase activity of human glutathione transferases
    • Hurst R, Bao Y, Jemth P, Mannervik B, Williamson G (1998) Phospholipid hydroperoxide glutathione peroxidase activity of human glutathione transferas- es. Biochem J 332: 97-100.
    • (1998) Biochem J , vol.332 , pp. 97-100
    • Hurst, R.1    Bao, Y.2    Jemth, P.3    Mannervik, B.4    Williamson, G.5
  • 23
    • 0029869726 scopus 로고    scopus 로고
    • Cytoplasmic and peroxisomal catalases of the guinea pig liver: Evidence for two distinct proteins
    • Bulitta C, Ganea C, Fahimi HD, Volkl A (1996) Cytoplasmic and peroxisomal catalases of the guinea pig liver: evidence for two distinct proteins. Biochim Biophys Acta 1293: 55-62.
    • (1996) Biochim Biophys Acta , vol.1293 , pp. 55-62
    • Bulitta, C.1    Ganea, C.2    Fahimi, H.D.3    Volkl, A.4
  • 24
    • 0042905738 scopus 로고    scopus 로고
    • Catalase activity is regulated by c-Abl and Arg in the oxidative stress response
    • Cao C, Leng Y, Kufe D (2003) Catalase activity is regulated by c-Abl and Arg in the oxidative stress response. J Biol Chem 278: 29667-29675.
    • (2003) J Biol Chem , vol.278 , pp. 29667-29675
    • Cao, C.1    Leng, Y.2    Kufe, D.3
  • 25
    • 0026476480 scopus 로고
    • Copper,zinc superoxide dismutase is primarily a cytosolic protein in human cells
    • Crapo JD, Oury T, Rabouille C, Slot JW, Chang LY (1992) Copper,zinc superoxide dismutase is primarily a cytosolic protein in human cells. Proc Natl Acad Sci USA 89: 10405-10409.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10405-10409
    • Crapo, J.D.1    Oury, T.2    Rabouille, C.3    Slot, J.W.4    Chang, L.Y.5
  • 27
    • 0021471078 scopus 로고
    • Nucleo-cytoplasmic flux and intracellular mobility in single hepatocytes measured by fluorescence microphotolysis
    • Peters R (1984) Nucleo-cytoplasmic flux and intracellular mobility in single hepatocytes measured by fluorescence microphotolysis. EMBO J 3: 1831-1836.
    • (1984) EMBO J , vol.3 , pp. 1831-1836
    • Peters, R.1
  • 28
    • 67349272249 scopus 로고    scopus 로고
    • A nucleocytoplasmic malate dehydrogenase regulates p53 transcriptional activity in response to metabolic stress
    • Lee SM, Kim JH, Cho EJ, Youn HD (2009) A nucleocytoplasmic malate dehydrogenase regulates p53 transcriptional activity in response to metabolic stress. Cell Death Diff 16: 738-748.
    • (2009) Cell Death Diff , vol.16 , pp. 738-748
    • Lee, S.M.1    Kim, J.H.2    Cho, E.J.3    Youn, H.D.4
  • 29
    • 0041352962 scopus 로고    scopus 로고
    • S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component
    • Zheng L, Roeder RG, Luo YS (2003) S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component. Cell 114: 255-266.
    • (2003) Cell , vol.114 , pp. 255-266
    • Zheng, L.1    Roeder, R.G.2    Luo, Y.S.3
  • 30
    • 77951616674 scopus 로고    scopus 로고
    • The nuclear envelope in genome organization, expression and stability
    • Mekhail K, Moazed D (2010) The nuclear envelope in genome organization, expression and stability. Nat Rev Mol Cell Biol 11: 317-328.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 317-328
    • Mekhail, K.1    Moazed, D.2
  • 31
    • 59149085789 scopus 로고    scopus 로고
    • Patterns of evolutionary conservation in the nesprin genes highlight probable functionally important protein domains and isoforms
    • Simpson JG, Roberts RG (2008) Patterns of evolutionary conservation in the nesprin genes highlight probable functionally important protein domains and isoforms. Biochem Soc Trans 36: 1359-1367.
    • (2008) Biochem Soc Trans , vol.36 , pp. 1359-1367
    • Simpson, J.G.1    Roberts, R.G.2
  • 32
    • 84954358251 scopus 로고    scopus 로고
    • Sun1 forms immobile macromolecular assemblies at the nuclear envelope
    • Lu W, Gotzmann J, Sironi L, Jaeger VM, Schneider M, et al. (2008) Sun1 forms immobile macromolecular assemblies at the nuclear envelope. Biochim Biophys Acta 1783: 2415-2426.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 2415-2426
    • Lu, W.1    Gotzmann, J.2    Sironi, L.3    Jaeger, V.M.4    Schneider, M.5
  • 33
    • 71549117899 scopus 로고    scopus 로고
    • The nuclear envelope as a signaling node in development and disease
    • Dauer WT, Worman HJ (2009) The nuclear envelope as a signaling node in development and disease. Dev Cell 17: 626-638.
    • (2009) Dev Cell , vol.17 , pp. 626-638
    • Dauer, W.T.1    Worman, H.J.2
  • 34
    • 39049148153 scopus 로고    scopus 로고
    • Aggresome formation and neurodegenerative diseases: Therapeutic implications
    • Olzmann JA, Li L, Chin LS (2008) Aggresome formation and neurodegenerative diseases: therapeutic implications. Curr Med Chem 15: 47-60.
    • (2008) Curr Med Chem , vol.15 , pp. 47-60
    • Olzmann, J.A.1    Li, L.2    Chin, L.S.3
  • 36
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipides from animal tissues
    • Folch J, Lees M, Stanley GHS (1957) A simple method for the isolation and purification of total lipides from animal tissues. J Biol Chem 226: 497-509.
    • (1957) J Biol Chem , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Stanley, G.H.S.3
  • 37
    • 0343879238 scopus 로고
    • Assay of inorganic phosphate, total phosphate and phosphatases
    • Ames BN (1966) Assay of inorganic phosphate, total phosphate and phosphatases. Methods Enzymol 8: 115-118.
    • (1966) Methods Enzymol , vol.8 , pp. 115-118
    • Ames, B.N.1
  • 39
    • 84995059486 scopus 로고
    • Sub-cellular localization of calcium in Azolla-Anabaena symbiosis by chlorotetracycline, ESI and EELS
    • Canini A, Albertano P, Grilli Caiola M (1993) Sub-cellular localization of calcium in Azolla-Anabaena symbiosis by chlorotetracycline, ESI and EELS. Botanica Acta 106: 146-153.
    • (1993) Botanica Acta , vol.106 , pp. 146-153
    • Canini, A.1    Albertano, P.2    Grilli, C.M.3
  • 40
    • 37849030661 scopus 로고
    • Operations modes of electron spectroscopic imaging and electron energy-loss spectroscopy in a transmission electron microscope
    • Reimer L, Fromm I, Rennkamp R (1988) Operations modes of electron spectroscopic imaging and electron energy-loss spectroscopy in a transmission electron microscope. Ultramicroscopy 1: 1-5.
    • (1988) Ultramicroscopy , vol.1 , pp. 1-5
    • Reimer, L.1    Fromm, I.2    Rennkamp, R.3
  • 41
    • 41049100518 scopus 로고
    • A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase
    • Beers RF, Sizer IW (1952) A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem 195: 133-140.
    • (1952) J Biol Chem , vol.195 , pp. 133-140
    • Beers, R.F.1    Sizer, I.W.2
  • 42
    • 0022272481 scopus 로고
    • Glutathione peroxidase
    • Mannervik B (1985) Glutathione peroxidase. Methods Enzymol 113: 490-495.
    • (1985) Methods Enzymol , vol.113 , pp. 490-495
    • Mannervik, B.1
  • 43
    • 0016272750 scopus 로고
    • Involvement of superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase
    • Marklund S, Marklund G (1974) Involvement of superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur J Biochem 47: 469-474.
    • (1974) Eur J Biochem , vol.47 , pp. 469-474
    • Marklund, S.1    Marklund, G.2
  • 45
    • 0029034634 scopus 로고
    • Mass spectrometric analysis of rat liver cytosolic glutathione S-transferases: Modifications are limited to N-terminal processing
    • Yeh HI, Hsieh CH, Wang LY, Tsai SP, Hsu HY, et al. (1995) Mass spectrometric analysis of rat liver cytosolic glutathione S-transferases: modifica- tions are limited to N-terminal processing. Biochem J 308: 69-75.
    • (1995) Biochem J , vol.308 , pp. 69-75
    • Yeh, H.I.1    Hsieh, C.H.2    Wang, L.Y.3    Tsai, S.P.4    Hsu, H.Y.5
  • 46
    • 0023655586 scopus 로고
    • The separation of glutathione transferase subunits by using reverse-phase high- pressure liquid chromatography
    • Ostlund Farrants AK, Meyer DJ, Coles B, Southan C, Aitken A, et al. (1987) The separation of glutathione transferase subunits by using reverse-phase high- pressure liquid chromatography. Biochem J 245: 423-428.
    • (1987) Biochem J , vol.245 , pp. 423-428
    • Ostlund, F.A.K.1    Meyer, D.J.2    Coles, B.3    Southan, C.4    Aitken, A.5
  • 47
    • 0021359650 scopus 로고
    • The isozyme pattern of glutathione S-transferases in rat heart
    • Ishikawa T, Sies H (1984) The isozyme pattern of glutathione S-transferases in rat heart. FEBS Lett 169: 156-160.
    • (1984) FEBS Lett , vol.169 , pp. 156-160
    • Ishikawa, T.1    Sies, H.2
  • 50
    • 63049084861 scopus 로고    scopus 로고
    • The detection, correlation, and comparison of peptide precursor and product ions from data independent LC-MS with data dependant LC-MS/MS
    • Geromanos SJ, Vissers JP, Silva JC, Dorschel CA, Li GZ, et al. (2009) The detection, correlation, and comparison of peptide precursor and product ions from data independent LC-MS with data dependant LC-MS/MS. Proteomics 9: 1683-1695.
    • (2009) Proteomics , vol.9 , pp. 1683-1695
    • Geromanos, S.J.1    Vissers, J.P.2    Silva, J.C.3    Dorschel, C.A.4    Li, G.Z.5
  • 51
    • 63049138916 scopus 로고    scopus 로고
    • Database searching and accounting of multiplexed precursor and product ion spectra from the data independent analysis of simple and complex peptide mixtures
    • Li GZ, Vissers JP, Silva JC, Golick D, Gorenstein MV, et al. (2009) Database searching and accounting of multiplexed precursor and product ion spectra from the data independent analysis of simple and complex peptide mixtures.Proteomics 9: 1696-1719.
    • (2009) Proteomics , vol.9 , pp. 1696-1719
    • Li, G.Z.1    Vissers, J.P.2    Silva, J.C.3    Golick, D.4    Gorenstein, M.V.5
  • 52
    • 0023919963 scopus 로고
    • A simple technique for quantitation of low levels of DNA damage in individual cells
    • Singh NP, McCoy MT, Tice RR, Schneider EL (1988) A simple technique for quantitation of low levels of DNA damage in individual cells. Exp Cell Res 175: 184-191.
    • (1988) Exp Cell Res , vol.175 , pp. 184-191
    • Singh, N.P.1    McCoy, M.T.2    Tice, R.R.3    Schneider, E.L.4
  • 53
    • 0014546946 scopus 로고
    • Correlated morphometric and biochemical studies on the liver cell
    • Weibel ER, Stäubli W, Gnägi HR, Hess FA (1969) Correlated morphometric and biochemical studies on the liver cell. J Cell Biol 42: 68-91.
    • (1969) J Cell Biol , vol.42 , pp. 68-91
    • Weibel, E.R.1    Stäubli, W.2    Gnägi, H.R.3    Hess, F.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.