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Volumn 156, Issue 3-4, 2012, Pages 221-228

Differential gene expression in rainbow trout (Oncorhynchus mykiss) liver and ovary after exposure to zearalenone

Author keywords

Differential display PCR; Fishes; mRNA; Rainbow trout; Zearalenone

Indexed keywords

ALPHA ENOLASE; BETA CENTRACTIN; COMPLEMENTARY DNA; FERRITIN; MESSENGER RNA; NUCLEAR PROTEIN; PROTEIN BCCIP; PROTEIN C; UNCLASSIFIED DRUG; ZEARALENONE;

EID: 84866351591     PISSN: 15320456     EISSN: 18781659     Source Type: Journal    
DOI: 10.1016/j.cbpc.2012.05.005     Document Type: Article
Times cited : (14)

References (96)
  • 2
    • 33646484192 scopus 로고    scopus 로고
    • The protective effect of hydrated sodium calcium aluminosilicate against haematological, biochemical and pathological changes induced by zearalenone in mice
    • S. Abbès, Z. Ouanes, J.B. Salah-Abbès, Z. Houas, R. Oueslati, H. Bacha, and O. Othman The protective effect of hydrated sodium calcium aluminosilicate against haematological, biochemical and pathological changes induced by zearalenone in mice Toxicon 47 2006 567 574
    • (2006) Toxicon , vol.47 , pp. 567-574
    • Abbès, S.1    Ouanes, Z.2    Salah-Abbès, J.B.3    Houas, Z.4    Oueslati, R.5    Bacha, H.6    Othman, O.7
  • 3
    • 0142219463 scopus 로고    scopus 로고
    • DNA fragmentation, apoptosis and cell cycle arrest induced by zearalenone in cultured DOK, vero and caco-2 cells: Prevention by vitamin e
    • S. Abid-Essefi, I. Baudrimont, W. Hassen, Z. Ouanes, T.A. Mobio, R. Anane, E.E. Creppy, and H. Bacha DNA fragmentation, apoptosis and cell cycle arrest induced by zearalenone in cultured DOK, vero and caco-2 cells: prevention by vitamin E Toxicology 192 2003 237 248
    • (2003) Toxicology , vol.192 , pp. 237-248
    • Abid-Essefi, S.1    Baudrimont, I.2    Hassen, W.3    Ouanes, Z.4    Mobio, T.A.5    Anane, R.6    Creppy, E.E.7    Bacha, H.8
  • 4
    • 2342480564 scopus 로고    scopus 로고
    • Cytotoxicity, inhibition of DNA and protein syntheses and oxidative damage in cultured cells exposed to zearalenone
    • S. Abid-Essefi, Z. Ouanes, W. Hassen, I. Baudrimont, E. Creppy, and H. Bacha Cytotoxicity, inhibition of DNA and protein syntheses and oxidative damage in cultured cells exposed to zearalenone Toxicol. In Vitro 18 2004 467 474
    • (2004) Toxicol. in Vitro , vol.18 , pp. 467-474
    • Abid-Essefi, S.1    Ouanes, Z.2    Hassen, W.3    Baudrimont, I.4    Creppy, E.5    Bacha, H.6
  • 6
    • 0028239247 scopus 로고
    • Identification of multiple genes inbovine retinal pericytes altered by exposure to elevated levels of glucose by using mRNA differential display
    • L.P. Aiello, G.S. Robinson, Y.-W. Lin, Y. Nishio, and G.L. King Identification of multiple genes inbovine retinal pericytes altered by exposure to elevated levels of glucose by using mRNA differential display Proc. Natl. Acad. Sci. U.S.A. 91 1994 6231 6235
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 6231-6235
    • Aiello, L.P.1    Robinson, G.S.2    Lin, Y.-W.3    Nishio, Y.4    King, G.L.5
  • 7
    • 0034658839 scopus 로고    scopus 로고
    • Dynactin
    • V. Allan Dynactin Curr. Biol. 10 2000 R432
    • (2000) Curr. Biol. , vol.10 , pp. 432
    • Allan, V.1
  • 9
    • 0032835952 scopus 로고    scopus 로고
    • Fish model for assessing the in vivo estrogenic potency of the mycotoxin zearalenone and its metabolites
    • A. Arukwe, T. Grotmol, T.B. Haugen, F.R. Knudsen, and A. Goksoyr Fish model for assessing the in vivo estrogenic potency of the mycotoxin zearalenone and its metabolites Sci. Total Environ. 236 1999 153 161
    • (1999) Sci. Total Environ. , vol.236 , pp. 153-161
    • Arukwe, A.1    Grotmol, T.2    Haugen, T.B.3    Knudsen, F.R.4    Goksoyr, A.5
  • 10
    • 34447500398 scopus 로고    scopus 로고
    • Toxicities induced in cultured cells exposed to zearalenone: Apoptosis or mutagenesis?
    • I. Ayed-Boussema, Z. Ouanes, H. Bacha, and S. Abid Toxicities induced in cultured cells exposed to zearalenone: apoptosis or mutagenesis? J. Biochem. Mol. Toxicol. 21 2007 136 144
    • (2007) J. Biochem. Mol. Toxicol. , vol.21 , pp. 136-144
    • Ayed-Boussema, I.1    Ouanes, Z.2    Bacha, H.3    Abid, S.4
  • 11
    • 51949119422 scopus 로고    scopus 로고
    • The mycotoxin zearalenone induces apoptosis in human hepatocytes (HepG2) via p53-dependent mitochondrial signaling pathway
    • I. Ayed-Boussema, C. Bouaziz, K. Rjiba, K. Valenti, F. Laporte, H. Bacha, and W. Hassen The mycotoxin zearalenone induces apoptosis in human hepatocytes (HepG2) via p53-dependent mitochondrial signaling pathway Toxicol. In Vitro 22 2008 1671 1680
    • (2008) Toxicol. in Vitro , vol.22 , pp. 1671-1680
    • Ayed-Boussema, I.1    Bouaziz, C.2    Rjiba, K.3    Valenti, K.4    Laporte, F.5    Bacha, H.6    Hassen, W.7
  • 12
    • 78650210958 scopus 로고    scopus 로고
    • Zearalenone activates pregnane X receptor, constitutive androstane receptor and aryl hydrocarbon receptor and corresponding phase i target genes mRNA in primary cultures of human hepatocytes
    • I. Ayed-Boussema, J.M. Pascussi, P. Maurel, H. Bacha, and W. Hassen Zearalenone activates pregnane X receptor, constitutive androstane receptor and aryl hydrocarbon receptor and corresponding phase I target genes mRNA in primary cultures of human hepatocytes Environ. Toxicol. Pharmacol. 31 2011 79 87
    • (2011) Environ. Toxicol. Pharmacol. , vol.31 , pp. 79-87
    • Ayed-Boussema, I.1    Pascussi, J.M.2    Maurel, P.3    Bacha, H.4    Hassen, W.5
  • 14
    • 0036625843 scopus 로고    scopus 로고
    • Stress in fishes: A diversity of responses with particular reference to changes in circulating corticosteroids
    • B.A. Barton Stress in fishes: a diversity of responses with particular reference to changes in circulating corticosteroids Integr. Comp. Biol. 42 2002 517 525
    • (2002) Integr. Comp. Biol. , vol.42 , pp. 517-525
    • Barton, B.A.1
  • 15
    • 69749083169 scopus 로고    scopus 로고
    • Candidate biomarker discovery in plasma of juvenile cod (Gadus morhua) exposed to crude north sea oil, alkyl phenols and polycyclic aromatic hydrocarbons (PAHs)
    • A. Bohne-Kjersem, A. Skadsheim, A. Goksoyr, and B.E. Grosvik Candidate biomarker discovery in plasma of juvenile cod (Gadus morhua) exposed to crude north sea oil, alkyl phenols and polycyclic aromatic hydrocarbons (PAHs) Mar. Environ. Res. 68 2009 268 277
    • (2009) Mar. Environ. Res. , vol.68 , pp. 268-277
    • Bohne-Kjersem, A.1    Skadsheim, A.2    Goksoyr, A.3    Grosvik, B.E.4
  • 16
    • 84874192579 scopus 로고    scopus 로고
    • Differential gene expression in whitefish (Coregonus lavaretus) exposed to benzo[a]pyrene
    • M. Jankun, P. Brzuzan, P. Hliwa, M. Luczyński, Arch. Hydrobiol. Spec. Issues Advanc. Limnol.
    • P. Brzuzan, Ł. Jurczyk, and T. Foks Differential gene expression in whitefish (Coregonus lavaretus) exposed to benzo[a]pyrene M. Jankun, P. Brzuzan, P. Hliwa, M. Luczyński, Biology and Management of Coregonid Fishes - 2005 Arch. Hydrobiol. Spec. Issues Advanc. Limnol. 60 2007 147 155
    • (2007) Biology and Management of Coregonid Fishes - 2005 , vol.60 , pp. 147-155
    • Brzuzan, P.1    Jurczyk, Ł.2    Foks, T.3
  • 17
    • 0348226757 scopus 로고    scopus 로고
    • Physiological modulation of iron metabolism in rainbow trout (Oncorhynchus mykiss) fed low and high iron diets
    • P. Carriquiriborde, R.D. Handy, and S.J. Davies Physiological modulation of iron metabolism in rainbow trout (Oncorhynchus mykiss) fed low and high iron diets J. Exp. Biol. 207 2004 75 86
    • (2004) J. Exp. Biol. , vol.207 , pp. 75-86
    • Carriquiriborde, P.1    Handy, R.D.2    Davies, S.J.3
  • 19
    • 0026686929 scopus 로고
    • Centractin is an actin homologue associated with the centrosome
    • S.W. Clark, and D.I. Meyer Centractin is an actin homologue associated with the centrosome Nature 359 1992 246 250
    • (1992) Nature , vol.359 , pp. 246-250
    • Clark, S.W.1    Meyer, D.I.2
  • 20
    • 0032700476 scopus 로고    scopus 로고
    • Overexpression of normal and mutant Arp1α (centractin) differentially affects microtubule organization during mitosis and interphase
    • I.B. Clark, and D.I. Meyer Overexpression of normal and mutant Arp1α (centractin) differentially affects microtubule organization during mitosis and interphase J. Cell Sci. 112 1999 3507 3518
    • (1999) J. Cell Sci. , vol.112 , pp. 3507-3518
    • Clark, I.B.1    Meyer, D.I.2
  • 21
    • 0028670191 scopus 로고
    • β-Centractin: Characterization and distribution of a new member of the centractin family of actin-related proteins
    • S.W. Clark, O. Staub, I.B. Clark, E.L.F. Holzbaur, B.M. Paschal, R.B. Vallee, and D.I. Meyer β-Centractin: characterization and distribution of a new member of the centractin family of actin-related proteins Mol. Biol. Cell 5 1994 1301 1310
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1301-1310
    • Clark, S.W.1    Staub, O.2    Clark, I.B.3    Holzbaur, E.L.F.4    Paschal, B.M.5    Vallee, R.B.6    Meyer, D.I.7
  • 23
    • 21544447526 scopus 로고    scopus 로고
    • Regulation of blood coagulation by the protein C anticoagulant pathway: Novel insights into structure-function relationships and molecular recognition
    • B. Dahlbäck, and B.O. Villoutreix Regulation of blood coagulation by the protein C anticoagulant pathway: Novel insights into structure-function relationships and molecular recognition Arterioscler. Thromb. Vasc. Biol. 25 2005 1311 1320
    • (2005) Arterioscler. Thromb. Vasc. Biol. , vol.25 , pp. 1311-1320
    • Dahlbäck, B.1    Villoutreix, B.O.2
  • 24
    • 0028809562 scopus 로고
    • Differential display or differential dismay?
    • C. Debouck Differential display or differential dismay? Curr. Opin. Biol. 6 1995 597 599
    • (1995) Curr. Opin. Biol. , vol.6 , pp. 597-599
    • Debouck, C.1
  • 25
    • 33744782612 scopus 로고    scopus 로고
    • The mycoestrogen zearalenone induces CYP3A through activation of the pregnane X receptor
    • X. Ding, K. Lichti, and J.L. Staudinger The mycoestrogen zearalenone induces CYP3A through activation of the pregnane X receptor Toxicol. Sci. 91 2006 448 455
    • (2006) Toxicol. Sci. , vol.91 , pp. 448-455
    • Ding, X.1    Lichti, K.2    Staudinger, J.L.3
  • 26
    • 79960697121 scopus 로고    scopus 로고
    • Hsp70 expression as biomarkers of oxidative stress: Mycotoxins' exploration
    • E. El Golli-Bennour, and H. Bacha Hsp70 expression as biomarkers of oxidative stress: Mycotoxins' exploration Toxicology 287 2011 1 7
    • (2011) Toxicology , vol.287 , pp. 1-7
    • El Golli-Bennour, E.1    Bacha, H.2
  • 27
    • 0024558370 scopus 로고
    • The roles of protein C and thrombomodulin in the regulation of blood coagulation
    • C.T. Esmon The roles of protein C and thrombomodulin in the regulation of blood coagulation J. Biol. Chem. 264 1989 4743 4746
    • (1989) J. Biol. Chem. , vol.264 , pp. 4743-4746
    • Esmon, C.T.1
  • 28
    • 0038683379 scopus 로고    scopus 로고
    • Coagulation and inflammation
    • C.T. Esmon Coagulation and inflammation J. Endotoxin Res. 9 2003 192 198
    • (2003) J. Endotoxin Res. , vol.9 , pp. 192-198
    • Esmon, C.T.1
  • 29
    • 39549090848 scopus 로고    scopus 로고
    • Mycotoxins in cattle feeds and carry-over to dairy milk: A review
    • J. Fink-Gremmels Mycotoxins in cattle feeds and carry-over to dairy milk: a review Food Addit. Contam. 25 2008 172 180
    • (2008) Food Addit. Contam. , vol.25 , pp. 172-180
    • Fink-Gremmels, J.1
  • 31
    • 60549112730 scopus 로고    scopus 로고
    • Occurrence of estrogenic mycotoxin-zearalenone in aqueous environmental samples with various NOM content
    • K. Gromadzka, A. Waśkiewicz, P. Goliński, and J. Świetlik Occurrence of estrogenic mycotoxin-zearalenone in aqueous environmental samples with various NOM content Water Res. 43 2009 1051 1059
    • (2009) Water Res. , vol.43 , pp. 1051-1059
    • Gromadzka, K.1    Waśkiewicz, A.2    Goliński, P.3    Świetlik, J.4
  • 32
    • 0030479303 scopus 로고    scopus 로고
    • Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles
    • E.A. Holleran, M.K. Tokito, S. Karki, and E.L.F. Holzbaur Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles J. Cell Biol. 135 1996 1815 1829
    • (1996) J. Cell Biol. , vol.135 , pp. 1815-1829
    • Holleran, E.A.1    Tokito, M.K.2    Karki, S.3    Holzbaur, E.L.F.4
  • 33
    • 0031947483 scopus 로고    scopus 로고
    • The role of the dynactin complex in intracellular motility
    • E.A. Holleran, S. Karki, and E.L.F. Holzbaur The role of the dynactin complex in intracellular motility Int. Rev. Cytol. 182 1998 69 109
    • (1998) Int. Rev. Cytol. , vol.182 , pp. 69-109
    • Holleran, E.A.1    Karki, S.2    Holzbaur, E.L.F.3
  • 35
    • 80053026274 scopus 로고    scopus 로고
    • Effects of purified zearalenone on growth performance, organ size, serum metabolites, and oxidative stress in postweaning gilts
    • S.Z. Jiang, Z.B. Yang, W.R. Yang, J. Gao, F.X. Liu, J. Broomhead, and F. Chi Effects of purified zearalenone on growth performance, organ size, serum metabolites, and oxidative stress in postweaning gilts J. Anim. Sci. 89 2011 3008 3015
    • (2011) J. Anim. Sci. , vol.89 , pp. 3008-3015
    • Jiang, S.Z.1    Yang, Z.B.2    Yang, W.R.3    Gao, J.4    Liu, F.X.5    Broomhead, J.6    Chi, F.7
  • 36
    • 0041621020 scopus 로고    scopus 로고
    • Propiscin - A safe new anestetic for fish
    • K. Kazuń, and A.K. Siwicki Propiscin - a safe new anestetic for fish Arch. Pol. Fish. 9 2001 183 190
    • (2001) Arch. Pol. Fish. , vol.9 , pp. 183-190
    • Kazuń, K.1    Siwicki, A.K.2
  • 37
    • 0036360688 scopus 로고    scopus 로고
    • The investigation of the anabolic efficiancy and effect on the nonspecific immune system of zeranol in rainbow trout (Oncorhynchus mykiss, Walbaum)
    • O. Keles, A. Candan, T. Bakirel, and S. Karatas The investigation of the anabolic efficiancy and effect on the nonspecific immune system of zeranol in rainbow trout (Oncorhynchus mykiss, Walbaum) Turk. J. Vet. Anim. Sci. 26 2002 925 931
    • (2002) Turk. J. Vet. Anim. Sci. , vol.26 , pp. 925-931
    • Keles, O.1    Candan, A.2    Bakirel, T.3    Karatas, S.4
  • 38
    • 14744284637 scopus 로고    scopus 로고
    • Multifaceted roles of glycolytic enzymes
    • J.-w. Kim, and C.V. Dang Multifaceted roles of glycolytic enzymes Trends Biochem. Sci. 30 2005 142 150
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 142-150
    • Kim, J.-W.1    Dang, C.V.2
  • 39
    • 0027452550 scopus 로고
    • Regulating the fate of mRNA: The control of cellular iron metabolism
    • R.D. Klausner, T.A. Rouault, and J.B. Harford Regulating the fate of mRNA: the control of cellular iron metabolism Cell 72 1993 19 28
    • (1993) Cell , vol.72 , pp. 19-28
    • Klausner, R.D.1    Rouault, T.A.2    Harford, J.B.3
  • 40
    • 0344628564 scopus 로고    scopus 로고
    • Analytical methodologies for determining the occurrence of endocrine disrupting chemicals in sewage treatment plants and natural waters
    • A. Lagana, A. Bacaloni, I. De Leva, A. Faberi, G. Fago, and A. Marino Analytical methodologies for determining the occurrence of endocrine disrupting chemicals in sewage treatment plants and natural waters Anal. Chim. Acta 501 2004 79 88
    • (2004) Anal. Chim. Acta , vol.501 , pp. 79-88
    • Lagana, A.1    Bacaloni, A.2    De Leva, I.3    Faberi, A.4    Fago, G.5    Marino, A.6
  • 41
    • 0034793861 scopus 로고    scopus 로고
    • Stability of the fusarium mycotoxins nivalenol, deoxynivalenol and zearalenone in ground maize under typical cooking environments
    • D.R. Lauren, and W.A. Smith Stability of the fusarium mycotoxins nivalenol, deoxynivalenol and zearalenone in ground maize under typical cooking environments Food Addit. Contam. 18 2001 1011 1016
    • (2001) Food Addit. Contam. , vol.18 , pp. 1011-1016
    • Lauren, D.R.1    Smith, W.A.2
  • 42
    • 61349164205 scopus 로고    scopus 로고
    • Identification of copper-responsive genes in an early life stage of the fathead minnow Pimephales promelas
    • S.S. Lewis, and S.J. Keller Identification of copper-responsive genes in an early life stage of the fathead minnow Pimephales promelas Ecotoxicology 18 2009 281 292
    • (2009) Ecotoxicology , vol.18 , pp. 281-292
    • Lewis, S.S.1    Keller, S.J.2
  • 43
    • 0027328488 scopus 로고
    • Distribution and cloning of eukaryotic mRNAs by means of differential display: Refiniments and optimization
    • P. Liang, L. Averboukh, and A.B. Pardee Distribution and cloning of eukaryotic mRNAs by means of differential display: refiniments and optimization Nucleic Acids Res. 21 1993 3269 3275
    • (1993) Nucleic Acids Res. , vol.21 , pp. 3269-3275
    • Liang, P.1    Averboukh, L.2    Pardee, A.B.3
  • 44
    • 0035905743 scopus 로고    scopus 로고
    • Inhibition of breast and brain cancer cell growth by BCCIPα, an evolutionarily conserved nuclear protein that interacts with BRCA2
    • J. Liu, Y. Yuan, J. Huan, and Z. Shen Inhibition of breast and brain cancer cell growth by BCCIPα, an evolutionarily conserved nuclear protein that interacts with BRCA2 Oncogene 20 2001 336 345
    • (2001) Oncogene , vol.20 , pp. 336-345
    • Liu, J.1    Yuan, Y.2    Huan, J.3    Shen, Z.4
  • 46
    • 14044251525 scopus 로고    scopus 로고
    • The BRCA2-interacting protein BCCIP functions in RAD51 and BRCA2 focus formation and homologous recombinational repair
    • H. Lu, X. Guo, X. Meng, J. Liu, C. Allen, J. Wray, J.A. Nickoloff, and Z. Shen The BRCA2-interacting protein BCCIP functions in RAD51 and BRCA2 focus formation and homologous recombinational repair Mol. Cell. Biol. 25 2005 1949 1957
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 1949-1957
    • Lu, H.1    Guo, X.2    Meng, X.3    Liu, J.4    Allen, C.5    Wray, J.6    Nickoloff, J.A.7    Shen, Z.8
  • 47
    • 37549005555 scopus 로고    scopus 로고
    • BCCIP regulates homologous recombination by distinct domains and suppresses spontaneous DNA damage
    • H. Lu, J. Yue, X. Meng, J.A. Nickoloff, and Z. Shen BCCIP regulates homologous recombination by distinct domains and suppresses spontaneous DNA damage Nucleic Acids Res. 35 2007 7160 7170
    • (2007) Nucleic Acids Res. , vol.35 , pp. 7160-7170
    • Lu, H.1    Yue, J.2    Meng, X.3    Nickoloff, J.A.4    Shen, Z.5
  • 48
    • 83555174922 scopus 로고    scopus 로고
    • Exposure to cadmium chloride influences astrocyte-elevated gene-1 (AEG-1) expression in MDA-MB231 human breast cancer cells
    • C. Luparello, A. Longo, and M. Vetrano Exposure to cadmium chloride influences astrocyte-elevated gene-1 (AEG-1) expression in MDA-MB231 human breast cancer cells Biochimie 94 2012 207 213
    • (2012) Biochimie , vol.94 , pp. 207-213
    • Luparello, C.1    Longo, A.2    Vetrano, M.3
  • 49
    • 0030009844 scopus 로고    scopus 로고
    • Zearalenone induces modifications of haematological and biochemical parameters in rats
    • K. Maaroufi, L. Chekir, E.E. Creppy, F. Ellouz, and H. Bacha Zearalenone induces modifications of haematological and biochemical parameters in rats Toxicon 34 1996 535 540
    • (1996) Toxicon , vol.34 , pp. 535-540
    • Maaroufi, K.1    Chekir, L.2    Creppy, E.E.3    Ellouz, F.4    Bacha, H.5
  • 50
    • 0037413675 scopus 로고    scopus 로고
    • Genomic structure of the human BCCIP gene and its expression in cancer
    • X. Meng, J. Liu, and Z. Shen Genomic structure of the human BCCIP gene and its expression in cancer Gene 302 2003 139 146
    • (2003) Gene , vol.302 , pp. 139-146
    • Meng, X.1    Liu, J.2    Shen, Z.3
  • 51
    • 14044258059 scopus 로고    scopus 로고
    • BCCIP functions through p53 to regulate the expression of p21Waf1/Cip1
    • X. Meng, H. Lu, and Z. Shen BCCIP functions through p53 to regulate the expression of p21Waf1/Cip1 Cell Cycle 3 2004 1457 1462
    • (2004) Cell Cycle , vol.3 , pp. 1457-1462
    • Meng, X.1    Lu, H.2    Shen, Z.3
  • 52
    • 14044266503 scopus 로고    scopus 로고
    • Inhibition of G1 to S cell cycle progression by BCCIPβ
    • X. Meng, J. Liu, and Z. Shen Inhibition of G1 to S cell cycle progression by BCCIPβ Cell Cycle 3 2004 343 348
    • (2004) Cell Cycle , vol.3 , pp. 343-348
    • Meng, X.1    Liu, J.2    Shen, Z.3
  • 53
    • 33847261611 scopus 로고    scopus 로고
    • Abrogation of the transactivation activity of p53 by BCCIP down-regulation
    • X. Meng, J. Yue, Z. Liu, and Z. Shen Abrogation of the transactivation activity of p53 by BCCIP down-regulation J. Biol. Chem. 282 2007 1570 1576
    • (2007) J. Biol. Chem. , vol.282 , pp. 1570-1576
    • Meng, X.1    Yue, J.2    Liu, Z.3    Shen, Z.4
  • 54
    • 0031868919 scopus 로고    scopus 로고
    • Elimination of false positives generated through PCR re-amplification of differential display cDNA
    • G. Miele, L. Macrae, D. McBride, J. Manson, and M. Clinton Elimination of false positives generated through PCR re-amplification of differential display cDNA Biotechniques 25 1998 138 144
    • (1998) Biotechniques , vol.25 , pp. 138-144
    • Miele, G.1    MacRae, L.2    McBride, D.3    Manson, J.4    Clinton, M.5
  • 55
    • 0026236758 scopus 로고
    • Isolation and characterization of ferritin from the liver of the rainbow trout (Salmo gairdneri R.)
    • J.L. Miguel, M.I. Pablos, M.T. Agapito, and J.M. Recio Isolation and characterization of ferritin from the liver of the rainbow trout (Salmo gairdneri R.) Biochem. Cell Biol. 69 1991 735 741
    • (1991) Biochem. Cell Biol. , vol.69 , pp. 735-741
    • Miguel, J.L.1    Pablos, M.I.2    Agapito, M.T.3    Recio, J.M.4
  • 56
    • 0025819231 scopus 로고
    • Role of cell-surface lysines in plasminogen binding to cells: Identification of alpha-enolase as a candidate plasminogen receptor
    • L.A. Miles, C.M. Dahlberg, J. Plescia, J. Felez, K. Kato, and E.F. Plow Role of cell-surface lysines in plasminogen binding to cells: identification of alpha-enolase as a candidate plasminogen receptor Biochemistry 30 1991 1682 1691
    • (1991) Biochemistry , vol.30 , pp. 1682-1691
    • Miles, L.A.1    Dahlberg, C.M.2    Plescia, J.3    Felez, J.4    Kato, K.5    Plow, E.F.6
  • 57
    • 58149271120 scopus 로고    scopus 로고
    • Zearalenone and reproductive function in farm animals
    • F. Minervini, and M.E.D. Aquila Zearalenone and reproductive function in farm animals Int. J. Mol. Sci. 9 2008 2570 2584
    • (2008) Int. J. Mol. Sci. , vol.9 , pp. 2570-2584
    • Minervini, F.1    Aquila, M.E.D.2
  • 58
    • 34147119744 scopus 로고    scopus 로고
    • The cytoprotective protein C pathway
    • L.O. Mosnier, B.V. Zlokovic, and J.H. Griffin The cytoprotective protein C pathway Blood 109 2007 3161 3172
    • (2007) Blood , vol.109 , pp. 3161-3172
    • Mosnier, L.O.1    Zlokovic, B.V.2    Griffin, J.H.3
  • 59
    • 0030034186 scopus 로고    scopus 로고
    • Activated protein C attenuates endotoxin-induced pulmonary vascular injury by inhibiting activated leukocytes in rats
    • K. Murakami, K. Okajima, M. Uchiba, M. Johno, T. Nakagaki, H. Okabe, and K. Takatsuki Activated protein C attenuates endotoxin-induced pulmonary vascular injury by inhibiting activated leukocytes in rats Blood 87 1996 642 647
    • (1996) Blood , vol.87 , pp. 642-647
    • Murakami, K.1    Okajima, K.2    Uchiba, M.3    Johno, M.4    Nakagaki, T.5    Okabe, H.6    Takatsuki, K.7
  • 61
    • 70449499005 scopus 로고
    • Guide for the care and use of laboratory animals
    • National Institute of Health. Public Health Service Bethesda
    • NIH Guide for the Care and Use of Laboratory Animals NIH publication No. 86-23 1985 National Institute of Health. Public Health Service Bethesda
    • (1985) NIH Publication No. 86-23
    • Nih1
  • 62
    • 0036789519 scopus 로고    scopus 로고
    • Variation in gene expression within and among natural populations
    • M.F. Oleksiak, G.A. Churchill, and D.L. Crawford Variation in gene expression within and among natural populations Nat. Genet. 32 2002 261 266
    • (2002) Nat. Genet. , vol.32 , pp. 261-266
    • Oleksiak, M.F.1    Churchill, G.A.2    Crawford, D.L.3
  • 64
    • 0034613256 scopus 로고    scopus 로고
    • TOK-1, a novel p21(Cip1)-binding protein that cooperatively enhances p21-dependent inhibitory activity toward CDK2 kinase
    • T. Ono, H. Kitaura, H. Ugai, T. Murata, K.K. Yokoyama, S.M.M. Iguchi-Ariga, and H. Ariga TOK-1, a novel p21(Cip1)-binding protein that cooperatively enhances p21-dependent inhibitory activity toward CDK2 kinase J. Biol. Chem. 275 2000 31145 31154
    • (2000) J. Biol. Chem. , vol.275 , pp. 31145-31154
    • Ono, T.1    Kitaura, H.2    Ugai, H.3    Murata, T.4    Yokoyama, K.K.5    Iguchi-Ariga, S.M.M.6    Ariga, H.7
  • 65
    • 54449085184 scopus 로고    scopus 로고
    • Molecular, physiological and clinical aspects of the iron storage protein ferritin
    • K. Orino, and K. Watanabe Molecular, physiological and clinical aspects of the iron storage protein ferritin Vet. J. 178 2008 191 201
    • (2008) Vet. J. , vol.178 , pp. 191-201
    • Orino, K.1    Watanabe, K.2
  • 67
    • 12344305164 scopus 로고    scopus 로고
    • Zearalenone induces chromosome aberrations in mouse bone marrow: Preventive effect of 17β-estradiol, progesterone and vitamin e
    • Z. Ouanes, I. Ayed-Boussema, T. Baati, E.E. Creppy, and H. Bacha Zearalenone induces chromosome aberrations in mouse bone marrow: preventive effect of 17β-estradiol, progesterone and vitamin E Mutat. Res. Gen. Toxicol. Environ. 565 2005 139 149
    • (2005) Mutat. Res. Gen. Toxicol. Environ. , vol.565 , pp. 139-149
    • Ouanes, Z.1    Ayed-Boussema, I.2    Baati, T.3    Creppy, E.E.4    Bacha, H.5
  • 69
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • M.W. Pfaffl A new mathematical model for relative quantification in real-time RT-PCR Nucleic Acids Res. 29 2001 2002 2007
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2002-2007
    • Pfaffl, M.W.1
  • 70
    • 0036581160 scopus 로고    scopus 로고
    • Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR
    • M.W. Pfaffl, G.W. Horgan, and L. Dempfle Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR Nucleic Acids Res. 30 2002 1 10
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1-10
    • Pfaffl, M.W.1    Horgan, G.W.2    Dempfle, L.3
  • 71
    • 0042199018 scopus 로고    scopus 로고
    • Effects of sulfur mustard on transcription in human epidermal keratinocytes: Analysis by mRNA differential display
    • P.L. Platteborze Effects of sulfur mustard on transcription in human epidermal keratinocytes: analysis by mRNA differential display J. Appl. Toxicol. 23 2003 249 254
    • (2003) J. Appl. Toxicol. , vol.23 , pp. 249-254
    • Platteborze, P.L.1
  • 73
    • 0028839088 scopus 로고
    • The role of an enolaserelated molecule in plasminogen binding to cells
    • A. Redlitz, B.J. Fowler, E.F. Plow, and L.A. Miles The role of an enolaserelated molecule in plasminogen binding to cells Eur. J. Biochem. 227 1995 407 415
    • (1995) Eur. J. Biochem. , vol.227 , pp. 407-415
    • Redlitz, A.1    Fowler, B.J.2    Plow, E.F.3    Miles, L.A.4
  • 74
    • 7044241226 scopus 로고    scopus 로고
    • A differentially expressed enolase gene isolated from the gilthead sea bream (Sparus aurata) under high-density conditions is up-regulated in brain after in vivo lipopolysaccharide challenge
    • L. Ribas, J.V. Planas, B. Barton, C. Monetti, G. Bernadini, M. Saroglia, L. Tort, and S. Mackenzie A differentially expressed enolase gene isolated from the gilthead sea bream (Sparus aurata) under high-density conditions is up-regulated in brain after in vivo lipopolysaccharide challenge Aquaculture 241 2004 195 206
    • (2004) Aquaculture , vol.241 , pp. 195-206
    • Ribas, L.1    Planas, J.V.2    Barton, B.3    Monetti, C.4    Bernadini, G.5    Saroglia, M.6    Tort, L.7    MacKenzie, S.8
  • 75
    • 77954244905 scopus 로고    scopus 로고
    • Extra-nuclear signaling of ERα to the actin cytoskeleton in the central nervous system
    • A.M. Sanchez, and T. Simoncini Extra-nuclear signaling of ERα to the actin cytoskeleton in the central nervous system Steroids 75 2010 528 532
    • (2010) Steroids , vol.75 , pp. 528-532
    • Sanchez, A.M.1    Simoncini, T.2
  • 76
    • 78649749117 scopus 로고    scopus 로고
    • Short-term exposure to the environmentally relevant estrogenic mycotoxin zearalenone impairs reproduction in fish
    • P. Schwartz, K.L. Thorpe, T.D. Bucheli, F.E. Wettstein, and P. Burkhardt-Holm Short-term exposure to the environmentally relevant estrogenic mycotoxin zearalenone impairs reproduction in fish Sci. Total Environ. 409 2010 326 333
    • (2010) Sci. Total Environ. , vol.409 , pp. 326-333
    • Schwartz, P.1    Thorpe, K.L.2    Bucheli, T.D.3    Wettstein, F.E.4    Burkhardt-Holm, P.5
  • 77
    • 0030460724 scopus 로고    scopus 로고
    • Hypoxia response elements in the aldolase A, enolase 1, and lactate dehydrogenase a gene promoters contain essential binding sites for hypoxia-inducible factor 1
    • G.L. Semenza, B.-H. Jiang, S.W. Leung, R. Passantino, J.-P. Concordat, P. Maire, and A. Giallongo Hypoxia response elements in the aldolase A, enolase 1, and lactate dehydrogenase a gene promoters contain essential binding sites for hypoxia-inducible factor 1 J. Biol. Chem. 271 1996 32529 32537
    • (1996) J. Biol. Chem. , vol.271 , pp. 32529-32537
    • Semenza, G.L.1    Jiang, B.-H.2    Leung, S.W.3    Passantino, R.4    Concordat, J.-P.5    Maire, P.6    Giallongo, A.7
  • 78
    • 0020315938 scopus 로고
    • Neuron specific enolase (NSE) immunostaining a useful tool for the light microscopical detection of endocrine cell hyperplasia in adult rats exposed to asbestos
    • M.N. Sheppard, N.F. Johnson, and G.A. Cole Neuron specific enolase (NSE) immunostaining a useful tool for the light microscopical detection of endocrine cell hyperplasia in adult rats exposed to asbestos Histochemistry 74 1982 505 513
    • (1982) Histochemistry , vol.74 , pp. 505-513
    • Sheppard, M.N.1    Johnson, N.F.2    Cole, G.A.3
  • 80
    • 0028018395 scopus 로고
    • A rapid and simple PCR-based method for isolation of cDNAs from differentially expressed genes
    • B.P. Sokolov, and D.J. Prockop A rapid and simple PCR-based method for isolation of cDNAs from differentially expressed genes Nucleic Acids Res. 22 1994 4009 4015
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4009-4015
    • Sokolov, B.P.1    Prockop, D.J.2
  • 81
    • 33745835766 scopus 로고    scopus 로고
    • Haematological and biochemical parameters of weaned piglets fed on fodder mixture contaminated by zearalenone with addition of clinoptilolite
    • M. Šperanda, B. Liker, T. Šperanda, V. Šerić, Z. Antunović, Ž. Grabarević, D. Senčić, D. Grgurić, and Z. Steiner Haematological and biochemical parameters of weaned piglets fed on fodder mixture contaminated by zearalenone with addition of clinoptilolite Acta Vet. 56 2006 121 136
    • (2006) Acta Vet. , vol.56 , pp. 121-136
    • Šperanda, M.1    Liker, B.2    Šperanda, T.3    Šerić, V.4    Antunović, Z.5    Grabarević, Ž.6    Senčić, D.7    Grgurić, D.8    Steiner, Z.9
  • 82
    • 67650927414 scopus 로고    scopus 로고
    • Influence of the zearalenone on the activity of chosen liver enzymes in a rat
    • A. Stadnik, and A. Borzecki Influence of the zearalenone on the activity of chosen liver enzymes in a rat Ann. Agric. Environ. Med. 16 2009 31 35
    • (2009) Ann. Agric. Environ. Med. , vol.16 , pp. 31-35
    • Stadnik, A.1    Borzecki, A.2
  • 83
    • 0028220684 scopus 로고
    • Molecular cloning of five messenger RNAs differentially expressed in preneoplastic or neoplastic JB6 mouse epidermal cells: One is homologous to human tissue inhibitor of metalloproteinases-3
    • Y. Sun, G. Hegamyer, and N.H. Colburn Molecular cloning of five messenger RNAs differentially expressed in preneoplastic or neoplastic JB6 mouse epidermal cells: One is homologous to human tissue inhibitor of metalloproteinases-3 Cancer Res. 54 1994 1139 1144
    • (1994) Cancer Res. , vol.54 , pp. 1139-1144
    • Sun, Y.1    Hegamyer, G.2    Colburn, N.H.3
  • 85
    • 0023067301 scopus 로고
    • Ferritin: Structure, gene regulation, and cellular function in animals, plants, and microorganisms
    • E.C. Theil Ferritin: structure, gene regulation, and cellular function in animals, plants, and microorganisms Annu. Rev. Biochem. 56 1987 289 315
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 289-315
    • Theil, E.C.1
  • 86
    • 0344876449 scopus 로고    scopus 로고
    • Effects of the mycotoxins α- And β-zearalenol on regulation of progesterone synthesis in cultured granulosa cells from porcine ovaries
    • U. Tiemann, W. Tomek, F. Schneider, and J. Vanselow Effects of the mycotoxins α- and β-zearalenol on regulation of progesterone synthesis in cultured granulosa cells from porcine ovaries Reprod. Toxicol. 17 2003 673 681
    • (2003) Reprod. Toxicol. , vol.17 , pp. 673-681
    • Tiemann, U.1    Tomek, W.2    Schneider, F.3    Vanselow, J.4
  • 87
    • 0037093202 scopus 로고    scopus 로고
    • Regulation of ferritin genes and protein
    • F.M. Torti, and S.V. Torti Regulation of ferritin genes and protein Blood 99 2002 3505 3516
    • (2002) Blood , vol.99 , pp. 3505-3516
    • Torti, F.M.1    Torti, S.V.2
  • 88
    • 0034707208 scopus 로고    scopus 로고
    • Evolutionary history of the enolase gene family
    • M.R. Tracy, and S.B. Hedges Evolutionary history of the enolase gene family Gene 259 2000 129 138
    • (2000) Gene , vol.259 , pp. 129-138
    • Tracy, M.R.1    Hedges, S.B.2
  • 89
    • 27844572844 scopus 로고    scopus 로고
    • JunD activates transcription of the human ferritin H gene through an antioxidant response element during oxidative stress
    • Y. Tsuji JunD activates transcription of the human ferritin H gene through an antioxidant response element during oxidative stress Oncogene 51 2005 7567 7578
    • (2005) Oncogene , vol.51 , pp. 7567-7578
    • Tsuji, Y.1
  • 91
    • 77956903746 scopus 로고
    • Enolase
    • P.D. Boyer, 3rd ed.
    • F. Wold Enolase P.D. Boyer, 3rd ed. The Enzymes vol. 5 1971 499 538
    • (1971) The Enzymes , vol.5 , pp. 499-538
    • Wold, F.1
  • 92
    • 45849148051 scopus 로고    scopus 로고
    • Effects of cyclopenta[c]phenanthrene and its derivatives on zona radiata protein, ERα, and CYP1A mRNA expression in liver of rainbow trout (Oncorhynchus mykiss Walbaum)
    • M. Woźny, P. Brzuzan, M.K. Łuczyński, M. Góra, J. Bidzińska, and P. Jurkiewicz Effects of cyclopenta[c]phenanthrene and its derivatives on zona radiata protein, ERα, and CYP1A mRNA expression in liver of rainbow trout (Oncorhynchus mykiss Walbaum) Chem. Biol. Interact. 174 2008 60 68
    • (2008) Chem. Biol. Interact. , vol.174 , pp. 60-68
    • Woźny, M.1    Brzuzan, P.2    Łuczyński, M.K.3    Góra, M.4    Bidzińska, J.5    Jurkiewicz, P.6
  • 93
    • 84862886908 scopus 로고    scopus 로고
    • Preliminary evaluation of ER- and AhR-mediated gene expression patterns in rainbow trout (Oncorhynchus mykiss) liver after short-term exposure to zearalenone in binary mixtures
    • M. Woźny, P. Brzuzan, L. Wolińska, M. Góra, and M.K. Łuczyński Preliminary evaluation of ER- and AhR-mediated gene expression patterns in rainbow trout (Oncorhynchus mykiss) liver after short-term exposure to zearalenone in binary mixtures Environ. Biotechnol. 6 2010 16 23
    • (2010) Environ. Biotechnol. , vol.6 , pp. 16-23
    • Woźny, M.1    Brzuzan, P.2    Wolińska, L.3    Góra, M.4    Łuczyński, M.K.5
  • 94
    • 84862897197 scopus 로고    scopus 로고
    • Influence of zearalenone on selected biochemical parameters in juvenile rainbow trout (Oncorhynchus mykiss)
    • M. Woźny, P. Brzuzan, M. Gusiatin, E. Jakimiuk, S. Dobosz, and H. Kuźmiński Influence of zearalenone on selected biochemical parameters in juvenile rainbow trout (Oncorhynchus mykiss) Pol. J. Vet. Sci. 15 2012 221 225
    • (2012) Pol. J. Vet. Sci. , vol.15 , pp. 221-225
    • Woźny, M.1    Brzuzan, P.2    Gusiatin, M.3    Jakimiuk, E.4    Dobosz, S.5    Kuźmiński, H.6
  • 95
    • 0029861462 scopus 로고    scopus 로고
    • Molecular cloning and cold-inducible gene expression of ferritin H subunit isoforms in rainbow trout cells
    • M. Yamashita, N. Ojima, and T. Sakamoto Molecular cloning and cold-inducible gene expression of ferritin H subunit isoforms in rainbow trout cells J. Biol. Chem. 271 1996 26908 26913
    • (1996) J. Biol. Chem. , vol.271 , pp. 26908-26913
    • Yamashita, M.1    Ojima, N.2    Sakamoto, T.3
  • 96
    • 33751251394 scopus 로고    scopus 로고
    • Review on the toxicity, occurrence, metabolism, detoxification, regulations and intake of zearalenone: An oestrogenic mycotoxin
    • A. Zinedine, J.M. Soriano, J.C. MoltoÍ, and J. Manes Review on the toxicity, occurrence, metabolism, detoxification, regulations and intake of zearalenone: An oestrogenic mycotoxin Food Chem. Toxicol. 45 2007 1 18
    • (2007) Food Chem. Toxicol. , vol.45 , pp. 1-18
    • Zinedine, A.1    Soriano, J.M.2    Moltoí, J.C.3    Manes, J.4


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