메뉴 건너뛰기




Volumn 44, Issue 3, 1997, Pages 184-191

Effects of intracellular chelatable iron and oxidative stress on transcription of classical cellular glutathione peroxidase gene in murine erythroleukemia cells

Author keywords

classical cellular glutathione peroxidase mRNA; iron chelators; iron donors; murine erythroleukemia cells; oxidative stress

Indexed keywords

DACTINOMYCIN; DEFEROXAMINE; DEFEROXAMINE MESYLATE; GLUTATHIONE PEROXIDASE; HEXAMETHYLENEBISACETAMIDE; IRON; MESSENGER RNA; PYRIDOXAL ISONICOTINOYLHYDRAZONE; TERT BUTYL HYDROPEROXIDE; TRANSFERRIN;

EID: 0030752080     PISSN: 00282685     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (15)

References (43)
  • 2
    • 0026575576 scopus 로고
    • Evaluation of the iron chelation potential of hydrayones of pyridoxal, salicylaldehyde and 2-hydroxy-1-naphthyl-aldehyde using the hepatocyte in culture
    • BAKER, E., RICHARDSON, D., GROSS, S., PONKA, P.: Evaluation of the iron chelation potential of hydrayones of pyridoxal, salicylaldehyde and 2-hydroxy-1-naphthyl-aldehyde using the hepatocyte in culture. Hepatology, 15, 1992, 492-501.
    • (1992) Hepatology , vol.15 , pp. 492-501
    • Baker, E.1    Richardson, D.2    Gross, S.3    Ponka, P.4
  • 3
    • 0015919687 scopus 로고
    • The reaction of ferric salts with transferrin
    • BATES, G.W., SCHLABACH, M.R.: The reaction of ferric salts with transferrin. J. Biol. Chem., 248, 1973, 3228-3232.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3228-3232
    • Bates, G.W.1    Schlabach, M.R.2
  • 4
    • 0029053016 scopus 로고
    • Degradation of mRNA in eukaryotes
    • BELLMAN, C.A., PARKER, R.: Degradation of mRNA in eukaryotes. Cell, 81, 1995, 179-183.
    • (1995) Cell , vol.81 , pp. 179-183
    • Bellman, C.A.1    Parker, R.2
  • 5
    • 0017663106 scopus 로고
    • Increased glutathione peroxidase activity in α-thalassemia
    • BEUTLER, E., MATSUMOTO, F., POWARS, D., WARNER, J.: Increased glutathione peroxidase activity in α-thalassemia. Blood, 50, 1977, 647-655.
    • (1977) Blood , vol.50 , pp. 647-655
    • Beutler, E.1    Matsumoto, F.2    Powars, D.3    Warner, J.4
  • 6
    • 0020971311 scopus 로고
    • A rapid alkaline extraction method for the isolation of plasmid DNA
    • BIRNBOIM, H.C.: A rapid alkaline extraction method for the isolation of plasmid DNA. Methods Enzymol., 100, 1983, 243-255.
    • (1983) Methods Enzymol. , vol.100 , pp. 243-255
    • Birnboim, H.C.1
  • 7
    • 0022256894 scopus 로고
    • Iron metabolism in K 562 erythroleukemia cells
    • BOTTOMLEY, S.S., WOLFE, L.C., BRIDGES, K.R.: Iron metabolism in K 562 erythroleukemia cells. J. Biol. Chem., 260, 1985, 6811-6815.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6811-6815
    • Bottomley, S.S.1    Wolfe, L.C.2    Bridges, K.R.3
  • 8
    • 0020731805 scopus 로고
    • Quantitative binding of covalently closed circular DNA to nitrocellulose in NaI
    • BRESSER, J., GILLESPIE, D.: Quantitative binding of covalently closed circular DNA to nitrocellulose in NaI. Anal. Biochem., 129, 1983, 357-364.
    • (1983) Anal. Biochem. , vol.129 , pp. 357-364
    • Bresser, J.1    Gillespie, D.2
  • 9
    • 0017150761 scopus 로고
    • Plasma iron and erythrocytic glutathione peroxidase activity. A possible mechanism for oxidative haemolysis in iron deficiency anaemia
    • CELLERINO, R., GUIDI, G., PERONA, G.: Plasma iron and erythrocytic glutathione peroxidase activity. A possible mechanism for oxidative haemolysis in iron deficiency anaemia. Scand. J. Haematol., 17, 1976, 111-116.
    • (1976) Scand. J. Haematol. , vol.17 , pp. 111-116
    • Cellerino, R.1    Guidi, G.2    Perona, G.3
  • 10
    • 0022730806 scopus 로고
    • The structure of mouse glutathione peroxidase gene: The selenocysteine in the active site is encoded by the "termination" codon, TGA
    • CHAMBERS, I., FRAMPTON, J., GOLDFARB, P., AFFARA, N., MCBAIN, W., HARRISON, P.R.: The structure of mouse glutathione peroxidase gene: The selenocysteine in the active site is encoded by the "termination" codon, TGA. EMBO J., 5, 1986, 1221-1225.
    • (1986) EMBO J. , vol.5 , pp. 1221-1225
    • Chambers, I.1    Frampton, J.2    Goldfarb, P.3    Affara, N.4    Mcbain, W.5    Harrison, P.R.6
  • 11
    • 0028907003 scopus 로고
    • A 3' untranslated region of catalase mRNA composed of a stem-loop and dinucleotide repeat elements binds a 69 kDa redox-sensitive protein
    • CLERCH, L.B.: A 3' untranslated region of catalase mRNA composed of a stem-loop and dinucleotide repeat elements binds a 69 kDa redox-sensitive protein. Arch. Biochem. Biophys., 317, 1995, 267-274.
    • (1995) Arch. Biochem. Biophys. , vol.317 , pp. 267-274
    • Clerch, L.B.1
  • 12
    • 0030585357 scopus 로고    scopus 로고
    • Evidence that glutathione peroxidase RNA and manganese superoxide dismutase RNA bind the same protein
    • CLERCH, L.B., WRIGHT, A., CHUNG, D.J.: Evidence that glutathione peroxidase RNA and manganese superoxide dismutase RNA bind the same protein. Biochem. Biophys. Res. Commun., 222, 1996, 590-594.
    • (1996) Biochem. Biophys. Res. Commun. , vol.222 , pp. 590-594
    • Clerch, L.B.1    Wright, A.2    Chung, D.J.3
  • 13
    • 0027771175 scopus 로고
    • Identification of oxygen responsive elements in the 5'-flanking region of the human glutathione peroxidase gene
    • COWAN, D.B., WEISEL, R.D., WILLIAMS, W.G., MICKLE, D.A.G.: Identification of oxygen responsive elements in the 5'-flanking region of the human glutathione peroxidase gene. J. Biol. Chem., 268, 1993, 26904-26910.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26904-26910
    • Cowan, D.B.1    Weisel, R.D.2    Williams, W.G.3    Mickle, D.A.G.4
  • 14
    • 1842516932 scopus 로고
    • Chemistry and pharmacology of desferrioxamine as an aluminium chelator
    • Ed.: DeBroe, M.E. Toronto, Hogrefe and Huber Publishers
    • DAY, J.P., HEWITT, C.D., ACKRILL, P.: Chemistry and pharmacology of desferrioxamine as an aluminium chelator. In: Aluminium and Iron Overload in Haemodialysis. Ed.: DeBroe, M.E. Toronto, Hogrefe and Huber Publishers 1989, 42-48.
    • (1989) Aluminium and Iron Overload in Haemodialysis , pp. 42-48
    • Day, J.P.1    Hewitt, C.D.2    Ackrill, P.3
  • 15
    • 0014013696 scopus 로고
    • A membrane-filter technique for the detection of complementary DNA
    • DENHARDT, D.: A membrane-filter technique for the detection of complementary DNA. Biochem. Biophys. Res. Commun., 23, 1968, 641-652.
    • (1968) Biochem. Biophys. Res. Commun. , vol.23 , pp. 641-652
    • Denhardt, D.1
  • 16
    • 0015009308 scopus 로고
    • Hemoglobin synthesis in murine virus-induced leukemic cells in vitro: Stimulation of erythroid differentiation by dimethyl sulfoxide
    • FRIEND, C., SCHER, W., HOLLAND, J.G., SATO, T.: Hemoglobin synthesis in murine virus-induced leukemic cells in vitro: Stimulation of erythroid differentiation by dimethyl sulfoxide. Proc. Natl. Acad. Sci. USA, 68, 1971, 378-382.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 378-382
    • Friend, C.1    Scher, W.2    Holland, J.G.3    Sato, T.4
  • 17
    • 0027256146 scopus 로고
    • Ferrochelatase, glutathione peroxidase and transferrin receptor mRNA synthesis and levels in mouse erythroleukemia cells
    • FUCHS, O.: Ferrochelatase, glutathione peroxidase and transferrin receptor mRNA synthesis and levels in mouse erythroleukemia cells. Stem Cells, Suppl. 1, 11, 1993, 13-23.
    • (1993) Stem Cells , vol.11 , Issue.1 SUPPL. , pp. 13-23
    • Fuchs, O.1
  • 18
    • 0025113082 scopus 로고
    • The regulation of transferrin receptor and glutathione peroxidase mRNA synthesis by changes in intracellular iron levels
    • FUCHS, O., BOROVA, J., NEUWIRT, J.: The regulation of transferrin receptor and glutathione peroxidase mRNA synthesis by changes in intracellular iron levels. Biomed. Biochim. Acta, 49, 1990, S47-S52.
    • (1990) Biomed. Biochim. Acta , vol.49
    • Fuchs, O.1    Borova, J.2    Neuwirt, J.3
  • 19
    • 8544249929 scopus 로고
    • The effect of iron chelators or iron donors on the expression of transferrin receptor and glutathione peroxidase genes
    • FUCHS, O., BOROVA, J., NEUWIRT, J.: The effect of iron chelators or iron donors on the expression of transferrin receptor and glutathione peroxidase genes. Plzeň. Lék. Sborn., Suppl., 62, 1990, 115-116.
    • (1990) Plzeň. Lék. Sborn., Suppl. , vol.62 , pp. 115-116
    • Fuchs, O.1    Borova, J.2    Neuwirt, J.3
  • 21
    • 0021114596 scopus 로고
    • Rapid purification of plasmid DNA by a single centrifugation in a two-step cesium chloride ethidium bromide gradient
    • GARGER, S.J., GRIFFITH, O.M., GRILL, L.K.: Rapid purification of plasmid DNA by a single centrifugation in a two-step cesium chloride ethidium bromide gradient. Biochem. Biophys. Res. Commun., 117, 1983, 835-842.
    • (1983) Biochem. Biophys. Res. Commun. , vol.117 , pp. 835-842
    • Garger, S.J.1    Griffith, O.M.2    Grill, L.K.3
  • 22
    • 0018942275 scopus 로고
    • Erythrocyte superoxide dismutase catalase and glutathione peroxidase activities in β-thalassaemia (major and minor)
    • GERLI, G.C., BERETTA, L., BIANCHI, M., PELLEGATTA, A., AGOSTONI, A.: Erythrocyte superoxide dismutase catalase and glutathione peroxidase activities in β-thalassaemia (major and minor). Scand. J. Haematol., 25, 1980, 87-92.
    • (1980) Scand. J. Haematol. , vol.25 , pp. 87-92
    • Gerli, G.C.1    Beretta, L.2    Bianchi, M.3    Pellegatta, A.4    Agostoni, A.5
  • 23
    • 0018582229 scopus 로고
    • Inhibition of the iron-catalyzed formation of hydroxyl radicals from superoxide and of lipid peroxidation by desferrioxamine
    • GUTTERIDGE, J.M.C., RICHMOND, R., HALLFWELL, B.: Inhibition of the iron-catalyzed formation of hydroxyl radicals from superoxide and of lipid peroxidation by desferrioxamine. Biochem. J., 184, 1979, 469-472.
    • (1979) Biochem. J. , vol.184 , pp. 469-472
    • Gutteridge, J.M.C.1    Richmond, R.2    Hallfwell, B.3
  • 24
    • 0024790459 scopus 로고
    • Protection against tissue damage in vivo by desferrioxamine: What is its mechanism of action?
    • HALLIWELL, B.: Protection against tissue damage in vivo by desferrioxamine: What is its mechanism of action? Free Radical Biol. Med., 7, 1989, 645-651.
    • (1989) Free Radical Biol. Med. , vol.7 , pp. 645-651
    • Halliwell, B.1
  • 25
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • HALLIWELL, B., GUTTERIDGE, J.M.C.: Role of free radicals and catalytic metal ions in human disease: An overview. Methods Enzymol., 186, 1990, 1-85.
    • (1990) Methods Enzymol. , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 26
    • 0017133428 scopus 로고
    • Analysis of erythropoiesis at the molecular level
    • HARRISON, P.R.: Analysis of erythropoiesis at the molecular level. Nature, 262, 1976, 353-356
    • (1976) Nature , vol.262 , pp. 353-356
    • Harrison, P.R.1
  • 27
    • 0002853321 scopus 로고
    • Iron chelators
    • Eds: Brock, J.H., Halliday, J.W., Pippard, M.J., Powell, L.W. London, W.B. Saunders Comp. Ltd.
    • HERSHKO, C.: Iron chelators. In: Iron Metabolism in Health and Disease. Eds: Brock, J.H., Halliday, J.W., Pippard, M.J., Powell, L.W. London, W.B. Saunders Comp. Ltd. 1994, 391-426.
    • (1994) Iron Metabolism in Health and Disease , pp. 391-426
    • Hershko, C.1
  • 28
    • 7444249085 scopus 로고
    • The biochemistry of desferrioxamine and its relation to iron metabolism
    • KEBERLE, H.: The biochemistry of desferrioxamine and its relation to iron metabolism. Ann. N.Y. Acad. Sci., 119, 1964, 758-768.
    • (1964) Ann. N.Y. Acad. Sci. , vol.119 , pp. 758-768
    • Keberle, H.1
  • 29
    • 0026738247 scopus 로고
    • The 5'untranslated region of the human cellular glutathione peroxidase gene is indispensable for its expression in COS-7 cells
    • KURATA, H., KAMOSHITA, K., KAWAI, E., SUKENAGA, U., MIZUTANI, T: The 5'untranslated region of the human cellular glutathione peroxidase gene is indispensable for its expression in COS-7 cells. FEBS Lett., 312, 1992, 10-14.
    • (1992) FEBS Lett. , vol.312 , pp. 10-14
    • Kurata, H.1    Kamoshita, K.2    Kawai, E.3    Sukenaga, U.4    Mizutani, T.5
  • 30
    • 0023023013 scopus 로고
    • Control of heme synthesis during Friend cell differentiation: Role of iron and transferrin
    • LASKEY, J.D., PONKA, P., SCHULMAN, H.M.: Control of heme synthesis during Friend cell differentiation: Role of iron and transferrin. J. Cell. Physiol., 129, 1986, 185-192.
    • (1986) J. Cell. Physiol. , vol.129 , pp. 185-192
    • Laskey, J.D.1    Ponka, P.2    Schulman, H.M.3
  • 31
  • 32
    • 0027386089 scopus 로고
    • Transcriptional up-regulation of the mouse cytosolic glutathione peroxidase gene in erythroid cells is due to a tissue-specific 3'enhancer containing functionally important CACC/GT motifs and binding sites for GATA and Ets transcription factors
    • O'PREY, J., RAMSAY, S., CHAMBERS, I., HARRISON, P.R.: Transcriptional up-regulation of the mouse cytosolic glutathione peroxidase gene in erythroid cells is due to a tissue-specific 3'enhancer containing functionally important CACC/GT motifs and binding sites for GATA and Ets transcription factors. Mol. Cell. Biol., 13, 1993, 6290-6303.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6290-6303
    • O'Prey, J.1    Ramsay, S.2    Chambers, I.3    Harrison, P.R.4
  • 33
    • 0018394556 scopus 로고
    • Mobilization of iron from reticulocytes. Identification of pyridoxal isonicotinoyl hydrazone as a new iron chelating agent
    • PONKA, P., BOROVA, J., NEUWIRT, J., FUCHS, O.: Mobilization of iron from reticulocytes. Identification of pyridoxal isonicotinoyl hydrazone as a new iron chelating agent. FEBS Lett, 97, 1979, 317-321.
    • (1979) FEBS Lett , vol.97 , pp. 317-321
    • Ponka, P.1    Borova, J.2    Neuwirt, J.3    Fuchs, O.4
  • 34
    • 0018798539 scopus 로고
    • A study of intracellular iron metabolism using pyridoxal isonicotinoyl hydrazone and other synthetic chelating agents
    • PONKA, P., BOROVA, J., NEUWIRT, J., FUCHS, O., NECAS, E.: A study of intracellular iron metabolism using pyridoxal isonicotinoyl hydrazone and other synthetic chelating agents. Biochim. Biophys. Acta, 586, 1979, 278-297.
    • (1979) Biochim. Biophys. Acta , vol.586 , pp. 278-297
    • Ponka, P.1    Borova, J.2    Neuwirt, J.3    Fuchs, O.4    Necas, E.5
  • 35
    • 0026081935 scopus 로고
    • The release of iron and transferrin by the human malignant melanoma cell
    • RICHARDSON, D.R., BAKER, E.: The release of iron and transferrin by the human malignant melanoma cell. Biochim. Biophys. Acta, 1091, 1991, 294-302.
    • (1991) Biochim. Biophys. Acta , vol.1091 , pp. 294-302
    • Richardson, D.R.1    Baker, E.2
  • 36
    • 0028158768 scopus 로고
    • The effect of the iron (III) chelator, desferrioxamine, on iron and transferrin uptake by the human malignant melanoma cell
    • RICHARDSON, D.R., PONKA, P., BAKER, E.: The effect of the iron (III) chelator, desferrioxamine, on iron and transferrin uptake by the human malignant melanoma cell. Cancer Res., 54, 1994, 685-689.
    • (1994) Cancer Res. , vol.54 , pp. 685-689
    • Richardson, D.R.1    Ponka, P.2    Baker, E.3
  • 37
    • 0017375464 scopus 로고
    • Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with polymerase I
    • RIGBY, P.W.J., PICKMANN, M., RHODES, C., BERG, P.: Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with polymerase I. J.Mol. Biol., 113, 1977, 237-251.
    • (1977) J.Mol. Biol. , vol.113 , pp. 237-251
    • Rigby, P.W.J.1    Pickmann, M.2    Rhodes, C.3    Berg, P.4
  • 38
    • 0015986673 scopus 로고
    • Decreased glutathione peroxidase activity secondary to severe iron deficiency: A possible mechanism responsible for the short-ened life span of the iron-deficient red cell
    • RODVIEN, R., GILLUM, A., WEINTRAUB, L.R.: Decreased glutathione peroxidase activity secondary to severe iron deficiency: A possible mechanism responsible for the short-ened life span of the iron-deficient red cell. Blood, 43, 1974, 281-289.
    • (1974) Blood , vol.43 , pp. 281-289
    • Rodvien, R.1    Gillum, A.2    Weintraub, L.R.3
  • 39
    • 0029165020 scopus 로고
    • mRNA stability in mammalian cells
    • Ross, J.: mRNA stability in mammalian cells. Microbiol. Rev., 59, 1995, 423-450.
    • (1995) Microbiol. Rev. , vol.59 , pp. 423-450
    • Ross, J.1
  • 40
    • 0026710009 scopus 로고
    • The role of iron in oxygen-mediated toxicities
    • RYAN, T.P., AUST, S.D.: The role of iron in oxygen-mediated toxicities. Crit. Rev. Toxicol., 22, 1992, 119-141.
    • (1992) Crit. Rev. Toxicol. , vol.22 , pp. 119-141
    • Ryan, T.P.1    Aust, S.D.2
  • 41
    • 0008403047 scopus 로고
    • Analysis of transcriptional initiation in isolated nuclei
    • Ed.: Murray, E.J. Clifton, The Humana Press Inc.
    • STOTT, D.: Analysis of transcriptional initiation in isolated nuclei. In: Methods in Molecular Biology, Vol. 7. Gene Transfer and Expression Protocols. Ed.: Murray, E.J. Clifton, The Humana Press Inc. 1991, 327-335.
    • (1991) Methods in Molecular Biology, Vol. 7. Gene Transfer and Expression Protocols , vol.7 , pp. 327-335
    • Stott, D.1
  • 42
    • 0019061278 scopus 로고
    • Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose
    • THOMAS, P.S.: Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc. Natl. Acad. Sci. USA, 77, 1980, 5201-5205.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5201-5205
    • Thomas, P.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.