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Volumn 102, Issue 9, 2003, Pages 3404-3411

Effects of iron regulatory protein regulation on iron homeostasis during hypoxia

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; FERRITIN; IRON 55; IRON REGULATORY FACTOR; MESSENGER RNA; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 2; POLYADENYLATED RNA; RNA; SULFUR 35; TRANSFERRIN RECEPTOR;

EID: 0142183440     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood-2003-02-0433     Document Type: Article
Times cited : (77)

References (72)
  • 1
    • 0029842459 scopus 로고    scopus 로고
    • Oxygen sensing and molecular adaptation to hypoxia
    • Bunn HF, Poyton RO. Oxygen sensing and molecular adaptation to hypoxia. Physiol Rev. 1996;76:839-885.
    • (1996) Physiol Rev , vol.76 , pp. 839-885
    • Bunn, H.F.1    Poyton, R.O.2
  • 2
    • 0034647742 scopus 로고    scopus 로고
    • Role of hypoxia-inducible factor-1 in transcriptional activation of ceruloplasmin by iron deficiency
    • Mukhopadhyay CK, Mazumder B, Fox PL. Role of hypoxia-inducible factor-1 in transcriptional activation of ceruloplasmin by iron deficiency. J Biol Chem. 2000;275:21048-21054.
    • (2000) J Biol Chem , vol.275 , pp. 21048-21054
    • Mukhopadhyay, C.K.1    Mazumder, B.2    Fox, P.L.3
  • 3
    • 0030792094 scopus 로고    scopus 로고
    • Oxygen-regulated transferrin expression is mediated by hypoxia-inducible factor-1
    • Rolfs A, Kvietikova I, Gassmann M, Wenger RH. Oxygen-regulated transferrin expression is mediated by hypoxia-inducible factor-1. J Biol Chem. 1997;272:20055-20062.
    • (1997) J Biol Chem , vol.272 , pp. 20055-20062
    • Rolfs, A.1    Kvietikova, I.2    Gassmann, M.3    Wenger, R.H.4
  • 4
    • 0000655498 scopus 로고    scopus 로고
    • Identification of a hypoxia response element in the transferrin receptor gene
    • Lok CN, Ponka P. Identification of a hypoxia response element in the transferrin receptor gene. J Biol Chem. 1999;274:24147-24152.
    • (1999) J Biol Chem , vol.274 , pp. 24147-24152
    • Lok, C.N.1    Ponka, P.2
  • 5
    • 0033588021 scopus 로고    scopus 로고
    • Transferrin receptor induction by hypoxia: HIF-1-mediated transcriptional activation and cell-specific post-transcriptional regulation
    • Tacchini L, Bianchi L, Bernelli-Zazzera A, Cairo G. Transferrin receptor induction by hypoxia: HIF-1-mediated transcriptional activation and cell-specific post-transcriptional regulation. J Biol Chem. 1999; 274:24142-24146.
    • (1999) J Biol Chem , vol.274 , pp. 24142-24146
    • Tacchini, L.1    Bianchi, L.2    Bernelli-Zazzera, A.3    Cairo, G.4
  • 6
    • 0036037635 scopus 로고    scopus 로고
    • From erythropoietin to oxygen: Hypoxia-inducible factor hydroxylases and the hypoxia signal pathway
    • Ratcliffe PJ. From erythropoietin to oxygen: hypoxia-inducible factor hydroxylases and the hypoxia signal pathway. Blood Purif. 2002;20:445-450.
    • (2002) Blood Purif , vol.20 , pp. 445-450
    • Ratcliffe, P.J.1
  • 7
    • 0021984681 scopus 로고
    • Oxygen-derived free radicals in postischemic tissue injury
    • McCord JM. Oxygen-derived free radicals in postischemic tissue injury. N Engl J Med. 1985;312:159-163.
    • (1985) N Engl J Med , vol.312 , pp. 159-163
    • McCord, J.M.1
  • 8
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett BS, Stadtman ER. Protein oxidation in aging, disease, and oxidative stress. J Biol Chem. 1997;272:20313-20316.
    • (1997) J Biol Chem , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 9
    • 0027359376 scopus 로고
    • Ischemia: From acidosis to oxidation
    • Levine RL. Ischemia: from acidosis to oxidation. FASEB J. 1993;7:1242-1246.
    • (1993) FASEB J , vol.7 , pp. 1242-1246
    • Levine, R.L.1
  • 10
    • 0028924795 scopus 로고
    • Desferal prevents against cell lysis induced by hydrogen peroxide to hypoxic hepatocytes: A role for free iron in hypoxia-mediated cellular injury
    • Lefebvre V, Buc-Calderon P. Desferal prevents against cell lysis induced by hydrogen peroxide to hypoxic hepatocytes: a role for free iron in hypoxia-mediated cellular injury. Chem Biol Interact. 1995;94:37-48.
    • (1995) Chem Biol Interact , vol.94 , pp. 37-48
    • Lefebvre, V.1    Buc-Calderon, P.2
  • 11
    • 0028202461 scopus 로고
    • Deferoxamine posttreatment reduces ischemic brain injury in neonatal rats
    • Palmer C, Roberts RL, Bero C. Deferoxamine posttreatment reduces ischemic brain injury in neonatal rats. Stroke. 1994;25:1039-1045.
    • (1994) Stroke , vol.25 , pp. 1039-1045
    • Palmer, C.1    Roberts, R.L.2    Bero, C.3
  • 12
    • 0028032714 scopus 로고
    • Extracellular iron chelators protect kidney cells from hypoxia/reoxygenation
    • Paller MS, Hedlund BE. Extracellular iron chelators protect kidney cells from hypoxia/reoxygenation. Free Radic Biol Med. 1994;17:597-603.
    • (1994) Free Radic Biol Med , vol.17 , pp. 597-603
    • Paller, M.S.1    Hedlund, B.E.2
  • 13
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • Hentze MW, Kuhn LC. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc Natl Acad Sci U S A. 1996;93:8175-8182.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kuhn, L.C.2
  • 14
    • 0033826764 scopus 로고    scopus 로고
    • Iron regulatory proteins and the molecular control of mammalian iron metabolism
    • Eisenstein RS. Iron regulatory proteins and the molecular control of mammalian iron metabolism. Annu Rev Nutr. 2000;20:627-662.
    • (2000) Annu Rev Nutr , vol.20 , pp. 627-662
    • Eisenstein, R.S.1
  • 16
    • 0030752458 scopus 로고    scopus 로고
    • Redox modulation of iron regulatory proteins by peroxynitrite
    • Bouton C, Hirling H, Drapier JC. Redox modulation of iron regulatory proteins by peroxynitrite. J Biol Chem. 1997;272:19969-19975.
    • (1997) J Biol Chem , vol.272 , pp. 19969-19975
    • Bouton, C.1    Hirling, H.2    Drapier, J.C.3
  • 17
    • 0037096190 scopus 로고    scopus 로고
    • The iron regulatory proteins: Targets and modulators of free radical reactions and oxidative damage(1,2)
    • Cairo G, Recalcati S, Pietrangelo A, Minotti G. The iron regulatory proteins: targets and modulators of free radical reactions and oxidative damage(1,2). Free Radic Biol Med. 2002;32:1237-1243.
    • (2002) Free Radic Biol Med , vol.32 , pp. 1237-1243
    • Cairo, G.1    Recalcati, S.2    Pietrangelo, A.3    Minotti, G.4
  • 18
    • 0032812762 scopus 로고    scopus 로고
    • Regulation of the iron regulatory proteins by reactive nitrogen and oxygen species
    • Hanson ES, Leibold EA. Regulation of the iron regulatory proteins by reactive nitrogen and oxygen species. Gene Expr. 1999;7:367-376.
    • (1999) Gene Expr , vol.7 , pp. 367-376
    • Hanson, E.S.1    Leibold, E.A.2
  • 19
  • 20
    • 0029914953 scopus 로고    scopus 로고
    • Phosphorylation and activation of both iron regulatory proteins 1 and 2 in HL-60 cells
    • Schalinske KL, Eisenstein RS. Phosphorylation and activation of both iron regulatory proteins 1 and 2 in HL-60 cells. J Biol Chem. 1996;271:7168-7176.
    • (1996) J Biol Chem , vol.271 , pp. 7168-7176
    • Schalinske, K.L.1    Eisenstein, R.S.2
  • 21
    • 0032417611 scopus 로고    scopus 로고
    • Novel role of phosphorylation in Fe-S cluster stability revealed by phosphomimetic mutations at Ser-138 of iron regulatory protein 1
    • Brown NM, Anderson SA, Steffen DW, et al. Novel role of phosphorylation in Fe-S cluster stability revealed by phosphomimetic mutations at Ser-138 of iron regulatory protein 1. Proc Natl Acad Sci U S A. 1998;95:15235-15240.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 15235-15240
    • Brown, N.M.1    Anderson, S.A.2    Steffen, D.W.3
  • 22
    • 0032571304 scopus 로고    scopus 로고
    • Regulation of iron regulatory protein 1 during hypoxia and hypoxia/reoxygenation
    • Hanson ES, Leibold EA. Regulation of iron regulatory protein 1 during hypoxia and hypoxia/reoxygenation. J Biol Chem. 1998;273:7588-7593.
    • (1998) J Biol Chem , vol.273 , pp. 7588-7593
    • Hanson, E.S.1    Leibold, E.A.2
  • 23
    • 0033582451 scopus 로고    scopus 로고
    • Hypoxia posttranslationally activates iron-regulatory protein 2
    • Hanson ES, Foot LM, Leibold EA. Hypoxia posttranslationally activates iron-regulatory protein 2. J Biol Chem. 1999;274:5047-5052.
    • (1999) J Biol Chem , vol.274 , pp. 5047-5052
    • Hanson, E.S.1    Foot, L.M.2    Leibold, E.A.3
  • 24
    • 0035847120 scopus 로고    scopus 로고
    • Effects of hyperoxia and iron on iron regulatory protein-1 activity and the ferritin synthesis in mouse peritoneal macrophages
    • Kuriyama-Matsumura K, Sato H, Suzuki M, Bannai S. Effects of hyperoxia and iron on iron regulatory protein-1 activity and the ferritin synthesis in mouse peritoneal macrophages. Biochim Biophys Acta. 2001;1544:370-377.
    • (2001) Biochim Biophys Acta , vol.1544 , pp. 370-377
    • Kuriyama-Matsumura, K.1    Sato, H.2    Suzuki, M.3    Bannai, S.4
  • 25
    • 0032504538 scopus 로고    scopus 로고
    • Regulation of ferritin synthesis and iron regulatory protein 1 by oxygen in mouse peritoneal macrophages
    • Kuriyama-Matsumura K, Sato H, Yamaguchi M, Bannai S. Regulation of ferritin synthesis and iron regulatory protein 1 by oxygen in mouse peritoneal macrophages. Biochem Biophys Res Commun. 1998;249:241-246.
    • (1998) Biochem Biophys Res Commun , vol.249 , pp. 241-246
    • Kuriyama-Matsumura, K.1    Sato, H.2    Yamaguchi, M.3    Bannai, S.4
  • 26
    • 0033548251 scopus 로고    scopus 로고
    • Hypoxia alters iron-regulatory protein-1 binding capacity and modulates cellular iron homeostasis in human hepatoma and erythroleukemia cells
    • Toth I, Yuan L, Rogers JT, Boyce H, Bridges KR. Hypoxia alters iron-regulatory protein-1 binding capacity and modulates cellular iron homeostasis in human hepatoma and erythroleukemia cells. J Biol Chem. 1999;274:4467-4473.
    • (1999) J Biol Chem , vol.274 , pp. 4467-4473
    • Toth, I.1    Yuan, L.2    Rogers, J.T.3    Boyce, H.4    Bridges, K.R.5
  • 27
    • 0030880742 scopus 로고    scopus 로고
    • Induction of ferritin synthesis in ischemic-reperfused rat liver: Analysis of the molecular mechanisms
    • Tacchini L, Recalcati S, Bernelli-Zazzera A, Cairo G. Induction of ferritin synthesis in ischemic-reperfused rat liver: analysis of the molecular mechanisms. Gastroenterology. 1997;113:946-953.
    • (1997) Gastroenterology , vol.113 , pp. 946-953
    • Tacchini, L.1    Recalcati, S.2    Bernelli-Zazzera, A.3    Cairo, G.4
  • 28
    • 0036291808 scopus 로고    scopus 로고
    • Transferrin receptor gene expression and transferrin-bound iron uptake are increased during postischemic rat liver reperfusion
    • Tacchini L, Poli DF, Bernelli-Zazzera A, Cairo G. Transferrin receptor gene expression and transferrin-bound iron uptake are increased during postischemic rat liver reperfusion. Hepatology. 2002;36:103-111.
    • (2002) Hepatology , vol.36 , pp. 103-111
    • Tacchini, L.1    Poli, D.F.2    Bernelli-Zazzera, A.3    Cairo, G.4
  • 29
    • 0030063971 scopus 로고    scopus 로고
    • Modulation of iron regulatory protein functions: Further insights into the role of nitrogen- and oxygen-derived reactive species
    • Bouton C, Raveau M, Drapier JC. Modulation of iron regulatory protein functions: further insights into the role of nitrogen- and oxygen-derived reactive species. J Biol Chem. 1996;271:2300-2306.
    • (1996) J Biol Chem , vol.271 , pp. 2300-2306
    • Bouton, C.1    Raveau, M.2    Drapier, J.C.3
  • 30
    • 0026806913 scopus 로고
    • Inactivation-reactivation of aconitase in Escherichia coli: A sensitive measure of superoxide radical
    • Gardner PR, Fridovich I. Inactivation-reactivation of aconitase in Escherichia coli: a sensitive measure of superoxide radical. J Biol Chem. 1992;267:8757-8763.
    • (1992) J Biol Chem , vol.267 , pp. 8757-8763
    • Gardner, P.R.1    Fridovich, I.2
  • 31
    • 0032006692 scopus 로고    scopus 로고
    • Nitric oxide-mediated induction of ferritin synthesis in J774 macrophages by inflammatory cytokines: Role of selective iron regulatory protein-2 down-regulation
    • Recalcati S, Taramelli D, Conte D, Cairo G. Nitric oxide-mediated induction of ferritin synthesis in J774 macrophages by inflammatory cytokines: role of selective iron regulatory protein-2 down-regulation. Blood. 1998;91:1059-1066.
    • (1998) Blood , vol.91 , pp. 1059-1066
    • Recalcati, S.1    Taramelli, D.2    Conte, D.3    Cairo, G.4
  • 32
    • 0029927715 scopus 로고    scopus 로고
    • Differential regulation of IRP1 and IRP2 by nitric oxide in rat hepatoma cells
    • Phillips JD, Kinikini DV, Yu Y, Guo B, Leibold EA. Differential regulation of IRP1 and IRP2 by nitric oxide in rat hepatoma cells. Blood. 1996;87:2983-2992.
    • (1996) Blood , vol.87 , pp. 2983-2992
    • Phillips, J.D.1    Kinikini, D.V.2    Yu, Y.3    Guo, B.4    Leibold, E.A.5
  • 33
    • 0037062606 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite activate the iron regulatory protein-1 of J774A.1 macrophages by direct disassembly of the Fe-S cluster of cytoplasmic aconitase
    • Cairo G, Ronchi R, Recalcati S, Campanella A, Minotti G. Nitric oxide and peroxynitrite activate the iron regulatory protein-1 of J774A.1 macrophages by direct disassembly of the Fe-S cluster of cytoplasmic aconitase. Biochemistry. 2002;41:7435-7442.
    • (2002) Biochemistry , vol.41 , pp. 7435-7442
    • Cairo, G.1    Ronchi, R.2    Recalcati, S.3    Campanella, A.4    Minotti, G.5
  • 34
    • 0034089867 scopus 로고    scopus 로고
    • Effects of interferon-gamma and lipopolysaccharide on macrophage iron metabolism are mediated by nitric oxide-induced degradation of iron regulatory protein 2
    • Kim S, Ponka P. Effects of interferon-gamma and lipopolysaccharide on macrophage iron metabolism are mediated by nitric oxide-induced degradation of iron regulatory protein 2. J Biol Chem. 2000;275:6220-6226.
    • (2000) J Biol Chem , vol.275 , pp. 6220-6226
    • Kim, S.1    Ponka, P.2
  • 35
    • 0024121621 scopus 로고
    • Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated region of ferritin heavy- and light-subunit mRNAs
    • Leibold EA, Munro HN. Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated region of ferritin heavy- and light-subunit mRNAs. Proc Natl Acad Sci U S A. 1988;85:2171-2175.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 2171-2175
    • Leibold, E.A.1    Munro, H.N.2
  • 36
    • 0026736834 scopus 로고
    • The iron-responsive element binding protein: Purification, cloning, and regulation in rat liver
    • Yu Y, Radisky E, Leibold EA. The iron-responsive element binding protein: purification, cloning, and regulation in rat liver. J Biol Chem. 1992;267:19005-19010.
    • (1992) J Biol Chem , vol.267 , pp. 19005-19010
    • Yu, Y.1    Radisky, E.2    Leibold, E.A.3
  • 37
    • 0028131454 scopus 로고
    • Iron regulates cytoplasmic levels of a novel iron-responsive element-binding protein without aconitase activity
    • Guo B, Yu Y, Leibold EA. Iron regulates cytoplasmic levels of a novel iron-responsive element-binding protein without aconitase activity. J Biol Chem. 1994;269:24252-24260.
    • (1994) J Biol Chem , vol.269 , pp. 24252-24260
    • Guo, B.1    Yu, Y.2    Leibold, E.A.3
  • 38
    • 0021174049 scopus 로고
    • Gene transfer, expression, and molecular cloning of the human transferrin receptor gene
    • Kuhn LC, McClelland A, Ruddle FH. Gene transfer, expression, and molecular cloning of the human transferrin receptor gene. Cell. 1984;37:95-103.
    • (1984) Cell , vol.37 , pp. 95-103
    • Kuhn, L.C.1    McClelland, A.2    Ruddle, F.H.3
  • 40
    • 0023445376 scopus 로고
    • Conservation of ferritin heavy subunit gene structure: Implications for the regulation of ferritin gene expression
    • Murray MT, White K, Munro HN. Conservation of ferritin heavy subunit gene structure: implications for the regulation of ferritin gene expression. Proc Natl Acad Sci U S A. 1987;84:7438-7442.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 7438-7442
    • Murray, M.T.1    White, K.2    Munro, H.N.3
  • 41
    • 0025009117 scopus 로고
    • Cloning of the cDNA encoding an RNA regulatory protein- the human iron-responsive element-binding protein
    • Rouault TA, Tang CK, Kaptain S, et al. Cloning of the cDNA encoding an RNA regulatory protein- the human iron-responsive element-binding protein. Proc Natl Acad Sci U S A. 1990;87:7958-7962.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 7958-7962
    • Rouault, T.A.1    Tang, C.K.2    Kaptain, S.3
  • 42
    • 0021112587 scopus 로고
    • The role of iron in the activation-inactivation of aconitase
    • Kennedy MC, Emptage MH, Dreyer JL, Beinert H. The role of iron in the activation-inactivation of aconitase. J Biol Chem. 1983;258:11098-11105.
    • (1983) J Biol Chem , vol.258 , pp. 11098-11105
    • Kennedy, M.C.1    Emptage, M.H.2    Dreyer, J.L.3    Beinert, H.4
  • 43
    • 0029034338 scopus 로고
    • Characterization and expression of iron regulatory protein 2 (IRP2): Presence of multiple IRP2 transcripts regulated by intracellular iron levels
    • Guo B, Brown FM, Phillips JD, Yu Y, Leibold EA. Characterization and expression of iron regulatory protein 2 (IRP2): presence of multiple IRP2 transcripts regulated by intracellular iron levels. J Biol Chem. 1995;270:16529-16535.
    • (1995) J Biol Chem , vol.270 , pp. 16529-16535
    • Guo, B.1    Brown, F.M.2    Phillips, J.D.3    Yu, Y.4    Leibold, E.A.5
  • 44
    • 0027050315 scopus 로고
    • Cellular regulation of the iron-responsive element binding protein: Disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding
    • Haile DJ, Rouault TA, Harford JB, et al. Cellular regulation of the iron-responsive element binding protein: disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding. Proc Natl Acad Sci U S A. 1992;89:11735-11739.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 11735-11739
    • Haile, D.J.1    Rouault, T.A.2    Harford, J.B.3
  • 45
    • 0019804406 scopus 로고
    • Biosynthesis of the human transferrin receptor in cultured cells
    • Omary MB, Trowbridge IS. Biosynthesis of the human transferrin receptor in cultured cells. J Biol Chem. 1981;256:12888-12892.
    • (1981) J Biol Chem , vol.256 , pp. 12888-12892
    • Omary, M.B.1    Trowbridge, I.S.2
  • 49
    • 0033984237 scopus 로고    scopus 로고
    • Nramp2 expression is associated with pH-dependent iron uptake across the apical membrane of human intestinal Caco-2 cells
    • Tandy S, Williams M, Leggett A, et al. Nramp2 expression is associated with pH-dependent iron uptake across the apical membrane of human intestinal Caco-2 cells. J Biol Chem. 2000;275:1023-1029.
    • (2000) J Biol Chem , vol.275 , pp. 1023-1029
    • Tandy, S.1    Williams, M.2    Leggett, A.3
  • 50
    • 0030755366 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian proton-coupled metal-ion transporter
    • Gunshin H, Mackenzie B, Berger UV, et al. Cloning and characterization of a mammalian proton-coupled metal-ion transporter. Nature. 1997;388:482-488.
    • (1997) Nature , vol.388 , pp. 482-488
    • Gunshin, H.1    Mackenzie, B.2    Berger, U.V.3
  • 51
    • 0029029016 scopus 로고
    • Hypoxia alters iron homeostasis and induces ferritin synthesis in oligodendrocytes
    • Qi Y, Jamindar TM, Dawson G. Hypoxia alters iron homeostasis and induces ferritin synthesis in oligodendrocytes. J Neurochem. 1995;64:2458-2464.
    • (1995) J Neurochem , vol.64 , pp. 2458-2464
    • Qi, Y.1    Jamindar, T.M.2    Dawson, G.3
  • 52
    • 0035827697 scopus 로고    scopus 로고
    • 2 on the expression and function of iron-responsive element-containing mRNAs in B6 fibroblasts
    • 2 on the expression and function of iron-responsive element-containing mRNAs in B6 fibroblasts. J Biol Chem. 2001;276:19738-19745.
    • (2001) J Biol Chem , vol.276 , pp. 19738-19745
    • Caltagirone, A.1    Weiss, G.2    Pantopoulos, K.3
  • 53
    • 0002840502 scopus 로고    scopus 로고
    • Ferritin and iron biomineralization
    • Suslick KS, ed. Oxford, United Kingdom: Pergamon Press
    • Waldo GS, Theil EC. Ferritin and iron biomineralization. In: Suslick KS, ed. Comprehensive Supramolecular Chemistry. Oxford, United Kingdom: Pergamon Press; 1996:65-89.
    • (1996) Comprehensive Supramolecular Chemistry , pp. 65-89
    • Waldo, G.S.1    Theil, E.C.2
  • 54
    • 0033571363 scopus 로고    scopus 로고
    • H-ferritin subunit overexpression in erythroid cells reduces the oxidative stress response and induces multidrug resistance properties
    • Epsztejn S, Glickstein H, Picard V, et al. H-ferritin subunit overexpression in erythroid cells reduces the oxidative stress response and induces multidrug resistance properties. Blood. 1999;94:3593-3603.
    • (1999) Blood , vol.94 , pp. 3593-3603
    • Epsztejn, S.1    Glickstein, H.2    Picard, V.3
  • 55
    • 0028928738 scopus 로고
    • Induction of ferritin synthesis by oxidative stress: Transcriptional and post-transcriptional regulation by expansion of the "free" iron pool
    • Cairo G, Tacchini L, Pogliaghi G, Anzon E, Tomasi A, Bernelli-Zazzera A. Induction of ferritin synthesis by oxidative stress: transcriptional and post-transcriptional regulation by expansion of the "free" iron pool. J Biol Chem. 1995;270:700-703.
    • (1995) J Biol Chem , vol.270 , pp. 700-703
    • Cairo, G.1    Tacchini, L.2    Pogliaghi, G.3    Anzon, E.4    Tomasi, A.5    Bernelli-Zazzera, A.6
  • 56
    • 0033853838 scopus 로고    scopus 로고
    • Coordinate transcriptional and translational regulation of ferritin in response to oxidative stress
    • Tsuji Y, Ayaki H, Whitman SP, Morrow CS, Torti SV, Torti FM. Coordinate transcriptional and translational regulation of ferritin in response to oxidative stress. Mol Cell Biol. 2000;20:5818-5827.
    • (2000) Mol Cell Biol , vol.20 , pp. 5818-5827
    • Tsuji, Y.1    Ayaki, H.2    Whitman, S.P.3    Morrow, C.S.4    Torti, S.V.5    Torti, F.M.6
  • 57
    • 0037125975 scopus 로고    scopus 로고
    • Nitrogen monoxide-mediated control of ferritin synthesis: Implications for macrophage iron homeostasis
    • Kim S, Ponka P. Nitrogen monoxide-mediated control of ferritin synthesis: implications for macrophage iron homeostasis. Proc Natl Acad Sci U S A. 2002;99:12214-12219.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 12214-12219
    • Kim, S.1    Ponka, P.2
  • 58
    • 0034721576 scopus 로고    scopus 로고
    • Differential regulation of H- and L-ferritin messenger RNA subunits, ferritin protein and iron following focal cerebral ischemia-reperfusion
    • Chi SI, Wang CK, Chen JJ, Chau LY, Lin TN. Differential regulation of H- and L-ferritin messenger RNA subunits, ferritin protein and iron following focal cerebral ischemia-reperfusion. Neuroscience. 2000;100:475-484.
    • (2000) Neuroscience , vol.100 , pp. 475-484
    • Chi, S.I.1    Wang, C.K.2    Chen, J.J.3    Chau, L.Y.4    Lin, T.N.5
  • 60
    • 0032508548 scopus 로고    scopus 로고
    • Loops and bulge/loops in iron-responsive element isoforms influence iron regulatory protein binding: Fine-tuning of mRNA regulation?
    • Ke Y, Wu J, Leibold EA, Walden WE, Theil EC. Loops and bulge/loops in iron-responsive element isoforms influence iron regulatory protein binding: fine-tuning of mRNA regulation? J Biol Chem. 1998;273:23637-23640.
    • (1998) J Biol Chem , vol.273 , pp. 23637-23640
    • Ke, Y.1    Wu, J.2    Leibold, E.A.3    Walden, W.E.4    Theil, E.C.5
  • 61
    • 0028114730 scopus 로고
    • Iron regulatory elements (IREs): A family of mRNA non-coding sequences
    • Theil EC. Iron regulatory elements (IREs): a family of mRNA non-coding sequences. Biochem J. 1994;304:1-11.
    • (1994) Biochem J , vol.304 , pp. 1-11
    • Theil, E.C.1
  • 62
    • 0032488980 scopus 로고    scopus 로고
    • Iron differentially stimulates translation of mitochondrial aconitase and ferritin mRNAs in mammalian cells: Implications for iron regulatory proteins as regulators of mitochondrial citrate utilization
    • Schalinske KL, Chen OS, Eisenstein RS. Iron differentially stimulates translation of mitochondrial aconitase and ferritin mRNAs in mammalian cells: implications for iron regulatory proteins as regulators of mitochondrial citrate utilization. J Biol Chem. 1998;273:3740-3746.
    • (1998) J Biol Chem , vol.273 , pp. 3740-3746
    • Schalinske, K.L.1    Chen, O.S.2    Eisenstein, R.S.3
  • 63
    • 0037044717 scopus 로고    scopus 로고
    • Multiple, conserved iron responsive elements in the 3′ untranslated region of transferrin receptor mRNA enhance binding of iron regulatory protein 2
    • Erlitzki R, Long JC, Theil EC. Multiple, conserved iron responsive elements in the 3′ untranslated region of transferrin receptor mRNA enhance binding of iron regulatory protein 2. J Biol Chem. 2002;277:42579-42587.
    • (2002) J Biol Chem , vol.277 , pp. 42579-42587
    • Erlitzki, R.1    Long, J.C.2    Theil, E.C.3
  • 64
    • 0023609748 scopus 로고
    • Modification of iron uptake and lipid peroxidation by hypoxia, ascorbic acid, and alpha-tocopherol in iron-loaded rat myocardial cell cultures
    • Hershko C, Link G, Pinson A. Modification of iron uptake and lipid peroxidation by hypoxia, ascorbic acid, and alpha-tocopherol in iron-loaded rat myocardial cell cultures. J Lab Clin Med. 1987;110:355-361.
    • (1987) J Lab Clin Med , vol.110 , pp. 355-361
    • Hershko, C.1    Link, G.2    Pinson, A.3
  • 65
    • 0037184526 scopus 로고    scopus 로고
    • Mechanisms of cellular iron acquisition: Another iron in the fire
    • Kaplan J. Mechanisms of cellular iron acquisition: another iron in the fire. Cell. 2002;111:603-606.
    • (2002) Cell , vol.111 , pp. 603-606
    • Kaplan, J.1
  • 67
    • 0034466201 scopus 로고    scopus 로고
    • Reactive oxygen species as regulators of oxygen dependent gene expression
    • Fandrey J, Genius J. Reactive oxygen species as regulators of oxygen dependent gene expression. Adv Exp Med Biol. 2000;475:153-159.
    • (2000) Adv Exp Med Biol , vol.475 , pp. 153-159
    • Fandrey, J.1    Genius, J.2
  • 68
    • 0029055581 scopus 로고
    • Rapid responses to oxidative stress mediated by iron regulatory protein
    • Pantopoulos K, Hentze MW. Rapid responses to oxidative stress mediated by iron regulatory protein. EMBO J. 1995;14:2917-2924.
    • (1995) EMBO J , vol.14 , pp. 2917-2924
    • Pantopoulos, K.1    Hentze, M.W.2
  • 69
    • 0030873539 scopus 로고    scopus 로고
    • An EPR investigation of the products of the reaction of cytosolic and mitochondrial aconitases with nitric oxide
    • Kennedy MC, Antholine WE, Beinert H. An EPR investigation of the products of the reaction of cytosolic and mitochondrial aconitases with nitric oxide. J Biol Chem. 1997;272:20340-20347.
    • (1997) J Biol Chem , vol.272 , pp. 20340-20347
    • Kennedy, M.C.1    Antholine, W.E.2    Beinert, H.3
  • 71
    • 0034717027 scopus 로고    scopus 로고
    • The aconitase function of iron regulatory protein 1: Genetic studies in yeast implicate its role in iron-mediated redox regulation
    • Narahari J, Ma R, Wang M, Walden WE. The aconitase function of iron regulatory protein 1: genetic studies in yeast implicate its role in iron-mediated redox regulation. J Biol Chem. 2000;275:16227-16234.
    • (2000) J Biol Chem , vol.275 , pp. 16227-16234
    • Narahari, J.1    Ma, R.2    Wang, M.3    Walden, W.E.4
  • 72
    • 0141890273 scopus 로고    scopus 로고
    • Oxygen and iron regulation of iron regulatory protein 2
    • Hanson ES, Rawlins ML, Leibold EA. Oxygen and iron regulation of iron regulatory protein 2. J Biol Chem. 2003;278:40337-40342.
    • (2003) J Biol Chem , vol.278 , pp. 40337-40342
    • Hanson, E.S.1    Rawlins, M.L.2    Leibold, E.A.3


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