메뉴 건너뛰기




Volumn 65, Issue , 2013, Pages 1174-1194

The complex interplay of iron metabolism, reactive oxygen species, and reactive nitrogen species: Insights into the potential of various iron therapies to induce oxidative and nitrosative stress

Author keywords

Free radicals; Intravenous iron; Nitrosative stress; Oral iron; Oxidative stress; Reactive nitrogen species; Reactive oxygen species

Indexed keywords

C REACTIVE PROTEIN; CATALASE; COPPER ZINC SUPEROXIDE DISMUTASE; DEXTRAN; DEXTRAN SULFATE; FERROPORTIN; FERROUS FUMARATE; FERROUS SULFATE; HEPCIDIN; HYDROGEN PEROXIDE; HYDROXYL RADICAL; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 2ALPHA; INDUCIBLE NITRIC OXIDE SYNTHASE; INTERLEUKIN 6; IRON; IRON COMPLEX; IRON DEXTRAN; MALONALDEHYDE; MESSENGER RNA; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 2; NITRIC OXIDE; PEROXIREDOXIN 2; PEROXYNITRITE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; STAT3 PROTEIN; TRANSFERRIN;

EID: 84884950378     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2013.09.001     Document Type: Review
Times cited : (330)

References (345)
  • 2
    • 84885432933 scopus 로고    scopus 로고
    • Redox-active metals: Iron and copper
    • K. Pantopoulos, H.M. Schipper, Nova Sci. Pub Hauppauge, NY
    • W.H. Koppenol, and P.L. Bounds Redox-active metals: iron and copper K. Pantopoulos, H.M. Schipper, Principles of free radical biomedicine 2011 Nova Sci. Pub Hauppauge, NY 91 111
    • (2011) Principles of Free Radical Biomedicine , pp. 91-111
    • Koppenol, W.H.1    Bounds, P.L.2
  • 3
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • W. Dröge Free radicals in the physiological control of cell function Physiol. Rev. 82 2002 47 95 (Pubitemid 34654215)
    • (2002) Physiological Reviews , vol.82 , Issue.1 , pp. 47-95
    • Droge, W.1
  • 4
    • 80053124673 scopus 로고    scopus 로고
    • Taking a good look at free radicals in the aging process
    • S. Hekimi, J. Lapointe, and Y. Wen Taking a good look at free radicals in the aging process Trends Cell Biol. 21 2011 569 576
    • (2011) Trends Cell Biol. , vol.21 , pp. 569-576
    • Hekimi, S.1    Lapointe, J.2    Wen, Y.3
  • 5
    • 78650890352 scopus 로고    scopus 로고
    • Regulation of autophagy by ROS: Physiology and pathology
    • R. Scherz-Shouval, and Z. Elazar Regulation of autophagy by ROS: physiology and pathology Trends Biochem. Sci. 36 2011 30 38
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 30-38
    • Scherz-Shouval, R.1    Elazar, Z.2
  • 6
    • 0034782946 scopus 로고    scopus 로고
    • Redox signaling in macrophages
    • DOI 10.1016/S0098-2997(01)00010-3, PII S0098299701000103
    • H.J. Forman, and M. Torres Redox signaling in macrophages Mol. Aspects Med. 22 2001 189 216 (Pubitemid 33000522)
    • (2001) Molecular Aspects of Medicine , vol.22 , Issue.4-5 , pp. 189-216
    • Jay Forman, H.1    Torres, M.2
  • 11
    • 78449290415 scopus 로고    scopus 로고
    • The struggle for iron - A metal at the host-pathogen interface
    • M. Nairz, A. Schroll, T. Sonnweber, and G. Weiss The struggle for iron - a metal at the host-pathogen interface Cell Microbiol. 12 2010 1691 1702
    • (2010) Cell Microbiol. , vol.12 , pp. 1691-1702
    • Nairz, M.1    Schroll, A.2    Sonnweber, T.3    Weiss, G.4
  • 12
    • 80255137555 scopus 로고    scopus 로고
    • The role of lysosomes in iron metabolism and recycling
    • T. Kurz, J.W. Eaton, and U.T. Brunk The role of lysosomes in iron metabolism and recycling Int. J. Biochem. Cell Biol. 43 2011 1686 1697
    • (2011) Int. J. Biochem. Cell Biol. , vol.43 , pp. 1686-1697
    • Kurz, T.1    Eaton, J.W.2    Brunk, U.T.3
  • 13
    • 0029815291 scopus 로고    scopus 로고
    • Superoxide and hydrogen peroxide-dependent inhibition of iron regulatory protein activity: A protective stratagem against oxidative injury
    • G. Cairo, E. Castrusini, G. Minotti, and A. Bernelli-Zazzera Superoxide and hydrogen peroxide-dependent inhibition of iron regulatory protein activity: a protective stratagem against oxidative injury FASEB J. 10 1996 1326 1335 (Pubitemid 26313536)
    • (1996) FASEB Journal , vol.10 , Issue.11 , pp. 1326-1335
    • Cairo, G.1    Castrusini, E.2    Minotti, G.3    Bernelli-Zazzera, A.4
  • 14
    • 0029055581 scopus 로고
    • Rapid responses to oxidative stress mediated by iron regulatory protein
    • K. Pantopoulos, and M.W. Hentze Rapid responses to oxidative stress mediated by iron regulatory protein EMBO J. 14 1995 2917 2924
    • (1995) EMBO J. , vol.14 , pp. 2917-2924
    • Pantopoulos, K.1    Hentze, M.W.2
  • 15
    • 1642504730 scopus 로고    scopus 로고
    • Nitric oxide and iron: Effect of iron overload on nitric oxide production in endotoxemia
    • DOI 10.1016/j.mam.2004.02.015, PII S0098299704000160
    • M. Galleano, M. Simontacchi, and S. Puntarulo Nitric oxide and iron: effect of iron overload on nitric oxide production in endotoxemia Mol. Aspects Med. 25 2004 141 154 (Pubitemid 38401938)
    • (2004) Molecular Aspects of Medicine , vol.25 , Issue.1-2 , pp. 141-154
    • Galleano, M.1    Simontacchi, M.2    Puntarulo, S.3
  • 17
    • 40949165720 scopus 로고    scopus 로고
    • The nitric oxide-iron interplay in mammalian cells: Transport and storage of dinitrosyl iron complexes
    • D.R. Richardson, and H.C. Lok The nitric oxide-iron interplay in mammalian cells: transport and storage of dinitrosyl iron complexes Biochim. Biophys. Acta 1780 2008 638 651
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 638-651
    • Richardson, D.R.1    Lok, H.C.2
  • 18
    • 0027301897 scopus 로고
    • Biosynthesis of nitric oxide activates iron regulatory factor in macrophages
    • J.C. Drapier, H. Hirling, J. Wietzerbin, P. Kaldy, and L.C. Kuhn Biosynthesis of nitric oxide activates iron regulatory factor in macrophages EMBO J. 12 1993 3643 3649 (Pubitemid 23256451)
    • (1993) EMBO Journal , vol.12 , Issue.9 , pp. 3643-3649
    • Drapier, J.-C.1    Hirling, H.2    Wietzerbin, J.3    Kaldy, P.4    Kuhn, L.C.5
  • 22
    • 0033230590 scopus 로고    scopus 로고
    • Identification of RNA-binding surfaces in iron regulatory protein-1
    • DOI 10.1093/emboj/18.21.6073
    • P. Kaldy, E. Menotti, R. Moret, and L.C. Kuhn Identification of RNA-binding surfaces in iron regulatory protein-1 EMBO J. 18 1999 6073 6083 (Pubitemid 29515683)
    • (1999) EMBO Journal , vol.18 , Issue.21 , pp. 6073-6083
    • Kaldy, P.1    Menotti, E.2    Moret, R.3    Kuhn, L.C.4
  • 23
    • 0028276577 scopus 로고
    • The bifunctional iron-responsive element binding protein/cytosolic aconitase: The role of active-site residues in ligand binding and regulation
    • DOI 10.1073/pnas.91.15.7321
    • C.C. Philpott, R.D. Klausner, and T.A. Rouault The bifunctional iron-responsive element binding protein/cytosolic aconitase: the role of active-site residues in ligand binding and regulation Proc. Natl. Acad. Sci. USA 91 1994 7321 7325 (Pubitemid 24226855)
    • (1994) Proceedings of the National Academy of Sciences of the United States of America , vol.91 , Issue.15 , pp. 7321-7325
    • Philpott, C.C.1    Klausner, R.D.2    Rouault, T.A.3
  • 27
    • 0033563095 scopus 로고    scopus 로고
    • Central role of transcription factor NF-IL6 for cytokine and iron- mediated regulation of murine inducible nitric oxide synthase expression
    • M. Dlaska, and G. Weiss Central role of transcription factor NF-IL6 for cytokine and iron-mediated regulation of murine inducible nitric oxide synthase expression J. Immunol. 162 1999 6171 6177 (Pubitemid 29314979)
    • (1999) Journal of Immunology , vol.162 , Issue.10 , pp. 6171-6177
    • Dlaska, M.1    Weiss, G.2
  • 28
    • 0030911247 scopus 로고    scopus 로고
    • Functional requirement of the hypoxia-responsive element in the activation of the inducible nitric oxide synthase promoter by the iron chelator desferrioxamine
    • DOI 10.1074/jbc.272.18.12236
    • G. Melillo, L.S. Taylor, A. Brooks, T. Musso, G.W. Cox, and L. Varesio Functional requirement of the hypoxia-responsive element in the activation of the inducible nitric oxide synthase promoter by the iron chelator desferrioxamine J. Biol. Chem. 272 1997 12236 12243 (Pubitemid 27202810)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.18 , pp. 12236-12243
    • Melillo, G.1    Taylor, L.S.2    Brooks, A.3    Musso, T.4    Cox, G.W.5    Varesio, L.6
  • 30
    • 58149345129 scopus 로고    scopus 로고
    • Nramp1-functionality increases iNOS expression via repression of IL-10 formation
    • G. Fritsche, M. Nairz, E.R. Werner, H.C. Barton, and G. Weiss Nramp1-functionality increases iNOS expression via repression of IL-10 formation Eur. J. Immunol. 38 2008 3060 3067
    • (2008) Eur. J. Immunol. , vol.38 , pp. 3060-3067
    • Fritsche, G.1    Nairz, M.2    Werner, E.R.3    Barton, H.C.4    Weiss, G.5
  • 32
    • 78649753411 scopus 로고    scopus 로고
    • Detection, evaluation, and management of iron-restricted erythropoiesis
    • L.T. Goodnough, E. Nemeth, and T. Ganz Detection, evaluation, and management of iron-restricted erythropoiesis Blood 116 2010 4754 4761
    • (2010) Blood , vol.116 , pp. 4754-4761
    • Goodnough, L.T.1    Nemeth, E.2    Ganz, T.3
  • 33
    • 84863807852 scopus 로고    scopus 로고
    • Iron deficiency syndromes and iron-restricted erythropoiesis (CME)
    • L.T. Goodnough Iron deficiency syndromes and iron-restricted erythropoiesis (CME) Transfusion 52 2012 1584 1592
    • (2012) Transfusion , vol.52 , pp. 1584-1592
    • Goodnough, L.T.1
  • 34
  • 36
    • 0036167978 scopus 로고    scopus 로고
    • Superoxide dismutase and glutathione peroxidase in erythrocytes of patients with iron deficiency anemia: Effects of different treatment modalities
    • M. Isler, N. Delibas, M. Guclu, F. Gultekin, R. Sutcu, M. Bahceci, and A. Kosar Superoxide dismutase and glutathione peroxidase in erythrocytes of patients with iron deficiency anemia: effects of different treatment modalities Croat. Med. J. 43 2002 16 19 (Pubitemid 34157859)
    • (2002) Croatian Medical Journal , vol.43 , Issue.1 , pp. 16-19
    • Isler, M.1    Delibas, N.2    Guclu, M.3    Gultekin, F.4    Sutcu, R.5    Bahceci, M.6    Kosar, A.7
  • 37
    • 1642561883 scopus 로고    scopus 로고
    • Effect of iron supplementation on oxidative stress and antioxidant status in iron-deficiency anemia
    • DOI 10.1385/BTER:96:1-3:117
    • E. Kurtoglu, A. Ugur, A.K. Baltaci, and L. Undar Effect of iron supplementation on oxidative stress and antioxidant status in iron-deficiency anemia Biol. Trace Elem. Res. 96 2003 117 123 (Pubitemid 38130498)
    • (2003) Biological Trace Element Research , vol.96 , Issue.1-3 , pp. 117-123
    • Kurtoglu, E.1    Ugur, A.2    Baltaci, A.K.3    Undar, L.4
  • 38
    • 0036934708 scopus 로고    scopus 로고
    • Iron deficiency anemia increases nitric oxide production in healthy adolescents
    • DOI 10.1007/s00277-001-0409-4
    • J.W. Choi, S.H. Pai, S.K. Kim, M. Ito, C.S. Park, and Y.N. Cha Iron deficiency anemia increases nitric oxide production in healthy adolescents Ann. Hematol. 81 2002 1 6 (Pubitemid 36075487)
    • (2002) Annals of Hematology , vol.81 , Issue.1 , pp. 1-6
    • Choi, J.W.1    Pai, S.H.2    Kim, S.K.3    Ito, M.4    Park, C.S.5    Cha, Y.N.6
  • 39
    • 25144483332 scopus 로고    scopus 로고
    • Dietary iron deficiency induces ventricular dilation, mitochondrial ultrastructural aberrations and cytochrome c release: Involvement of nitric oxide synthase and protein tyrosine nitration
    • DOI 10.1042/CS20040278
    • F. Dong, X. Zhang, B. Culver, H.G. Chew Jr, R.O. Kelley, and J. Ren Dietary iron deficiency induces ventricular dilation, mitochondrial ultrastructural aberrations and cytochrome c release: involvement of nitric oxide synthase and protein tyrosine nitration Clin. Sci. (London) 109 2005 277 286 (Pubitemid 41337132)
    • (2005) Clinical Science , vol.109 , Issue.3 , pp. 277-286
    • Dong, F.1    Zhang, X.2    Culver, B.3    Chew Jr., H.G.4    Kelley, R.O.5    Ren, J.6
  • 40
    • 0030839372 scopus 로고    scopus 로고
    • Up-regulation of renal and vascular nitric oxide synthase in iron- deficiency anemia
    • Z. Ni, S. Morcos, and N.D. Vaziri Up-regulation of renal and vascular nitric oxide synthase in iron-deficiency anemia Kidney Int. 52 1997 195 201 (Pubitemid 27321830)
    • (1997) Kidney International , vol.52 , Issue.1 , pp. 195-201
    • Ni, Z.1    Morcos, S.2    Vaziri, N.D.3
  • 41
    • 14644389345 scopus 로고    scopus 로고
    • Iron deficiency: A concise review
    • DOI 10.1002/ajh.20249
    • J. Umbreit Iron deficiency: a concise review Am. J. Hematol. 78 2005 225 231 (Pubitemid 40316503)
    • (2005) American Journal of Hematology , vol.78 , Issue.3 , pp. 225-231
    • Umbreit, J.1
  • 42
    • 57249114491 scopus 로고    scopus 로고
    • Intravenous iron therapy: A summary of treatment options and review of guidelines
    • S. Silverstein, J. Gilreath, and G. Rodgers Intravenous iron therapy: a summary of treatment options and review of guidelines J. Pharm. Pract. 21 2008 431 443
    • (2008) J. Pharm. Pract. , vol.21 , pp. 431-443
    • Silverstein, S.1    Gilreath, J.2    Rodgers, G.3
  • 44
    • 20744437023 scopus 로고    scopus 로고
    • Chronic iron overload enhances inducible nitric oxide synthase expression in rat liver
    • DOI 10.1016/j.niox.2005.04.009, PII S1089860305000467
    • P. Cornejo, P. Varela, L.A. Videla, and V. Fernandez Chronic iron overload enhances inducible nitric oxide synthase expression in rat liver Nitric Oxide 13 2005 54 61 (Pubitemid 40853969)
    • (2005) Nitric Oxide - Biology and Chemistry , vol.13 , Issue.1 , pp. 54-61
    • Cornejo, P.1    Varela, P.2    Videla, L.A.3    Fernandez, V.4
  • 45
    • 27644588712 scopus 로고    scopus 로고
    • Effects of ferrous sulphate and non-ionic iron-polymaltose complex on markers of oxidative tissue damage in patients with inflammatory bowel disease
    • DOI 10.1111/j.1365-2036.2005.02652.x
    • K. Erichsen, R.J. Ulvik, T. Grimstad, A. Berstad, R.K. Berge, and T. Hausken Effects of ferrous sulphate and non-ionic iron-polymaltose complex on markers of oxidative tissue damage in patients with inflammatory bowel disease Aliment. Pharmacol. Ther. 22 2005 831 838 (Pubitemid 41564363)
    • (2005) Alimentary Pharmacology and Therapeutics , vol.22 , Issue.9 , pp. 831-838
    • Erichsen, K.1    Ulvik, R.J.2    Grimstad, T.3    Berstad, A.4    Berge, R.K.5    Hausken, T.6
  • 46
    • 0036270885 scopus 로고    scopus 로고
    • Dietary iron supplementation enhances DSS-induced colitis and associated colorectal carcinoma development in mice
    • DOI 10.1023/A:1015362228659
    • D.N. Seril, J. Liao, K.L. Ho, A. Warsi, C.S. Yang, and G.Y. Yang Dietary iron supplementation enhances DSS-induced colitis and associated colorectal carcinoma development in mice Dig. Dis. Sci. 47 2002 1266 1278 (Pubitemid 34606629)
    • (2002) Digestive Diseases and Sciences , vol.47 , Issue.6 , pp. 1266-1278
    • Seril, D.N.1    Liao, J.2    Ho, K.-L.K.3    Warsi, A.4    Yang, C.S.5    Yang, G.-Y.6
  • 47
    • 46349099835 scopus 로고    scopus 로고
    • Comparative study of gastrointestinal tract and liver toxicity of ferrous sulfate, iron amino chelate and iron polymaltose complex in normal rats
    • J.E. Toblli, G. Cao, L. Olivieri, and M. Angerosa Comparative study of gastrointestinal tract and liver toxicity of ferrous sulfate, iron amino chelate and iron polymaltose complex in normal rats Pharmacology 82 2008 127 137
    • (2008) Pharmacology , vol.82 , pp. 127-137
    • Toblli, J.E.1    Cao, G.2    Olivieri, L.3    Angerosa, M.4
  • 48
    • 84885433420 scopus 로고    scopus 로고
    • Effects of iron polymaltose complex, ferrous fumarate and ferrous sulfate treatments in anemic pregnant rats, their fetuses and placentas
    • J.E. Toblli, G. Cao, L. Oliveri, and M. Angerosa Effects of iron polymaltose complex, ferrous fumarate and ferrous sulfate treatments in anemic pregnant rats, their fetuses and placentas Inflamm. Allergy Drug Targets 12 2013 190 198
    • (2013) Inflamm. Allergy Drug Targets , vol.12 , pp. 190-198
    • Toblli, J.E.1    Cao, G.2    Oliveri, L.3    Angerosa, M.4
  • 49
    • 0033181106 scopus 로고    scopus 로고
    • Oral supplementation with ferrous sulfate but not with nonionic iron polymaltose complex increases the susceptibility of plasma lipoproteins to oxidation
    • DOI 10.1016/S0271-5317(99)00073-1, PII S0271531799000731
    • T.-P. Tuomainen, K. Nyyssönen, E. Porkkala-Sarataho, R. Salonen, J. Baumgartner, P. Geisser, and J.T. Salonen Oral supplementation with ferrous sulfate but not with non-ionic iron polymaltose complex increases the susceptibility of plasma lipoproteins to oxidation Nutr. Res. 19 1999 1121 1132 (Pubitemid 29297738)
    • (1999) Nutrition Research , vol.19 , Issue.8 , pp. 1121-1132
    • Tuomainen, T.-P.1    Nyyssonen, K.2    Porkkala-Sarataho, E.3    Salonen, R.4    Baumgartner, J.A.5    Geisser, P.6    Salonen, J.T.7
  • 50
    • 2442677622 scopus 로고    scopus 로고
    • Oxidative stress and renal injury with intravenous iron-in patients with chronic kidney disease
    • DOI 10.1111/j.1523-1755.2004.00648.x
    • R. Agarwal, N. Vasavada, N.G. Sachs, and S. Chase Oxidative stress and renal injury with intravenous iron in patients with chronic kidney disease Kidney Int. 65 2004 2279 2289 (Pubitemid 38670014)
    • (2004) Kidney International , vol.65 , Issue.6 , pp. 2279-2289
    • Agarwal, R.1    Vasavada, N.2    Sachs, N.G.3    Chase, S.4
  • 51
    • 84868139585 scopus 로고    scopus 로고
    • Effect of intravenous vitamin C on cytokine activation and oxidative stress in end-stage renal disease patients receiving intravenous iron sucrose
    • T.A. Conner, C. McQuade, J. Olp, and A.B. Pai Effect of intravenous vitamin C on cytokine activation and oxidative stress in end-stage renal disease patients receiving intravenous iron sucrose Biometals 25 2012 961 969
    • (2012) Biometals , vol.25 , pp. 961-969
    • Conner, T.A.1    McQuade, C.2    Olp, J.3    Pai, A.B.4
  • 52
    • 0035961229 scopus 로고    scopus 로고
    • Iron-induced changes in nitric oxide and superoxide radical generation in rat liver after lindane or thyroid hormone treatment
    • DOI 10.1016/S0378-4274(00)00295-2, PII S0378427400002952
    • P. Cornejo, G. Tapia, S. Puntarulo, M. Galleano, L.A. Videla, and V. Fernandez Iron-induced changes in nitric oxide and superoxide radical generation in rat liver after lindane or thyroid hormone treatment Toxicol. Lett. 119 2001 87 93 (Pubitemid 32304369)
    • (2001) Toxicology Letters , vol.119 , Issue.2 , pp. 87-93
    • Cornejo, P.1    Tapia, G.2    Puntarulo, S.3    Galleano, M.4    Videla, L.A.5    Fernandez, V.6
  • 53
    • 61649124758 scopus 로고    scopus 로고
    • Lipid peroxidation products formation with various intravenous iron preparations in chronic kidney disease
    • A. Ganguli, H.S. Kohli, M. Khullar, G.K. Lal, V. Jha, and V. Sakhuja Lipid peroxidation products formation with various intravenous iron preparations in chronic kidney disease Renal Failure 31 2009 106 110
    • (2009) Renal Failure , vol.31 , pp. 106-110
    • Ganguli, A.1    Kohli, H.S.2    Khullar, M.3    Lal, G.K.4    Jha, V.5    Sakhuja, V.6
  • 54
    • 0033281707 scopus 로고    scopus 로고
    • Enhanced oxidative stress in haemodialysis patients receiving intravenous iron therapy
    • P.S. Lim, Y.H. Wei, Y.L. Yu, and B. Kho Enhanced oxidative stress in haemodialysis patients receiving intravenous iron therapy Nephrol. Dial. Transplant. 14 1999 2680 2687 (Pubitemid 32208386)
    • (1999) Nephrology Dialysis Transplantation , vol.14 , Issue.11 , pp. 2680-2687
    • Lim, P.-S.1    Wei, Y.-H.2    Yu, Y.L.3    Kho, B.4
  • 55
    • 79955871927 scopus 로고    scopus 로고
    • Nitrative and oxidative modifications of enolase are associated with iron in iron-overload rats and in vitro
    • N. Lu, X. Li, J. Li, W. Xu, H. Li, and Z. Gao Nitrative and oxidative modifications of enolase are associated with iron in iron-overload rats and in vitro J. Biol. Inorg. Chem. 16 2011 481 490
    • (2011) J. Biol. Inorg. Chem. , vol.16 , pp. 481-490
    • Lu, N.1    Li, X.2    Li, J.3    Xu, W.4    Li, H.5    Gao, Z.6
  • 58
    • 79959801240 scopus 로고    scopus 로고
    • Acute oxidative stress following intravenous iron injection in patients on chronic hemodialysis: A comparison of iron-sucrose and iron-dextran
    • B.V. Stefánsson, B. Haraldsson, and U. Nilsson Acute oxidative stress following intravenous iron injection in patients on chronic hemodialysis: a comparison of iron-sucrose and iron-dextran Nephron Clin. Pract 118 2011 c249 c256
    • (2011) Nephron Clin. Pract , vol.118
    • Stefánsson, B.V.1    Haraldsson, B.2    Nilsson, U.3
  • 59
    • 66149166994 scopus 로고    scopus 로고
    • Differences between original intravenous iron sucrose and iron sucrose similar preparations
    • J.E. Toblli, G. Cao, L. Oliveri, and M. Angerosa Differences between original intravenous iron sucrose and iron sucrose similar preparations Drug Res. 59 2009 176 190
    • (2009) Drug Res. , vol.59 , pp. 176-190
    • Toblli, J.E.1    Cao, G.2    Oliveri, L.3    Angerosa, M.4
  • 61
    • 79952200956 scopus 로고    scopus 로고
    • Comparison of the renal, cardiovascular and hepatic toxicity data of original intravenous iron compounds
    • J.E. Toblli, G. Cao, L. Olivieri, and M. Angerosa Comparison of the renal, cardiovascular and hepatic toxicity data of original intravenous iron compounds Nephrol. Dial. Transplant. 25 2010 3631 3640
    • (2010) Nephrol. Dial. Transplant. , vol.25 , pp. 3631-3640
    • Toblli, J.E.1    Cao, G.2    Olivieri, L.3    Angerosa, M.4
  • 62
    • 79961113223 scopus 로고    scopus 로고
    • Assessment of the extent of oxidative stress induced by intravenous ferumoxytol, ferric carboxymaltose, iron sucrose and iron dextran in a nonclinical model
    • J.E. Toblli, G. Cao, L. Oliveri, and M. Angerosa Assessment of the extent of oxidative stress induced by intravenous ferumoxytol, ferric carboxymaltose, iron sucrose and iron dextran in a nonclinical model Drug Res. 61 2011 399 410
    • (2011) Drug Res. , vol.61 , pp. 399-410
    • Toblli, J.E.1    Cao, G.2    Oliveri, L.3    Angerosa, M.4
  • 63
    • 80055101805 scopus 로고    scopus 로고
    • Evaluation of toxicity and oxidative stress induced by intravenous iron isomaltoside 1000 in a nonclinical model
    • J.E. Toblli, G. Cao, L. Oliveri, and M. Angerosa Evaluation of toxicity and oxidative stress induced by intravenous iron isomaltoside 1000 in a nonclinical model Drug Res. 61 2011 553 565
    • (2011) Drug Res. , vol.61 , pp. 553-565
    • Toblli, J.E.1    Cao, G.2    Oliveri, L.3    Angerosa, M.4
  • 64
    • 84855837518 scopus 로고    scopus 로고
    • Comparison of oxidative stress and inflammation induced by different intravenous iron sucrose similar preparations in a rat model
    • J.E. Toblli, G. Cao, L. Oliveri, and M. Angerosa Comparison of oxidative stress and inflammation induced by different intravenous iron sucrose similar preparations in a rat model Inflamm. Allergy Drug Targets 11 2012 66 78
    • (2012) Inflamm. Allergy Drug Targets , vol.11 , pp. 66-78
    • Toblli, J.E.1    Cao, G.2    Oliveri, L.3    Angerosa, M.4
  • 65
    • 3042769328 scopus 로고    scopus 로고
    • Parenteral iron nephrotoxicity: Potential mechanisms and consequences
    • DOI 10.1111/j.1523-1755.2004.00716.x
    • R.A. Zager, A.C. Johnson, and S.Y. Hanson Parenteral iron nephrotoxicity: potential mechanisms and consequences Kidney Int. 66 2004 144 156 (Pubitemid 38870090)
    • (2004) Kidney International , vol.66 , Issue.1 , pp. 144-156
    • Zager, R.A.1    Johnson, A.C.M.2    Hanson, S.Y.3
  • 66
    • 0034535034 scopus 로고    scopus 로고
    • Association of renal injury with increased oxygen free radical activity and altered nitric oxide metabolism in chronic experimental hemosiderosis
    • X.J. Zhou, Z. Laszik, X.Q. Wang, F.G. Silva, and N.D. Vaziri Association of renal injury with increased oxygen free radical activity and altered nitric oxide metabolism in chronic experimental hemosiderosis Lab. Invest. 80 2000 1905 1914 (Pubitemid 32012758)
    • (2000) Laboratory Investigation , vol.80 , Issue.12 , pp. 1905-1914
    • Zhou, X.J.1    Laszik, Z.2    Wang, X.Q.3    Silva, F.G.4    Vaziri, N.D.5
  • 68
    • 0020491099 scopus 로고
    • Kinetics and mechanism of the reduction of ferricytochrome c by the superoxide anion
    • J. Butler, W.H. Koppenol, and E. Margoliash Kinetics and mechanism of the reduction of ferricytochrome c by the superoxide anion J. Biol. Chem. 257 1982 10747 10750
    • (1982) J. Biol. Chem. , vol.257 , pp. 10747-10750
    • Butler, J.1    Koppenol, W.H.2    Margoliash, E.3
  • 71
    • 0028876897 scopus 로고
    • Oxygen and xenobiotic reductase activities of cytochrome P450
    • A.R. Goeptar, H. Scheerens, and N.P. Vermeulen Oxygen and xenobiotic reductase activities of cytochrome P450 Crit. Rev. Toxicol. 25 1995 25 65
    • (1995) Crit. Rev. Toxicol. , vol.25 , pp. 25-65
    • Goeptar, A.R.1    Scheerens, H.2    Vermeulen, N.P.3
  • 72
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and ugly
    • J.S. Beckman, and W.H. Koppenol Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly Am. J. Physiol. 271 1996 C1424 C1437
    • (1996) Am. J. Physiol. , vol.271
    • Beckman, J.S.1    Koppenol, W.H.2
  • 73
    • 18244390487 scopus 로고    scopus 로고
    • Myeloperoxidase: Friend and foe
    • DOI 10.1189/jlb.1204697
    • S.J. Klebanoff Myeloperoxidase: friend and foe J. Leukocyte Biol. 77 2005 598 625 (Pubitemid 40628741)
    • (2005) Journal of Leukocyte Biology , vol.77 , Issue.5 , pp. 598-625
    • Klebanoff, S.J.1
  • 75
    • 0026740508 scopus 로고
    • Biologically relevant metal ion-dependent hydroxyl radical generation: An update
    • B. Halliwell, and J.M. Gutteridge Biologically relevant metal ion-dependent hydroxyl radical generation: an update FEBS Lett. 307 1992 108 112
    • (1992) FEBS Lett. , vol.307 , pp. 108-112
    • Halliwell, B.1    Gutteridge, J.M.2
  • 76
    • 77954142511 scopus 로고    scopus 로고
    • Electrode potentials of partially reduced oxygen species, from dioxygen to water
    • W.H. Koppenol, D.M. Stanbury, and P.L. Bounds Electrode potentials of partially reduced oxygen species, from dioxygen to water Free Radic. Biol. Med. 49 2010 317 322
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 317-322
    • Koppenol, W.H.1    Stanbury, D.M.2    Bounds, P.L.3
  • 77
    • 0033565994 scopus 로고    scopus 로고
    • Oxygen and nitrogen are pro-carcinogens. Damage to DNA by reactive oxygen, chlorine and nitrogen species: Measurement, mechanism and the effects of nutrition
    • DOI 10.1016/S1383-5742(99)00009-5, PII S1383574299000095
    • B. Halliwell Oxygen and nitrogen are pro-carcinogens. Damage to DNA by reactive oxygen, chlorine and nitrogen species: measurement, mechanism and the effects of nutrition Mutat. Res. 443 1999 37 52 (Pubitemid 29327265)
    • (1999) Mutation Research - Genetic Toxicology and Environmental Mutagenesis , vol.443 , Issue.1-2 , pp. 37-52
    • Halliwell, B.1
  • 78
    • 33846389920 scopus 로고    scopus 로고
    • Nitric-oxide synthase: A cytochrome P450 family foster child
    • DOI 10.1016/j.bbagen.2006.08.019, PII S0304416506002376
    • A.C. Gorren, and B. Mayer Nitric-oxide synthase: a cytochrome P450 family foster child Biochim. Biophys. Acta 1770 2007 432 445 (Pubitemid 46136746)
    • (2007) Biochimica et Biophysica Acta - General Subjects , vol.1770 , Issue.3 , pp. 432-445
    • Gorren, A.C.F.1    Mayer, B.2
  • 79
    • 0027104253 scopus 로고
    • Biochemistry of nitric oxide and its redox-activated forms
    • J.S. Stamler, D.J. Singel, and J. Loscalzo Biochemistry of nitric oxide and its redox-activated forms Science 258 1992 1898 1902 (Pubitemid 23026727)
    • (1992) Science , vol.258 , Issue.5090 , pp. 1898-1902
    • Stamler, J.S.1    Singel, D.J.2    Loscalzo, J.3
  • 81
    • 0026551016 scopus 로고
    • Haem-dependent activation of cytosolic guanylate cyclase by nitric oxide: A widespread signal transduction mechanism
    • L.J. Ignarro Haem-dependent activation of cytosolic guanylate cyclase by nitric oxide: a widespread signal transduction mechanism Biochem. Soc. Trans. 20 1992 465 469
    • (1992) Biochem. Soc. Trans. , vol.20 , pp. 465-469
    • Ignarro, L.J.1
  • 82
    • 84861321238 scopus 로고    scopus 로고
    • Connecting the chemical and biological properties of nitric oxide
    • J.C. Toledo Jr, and O. Augusto Connecting the chemical and biological properties of nitric oxide Chem. Res. Toxicol. 25 2012 975 989
    • (2012) Chem. Res. Toxicol. , vol.25 , pp. 975-989
    • Toledo, Jr.J.C.1    Augusto, O.2
  • 83
    • 0028092958 scopus 로고
    • Nitric oxide synthases: Roles, tolls, and controls
    • DOI 10.1016/0092-8674(94)90266-6
    • C. Nathan, and Q.W. Xie Nitric oxide synthases: roles, tolls, and controls Cell 78 1994 915 918 (Pubitemid 24292319)
    • (1994) Cell , vol.78 , Issue.6 , pp. 915-918
    • Nathan, C.1    Xie, Q.-W.2
  • 84
    • 0034769118 scopus 로고    scopus 로고
    • Nitric oxide and the immune response
    • DOI 10.1038/ni1001-907
    • C. Bogdan Nitric oxide and the immune response Nat. Immunol. 2 2001 907 916 (Pubitemid 32976162)
    • (2001) Nature Immunology , vol.2 , Issue.10 , pp. 907-916
    • Bogdan, C.1
  • 85
    • 30444439216 scopus 로고    scopus 로고
    • The discovery of nitric oxide and its role in vascular biology
    • DOI 10.1038/sj.bjp.0706458, PII 0706458
    • S. Moncada, and E.A. Higgs The discovery of nitric oxide and its role in vascular biology Br. J. Pharmacol. 147 Suppl. 1 2006 S193 S201 (Pubitemid 43077277)
    • (2006) British Journal of Pharmacology , vol.147 , Issue.SUPPL. 1
    • Moncada, S.1    Higgs, E.A.2
  • 86
    • 0025117611 scopus 로고
    • EPR demonstration of iron-nitrosyl complex formation by cytotoxic activated macrophages
    • J.R. Lancaster Jr, and J.B. Hibbs Jr. EPR demonstration of iron-nitrosyl complex formation by cytotoxic activated macrophages Proc. Natl. Acad. Sci. USA 87 1990 1223 1227
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1223-1227
    • Lancaster, Jr.J.R.1    Hibbs, Jr.J.B.2
  • 88
    • 84870524092 scopus 로고    scopus 로고
    • A comparison of the chemistry associated with the biological signaling and actions of nitroxyl (HNO) and nitric oxide (NO)
    • J.M. Fukuto, C.J. Cisneros, and R.L. Kinkade A comparison of the chemistry associated with the biological signaling and actions of nitroxyl (HNO) and nitric oxide (NO) J. Inorg. Biochem. 118 2013 201 208
    • (2013) J. Inorg. Biochem. , vol.118 , pp. 201-208
    • Fukuto, J.M.1    Cisneros, C.J.2    Kinkade, R.L.3
  • 89
    • 0037245344 scopus 로고    scopus 로고
    • Comparison of the reactivity of nitric oxide and nitroxyl with heme proteins: A chemical discussion of the differential biological effects of these redox related products of NOS
    • DOI 10.1016/S0162-0134(02)00498-1, PII S0162013402004981
    • K.M. Miranda, R.W. Nims, D.D. Thomas, M.G. Espey, D. Citrin, M.D. Bartberger, N. Paolocci, J.M. Fukuto, M. Feelisch, and D.A. Wink Comparison of the reactivity of nitric oxide and nitroxyl with heme proteins: a chemical discussion of the differential biological effects of these redox related products of NOS J. Inorg. Biochem. 93 2003 52 60 (Pubitemid 36132133)
    • (2003) Journal of Inorganic Biochemistry , vol.93 , Issue.1-2 , pp. 52-60
    • Miranda, K.M.1    Nims, R.W.2    Thomas, D.D.3    Espey, M.G.4    Citrin, D.5    Bartberger, M.D.6    Paolocci, N.7    Fukuto, J.M.8    Feelisch, M.9    Wink, D.A.10
  • 90
    • 0037172177 scopus 로고    scopus 로고
    • The rate constant of the reaction of superoxide with nitrogen monoxide: Approaching the diffusion limit
    • DOI 10.1021/jp025518z
    • T. Nauser, and W.H. Koppenol The rate constant of the reaction of superoxide with nitrogen monoxide: approaching the diffusion limit J. Phys. Chem. A 106 2002 4084 4086 (Pubitemid 35290100)
    • (2002) Journal of Physical Chemistry A , vol.106 , Issue.16 , pp. 4084-4086
    • Nauser, T.1    Koppenol, W.H.2
  • 91
    • 0027194540 scopus 로고
    • A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds
    • DOI 10.1038/364626a0
    • S.A. Lipton, Y.B. Choi, Z.H. Pan, S.Z. Lei, H.S. Chen, N.J. Sucher, J. Loscalzo, D.J. Singel, and J.S. Stamler A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds Nature 364 1993 626 632 (Pubitemid 23274719)
    • (1993) Nature , vol.364 , Issue.6438 , pp. 626-632
    • Lipton, S.A.1    Choi, Y.-B.2    Pan, Z.-H.3    Lei, S.Z.4    Chen, H.-S.V.5    Sucher, N.J.6    Loscalzo, J.7    Singel, D.J.8    Stamler, J.S.9
  • 92
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • DOI 10.1152/physrev.00029.2006
    • P. Pacher, J.S. Beckman, and L. Liaudet Nitric oxide and peroxynitrite in health and disease Physiol. Rev. 87 2007 315 424 (Pubitemid 46217686)
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 93
    • 0015982070 scopus 로고
    • Mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance: Evidence that only half the active sites function in catalysis
    • E.M. Fielden, P.B. Roberts, R.C. Bray, D.J. Lowe, G.N. Mautner, G. Rotilio, and L. Calabrese Mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance: evidence that only half the active sites function in catalysis Biochem. J. 139 1974 49 60
    • (1974) Biochem. J. , vol.139 , pp. 49-60
    • Fielden, E.M.1    Roberts, P.B.2    Bray, R.C.3    Lowe, D.J.4    Mautner, G.N.5    Rotilio, G.6    Calabrese, L.7
  • 94
    • 84868089379 scopus 로고    scopus 로고
    • Peroxynitrous acid: Controversy and consensus surrounding an enigmatic oxidant
    • W.H. Koppenol, P.L. Bounds, T. Nauser, R. Kissner, and H. Rüegger Peroxynitrous acid: controversy and consensus surrounding an enigmatic oxidant Dalton Trans. 41 2012 13779 13787
    • (2012) Dalton Trans. , vol.41 , pp. 13779-13787
    • Koppenol, W.H.1    Bounds, P.L.2    Nauser, T.3    Kissner, R.4    Rüegger, H.5
  • 95
    • 11944262823 scopus 로고
    • Rapid reaction between peroxonitrite and carbon dioxide: Implications for biological activity
    • S.V. Lymar, and J.K. Hurst Rapid reaction between peroxonitrite and carbon dioxide: implications for biological activity J. Am. Chem. Soc. 117 1995 8867 8868
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 8867-8868
    • Lymar, S.V.1    Hurst, J.K.2
  • 96
    • 34250358561 scopus 로고    scopus 로고
    • Mechanisms of oxidation of guanine in DNA by carbonate radical anion, a decomposition product of nitrosoperoxycarbonate
    • DOI 10.1002/chem.200601434
    • Y.A. Lee, B.H. Yun, S.K. Kim, Y. Margolin, P.C. Dedon, N.E. Geacintov, and V. Shafirovich Mechanisms of oxidation of guanine in DNA by carbonate radical anion, a decomposition product of nitrosoperoxycarbonate Chemistry 13 2007 4571 4581 (Pubitemid 46925564)
    • (2007) Chemistry - A European Journal , vol.13 , Issue.16 , pp. 4571-4581
    • Lee, Y.A.1    Yun, B.H.2    Kim, S.K.3    Margolin, Y.4    Dedon, P.C.5    Geacintov, N.E.6    Shafirovich, V.7
  • 97
    • 0030250041 scopus 로고    scopus 로고
    • Carbon dioxide enhancement of peroxynitrite-mediated protein tyrosine nitration
    • DOI 10.1006/abbi.1996.0362
    • A. Gow, D. Duran, S.R. Thom, and H. Ischiropoulos Carbon dioxide enhancement of peroxynitrite-mediated protein tyrosine nitration Arch. Biochem. Biophys. 333 1996 42 48 (Pubitemid 26276972)
    • (1996) Archives of Biochemistry and Biophysics , vol.333 , Issue.1 , pp. 42-48
    • Andrew, G.1    Duran, D.2    Thom, S.R.3    Ischiropoulos, H.4
  • 100
    • 0032411442 scopus 로고    scopus 로고
    • Kinetic study of the reaction of glutathione peroxidase with peroxynitrite
    • DOI 10.1021/tx980086y
    • K. Briviba, R. Kissner, W.H. Koppenol, and H. Sies Kinetic study of the reaction of glutathione peroxidase with peroxynitrite Chem. Res. Toxicol. 11 1998 1398 1401 (Pubitemid 29013611)
    • (1998) Chemical Research in Toxicology , vol.11 , Issue.12 , pp. 1398-1401
    • Briviba, K.1    Kissner, R.2    Koppenol, W.H.3    Sies, H.4
  • 101
  • 102
    • 84862831362 scopus 로고    scopus 로고
    • Cellular and mitochondrial iron homeostasis in vertebrates
    • C. Chen, and B.H. Paw Cellular and mitochondrial iron homeostasis in vertebrates Biochim. Biophys. Acta 1823 2012 1459 1467
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 1459-1467
    • Chen, C.1    Paw, B.H.2
  • 103
    • 84861355868 scopus 로고    scopus 로고
    • Hepcidin and iron homeostasis
    • T. Ganz, and E. Nemeth Hepcidin and iron homeostasis Biochim. Biophys. Acta 1823 2012 1434 1443
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 1434-1443
    • Ganz, T.1    Nemeth, E.2
  • 104
    • 77954249308 scopus 로고    scopus 로고
    • Two to tango: Regulation of mammalian iron metabolism
    • M.W. Hentze, M.U. Muckenthaler, B. Galy, and C. Camaschella Two to tango: regulation of mammalian iron metabolism Cell 142 2010 24 38
    • (2010) Cell , vol.142 , pp. 24-38
    • Hentze, M.W.1    Muckenthaler, M.U.2    Galy, B.3    Camaschella, C.4
  • 107
    • 24744438847 scopus 로고    scopus 로고
    • The macrophage: A cellular factory at the interphase between iron and immunity for the control of infections
    • DOI 10.1007/s10534-005-3710-1
    • I. Theurl, G. Fritsche, S. Ludwiczek, K. Garimorth, R. Bellmann-Weiler, and G. Weiss The macrophage: a cellular factory at the interphase between iron and immunity for the control of infections Biometals 18 2005 359 367 (Pubitemid 41298020)
    • (2005) BioMetals , vol.18 , Issue.4 , pp. 359-367
    • Theurl, I.1    Fritsche, G.2    Ludwiczek, S.3    Garimorth, K.4    Bellmann-Weiler, R.5    Weiss, G.6
  • 113
    • 0034733635 scopus 로고    scopus 로고
    • A novel mammalian iron-regulated protein involved in intracellular iron metabolism
    • DOI 10.1074/jbc.M000713200
    • S. Abboud, and D.J. Haile A novel mammalian iron-regulated protein involved in intracellular iron metabolism J. Biol. Chem. 275 2000 19906 19912 (Pubitemid 30441595)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.26 , pp. 19906-19912
    • Abboud, S.1    Haile, D.J.2
  • 115
    • 0032909207 scopus 로고    scopus 로고
    • Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse
    • DOI 10.1038/5979
    • C.D. Vulpe, Y.M. Kuo, T.L. Murphy, L. Cowley, C. Askwith, N. Libina, J. Gitschier, and G.J. Anderson Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse Nat. Genet. 21 1999 195 199 (Pubitemid 29070366)
    • (1999) Nature Genetics , vol.21 , Issue.2 , pp. 195-199
    • Vulpe, C.D.1    Kuo, Y.-M.2    Murphy, T.L.3    Cowley, L.4    Askwith, C.5    Libina, N.6    Gitschier, J.7    Anderson, G.I.8
  • 116
    • 34547652466 scopus 로고    scopus 로고
    • Nutritional iron deficiency
    • DOI 10.1016/S0140-6736(07)61235-5, PII S0140673607612355
    • M.B. Zimmermann, and R.F. Hurrell Nutritional iron deficiency Lancet 370 2007 511 520 (Pubitemid 47214636)
    • (2007) Lancet , vol.370 , Issue.9586 , pp. 511-520
    • Zimmermann, M.B.1    Hurrell, R.F.2
  • 117
    • 28444488323 scopus 로고    scopus 로고
    • Presence of the iron exporter ferroportin at the plasma membrane of macrophages is enhanced by iron loading and down-regulated by hepcidin
    • DOI 10.1182/blood-2005-06-2398
    • C. Delaby, N. Pilard, A.S. Goncalves, C. Beaumont, and F. Canonne-Hergaux Presence of the iron exporter ferroportin at the plasma membrane of macrophages is enhanced by iron loading and down-regulated by hepcidin Blood 106 2005 3979 3984 (Pubitemid 41739041)
    • (2005) Blood , vol.106 , Issue.12 , pp. 3979-3984
    • Delaby, C.1    Pilard, N.2    Goncalves, A.S.3    Beaumont, C.4    Canonne-Hergaux, F.5
  • 118
    • 84864471423 scopus 로고    scopus 로고
    • Subcellular localization of iron and heme metabolism related proteins at early stages of erythrophagocytosis
    • C. Delaby, C. Rondeau, C. Pouzet, A. Willemetz, N. Pilard, M. Desjardins, and F. Canonne-Hergaux Subcellular localization of iron and heme metabolism related proteins at early stages of erythrophagocytosis PLoS One 7 2012 e42199
    • (2012) PLoS One , vol.7 , pp. 42199
    • Delaby, C.1    Rondeau, C.2    Pouzet, C.3    Willemetz, A.4    Pilard, N.5    Desjardins, M.6    Canonne-Hergaux, F.7
  • 121
    • 54049156405 scopus 로고    scopus 로고
    • The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel
    • X.P. Dong, X. Cheng, E. Mills, M. Delling, F. Wang, T. Kurz, and H. Xu The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel Nature 455 2008 992 996
    • (2008) Nature , vol.455 , pp. 992-996
    • Dong, X.P.1    Cheng, X.2    Mills, E.3    Delling, M.4    Wang, F.5    Kurz, T.6    Xu, H.7
  • 123
    • 84857373097 scopus 로고    scopus 로고
    • Non-transferrin bound iron: A key role in iron overload and iron toxicity
    • P. Brissot, M. Ropert, L.C. Le, and O. Loreal Non-transferrin bound iron: a key role in iron overload and iron toxicity Biochim. Biophys. Acta 1820 2012 403 410
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 403-410
    • Brissot, P.1    Ropert, M.2    Le, L.C.3    Loreal, O.4
  • 125
    • 0141705304 scopus 로고    scopus 로고
    • Labile plasma iron in iron overload: Redox activity and susceptibility to chelation
    • DOI 10.1182/blood-2003-03-0807
    • B.P. Esposito, W. Breuer, P. Sirankapracha, P. Pootrakul, C. Hershko, and Z.I. Cabantchik Labile plasma iron in iron overload: redox activity and susceptibility to chelation Blood 102 2003 2670 2677 (Pubitemid 37193611)
    • (2003) Blood , vol.102 , Issue.7 , pp. 2670-2677
    • Esposito, B.P.1    Breuer, W.2    Sirankapracha, P.3    Pootrakul, P.4    Hershko, C.5    Cabantchik, Z.I.6
  • 126
    • 83555173402 scopus 로고    scopus 로고
    • Glutathione: A key component of the cytoplasmic labile iron pool
    • R.C. Hider, and X.L. Kong Glutathione: a key component of the cytoplasmic labile iron pool Biometals 24 2011 1179 1187
    • (2011) Biometals , vol.24 , pp. 1179-1187
    • Hider, R.C.1    Kong, X.L.2
  • 127
    • 67349100157 scopus 로고    scopus 로고
    • Ferritins: A family of molecules for iron storage, antioxidation and more
    • P. Arosio, R. Ingrassia, and P. Cavadini Ferritins: a family of molecules for iron storage, antioxidation and more Biochim. Biophys. Acta 1790 2009 589 599
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 589-599
    • Arosio, P.1    Ingrassia, R.2    Cavadini, P.3
  • 128
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • DOI 10.1016/0005-2728(96)00022-9
    • P.M. Harrison, and P. Arosio The ferritins: molecular properties, iron storage function and cellular regulation Biochim. Biophys. Acta 1275 1996 161 203 (Pubitemid 26248989)
    • (1996) Biochimica et Biophysica Acta - Bioenergetics , vol.1275 , Issue.3 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 129
    • 0018095305 scopus 로고
    • The iron-loaded cell - The cytopathology of iron storage: A review
    • G.W. Richter The iron-loaded cell - the cytopathology of iron storage: a review Am. J. Pathol. 91 1978 362 404
    • (1978) Am. J. Pathol. , vol.91 , pp. 362-404
    • Richter, G.W.1
  • 130
    • 84859956110 scopus 로고    scopus 로고
    • Coming into view: Eukaryotic iron chaperones and intracellular iron delivery
    • C.C. Philpott Coming into view: eukaryotic iron chaperones and intracellular iron delivery J. Biol. Chem. 287 2012 13518 13523
    • (2012) J. Biol. Chem. , vol.287 , pp. 13518-13523
    • Philpott, C.C.1
  • 131
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization
    • DOI 10.1126/science.1104742
    • E. Nemeth, M.S. Tuttle, J. Powelson, M.B. Vaughn, A. Donovan, D.M. Ward, T. Ganz, and J. Kaplan Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization Science 306 2004 2090 2093 (Pubitemid 40007660)
    • (2004) Science , vol.306 , Issue.5704 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3    Vaughn, M.D.4    Donovan, A.5    Ward, D.M.6    Ganz, T.7    Kaplan, J.8
  • 132
    • 0036727925 scopus 로고    scopus 로고
    • Hepcidin expression inversely correlates with the expression of duodenal iron transporters and iron absorption in rats
    • DOI 10.1053/gast.2002.35353
    • D.M. Frazer, S.J. Wilkins, E.M. Becker, C.D. Vulpe, A.T. McKie, D. Trinder, and G.J. Anderson Hepcidin expression inversely correlates with the expression of duodenal iron transporters and iron absorption in rats Gastroenterology 123 2002 835 844 (Pubitemid 34977090)
    • (2002) Gastroenterology , vol.123 , Issue.3 , pp. 835-844
    • Frazer, D.M.1    Wilkins, S.J.2    Becker, E.M.3    Vulpe, C.D.4    Mckie, A.T.5    Trinder, D.6    Anderson, G.J.7
  • 134
    • 79953223315 scopus 로고    scopus 로고
    • Intestinal DMT1 cotransporter is down-regulated by hepcidin via proteasome internalization and degradation
    • C. Brasse-Lagnel, Z. Karim, P. Letteron, S. Bekri, A. Bado, and C. Beaumont Intestinal DMT1 cotransporter is down-regulated by hepcidin via proteasome internalization and degradation Gastroenterology 140 2011 1261 1271
    • (2011) Gastroenterology , vol.140 , pp. 1261-1271
    • Brasse-Lagnel, C.1    Karim, Z.2    Letteron, P.3    Bekri, S.4    Bado, A.5    Beaumont, C.6
  • 136
    • 79959562083 scopus 로고    scopus 로고
    • Serum and liver iron differently regulate the bone morphogenetic protein 6 (BMP6)-SMAD signaling pathway in mice
    • E. Corradini, D. Meynard, Q. Wu, S. Chen, P. Ventura, A. Pietrangelo, and J.L. Babitt Serum and liver iron differently regulate the bone morphogenetic protein 6 (BMP6)-SMAD signaling pathway in mice Hepatology 54 2011 273 284
    • (2011) Hepatology , vol.54 , pp. 273-284
    • Corradini, E.1    Meynard, D.2    Wu, Q.3    Chen, S.4    Ventura, P.5    Pietrangelo, A.6    Babitt, J.L.7
  • 138
    • 23944502314 scopus 로고    scopus 로고
    • Time-course analysis of hepcidin, serum iron, and plasma cytokine levels in humans injected with LPS
    • DOI 10.1182/blood-2005-03-1159
    • E. Kemna, P. Pickkers, E. Nemeth, H. van der Hoeven, and D. Swinkels Time-course analysis of hepcidin, serum iron, and plasma cytokine levels in humans injected with LPS Blood 106 2005 1864 1866 (Pubitemid 41208606)
    • (2005) Blood , vol.106 , Issue.5 , pp. 1864-1866
    • Kemna, E.1    Pickkers, P.2    Nemeth, E.3    Van Der Hoeven, H.4    Swinkels, D.5
  • 139
    • 2342510407 scopus 로고    scopus 로고
    • IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin
    • DOI 10.1172/JCI200420945
    • E. Nemeth, S. Rivera, V. Gabayan, C. Keller, S. Taudorf, B.K. Pedersen, and T. Ganz IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin J. Clin. Invest. 113 2004 1271 1276 (Pubitemid 39069926)
    • (2004) Journal of Clinical Investigation , vol.113 , Issue.9 , pp. 1271-1276
    • Nemeth, E.1    Rivera, S.2    Gabayan, V.3    Keller, C.4    Taudorf, S.5    Pedersen, B.K.6    Ganz, T.7
  • 142
    • 2542560427 scopus 로고    scopus 로고
    • Hereditary hemochromatosis - A new look at an old disease
    • A. Pietrangelo Hereditary hemochromatosis - a new look at an old disease N. Engl. J. Med. 350 2004 2383 2397
    • (2004) N. Engl. J. Med. , vol.350 , pp. 2383-2397
    • Pietrangelo, A.1
  • 144
    • 38349111676 scopus 로고    scopus 로고
    • Role of the hypoxia inducible factors HIF in iron metabolism
    • C. Peyssonnaux, V. Nizet, and R.S. Johnson Role of the hypoxia inducible factors HIF in iron metabolism Cell Cycle 7 2008 28 32
    • (2008) Cell Cycle , vol.7 , pp. 28-32
    • Peyssonnaux, C.1    Nizet, V.2    Johnson, R.S.3
  • 145
    • 0037217941 scopus 로고    scopus 로고
    • Hypoxic up-regulation of erythroid 5-aminolevulinate synthase
    • DOI 10.1182/blood-2002-03-0773
    • T. Hofer, R.H. Wenger, M.F. Kramer, G.C. Ferreira, and M. Gassmann Hypoxic up-regulation of erythroid 5-aminolevulinate synthase Blood 101 2003 348 350 (Pubitemid 36025930)
    • (2003) Blood , vol.101 , Issue.1 , pp. 348-350
    • Hofer, T.1    Wenger, R.H.2    Kramer, M.F.3    Ferreira, G.C.4    Gassmann, M.5
  • 146
    • 33947581110 scopus 로고    scopus 로고
    • Hypoxia inducible factor prolyl 4-hydroxylase enzymes: Center stage in the battle against hypoxia, metabolic compromise and oxidative stress
    • DOI 10.1007/s11064-006-9268-7
    • A. Siddiq, L.R. Aminova, and R.R. Ratan Hypoxia inducible factor prolyl 4-hydroxylase enzymes: center stage in the battle against hypoxia, metabolic compromise and oxidative stress Neurochem. Res. 32 2007 931 946 (Pubitemid 46481318)
    • (2007) Neurochemical Research , vol.32 , Issue.4-5 , pp. 931-946
    • Siddiq, A.1    Aminova, L.R.2    Ratan, R.R.3
  • 147
    • 0035887011 scopus 로고    scopus 로고
    • FIH-1: A novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity
    • DOI 10.1101/gad.924501
    • P.C. Mahon, K. Hirota, and G.L. Semenza FIH-1: a novel protein that interacts with HIF-1a and VHL to mediate repression of HIF-1 transcriptional activity Genes Dev. 15 2001 2675 2686 (Pubitemid 32988878)
    • (2001) Genes and Development , vol.15 , Issue.20 , pp. 2675-2686
    • Mahon, P.C.1    Hirota, K.2    Semenza, G.L.3
  • 148
    • 40949132841 scopus 로고    scopus 로고
    • Turn me on: Regulating HIF transcriptional activity
    • DOI 10.1038/sj.cdd.4402315, PII 4402315, The biology of Hypoxia-inducible factors
    • K. Lisy, and D.J. Peet Turn me on: regulating HIF transcriptional activity Cell Death Differ. 15 2008 642 649 (Pubitemid 351405067)
    • (2008) Cell Death and Differentiation , vol.15 , Issue.4 , pp. 642-649
    • Lisy, K.1    Peet, D.J.2
  • 151
    • 33947095427 scopus 로고    scopus 로고
    • ROS mediate the hypoxic repression of the hepcidin gene by inhibiting C/EBPα and STAT-3
    • S.O. Choi, Y.S. Cho, H.L. Kim, and J.W. Park ROS mediate the hypoxic repression of the hepcidin gene by inhibiting C/EBPα and STAT-3 Biochem. Biophys. Res. Commun. 356 2007 312 317
    • (2007) Biochem. Biophys. Res. Commun. , vol.356 , pp. 312-317
    • Choi, S.O.1    Cho, Y.S.2    Kim, H.L.3    Park, J.W.4
  • 155
    • 84870566647 scopus 로고    scopus 로고
    • Hypoxia-inducible factor regulates hepcidin via erythropoietin-induced erythropoiesis
    • Q. Liu, O. Davidoff, K. Niss, and V.H. Haase Hypoxia-inducible factor regulates hepcidin via erythropoietin-induced erythropoiesis J. Clin. Invest. 122 2012 4635 4644
    • (2012) J. Clin. Invest. , vol.122 , pp. 4635-4644
    • Liu, Q.1    Davidoff, O.2    Niss, K.3    Haase, V.H.4
  • 156
    • 34250835937 scopus 로고    scopus 로고
    • Evolution of the iron-responsive element
    • DOI 10.1261/rna.464807
    • P. Piccinelli, and T. Samuelsson Evolution of the iron-responsive element RNA 13 2007 952 966 (Pubitemid 46984887)
    • (2007) RNA , vol.13 , Issue.7 , pp. 952-966
    • Piccinelli, P.1    Samuelsson, T.2
  • 157
    • 33746361251 scopus 로고    scopus 로고
    • The role of iron regulatory proteins in mammalian iron homeostasis and disease
    • DOI 10.1038/nchembio807, PII NCHEMBIO807
    • T.A. Rouault The role of iron regulatory proteins in mammalian iron homeostasis and disease Nat. Chem. Biol. 2 2006 406 414 (Pubitemid 44114917)
    • (2006) Nature Chemical Biology , vol.2 , Issue.8 , pp. 406-414
    • Rouault, T.A.1
  • 158
    • 37449009448 scopus 로고    scopus 로고
    • Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum
    • B. Galy, D. Ferring-Appel, S. Kaden, H.J. Gröne, and M.W. Hentze Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum Cell Metab. 7 2008 79 85
    • (2008) Cell Metab. , vol.7 , pp. 79-85
    • Galy, B.1    Ferring-Appel, D.2    Kaden, S.3    Gröne, H.J.4    Hentze, M.W.5
  • 159
    • 10844282789 scopus 로고    scopus 로고
    • Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo
    • DOI 10.1126/science.1103786
    • E.G. Meyron-Holtz, M.C. Ghosh, and T.A. Rouault Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo Science 306 2004 2087 2090 (Pubitemid 40007659)
    • (2004) Science , vol.306 , Issue.5704 , pp. 2087-2090
    • Meyron-Holtz, E.G.1    Ghosh, M.C.2    Rouault, T.A.3
  • 160
    • 0036970050 scopus 로고    scopus 로고
    • Interactions of iron with reactive intermediates of oxygen and nitrogen
    • DOI 10.1159/000065697
    • A.J. Nappi, and E. Vass Interactions of iron with reactive intermediates of oxygen and nitrogen Dev. Neurosci. 24 2002 134 142 (Pubitemid 36151443)
    • (2002) Developmental Neuroscience , vol.24 , Issue.2-3 , pp. 134-142
    • Nappi, A.J.1    Vass, E.2
  • 161
    • 50949102412 scopus 로고    scopus 로고
    • Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network
    • M.U. Muckenthaler, B. Galy, and M.W. Hentze Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network Annu. Rev. Nutr. 28 2008 197 213
    • (2008) Annu. Rev. Nutr. , vol.28 , pp. 197-213
    • Muckenthaler, M.U.1    Galy, B.2    Hentze, M.W.3
  • 164
    • 84859317731 scopus 로고    scopus 로고
    • PH-induced mechanistic changeover from hydroxyl radicals to iron(IV) in the Fenton reaction
    • H. Bataineh, O. Pestovsky, and A. Bakac pH-induced mechanistic changeover from hydroxyl radicals to iron(IV) in the Fenton reaction Chem. Sci. 3 2012 1594 1599
    • (2012) Chem. Sci. , vol.3 , pp. 1594-1599
    • Bataineh, H.1    Pestovsky, O.2    Bakac, A.3
  • 165
    • 84860331697 scopus 로고    scopus 로고
    • Free radicals and antioxidants: Updating a personal view
    • B. Halliwell Free radicals and antioxidants: updating a personal view Nutr. Rev. 70 2012 257 265
    • (2012) Nutr. Rev. , vol.70 , pp. 257-265
    • Halliwell, B.1
  • 166
    • 84970583204 scopus 로고
    • Outer-sphere electron transfer reactions of ascorbate anions
    • N. Williams, and J. Yandell Outer-sphere electron transfer reactions of ascorbate anions Aust. J. Chem. 35 1982 1133 1144
    • (1982) Aust. J. Chem. , vol.35 , pp. 1133-1144
    • Williams, N.1    Yandell, J.2
  • 167
    • 33750214783 scopus 로고    scopus 로고
    • Fenton chemistry and iron chelation under physiologically relevant conditions: Electrochemistry and kinetics
    • DOI 10.1021/tx060101w
    • M. Merkofer, R. Kissner, R.C. Hider, U.T. Brunk, and W.H. Koppenol Fenton chemistry and iron chelation under physiologically relevant conditions: electrochemistry and kinetics Chem. Res. Toxicol. 19 2006 1263 1269 (Pubitemid 44607312)
    • (2006) Chemical Research in Toxicology , vol.19 , Issue.10 , pp. 1263-1269
    • Merkofer, M.1    Kissner, R.2    Hider, R.C.3    Brunk, U.T.4    Koppenol, W.H.5
  • 170
    • 0034531651 scopus 로고    scopus 로고
    • Iron regulatory proteins in pathobiology
    • DOI 10.1042/0264-6021:3520241
    • G. Cairo, and A. Pietrangelo Iron regulatory proteins in pathobiology Biochem. J. 352 Pt 2 2000 241 250 (Pubitemid 32011418)
    • (2000) Biochemical Journal , vol.352 , Issue.2 , pp. 241-250
    • Cairo, G.1    Pietrangelo, A.2
  • 171
    • 33745205646 scopus 로고    scopus 로고
    • Intralysosomal iron chelation protects against oxidative stress-induced cellular damage
    • T. Kurz, B. Gustafsson, and U.T. Brunk Intralysosomal iron chelation protects against oxidative stress-induced cellular damage FEBS J. 273 2006 3106 3117
    • (2006) FEBS J. , vol.273 , pp. 3106-3117
    • Kurz, T.1    Gustafsson, B.2    Brunk, U.T.3
  • 172
    • 79955588367 scopus 로고    scopus 로고
    • Cell sensitivity to oxidative stress is influenced by ferritin autophagy
    • T. Kurz, B. Gustafsson, and U.T. Brunk Cell sensitivity to oxidative stress is influenced by ferritin autophagy Free Radic. Biol. Med. 50 2011 1647 1658
    • (2011) Free Radic. Biol. Med. , vol.50 , pp. 1647-1658
    • Kurz, T.1    Gustafsson, B.2    Brunk, U.T.3
  • 173
    • 34247157226 scopus 로고    scopus 로고
    • Does the calcein-AM method assay the total cellular 'labile iron pool' or only a fraction of it?
    • DOI 10.1042/BJ20061840
    • M. Tenopoulou, T. Kurz, P.T. Doulias, D. Galaris, and U.T. Brunk Does the calcein-AM method assay the total cellular 'labile iron pool' or only a fraction of it? Biochem. J. 403 2007 261 266 (Pubitemid 46596581)
    • (2007) Biochemical Journal , vol.403 , Issue.2 , pp. 261-266
    • Tenopoulou, M.1    Kurz, T.2    Doulias, P.-T.3    Galaris, D.4    Brunk, U.T.5
  • 174
    • 34249815482 scopus 로고    scopus 로고
    • Autophagy, ageing and apoptosis: The role of oxidative stress and lysosomal iron
    • DOI 10.1016/j.abb.2007.01.013, PII S000398610700029X, Highlight Issue: Pro- and antiapoptotic Signalling
    • T. Kurz, A. Terman, and U.T. Brunk Autophagy, ageing and apoptosis: the role of oxidative stress and lysosomal iron Arch. Biochem. Biophys. 462 2007 220 230 (Pubitemid 46856317)
    • (2007) Archives of Biochemistry and Biophysics , vol.462 , Issue.2 , pp. 220-230
    • Kurz, T.1    Terman, A.2    Brunk, U.T.3
  • 175
    • 0035057746 scopus 로고    scopus 로고
    • Novel cellular defenses against iron and oxidation: Ferritin and autophagocytosis preserve lysosomal stability in airway epithelium
    • DOI 10.1179/135100001101536049
    • H.L. Persson, K.J. Nilsson, and U.T. Brunk Novel cellular defenses against iron and oxidation: ferritin and autophagocytosis preserve lysosomal stability in airway epithelium Redox Rep. 6 2001 57 63 (Pubitemid 32331570)
    • (2001) Redox Report , vol.6 , Issue.1 , pp. 57-63
    • Persson, H.L.1    Nilsson, K.J.2    Brunk, U.T.3
  • 176
    • 77955914915 scopus 로고    scopus 로고
    • Monitoring the efficiency of iron chelation therapy: The potential of nontransferrin-bound iron
    • R.C. Hider, A.M. Silva, M. Podinovskaia, and Y. Ma Monitoring the efficiency of iron chelation therapy: the potential of nontransferrin-bound iron Ann. N. Y. Acad. Sci. 1202 2010 94 99
    • (2010) Ann. N. Y. Acad. Sci. , vol.1202 , pp. 94-99
    • Hider, R.C.1    Silva, A.M.2    Podinovskaia, M.3    Ma, Y.4
  • 177
    • 69449101913 scopus 로고    scopus 로고
    • Influence of non-enzymatic post-translation modifications on the ability of human serum albumin to bind iron: Implications for non-transferrin-bound iron speciation
    • A.M. Silva, and R.C. Hider Influence of non-enzymatic post-translation modifications on the ability of human serum albumin to bind iron: implications for non-transferrin-bound iron speciation Biochim. Biophys. Acta 1794 2009 1449 1458
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 1449-1458
    • Silva, A.M.1    Hider, R.C.2
  • 179
    • 0035874476 scopus 로고    scopus 로고
    • Subcellular distribution of chelatable iron: A laser scanning microscopic study in isolated hepatocytes and liver endothelial cells
    • DOI 10.1042/0264-6021:3560061
    • F. Petrat, H. de Groot, and U. Rauen Subcellular distribution of chelatable iron: a laser scanning microscopic study in isolated hepatocytes and liver endothelial cells Biochem. J. 356 2001 61 69 (Pubitemid 34275706)
    • (2001) Biochemical Journal , vol.356 , Issue.1 , pp. 61-69
    • Petrat, F.1    De Groot, H.2    Rauen, U.3
  • 180
    • 56149121299 scopus 로고    scopus 로고
    • Translocation of iron from lysosomes into mitochondria is a key event during oxidative stress-induced hepatocellular injury
    • A. Uchiyama, J.S. Kim, K. Kon, H. Jaeschke, K. Ikejima, S. Watanabe, and J.J. Lemasters Translocation of iron from lysosomes into mitochondria is a key event during oxidative stress-induced hepatocellular injury Hepatology 48 2008 1644 1654
    • (2008) Hepatology , vol.48 , pp. 1644-1654
    • Uchiyama, A.1    Kim, J.S.2    Kon, K.3    Jaeschke, H.4    Ikejima, K.5    Watanabe, S.6    Lemasters, J.J.7
  • 181
    • 57649243073 scopus 로고    scopus 로고
    • Mitochondrial ferritin limits oxidative damage regulating mitochondrial iron availability: Hypothesis for a protective role in Friedreich ataxia
    • A. Campanella, E. Rovelli, P. Santambrogio, A. Cozzi, F. Taroni, and S. Levi Mitochondrial ferritin limits oxidative damage regulating mitochondrial iron availability: hypothesis for a protective role in Friedreich ataxia Hum. Mol. Genet. 18 2009 1 11
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 1-11
    • Campanella, A.1    Rovelli, E.2    Santambrogio, P.3    Cozzi, A.4    Taroni, F.5    Levi, S.6
  • 183
    • 77953810574 scopus 로고    scopus 로고
    • Cytosolic and mitochondrial ferritins in the regulation of cellular iron homeostasis and oxidative damage
    • P. Arosio, and S. Levi Cytosolic and mitochondrial ferritins in the regulation of cellular iron homeostasis and oxidative damage Biochim. Biophys. Acta 1800 2010 783 792
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 783-792
    • Arosio, P.1    Levi, S.2
  • 184
    • 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. 276 2001 19738 19745
    • (2001) J. Biol. Chem. , vol.276 , pp. 19738-19745
    • Caltagirone, A.1    Weiss, G.2    Pantopoulos, K.3
  • 185
    • 0028799569 scopus 로고
    • Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake
    • E.A. Martins, R.L. Robalinho, and R. Meneghini Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake Arch. Biochem. Biophys. 316 1995 128 134
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 128-134
    • Martins, E.A.1    Robalinho, R.L.2    Meneghini, R.3
  • 187
    • 0035933846 scopus 로고    scopus 로고
    • IRP1 activation by extracellular oxidative stress in the perfused rat liver
    • S. Mueller, K. Pantopoulos, C.A. Hubner, W. Stremmel, and M.W. Hentze IRP1 activation by extracellular oxidative stress in the perfused rat liver J. Biol. Chem. 276 2001 23192 23196
    • (2001) J. Biol. Chem. , vol.276 , pp. 23192-23196
    • Mueller, S.1    Pantopoulos, K.2    Hubner, C.A.3    Stremmel, W.4    Hentze, M.W.5
  • 188
    • 79951577653 scopus 로고    scopus 로고
    • Redox control of iron regulatory protein 2 stability
    • A. Hausmann, J. Lee, and K. Pantopoulos Redox control of iron regulatory protein 2 stability FEBS Lett. 585 2011 687 692
    • (2011) FEBS Lett. , vol.585 , pp. 687-692
    • Hausmann, A.1    Lee, J.2    Pantopoulos, K.3
  • 189
    • 34547125378 scopus 로고    scopus 로고
    • Sustained hydrogen peroxide induces iron uptake by transferrin receptor-1 independent of the iron regulatory protein/iron-responsive element network
    • DOI 10.1074/jbc.M702463200
    • B. Andriopoulos, S. Hegedusch, J. Mangin, H.D. Riedel, U. Hebling, J. Wang, K. Pantopoulos, and S. Mueller Sustained hydrogen peroxide induces iron uptake by transferrin receptor-1 independent of the iron regulatory protein/iron-responsive element network J. Biol. Chem. 282 2007 20301 20308 (Pubitemid 47100037)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.28 , pp. 20301-20308
    • Andriopoulos, B.1    Hegedusch, S.2    Mangin, J.3    Riedel, H.-D.4    Hebling, U.5    Wang, J.6    Pantopoulos, K.7    Mueller, S.8
  • 190
    • 10644232372 scopus 로고    scopus 로고
    • Oxidation-induced ferritin turnover in microglial cells: Role of proteasome
    • DOI 10.1016/j.freeradbiomed.2004.10.025, PII S0891584904008482
    • J. Mehlhase, G. Sandig, K. Pantopoulos, and T. Grune Oxidation-induced ferritin turnover in microglial cells: role of proteasome Free Radic. Biol. Med. 38 2005 276 285 (Pubitemid 39656137)
    • (2005) Free Radical Biology and Medicine , vol.38 , Issue.2 , pp. 276-285
    • Mehlhase, J.1    Sandig, G.2    Pantopoulos, K.3    Grune, T.4
  • 191
    • 84860703232 scopus 로고    scopus 로고
    • Role of reactive oxygen species in the regulation of HIF-1 by prolyl hydroxylase 2 under mild hypoxia
    • H. Niecknig, S. Tug, B.D. Reyes, M. Kirsch, J. Fandrey, and U. Berchner-Pfannschmidt Role of reactive oxygen species in the regulation of HIF-1 by prolyl hydroxylase 2 under mild hypoxia Free Radic. Res. 46 2012 705 717
    • (2012) Free Radic. Res. , vol.46 , pp. 705-717
    • Niecknig, H.1    Tug, S.2    Reyes, B.D.3    Kirsch, M.4    Fandrey, J.5    Berchner-Pfannschmidt, U.6
  • 192
    • 0032807550 scopus 로고    scopus 로고
    • Nitrosative and oxidative modulation of iron regulatory proteins
    • C. Bouton Nitrosative and oxidative modulation of iron regulatory proteins Cell. Mol. Life Sci. 55 1999 1043 1053 (Pubitemid 29361071)
    • (1999) Cellular and Molecular Life Sciences , vol.55 , Issue.8-9 , pp. 1043-1053
    • Bouton, C.1
  • 193
    • 0037096190 scopus 로고    scopus 로고
    • The iron regulatory proteins: Targets and modulators of free radical reactions and oxidative damage
    • DOI 10.1016/S0891-5849(02)00825-0, PII S0891584902008250
    • G. Cairo, S. Recalcati, A. Pietrangelo, and G. Minotti The iron regulatory proteins: targets and modulators of free radical reactions and oxidative damage Free Radic. Biol. Med. 32 2002 1237 1243 (Pubitemid 34607627)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.12 , pp. 1237-1243
    • Cairo, G.1    Recalcati, S.2    Pietrangelo, A.3    Minotti, G.4
  • 194
    • 36349031925 scopus 로고    scopus 로고
    • Bach1 repression of ferritin and thioredoxin reductase1 is heme-sensitive in cells and in vitro and coordinates expression with heme oxygenase1, β-globin, and NADP(H) quinone (Oxido) reductase1
    • DOI 10.1074/jbc.M700254200
    • K.J. Hintze, Y. Katoh, K. Igarashi, and E.C. Theil Bach1 repression of ferritin and thioredoxin reductase1 is heme-sensitive in cells and in vitro and coordinates expression with heme oxygenase1, b-globin, and NADP(H) quinone (oxido) reductase1 J. Biol. Chem. 282 2007 34365 34371 (Pubitemid 350159431)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.47 , pp. 34365-34371
    • Hintze, K.J.1    Katoh, Y.2    Igarashi, K.3    Theil, E.C.4
  • 196
    • 0028347813 scopus 로고
    • Identification of the EPR-active iron-nitrosyl complexes in mammalian ferritins
    • M. Lee, P. Arosio, A. Cozzi, and N.D. Chasteen Identification of the EPR-active iron-nitrosyl complexes in mammalian ferritins Biochemistry 33 1994 3679 3687 (Pubitemid 24116017)
    • (1994) Biochemistry , vol.33 , Issue.12 , pp. 3679-3687
    • Lee, M.1    Arosio, P.2    Cozzi, A.3    Chasteen, N.D.4
  • 197
    • 0027990370 scopus 로고
    • Nitric oxide inhibits neuronal nitric oxide synthase by interacting with the heme prosthetic group: Role of tetrahydrobiopterin in modulating the inhibitory action of nitric oxide
    • J.M. Griscavage, J.M. Fukuto, Y. Komori, and L.J. Ignarro Nitric oxide inhibits neuronal nitric oxide synthase by interacting with the heme prosthetic group: role of tetrahydrobiopterin in modulating the inhibitory action of nitric oxide J. Biol. Chem. 269 1994 21644 21649
    • (1994) J. Biol. Chem. , vol.269 , pp. 21644-21649
    • Griscavage, J.M.1    Fukuto, J.M.2    Komori, Y.3    Ignarro, L.J.4
  • 200
    • 27744590575 scopus 로고    scopus 로고
    • Inhibition of the Fenton reaction by nitrogen monoxide
    • DOI 10.1007/s00775-005-0019-z
    • C. Lu, and W.H. Koppenol Inhibition of the Fenton reaction by nitrogen monoxide J. Biol. Inorg. Chem. 10 2005 732 738 (Pubitemid 41598696)
    • (2005) Journal of Biological Inorganic Chemistry , vol.10 , Issue.7 , pp. 732-738
    • Lu, C.1    Koppenol, W.H.2
  • 201
    • 0038725739 scopus 로고    scopus 로고
    • Iron regulatory proteins as NO signal transducers
    • C. Bouton, and J.C. Drapier Iron regulatory proteins as NO signal transducers Sci. STKE 2003 2003 e17
    • (2003) Sci. STKE , vol.2003 , pp. 17
    • Bouton, C.1    Drapier, J.C.2
  • 202
    • 0037328284 scopus 로고    scopus 로고
    • Effects of nitrogen monoxide and carbon monoxide on molecular and cellular iron metabolism: Mirror-image effector molecules that target iron
    • DOI 10.1042/BJ20021302
    • R.N. Watts, P. Ponka, and D.R. Richardson Effects of nitrogen monoxide and carbon monoxide on molecular and cellular iron metabolism: mirror-image effector molecules that target iron Biochem. J. 369 2003 429 440 (Pubitemid 36246225)
    • (2003) Biochemical Journal , vol.369 , Issue.3 , pp. 429-440
    • Watts, R.N.1    Ponka, P.2    Richardson, D.R.3
  • 203
    • 0028784211 scopus 로고
    • The effect of redox-related species of nitrogen monoxide on transferrin and iron uptake and cellular proliferation of erythroleukemia (K562) cells
    • D.R. Richardson, V. Neumannova, E. Nagy, and P. Ponka The effect of redox-related species of nitrogen monoxide on transferrin and iron uptake and cellular proliferation of erythroleukemia (K562) cells Blood 86 1995 3211 3219
    • (1995) Blood , vol.86 , pp. 3211-3219
    • Richardson, D.R.1    Neumannova, V.2    Nagy, E.3    Ponka, P.4
  • 204
    • 0034646393 scopus 로고    scopus 로고
    • Nitrogen monoxide activates iron regulatory protein 1 RNA-binding activity by two possible mechanisms: Effect on the [4Fe-4S] cluster and iron mobilization from cells
    • DOI 10.1021/bi991099t
    • S.L. Wardrop, R.N. Watts, and D.R. Richardson Nitrogen monoxide activates iron regulatory protein 1 RNA-binding activity by two possible mechanisms: effect on the [4Fe-4S] cluster and iron mobilization from cells Biochemistry 39 2000 2748 2758 (Pubitemid 30148930)
    • (2000) Biochemistry , vol.39 , Issue.10 , pp. 2748-2758
    • Wardrop, S.L.1    Watts, R.N.2    Richardson, D.R.3
  • 205
    • 0028181460 scopus 로고
    • Nitric oxide and the post-transcriptional control of cellular iron traffic
    • DOI 10.1016/0962-8924(94)90179-1
    • K. Pantopoulos, G. Weiss, and M.W. Hentze Nitric oxide and the post-transcriptional control of cellular iron traffic Trends Cell Biol. 4 1994 82 86 (Pubitemid 24068105)
    • (1994) Trends in Cell Biology , vol.4 , Issue.3 , pp. 82-86
    • Pantopoulos, K.1    Weiss, G.2    Hentze, M.W.3
  • 206
    • 79959539376 scopus 로고    scopus 로고
    • Iron regulatory protein 1 outcompetes iron regulatory protein 2 in regulating cellular iron homeostasis in response to nitric oxide
    • A. Stys, B. Galy, R.R. Starzynski, E. Smuda, J.C. Drapier, P. Lipinski, and C. Bouton Iron regulatory protein 1 outcompetes iron regulatory protein 2 in regulating cellular iron homeostasis in response to nitric oxide J. Biol. Chem. 286 2011 22846 22854
    • (2011) J. Biol. Chem. , vol.286 , pp. 22846-22854
    • Stys, A.1    Galy, B.2    Starzynski, R.R.3    Smuda, E.4    Drapier, J.C.5    Lipinski, P.6    Bouton, C.7
  • 207
    • 34250706879 scopus 로고    scopus 로고
    • Nitric oxide stimulates heme oxygenase-1 gene transcription via the Nrf2/ARE complex to promote vascular smooth muscle cell survival
    • DOI 10.1016/j.cardiores.2007.03.004, PII S0008636307001101
    • X.M. Liu, K.J. Peyton, D. Ensenat, H. Wang, M. Hannink, J. Alam, and W. Durante Nitric oxide stimulates heme oxygenase-1 gene transcription via the Nrf2/ARE complex to promote vascular smooth muscle cell survival Cardiovasc. Res. 75 2007 381 389 (Pubitemid 46961918)
    • (2007) Cardiovascular Research , vol.75 , Issue.2 , pp. 381-389
    • Liu, X.-m.1    Peyton, K.J.2    Ensenat, D.3    Wang, H.4    Hannink, M.5    Alam, J.6    Durante, W.7
  • 208
    • 77953713414 scopus 로고    scopus 로고
    • Heme controls ferroportin1 (FPN1) transcription involving Bach1, Nrf2 and a MARE/ARE sequence motif at position -7007 of the FPN1 promoter
    • S. Marro, D. Chiabrando, E. Messana, J. Stolte, E. Turco, E. Tolosano, and M.U. Muckenthaler Heme controls ferroportin1 (FPN1) transcription involving Bach1, Nrf2 and a MARE/ARE sequence motif at position -7007 of the FPN1 promoter Haematologica 95 2010 1261 1268
    • (2010) Haematologica , vol.95 , pp. 1261-1268
    • Marro, S.1    Chiabrando, D.2    Messana, E.3    Stolte, J.4    Turco, E.5    Tolosano, E.6    Muckenthaler, M.U.7
  • 210
    • 0036319056 scopus 로고    scopus 로고
    • Impact of endogenous nitric oxide on microglial cell energy metabolism and labile iron pool
    • DOI 10.1046/j.1471-4159.2002.00864.x
    • B. Chenais, H. Morjani, and J.C. Drapier Impact of endogenous nitric oxide on microglial cell energy metabolism and labile iron pool J. Neurochem. 81 2002 615 623 (Pubitemid 34809340)
    • (2002) Journal of Neurochemistry , vol.81 , Issue.3 , pp. 615-623
    • Chenais, B.1    Morjani, H.2    Drapier, J.-C.3
  • 211
    • 0033566274 scopus 로고    scopus 로고
    • Induction of heme oxygenase-1 as a response in sensing the signals evoked by distinct nitric oxide donors
    • DOI 10.1016/S0006-2952(99)00097-0, PII S0006295299000970
    • E. Hara, K. Takahashi, K. Takeda, M. Nakayama, M. Yoshizawa, H. Fujita, K. Shirato, and S. Shibahara Induction of heme oxygenase-1 as a response in sensing the signals evoked by distinct nitric oxide donors Biochem. Pharmacol. 58 1999 227 236 (Pubitemid 29255939)
    • (1999) Biochemical Pharmacology , vol.58 , Issue.2 , pp. 227-236
    • Hara, E.1    Takahashi, K.2    Takeda, K.3    Nakayama, M.4    Yoshizawa, M.5    Fujita, H.6    Shirato, K.7    Shibahara, S.8
  • 212
    • 0032146141 scopus 로고    scopus 로고
    • Complex genetic response of human cells to sublethal levels of pure nitric oxide
    • J.C. Marquis, and B. Demple Complex genetic response of human cells to sublethal levels of pure nitric oxide Cancer Res. 58 1998 3435 3440 (Pubitemid 28371087)
    • (1998) Cancer Research , vol.58 , Issue.15 , pp. 3435-3440
    • Marquis, J.C.1    Demple, B.2
  • 213
    • 0242590646 scopus 로고    scopus 로고
    • Nitric oxide-mediated modulation of iron regulatory proteins: Implication for cellular iron homeostasis
    • S. Kim, and P. Ponka Nitric oxide-mediated modulation of iron regulatory proteins: implication for cellular iron homeostasis Blood Cells Mol. Dis. 29 2002 400 410
    • (2002) Blood Cells Mol. Dis. , vol.29 , pp. 400-410
    • Kim, S.1    Ponka, P.2
  • 214
    • 0032746973 scopus 로고    scopus 로고
    • Control of transferrin receptor expression via nitric oxide-mediated modulation of iron-regulatory protein 2
    • S. Kim, and P. Ponka Control of transferrin receptor expression via nitric oxide-mediated modulation of iron-regulatory protein 2 J. Biol. Chem. 274 1999 33035 33042 (Pubitemid 129535344)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.46 , pp. 33035-33042
    • Kim, S.1    Ponka, P.2
  • 215
    • 33644526911 scopus 로고    scopus 로고
    • Sodium nitroprusside promotes IRP2 degradation via an increase in intracellular iron and in the absence of S nitrosylation at C178
    • J. Wang, C. Fillebeen, G. Chen, B. Andriopoulos, and K. Pantopoulos Sodium nitroprusside promotes IRP2 degradation via an increase in intracellular iron and in the absence of S nitrosylation at C178 Mol. Cell. Biol. 26 2006 1948 1954
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1948-1954
    • Wang, J.1    Fillebeen, C.2    Chen, G.3    Andriopoulos, B.4    Pantopoulos, K.5
  • 216
    • 0028090219 scopus 로고
    • Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide
    • L. Castro, M. Rodriguez, and R. Radi Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide J. Biol. Chem. 269 1994 29409 29415 (Pubitemid 24365085)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.47 , pp. 29409-29415
    • Castro, L.1    Rodriguez, M.2    Radi, R.3
  • 217
    • 0027960215 scopus 로고
    • Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not
    • A. Hausladen, and I. Fridovich Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not J. Biol. Chem. 269 1994 29405 29408 (Pubitemid 24365084)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.47 , pp. 29405-29408
    • Hausladen, A.1    Fridovich, I.2
  • 218
    • 0030783602 scopus 로고    scopus 로고
    • Inactivation of dehydratase [4Fe-4S] clusters and disruption of iron homeostasis upon cell exposure to peroxynitrite
    • DOI 10.1074/jbc.272.44.27652
    • K. Keyer, and J.A. Imlay Inactivation of dehydratase [4Fe-4S] clusters and disruption of iron homeostasis upon cell exposure to peroxynitrite J. Biol. Chem. 272 1997 27652 27659 (Pubitemid 27473559)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.44 , pp. 27652-27659
    • Keyer, K.1    Imlay, J.A.2
  • 219
    • 0030752458 scopus 로고    scopus 로고
    • Redox modulation of iron regulatory proteins by peroxynitrite
    • DOI 10.1074/jbc.272.32.19969
    • C. Bouton, H. Hirling, and J.C. Drapier Redox modulation of iron regulatory proteins by peroxynitrite J. Biol. Chem. 272 1997 19969 19975 (Pubitemid 27340098)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.32 , pp. 19969-19975
    • Bouton, C.1    Hirling, H.2    Drapier, J.-C.3
  • 220
    • 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
    • DOI 10.1021/bi025756k
    • G. Cairo, R. Ronchi, S. Recalcati, A. Campanella, and G. Minotti 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 41 2002 7435 7442 (Pubitemid 34602462)
    • (2002) Biochemistry , vol.41 , Issue.23 , pp. 7435-7442
    • Cairo, G.1    Ronchi, R.2    Recalcati, S.3    Campanella, A.4    Minotti, G.5
  • 221
    • 0037663696 scopus 로고    scopus 로고
    • Peroxynitrite and nitric oxide differently target the iron-sulfur cluster and amino acid residues of human iron regulatory protein 1
    • DOI 10.1021/bi030041i
    • E. Soum, X. Brazzolotto, C. Goussias, C. Bouton, J.M. Moulis, T.A. Mattioli, and J.C. Drapier Peroxynitrite and nitric oxide differently target the iron-sulfur cluster and amino acid residues of human iron regulatory protein 1 Biochemistry 42 2003 7648 7654 (Pubitemid 36758929)
    • (2003) Biochemistry , vol.42 , Issue.25 , pp. 7648-7654
    • Soum, E.1    Brazzolotto, X.2    Goussias, C.3    Bouton, C.4    Moulis, J.-M.5    Mattioli, T.A.6    Drapier, J.-C.7
  • 222
    • 0037257199 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite promote complete disruption of the [4Fe-4S] cluster of recombinant human iron regulatory protein 1
    • DOI 10.1007/s00775-002-0412-9
    • E. Soum, and J.C. Drapier Nitric oxide and peroxynitrite promote complete disruption of the [4Fe-4S] cluster of recombinant human iron regulatory protein 1 J. Biol. Inorg. Chem. 8 2003 226 232 (Pubitemid 36168911)
    • (2003) Journal of Biological Inorganic Chemistry , vol.8 , Issue.1-2 , pp. 226-232
    • Soum, E.1    Drapier, J.-C.2
  • 225
    • 0030587961 scopus 로고    scopus 로고
    • D169) Mouse Strains
    • S.M. Vidal, E. Pinner, P. Lepage, S. Gauthier, and P. Gros Natural resistance to intracellular infections: Nramp1 encodes a membrane phosphoglycoprotein absent in macrophages from susceptible (Nramp1 D169) mouse strains J. Immunol. 157 1996 3559 3568 (Pubitemid 126449170)
    • (1996) Journal of Immunology , vol.157 , Issue.8 , pp. 3559-3568
    • Vidal, S.M.1    Pinner, E.2    Lepage, P.3    Gauthier, S.4    Gros, P.5
  • 226
    • 0036213294 scopus 로고    scopus 로고
    • The natural resistance-associated macrophage protein 1 Slc11a1 (formerly Nramp1) and iron metabolism in macrophages
    • DOI 10.1016/S1286-4579(02)01548-4, PII S1286457902015484
    • S. Wyllie, P. Seu, and J.A. Goss The natural resistance-associated macrophage protein 1 Slc11a1 (formerly Nramp1) and iron metabolism in macrophages Microbes Infect. 4 2002 351 359 (Pubitemid 34293641)
    • (2002) Microbes and Infection , vol.4 , Issue.3 , pp. 351-359
    • Wyllie, S.1    Seu, P.2    Goss, J.A.3
  • 227
    • 0043136713 scopus 로고    scopus 로고
    • Nramp1 functionality increases inducible nitric oxide synthase transcription via stimulation of IFN regulatory factor 1 expression
    • G. Fritsche, M. Dlaska, H. Barton, I. Theurl, K. Garimorth, and G. Weiss Nramp1 functionality increases inducible nitric oxide synthase transcription via stimulation of IFN regulatory factor 1 expression J. Immunol. 171 2003 1994 1998 (Pubitemid 36966483)
    • (2003) Journal of Immunology , vol.171 , Issue.4 , pp. 1994-1998
    • Fritsche, G.1    Dlaska, M.2    Barton, H.3    Theurl, I.4    Garimorth, K.5    Weiss, G.6
  • 228
    • 0029258822 scopus 로고
    • Nramp transfection transfers Ity/Lsh/Bcg-related pleiotropic effects on macrophage activation: Influence on oxidative burst and nitric oxide pathways
    • C.H. Barton, S.H. Whitehead, and J.M. Blackwell Nramp transfection transfers Ity/Lsh/Bcg-related pleiotropic effects on macrophage activation: influence on oxidative burst and nitric oxide pathways Mol. Med. 1 1995 267 279
    • (1995) Mol. Med. , vol.1 , pp. 267-279
    • Barton, C.H.1    Whitehead, S.H.2    Blackwell, J.M.3
  • 229
    • 33646732642 scopus 로고    scopus 로고
    • Nitrogen monoxide (NO)-mediated iron release from cells is linked to NO-induced glutathione efflux via multidrug resistance-associated protein 1
    • R.N. Watts, C. Hawkins, P. Ponka, and D.R. Richardson Nitrogen monoxide (NO)-mediated iron release from cells is linked to NO-induced glutathione efflux via multidrug resistance-associated protein 1 Proc. Natl. Acad. Sci. USA 103 2006 7670 7675
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7670-7675
    • Watts, R.N.1    Hawkins, C.2    Ponka, P.3    Richardson, D.R.4
  • 230
    • 67649781729 scopus 로고    scopus 로고
    • Dinitrosyl iron complexes with thiolate ligands: Physico-chemistry, biochemistry and physiology
    • A.F. Vanin Dinitrosyl iron complexes with thiolate ligands: physico-chemistry, biochemistry and physiology Nitric Oxide 21 2009 1 13
    • (2009) Nitric Oxide , vol.21 , pp. 1-13
    • Vanin, A.F.1
  • 233
    • 0034284314 scopus 로고    scopus 로고
    • Activation of macrophage cytostatic effector mechanisms during acute graft-versus-host disease: Release of intracellular iron and nitric oxide-mediated cytostasis
    • F.P. Nestel, R.N. Greene, K. Kichian, P. Ponka, and W.S. Lapp Activation of macrophage cytostatic effector mechanisms during acute graft-versus-host disease: release of intracellular iron and nitric oxide-mediated cytostasis Blood 96 2000 1836 1843 (Pubitemid 30661069)
    • (2000) Blood , vol.96 , Issue.5 , pp. 1836-1843
    • Nestel, F.P.1    Greene, R.N.2    Kichian, K.3    Ponka, P.4    Lapp, W.S.5
  • 234
    • 0035153971 scopus 로고    scopus 로고
    • Iron biology in immune function, muscle metabolism and neuronal functioning
    • J.L. Beard Iron biology in immune function, muscle metabolism and neuronal functioning J. Nutr. 131 2001 568S 579S
    • (2001) J. Nutr. , vol.131
    • Beard, J.L.1
  • 235
    • 0035930604 scopus 로고    scopus 로고
    • Heme deficiency selectively interrupts assembly of mitochondrial complex IV in human fibroblasts: Relevance to aging
    • H. Atamna, J. Liu, and B.N. Ames Heme deficiency selectively interrupts assembly of mitochondrial complex IV in human fibroblasts: relevance to aging J. Biol. Chem. 276 2001 48410 48416
    • (2001) J. Biol. Chem. , vol.276 , pp. 48410-48416
    • Atamna, H.1    Liu, J.2    Ames, B.N.3
  • 236
    • 0035863011 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space
    • DOI 10.1042/0264-6021:3530411
    • D. Han, E. Williams, and E. Cadenas Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space Biochem. J. 353 2001 411 416 (Pubitemid 32096952)
    • (2001) Biochemical Journal , vol.353 , Issue.2 , pp. 411-416
    • Han, D.1    Williams, E.2    Cadenas, E.3
  • 237
    • 0034661024 scopus 로고    scopus 로고
    • Superoxides from mitochondrial complex III: The role of manganese superoxide dismutase
    • S. Raha, G.E. McEachern, A.T. Myint, and B.H. Robinson Superoxides from mitochondrial complex III: the role of manganese superoxide dismutase Free Radic. Biol. Med. 29 2000 170 180
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 170-180
    • Raha, S.1    McEachern, G.E.2    Myint, A.T.3    Robinson, B.H.4
  • 239
    • 84855783899 scopus 로고    scopus 로고
    • Effects of iron deficiency anemia and its treatment with iron polymaltose complex in pregnant rats, their fetuses and placentas: Oxidative stress markers and pregnancy outcome
    • J.E. Toblli, G. Cao, L. Oliveri, and M. Angerosa Effects of iron deficiency anemia and its treatment with iron polymaltose complex in pregnant rats, their fetuses and placentas: oxidative stress markers and pregnancy outcome Placenta 33 2012 81 87
    • (2012) Placenta , vol.33 , pp. 81-87
    • Toblli, J.E.1    Cao, G.2    Oliveri, L.3    Angerosa, M.4
  • 240
    • 0032921569 scopus 로고    scopus 로고
    • Identification of copper/zinc superoxide dismutase as a novel nitric oxide-regulated gene in rat glomerular mesangial cells and kidneys of endotoxemic rats
    • S. Frank, K. Zacharowski, G.M. Wray, C. Thiemermann, and J. Pfeilschifter Identification of copper/zinc superoxide dismutase as a novel nitric oxide-regulated gene in rat glomerular mesangial cells and kidneys of endotoxemic rats FASEB J. 13 1999 869 882 (Pubitemid 29220699)
    • (1999) FASEB Journal , vol.13 , Issue.8 , pp. 869-882
    • Frank, S.1    Zacharowski, K.2    Wray, G.M.3    Thiemermann, C.4    Pfeilschifter, J.5
  • 242
    • 36549053552 scopus 로고    scopus 로고
    • Haemochromatosis
    • DOI 10.1016/S0140-6736(07)61782-6, PII S0140673607617826
    • P.C. Adams, and J.C. Barton Haemochromatosis Lancet 370 2007 1855 1860 (Pubitemid 350180034)
    • (2007) Lancet , vol.370 , Issue.9602 , pp. 1855-1860
    • Adams, P.C.1    Barton, J.C.2
  • 245
    • 80053615986 scopus 로고    scopus 로고
    • Disorders associated with systemic or local iron overload: From pathophysiology to clinical practice
    • G. Sebastiani, and K. Pantopoulos Disorders associated with systemic or local iron overload: from pathophysiology to clinical practice Metallomics 3 2011 971 986
    • (2011) Metallomics , vol.3 , pp. 971-986
    • Sebastiani, G.1    Pantopoulos, K.2
  • 246
    • 75049084543 scopus 로고    scopus 로고
    • Genetic mechanisms and modifying factors in hereditary hemochromatosis
    • G. Weiss Genetic mechanisms and modifying factors in hereditary hemochromatosis Nat. Rev. Gastroenterol. Hepatol. 7 2010 50 58
    • (2010) Nat. Rev. Gastroenterol. Hepatol. , vol.7 , pp. 50-58
    • Weiss, G.1
  • 247
    • 0021000035 scopus 로고
    • Iron overload disorders: Natural history, pathogenesis, diagnosis, and therapy
    • G.D. McLaren, W.A. Muir, and R.W. Kellermeyer Iron overload disorders: natural history, pathogenesis, diagnosis, and therapy Crit. Rev. Clin. Lab. Sci. 19 1983 205 266
    • (1983) Crit. Rev. Clin. Lab. Sci. , vol.19 , pp. 205-266
    • McLaren, G.D.1    Muir, W.A.2    Kellermeyer, R.W.3
  • 248
    • 28444454447 scopus 로고    scopus 로고
    • Hepatotoxicity of iron overload: Mechanisms of iron-induced hepatic fibrogenesis
    • DOI 10.1055/s-2005-923315
    • G.A. Ramm, and R.G. Ruddell Hepatotoxicity of iron overload: mechanisms of iron-induced hepatic fibrogenesis Semin. Liver Dis. 25 2005 433 449 (Pubitemid 41741260)
    • (2005) Seminars in Liver Disease , vol.25 , Issue.4 , pp. 433-449
    • Ramm, G.A.1    Ruddell, R.G.2
  • 249
    • 0025925346 scopus 로고
    • Alterations in the structure, physicochemical properties, and pH of hepatocyte lysosomes in experimental iron overload
    • B.M. Myers, F.G. Prendergast, R. Holman, S.M. Kuntz, and N.F. LaRusso Alterations in the structure, physicochemical properties, and pH of hepatocyte lysosomes in experimental iron overload J. Clin. Invest. 88 1991 1207 1215
    • (1991) J. Clin. Invest. , vol.88 , pp. 1207-1215
    • Myers, B.M.1    Prendergast, F.G.2    Holman, R.3    Kuntz, S.M.4    Larusso, N.F.5
  • 250
    • 0018860041 scopus 로고
    • Studies on the concentration and intracellular localization of iron proteins in liver biopsy specimens from patients with iron overload with special reference to their role in lysosomal disruption
    • C. Selden, M. Owen, J.M. Hopkins, and T.J. Peters Studies on the concentration and intracellular localization of iron proteins in liver biopsy specimens from patients with iron overload with special reference to their role in lysosomal disruption Br. J. Haematol. 44 1980 593 603 (Pubitemid 10129170)
    • (1980) British Journal of Haematology , vol.44 , Issue.4 , pp. 593-603
    • Selden, C.1    Owen, M.2    Hopkins, J.M.P.3    Peters, T.J.4
  • 253
    • 0032828466 scopus 로고    scopus 로고
    • Erosive injury to the upper gastrointestinal tract in patients receiving iron medication: An underrecognized entity
    • DOI 10.1097/00000478-199910000-00009
    • S.C. Abraham, J.H. Yardley, and T.T. Wu Erosive injury to the upper gastrointestinal tract in patients receiving iron medication: an underrecognized entity Am. J. Surg. Pathol. 23 1999 1241 1247 (Pubitemid 29474594)
    • (1999) American Journal of Surgical Pathology , vol.23 , Issue.10 , pp. 1241-1247
    • Abraham, S.C.1    Yardley, J.H.2    Wu, T.-T.3
  • 255
    • 74249109578 scopus 로고    scopus 로고
    • Melanosis ilei associated with chronic ingestion of oral iron
    • J.M. Cha, J.I. Lee, K.R. Joo, S.W. Jung, and H.P. Shin Melanosis ilei associated with chronic ingestion of oral iron Gut Liver 3 2009 315 317
    • (2009) Gut Liver , vol.3 , pp. 315-317
    • Cha, J.M.1    Lee, J.I.2    Joo, K.R.3    Jung, S.W.4    Shin, H.P.5
  • 257
    • 50049084034 scopus 로고    scopus 로고
    • Iron-induced mucosal pathology of the upper gastrointestinal tract: A common finding in patients on oral iron therapy
    • P. Kaye, K. Abdulla, J. Wood, P. James, S. Foley, K. Ragunath, and J. Atherton Iron-induced mucosal pathology of the upper gastrointestinal tract: a common finding in patients on oral iron therapy Histopathology 53 2008 311 317
    • (2008) Histopathology , vol.53 , pp. 311-317
    • Kaye, P.1    Abdulla, K.2    Wood, J.3    James, P.4    Foley, S.5    Ragunath, K.6    Atherton, J.7
  • 259
    • 42549148867 scopus 로고    scopus 로고
    • Non-transferrin-bound iron in plasma following administration of oral iron drugs
    • DOI 10.1007/s10534-007-9116-5
    • B. Dresow, D. Petersen, R. Fischer, and P. Nielsen Non-transferrin-bound iron in plasma following administration of oral iron drugs Biometals 21 2008 273 276 (Pubitemid 351579742)
    • (2008) BioMetals , vol.21 , Issue.3 , pp. 273-276
    • Dresow, B.1    Petersen, D.2    Fischer, R.3    Nielsen, P.4
  • 261
    • 84863005759 scopus 로고    scopus 로고
    • Oral administration of ferrous sulfate, but not of iron polymaltose or sodium iron ethylenediaminetetraacetic acid (NaFeEDTA), results in a substantial increase of non-transferrin-bound iron in healthy iron-adequate men
    • K. Schümann, N.W. Solomons, M.E. Romero-Abal, M. Orozco, G. Weiss, and J. Marx Oral administration of ferrous sulfate, but not of iron polymaltose or sodium iron ethylenediaminetetraacetic acid (NaFeEDTA), results in a substantial increase of non-transferrin-bound iron in healthy iron-adequate men Food Nutr. Bull. 33 2012 128 136
    • (2012) Food Nutr. Bull. , vol.33 , pp. 128-136
    • Schümann, K.1    Solomons, N.W.2    Romero-Abal, M.E.3    Orozco, M.4    Weiss, G.5    Marx, J.6
  • 263
    • 34447345399 scopus 로고    scopus 로고
    • Safety and efficacy of iron (III)-hydroxide polymaltose complex: A review of over 25 years experience
    • P. Geisser Safety and efficacy of iron(III)-hydroxide polymaltose complex/a review of over 25 years experience Drug Res. 57 2007 439 452 (Pubitemid 47055995)
    • (2007) Arzneimittel-Forschung/Drug Research , vol.57 , Issue.6 , pp. 439-452
    • Geisser, P.1
  • 264
    • 80053936343 scopus 로고    scopus 로고
    • Efficacy and safety of oral iron(III) polymaltose complex versus ferrous sulfate in pregnant women with iron-deficiency anemia: A multicenter, randomized, controlled study
    • R. Ortiz, J.E. Toblli, J.D. Romero, B. Monterrosa, C. Frer, E. Macagno, and C. Breymann Efficacy and safety of oral iron(III) polymaltose complex versus ferrous sulfate in pregnant women with iron-deficiency anemia: a multicenter, randomized, controlled study J. Matern. Fetal Neonatal Med. 24 2011 1347 1352
    • (2011) J. Matern. Fetal Neonatal Med. , vol.24 , pp. 1347-1352
    • Ortiz, R.1    Toblli, J.E.2    Romero, J.D.3    Monterrosa, B.4    Frer, C.5    Macagno, E.6    Breymann, C.7
  • 265
    • 34447317825 scopus 로고    scopus 로고
    • Iron (III)-hydroxide polymaltose complex in iron deficiency anemia: Review and meta-analysis
    • J.E. Toblli, and R. Brignoli Iron(III)-hydroxide polymaltose complex in iron deficiency anemia/review and meta-analysis Drug Res. 57 2007 431 438 (Pubitemid 47055994)
    • (2007) Arzneimittel-Forschung/Drug Research , vol.57 , Issue.6 , pp. 431-438
    • Toblli, J.E.1    Brignoli, R.2
  • 266
    • 0021742792 scopus 로고
    • Iron pharmacokinetics after administration of ferric-hydroxide- polymaltose complex in rats
    • P. Geisser, and A. Müller Iron pharmacokinetics after administration of ferric-hydroxide-polymaltose complex in rats Drug Res. 34 1984 1560 1569 (Pubitemid 15209192)
    • (1984) Arzneimittel-Forschung/Drug Research , vol.34 , Issue.11 , pp. 1560-1569
    • Geisser, P.1    Muller, A.2
  • 267
    • 34447314965 scopus 로고    scopus 로고
    • Iron therapy, oxidative stress and immunology
    • R.K. Chandra, TSAR Health Toronto
    • P. Geisser Iron therapy, oxidative stress and immunology R.K. Chandra, Nutrition and Immunology in the 21st Century 2004 TSAR Health Toronto 53 65
    • (2004) Nutrition and Immunology in the 21st Century , pp. 53-65
    • Geisser, P.1
  • 269
    • 84864618579 scopus 로고    scopus 로고
    • Comparison of early gastrointestinal tract and liver toxicity of the originator iron polymaltose complex (IPC) and an IPC similar preparation in non-anemic rats
    • J.E. Toblli, G. Cao, and M. Angerosa Comparison of early gastrointestinal tract and liver toxicity of the originator iron polymaltose complex (IPC) and an IPC similar preparation in non-anemic rats Int. J. Clin. Pharmacol. Ther. 50 2012 573 583
    • (2012) Int. J. Clin. Pharmacol. Ther. , vol.50 , pp. 573-583
    • Toblli, J.E.1    Cao, G.2    Angerosa, M.3
  • 273
    • 79955045302 scopus 로고    scopus 로고
    • Clinical use of intravenous iron: Administration, efficacy, and safety
    • M. Auerbach, and H. Ballard Clinical use of intravenous iron: administration, efficacy, and safety Hematol. Am. Soc. Hematol. Educ. Program 2010 2010 338 347
    • (2010) Hematol. Am. Soc. Hematol. Educ. Program , vol.2010 , pp. 338-347
    • Auerbach, M.1    Ballard, H.2
  • 274
    • 77956806828 scopus 로고    scopus 로고
    • The efficacy and safety of current intravenous iron preparations for the management of iron-deficiency anaemia: A review
    • W.Y. Qunibi The efficacy and safety of current intravenous iron preparations for the management of iron-deficiency anaemia: a review Drug Res. 60 2010 399 412
    • (2010) Drug Res. , vol.60 , pp. 399-412
    • Qunibi, W.Y.1
  • 275
    • 84872225362 scopus 로고    scopus 로고
    • Comparison of adverse event profile of intravenous iron sucrose and iron sucrose similar in postpartum and gynecologic operative patients
    • E.S. Lee, B.R. Park, J.S. Kim, G.Y. Choi, J.J. Lee, and I.S. Lee Comparison of adverse event profile of intravenous iron sucrose and iron sucrose similar in postpartum and gynecologic operative patients Curr. Med. Res. Opin. 29 2013 141 147
    • (2013) Curr. Med. Res. Opin. , vol.29 , pp. 141-147
    • Lee, E.S.1    Park, B.R.2    Kim, J.S.3    Choi, G.Y.4    Lee, J.J.5    Lee, I.S.6
  • 277
    • 84856507284 scopus 로고    scopus 로고
    • Clinical case reports raise doubts about the therapeutic equivalence of an iron sucrose similar preparation compared with iron sucrose originator
    • J. Stein, A. Dignass, and K.U. Chow Clinical case reports raise doubts about the therapeutic equivalence of an iron sucrose similar preparation compared with iron sucrose originator Curr. Med. Res. Opin. 28 2012 241 243
    • (2012) Curr. Med. Res. Opin. , vol.28 , pp. 241-243
    • Stein, J.1    Dignass, A.2    Chow, K.U.3
  • 278
    • 0032934971 scopus 로고    scopus 로고
    • Pharmacokinetics and red cell utilization of iron(III) hydroxide- sucrose complex in anaemic patients: A study using positron emission tomography
    • DOI 10.1046/j.1365-2141.1999.01179.x
    • S. Beshara, H. Lundqvist, J. Sundin, M. Lubberink, V. Tolmachev, S. Valind, G. Antoni, B. Långström, and B.G. Danielson Pharmacokinetics and red cell utilization of iron(III) hydroxide-sucrose complex in anaemic patients: a study using positron emission tomography Br. J. Haematol. 104 1999 296 302 (Pubitemid 29083337)
    • (1999) British Journal of Haematology , vol.104 , Issue.2 , pp. 296-302
    • Beshara, S.1    Lundqvist, H.2    Sundin, J.3    Lubberink, M.4    Tolmachev, V.5    Valind, S.6    Antoni, G.7    Langstrom, B.8    Danielson, B.G.9
  • 280
    • 84934437962 scopus 로고    scopus 로고
    • Role of carbohydrate receptors in the macrophage uptake of dextran-coated iron oxide nanoparticles
    • Y. Chao, P.P. Karmali, and D. Simberg Role of carbohydrate receptors in the macrophage uptake of dextran-coated iron oxide nanoparticles Adv. Exp. Med. Biol. 733 2012 115 123
    • (2012) Adv. Exp. Med. Biol. , vol.733 , pp. 115-123
    • Chao, Y.1    Karmali, P.P.2    Simberg, D.3
  • 281
    • 9644257204 scopus 로고    scopus 로고
    • Structure, chemistry, and pharmacokinetics of intravenous iron agents
    • DOI 10.1097/01.ASN.0000143814.49713.C5
    • B.G. Danielson Structure, chemistry, and pharmacokinetics of intravenous iron agents J. Am. Soc. Nephrol. 15 Suppl. 2 2004 S93 S98 (Pubitemid 39578822)
    • (2004) Journal of the American Society of Nephrology , vol.15 , Issue.SUPPL. 2
    • Danielson, B.G.1
  • 283
    • 79953724862 scopus 로고    scopus 로고
    • The pharmacokinetics and pharmacodynamics of iron preparations
    • P. Geisser, and S. Burckhardt The pharmacokinetics and pharmacodynamics of iron preparations Pharmaceutics 3 2011 12 33
    • (2011) Pharmaceutics , vol.3 , pp. 12-33
    • Geisser, P.1    Burckhardt, S.2
  • 284
    • 24344434227 scopus 로고    scopus 로고
    • Pathways for the regulation of body iron homeostasis in response to experimental iron overload
    • DOI 10.1016/j.jhep.2005.03.030, PII S0168827805003168
    • I. Theurl, S. Ludwiczek, P. Eller, M. Seifert, E. Artner, P. Brunner, and G. Weiss Pathways for the regulation of body iron homeostasis in response to experimental iron overload J. Hepatol. 43 2005 711 719 (Pubitemid 41253240)
    • (2005) Journal of Hepatology , vol.43 , Issue.4 , pp. 711-719
    • Theurl, I.1    Ludwiczek, S.2    Eller, P.3    Seifert, M.4    Artner, E.5    Brunner, P.6    Weiss, G.7
  • 285
    • 84872346162 scopus 로고    scopus 로고
    • Differences in activation of mouse hepcidin by dietary iron and parenterally administered iron dextran: Compartmentalization is critical for iron sensing
    • A. Daba, K. Gkouvatsos, G. Sebastiani, and K. Pantopoulos Differences in activation of mouse hepcidin by dietary iron and parenterally administered iron dextran: compartmentalization is critical for iron sensing J. Mol. Med. (Berlin) 91 2013 95 102
    • (2013) J. Mol. Med. (Berlin) , vol.91 , pp. 95-102
    • Daba, A.1    Gkouvatsos, K.2    Sebastiani, G.3    Pantopoulos, K.4
  • 288
    • 1342306211 scopus 로고    scopus 로고
    • Labile iron in parenteral iron formulations: A quantitative and comparative study
    • DOI 10.1093/ndt/gfg579
    • D. van Wyck, J. Anderson, and K. Johnson Labile iron in parenteral iron formulations: a quantitative and comparative study Nephrol. Dial. Transplant. 19 2004 561 565 (Pubitemid 38263113)
    • (2004) Nephrology Dialysis Transplantation , vol.19 , Issue.3 , pp. 561-565
    • Van Wyck, D.B.1    Anderson, J.2    Johnson, K.3
  • 291
    • 0026679838 scopus 로고
    • Structure/histotoxicity relationship of parenteral iron preparations
    • P. Geisser, M. Baer, and E. Schaub Structure/histotoxicity relationship of parenteral iron preparations Drug Res. 42 1992 1439 1452 (Pubitemid 23007362)
    • (1992) Arzneimittel-Forschung/Drug Research , vol.42 , Issue.12 , pp. 1439-1452
    • Geisser, P.1    Baer, M.2    Schaub, E.3
  • 292
    • 77955456688 scopus 로고    scopus 로고
    • Parenteral iron formulations differentially affect MCP-1, HO-1, and NGAL gene expression and renal responses to injury
    • A.C. Johnson, K. Becker, and R.A. Zager Parenteral iron formulations differentially affect MCP-1, HO-1, and NGAL gene expression and renal responses to injury Am. J. Physiol. Renal Physiol 299 2010 F426 F435
    • (2010) Am. J. Physiol. Renal Physiol , vol.299
    • Johnson, A.C.1    Becker, K.2    Zager, R.A.3
  • 293
    • 33644972818 scopus 로고    scopus 로고
    • Effects of intravenous ABT-870 (iron (III)-hydroxide oligosaccharide) on mean arterial pressure and heart rate in the anaesthetized beagle: Comparison with other iron-containing haematinic agents
    • DOI 10.1111/j.1440-1681.2005.04299.x
    • L.C. Preusser, R.M. Fryer, A. Gerhardt, Y. Hu, L. Delgado-Herrera, J.Z. Melnick, L.A. Williams, B.F. Cox, and G.A. Reinhart Effects of intravenous ABT-870 (iron(III)-hydroxide oligosaccharide) on mean arterial pressure and heart rate in the anaesthetized beagle: comparison with other iron-containing haematinic agents Clin. Exp. Pharmacol. Physiol. 32 2005 1020 1026 (Pubitemid 43906810)
    • (2005) Clinical and Experimental Pharmacology and Physiology , vol.32 , Issue.12 , pp. 1020-1026
    • Preusser, L.C.1    Fryer, R.M.2    Gerhardt, A.3    Hu, Y.4    Delgado-Herrera, L.5    Melnick, J.Z.6    Williams, L.A.7    Cox, B.F.8    Reinhart, G.A.9
  • 294
    • 36448948292 scopus 로고    scopus 로고
    • Comparative toxicity and cell-tissue distribution study on nanoparticular iron complexes using avian embryos and HepG2-cells
    • DOI 10.1016/j.trsl.2007.09.001, PII S1931524407002332
    • S. Roth, P. Langguth, K. Spicher, and H. Enzmann Comparative toxicity and cell-tissue distribution study on nanoparticular iron complexes using avian embryos and HepG2-cells Transl. Res. 151 2008 36 44 (Pubitemid 350167044)
    • (2008) Translational Research , vol.151 , Issue.1 , pp. 36-44
    • Roth, S.1    Langguth, P.2    Spicher, K.3    Enzmann, H.4
  • 295
    • 84862491003 scopus 로고    scopus 로고
    • Iron sucrose impairs phagocytic function and promotes apoptosis in polymorphonuclear leukocytes
    • H. Ichii, Y. Masuda, T. Hassanzadeh, M. Saffarian, S. Gollapudi, and N.D. Vaziri Iron sucrose impairs phagocytic function and promotes apoptosis in polymorphonuclear leukocytes Am. J. Nephrol. 36 2012 50 57
    • (2012) Am. J. Nephrol. , vol.36 , pp. 50-57
    • Ichii, H.1    Masuda, Y.2    Hassanzadeh, T.3    Saffarian, M.4    Gollapudi, S.5    Vaziri, N.D.6
  • 297
    • 77955536989 scopus 로고    scopus 로고
    • Effect of different intravenous iron preparations on lymphocyte intracellular reactive oxygen species generation and subpopulation survival
    • A. Gupta, J. Zhuo, J. Zha, S. Reddy, J. Olp, and A. Pai Effect of different intravenous iron preparations on lymphocyte intracellular reactive oxygen species generation and subpopulation survival BMC Nephrol. 11 2010 16
    • (2010) BMC Nephrol. , vol.11 , pp. 16
    • Gupta, A.1    Zhuo, J.2    Zha, J.3    Reddy, S.4    Olp, J.5    Pai, A.6
  • 298
    • 84855162952 scopus 로고    scopus 로고
    • Iron sucrose promotes endothelial injury and dysfunction and monocyte adhesion/infiltration
    • V.S. Kamanna, S.H. Ganji, S. Shelkovnikov, K. Norris, and N.D. Vaziri Iron sucrose promotes endothelial injury and dysfunction and monocyte adhesion/infiltration Am. J. Nephrol. 35 2012 114 119
    • (2012) Am. J. Nephrol. , vol.35 , pp. 114-119
    • Kamanna, V.S.1    Ganji, S.H.2    Shelkovnikov, S.3    Norris, K.4    Vaziri, N.D.5
  • 299
    • 85067744639 scopus 로고    scopus 로고
    • Differential effect of IV iron compounds on intracellular reactive oxygen species (ROS) generation in aortic coronary endothelial cells
    • Pittsburgh, PA. [Abstract 431e] conference dates: October 16-19
    • Patel, H.; Prokopienko, A.; Gertzberg, N.; Neumann, P.; Johnson, A.; Barton Pai, A. Differential effect of IV iron compounds on intracellular reactive oxygen species (ROS) generation in aortic coronary endothelial cells. In American College of Clinical Pharmacy 2011 Annual Meeting Abstracts. Pittsburgh, PA. [Abstract 431e] conference dates: October 16-19, 2011.
    • (2011) American College of Clinical Pharmacy 2011 Annual Meeting Abstracts
    • Patel, H.1    Prokopienko, A.2    Gertzberg, N.3    Neumann, P.4    Johnson, A.5    Barton Pai, A.6
  • 300
    • 77955390090 scopus 로고    scopus 로고
    • In vitro study on the effects of iron sucrose, ferric gluconate and iron dextran on redox-active iron and oxidative stress
    • B. Sturm, H. Steinkellner, N. Ternes, H. Goldenberg, and B. Scheiber-Mojdehkar In vitro study on the effects of iron sucrose, ferric gluconate and iron dextran on redox-active iron and oxidative stress Drug Res. 60 2010 459 465
    • (2010) Drug Res. , vol.60 , pp. 459-465
    • Sturm, B.1    Steinkellner, H.2    Ternes, N.3    Goldenberg, H.4    Scheiber-Mojdehkar, B.5
  • 301
    • 36048936382 scopus 로고    scopus 로고
    • Iron availability and complex stability of iron hydroxyethyl starch and iron dextran - A comparative in vitro study with liver cells and macrophages
    • DOI 10.1093/ndt/gfm315
    • N. Ternes, B. Scheiber-Mojdehkar, G. Landgraf, H. Goldenberg, and B. Sturm Iron availability and complex stability of iron hydroxyethyl starch and iron dextran: a comparative in vitro study with liver cells and macrophages Nephrol. Dial. Transplant. 22 2007 2824 2830 (Pubitemid 350093433)
    • (2007) Nephrology Dialysis Transplantation , vol.22 , Issue.10 , pp. 2824-2830
    • Ternes, N.1    Scheiber-Mojdehkar, B.2    Landgraf, G.3    Goldenberg, H.4    Sturm, B.5
  • 302
    • 0036280354 scopus 로고    scopus 로고
    • Parenteral iron formulations: A comparative toxicologic analysis and mechanisms of cell injury
    • DOI 10.1053/ajkd.2002.33917
    • R.A. Zager, A.C. Johnson, S.Y. Hanson, and H. Wasse Parenteral iron formulations: a comparative toxicologic analysis and mechanisms of cell injury Am. J. Kidney Dis. 40 2002 90 103 (Pubitemid 34701216)
    • (2002) American Journal of Kidney Diseases , vol.40 , Issue.1 , pp. 90-103
    • Zager, R.A.1    Johnson, A.C.M.2    Hanson, S.Y.3    Wasse, H.4
  • 303
    • 79951865444 scopus 로고    scopus 로고
    • A comparative look at the safety profiles of intravenous iron products used in the hemodialysis population
    • E. Coppol, J. Shelly, S. Cheng, Y. Kaakeh, and B. Shepler A comparative look at the safety profiles of intravenous iron products used in the hemodialysis population Ann. Pharmacother. 45 2011 241 247
    • (2011) Ann. Pharmacother. , vol.45 , pp. 241-247
    • Coppol, E.1    Shelly, J.2    Cheng, S.3    Kaakeh, Y.4    Shepler, B.5
  • 306
    • 84866478796 scopus 로고    scopus 로고
    • Epidemic of iron overload in dialysis population caused by intravenous iron products: A plea for moderation
    • N.D. Vaziri Epidemic of iron overload in dialysis population caused by intravenous iron products: a plea for moderation Am. J. Med. 125 2012 951 952
    • (2012) Am. J. Med. , vol.125 , pp. 951-952
    • Vaziri, N.D.1
  • 307
    • 0037430971 scopus 로고    scopus 로고
    • Oxidative stress in cell culture: An under-appreciated problem?
    • DOI 10.1016/S0014-5793(03)00235-7
    • B. Halliwell Oxidative stress in cell culture: an under-appreciated problem? FEBS Lett. 540 2003 3 6 (Pubitemid 36398024)
    • (2003) FEBS Letters , vol.540 , Issue.1-3 , pp. 3-6
    • Halliwell, B.1
  • 308
    • 79952442409 scopus 로고    scopus 로고
    • Free radicals and antioxidants - Quo vadis?
    • B. Halliwell Free radicals and antioxidants - quo vadis? Trends Pharmacol. Sci. 32 2011 125 130
    • (2011) Trends Pharmacol. Sci. , vol.32 , pp. 125-130
    • Halliwell, B.1
  • 311
    • 0038122576 scopus 로고    scopus 로고
    • Labile iron in parenteral iron formulations and its potential for generating plasma nontransferrin-bound iron in dialysis patients
    • DOI 10.1046/j.1365-2362.2002.0320s1042.x
    • B.P. Esposito, W. Breuer, I. Slotki, and Z.I. Cabantchik Labile iron in parenteral iron formulations and its potential for generating plasma nontransferrin-bound iron in dialysis patients Eur. J. Clin. Invest. 32 Suppl. 1 2002 42 49 (Pubitemid 41704987)
    • (2002) European Journal of Clinical Investigation , vol.32 , Issue.SUPPL. 1 , pp. 42-49
    • Esposito, B.P.1    Breuer, W.2    Slotki, I.3    Cabantchik, Z.I.4
  • 313
    • 0033756150 scopus 로고    scopus 로고
    • Catalytically active iron and bacterial growth in serum of haemodialysis patients after i.V. Iron-saccharate administration
    • J. Parkkinen, L. von Bonsdorff, S. Peltonen, C. Grönhagen-Riska, and K. Rosenlöf Catalytically active iron and bacterial growth in serum of haemodialysis patients after i.v. iron-saccharate administration Nephrol. Dial. Transplant. 15 2000 1827 1834
    • (2000) Nephrol. Dial. Transplant. , vol.15 , pp. 1827-1834
    • Parkkinen, J.1    Von Bonsdorff, L.2    Peltonen, S.3    Grönhagen-Riska, C.4    Rosenlöf, K.5
  • 315
    • 79960102454 scopus 로고    scopus 로고
    • Non-transferrin bound iron, cytokine activation and intracellular reactive oxygen species generation in hemodialysis patients receiving intravenous iron dextran or iron sucrose
    • A.B. Pai, T. Conner, C.R. McQuade, J. Olp, and P. Hicks Non-transferrin bound iron, cytokine activation and intracellular reactive oxygen species generation in hemodialysis patients receiving intravenous iron dextran or iron sucrose Biometals 24 2011 603 613
    • (2011) Biometals , vol.24 , pp. 603-613
    • Pai, A.B.1    Conner, T.2    McQuade, C.R.3    Olp, J.4    Hicks, P.5
  • 317
    • 0034051716 scopus 로고    scopus 로고
    • Hemodialysis impairs endothelial function via oxidative stress: Effects of vitamin E-coated dialyzer
    • H. Miyazaki, H. Matsuoka, H. Itabe, M. Usui, S. Ueda, S. Okuda, and T. Imaizumi Hemodialysis impairs endothelial function via oxidative stress: effects of vitamin E-coated dialyzer Circulation 101 2000 1002 1006 (Pubitemid 30131702)
    • (2000) Circulation , vol.101 , Issue.9 , pp. 1002-1006
    • Miyazaki, H.1    Matsuoka, H.2    Itabe, H.3    Usui, M.4    Ueda, S.5    Okuda, S.6    Imaizumi, T.7
  • 319
    • 84872791896 scopus 로고    scopus 로고
    • Use of intravenous iron supplementation in chronic kidney disease: An update
    • I.C. Macdougall, and P. Geisser Use of intravenous iron supplementation in chronic kidney disease: an update Iran J. Kidney Dis. 7 2013 9 22
    • (2013) Iran J. Kidney Dis. , vol.7 , pp. 9-22
    • Macdougall, I.C.1    Geisser, P.2
  • 320
    • 84866531103 scopus 로고    scopus 로고
    • Iron levels in polarized macrophages: Regulation of immunity and autoimmunity
    • S. Recalcati, M. Locati, E. Gammella, P. Invernizzi, and G. Cairo Iron levels in polarized macrophages: regulation of immunity and autoimmunity Autoimmun. Rev. 11 2012 883 889
    • (2012) Autoimmun. Rev. , vol.11 , pp. 883-889
    • Recalcati, S.1    Locati, M.2    Gammella, E.3    Invernizzi, P.4    Cairo, G.5
  • 321
    • 79957723868 scopus 로고    scopus 로고
    • Iron trafficking and metabolism in macrophages: Contribution to the polarized phenotype
    • G. Cairo, S. Recalcati, A. Mantovani, and M. Locati Iron trafficking and metabolism in macrophages: contribution to the polarized phenotype Trends Immunol. 32 2011 241 247
    • (2011) Trends Immunol. , vol.32 , pp. 241-247
    • Cairo, G.1    Recalcati, S.2    Mantovani, A.3    Locati, M.4
  • 323
    • 84866308062 scopus 로고    scopus 로고
    • Heme and haemoglobin direct macrophage Mhem phenotype and counter foam cell formation in areas of intraplaque haemorrhage
    • J.J. Boyle Heme and haemoglobin direct macrophage Mhem phenotype and counter foam cell formation in areas of intraplaque haemorrhage Curr. Opin. Lipidol. 23 2012 453 461
    • (2012) Curr. Opin. Lipidol. , vol.23 , pp. 453-461
    • Boyle, J.J.1
  • 327
    • 79952169985 scopus 로고    scopus 로고
    • Impact of iron treatment on immune effector function and cellular iron status of circulating monocytes in dialysis patients
    • T. Sonnweber, I. Theurl, M. Seifert, A. Schroll, S. Eder, G. Mayer, and G. Weiss Impact of iron treatment on immune effector function and cellular iron status of circulating monocytes in dialysis patients Nephrol. Dial. Transplant. 26 2011 977 987
    • (2011) Nephrol. Dial. Transplant. , vol.26 , pp. 977-987
    • Sonnweber, T.1    Theurl, I.2    Seifert, M.3    Schroll, A.4    Eder, S.5    Mayer, G.6    Weiss, G.7
  • 328
    • 0038119551 scopus 로고    scopus 로고
    • Effect of iron treatment on circulating cytokine levels in ESRD patients receiving recombinant human erythropoietin
    • DOI 10.1046/j.1523-1755.2003.00099.x
    • G. Weiss, E. Meusburger, G. Radacher, K. Garimorth, U. Neyer, and G. Mayer Effect of iron treatment on circulating cytokine levels in ESRD patients receiving recombinant human erythropoietin Kidney Int. 64 2003 572 578 (Pubitemid 36871928)
    • (2003) Kidney International , vol.64 , Issue.2 , pp. 572-578
    • Weiss, G.1    Meusburger, E.2    Radacher, G.3    Garimorth, K.4    Neyer, U.5    Mayer, G.6
  • 329
    • 84878024210 scopus 로고    scopus 로고
    • Acute and sub-acute effect of ferric carboxymaltose on inflammation and adhesion molecules in patients with predialysis chronic renal failure
    • M. Prats, R. Font, C. García-Ruiz, C. Cabré, M. Muñoz-Cortés, M.R. Nogués, M. Jariod, M. Romeu, and A. Martínez-Vea Acute and sub-acute effect of ferric carboxymaltose on inflammation and adhesion molecules in patients with predialysis chronic renal failure Nefrologia 33 2013 355 361
    • (2013) Nefrologia , vol.33 , pp. 355-361
    • Prats, M.1    Font, R.2    García-Ruiz, C.3    Cabré, C.4    Muñoz-Cortés, M.5    Nogués, M.R.6    Jariod, M.7    Romeu, M.8    Martínez-Vea, A.9
  • 331
    • 0014578054 scopus 로고
    • Characteristics of iron dextran utilization in man
    • P.A. Henderson, and R.S. Hillman Characteristics of iron dextran utilization in man Blood 34 1969 357 375
    • (1969) Blood , vol.34 , pp. 357-375
    • Henderson, P.A.1    Hillman, R.S.2
  • 332
    • 0015462432 scopus 로고
    • Availability of iron dextran for hemoglobin synthesis as studied with phlebotomy
    • K.S. Olsson, and A. Weinfeld Availability of iron dextran for hemoglobin synthesis as studied with phlebotomy Acta Med. Scand. 192 1972 543 549
    • (1972) Acta Med. Scand. , vol.192 , pp. 543-549
    • Olsson, K.S.1    Weinfeld, A.2
  • 333
    • 0014249766 scopus 로고
    • The metabolism of iron-dextran given as a total-dose infusion to iron deficient Jamaican subjects
    • J.K. Wood, P.F. Milner, and U.N. Pathak The metabolism of iron-dextran given as a total-dose infusion to iron deficient Jamaican subjects Br. J. Haematol. 14 1968 119 129
    • (1968) Br. J. Haematol. , vol.14 , pp. 119-129
    • Wood, J.K.1    Milner, P.F.2    Pathak, U.N.3
  • 334
    • 0036096073 scopus 로고    scopus 로고
    • Patterns of iron distribution in liver cells in β-thalassemia studied by X-ray microanalysis
    • G. Faa, M. Terlizzo, C. Gerosa, T. Congiu, and E. Angelucci Patterns of iron distribution in liver cells in beta-thalassemia studied by X-ray microanalysis Haematologica 87 2002 479 484 (Pubitemid 34533272)
    • (2002) Haematologica , vol.87 , Issue.5 , pp. 479-484
    • Faa, G.1    Terlizzo, M.2    Gerosa, C.3    Congiu, T.4    Angelucci, E.5
  • 335
    • 0023856163 scopus 로고
    • Iron release from haemosiderin and production of iron-catalysed hydroxyl radicals in vitro
    • M. Ozaki, T. Kawabata, and M. Awai Iron release from haemosiderin and production of iron-catalysed hydroxyl radicals in vitro Biochem. J. 250 1988 589 595 (Pubitemid 18067911)
    • (1988) Biochemical Journal , vol.250 , Issue.2 , pp. 589-595
    • Ozaki, M.1    Kawabata, T.2    Awai, M.3
  • 336
  • 337
    • 79952562826 scopus 로고    scopus 로고
    • Oxidative depolymerization of polysaccharides by reactive oxygen/nitrogen species
    • J. Duan, and D.L. Kasper Oxidative depolymerization of polysaccharides by reactive oxygen/nitrogen species Glycobiology 21 2011 401 409
    • (2011) Glycobiology , vol.21 , pp. 401-409
    • Duan, J.1    Kasper, D.L.2
  • 338
    • 84879245725 scopus 로고    scopus 로고
    • Committee for Medicinal Products for Human Use EMA/CHMP/221776/2012, 1-79 London, UK: European Medicines Agency
    • Committee for Medicinal Products for Human Use. CHMP assessment report Rienso. EMA/CHMP/221776/2012, 1-79. 2012. London, UK: European Medicines Agency.
    • (2012) CHMP Assessment Report Rienso
  • 339
    • 77957298110 scopus 로고    scopus 로고
    • Lysosomal degradation of the carboxydextran shell of coated superparamagnetic iron oxide nanoparticles and the fate of professional phagocytes
    • O. Lunov, T. Syrovets, C. Röcker, K. Tron, G.U. Nienhaus, V. Rasche, V. Mailänder, K. Landfester, and T. Simmet Lysosomal degradation of the carboxydextran shell of coated superparamagnetic iron oxide nanoparticles and the fate of professional phagocytes Biomaterials 31 2010 9015 9022
    • (2010) Biomaterials , vol.31 , pp. 9015-9022
    • Lunov, O.1    Syrovets, T.2    Röcker, C.3    Tron, K.4    Nienhaus, G.U.5    Rasche, V.6    Mailänder, V.7    Landfester, K.8    Simmet, T.9
  • 341
    • 77956860272 scopus 로고    scopus 로고
    • The new generation of intravenous iron: Chemistry, pharmacology, and toxicology of ferric carboxymaltose
    • F. Funk, P. Ryle, C. Canclini, S. Neiser, and P. Geisser The new generation of intravenous iron: chemistry, pharmacology, and toxicology of ferric carboxymaltose Drug Res. 60 2010 345 353
    • (2010) Drug Res. , vol.60 , pp. 345-353
    • Funk, F.1    Ryle, P.2    Canclini, C.3    Neiser, S.4    Geisser, P.5
  • 342
    • 0029894558 scopus 로고    scopus 로고
    • Pharmacokinetics of iron(III)-hydroxide sucrose complex after a single intravenous dose in healthy volunteers
    • B.G. Danielson, T. Salmonson, H. Derendorf, and P. Geisser Pharmacokinetics of iron(III)-hydroxide sucrose complex after a single intravenous dose in healthy volunteers Drug Res. 46 1996 615 621 (Pubitemid 26201372)
    • (1996) Arzneimittel-Forschung/Drug Research , vol.46 , Issue.6 , pp. 615-621
    • Danielson, B.G.1    Salmonson, T.2    Derendorf, H.3    Geisser, P.4
  • 344
    • 0027765905 scopus 로고
    • Invited review. Free radicals in disease processes: A compilation of cause and consequence
    • J.M. Gutteridge Free radicals in disease processes: a compilation of cause and consequence Free Radic. Res. Commun. 19 1993 141 158 (Pubitemid 23330337)
    • (1993) Free Radical Research Communications , vol.19 , Issue.3 , pp. 141-158
    • Gutteridge, J.M.C.1
  • 345
    • 77949387122 scopus 로고    scopus 로고
    • A longitudinal study of oxidative stress and antioxidant status in women with uncomplicated pregnancies throughout gestation
    • Hung, T.H.; Lo,L.M.; Chiu,T.H.; Li,M.J.; Yeh,Y.L.; Chen,S.F.; Hsieh,T.T.A longitudinal study of oxidative stress and antioxidant status in women with uncomplicated pregnancies throughout gestation. Reprod.Sci. 17:401409; 2010.
    • (2010) Reprod. Sci. , vol.17 , pp. 401-409
    • Hung, T.H.1    Lo, L.M.2    Chiu, T.H.3    Li, M.J.4    Yeh, Y.L.5    Chen, S.F.6    Hsieh, T.T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.