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Volumn 72, Issue , 2014, Pages 23-40

Physiology and pathophysiology of iron in hemoglobin-associated diseases

Author keywords

Chelation; Hemochromatosis; Hemoglobinopathy; Iron overload; Iron toxicity; Magnetic resonance imaging; ROS; Sickle cell disease; Thalassemia; Transfusion

Indexed keywords

FERRITIN; FERROPORTIN; HEPCIDIN; IRON; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 2; NON TRANSFERRIN BOUND IRON; TRANSFERRIN; UNCLASSIFIED DRUG; HEMOGLOBIN; IRON CHELATING AGENT;

EID: 84899803096     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2014.03.039     Document Type: Review
Times cited : (127)

References (242)
  • 1
    • 84878504862 scopus 로고    scopus 로고
    • Treating thalassemia major-related iron overload: The role of deferiprone
    • V. Berdoukas, K. Farmaki, S. Carson, J. Wood, and T. Coates Treating thalassemia major-related iron overload: the role of deferiprone J. Blood Med. 3 2012 119 129
    • (2012) J. Blood Med. , vol.3 , pp. 119-129
    • Berdoukas, V.1    Farmaki, K.2    Carson, S.3    Wood, J.4    Coates, T.5
  • 4
    • 84885768132 scopus 로고    scopus 로고
    • Systemic iron homeostasis
    • T. Ganz Systemic iron homeostasis Physiol. Rev. 93 2013 1721 1741
    • (2013) Physiol. Rev. , vol.93 , pp. 1721-1741
    • Ganz, T.1
  • 5
    • 84899107851 scopus 로고    scopus 로고
    • The regulation of iron transport
    • D.M. Frazer, and G.J. Anderson The regulation of iron transport BioFactors 40 2 2014 206 214
    • (2014) BioFactors , vol.40 , Issue.2 , pp. 206-214
    • Frazer, D.M.1    Anderson, G.J.2
  • 7
    • 34247628002 scopus 로고    scopus 로고
    • Iron-regulatory proteins limit hypoxia-inducible factor-2alpha expression in iron deficiency
    • M. Sanchez, B. Galy, M.U. Muckenthaler, and M.W. Hentze Iron-regulatory proteins limit hypoxia-inducible factor-2alpha expression in iron deficiency Nat. Struct. Mol. Biol. 14 2007 420 426
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 420-426
    • Sanchez, M.1    Galy, B.2    Muckenthaler, M.U.3    Hentze, M.W.4
  • 8
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: MRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • M.W. Hentze, and L.C. Kuhn Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress Proc. Natl. Acad. Sci. USA 93 1996 8175 8182
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kuhn, L.C.2
  • 9
    • 84877978900 scopus 로고    scopus 로고
    • ZIP14 and DMT1 in the liver, pancreas, and heart are differentially regulated by iron deficiency and overload: Implications for tissue iron uptake in iron-related disorders
    • H. Nam, C.Y. Wang, L. Zhang, W. Zhang, S. Hojyo, T. Fukada, and M.D. Knutson ZIP14 and DMT1 in the liver, pancreas, and heart are differentially regulated by iron deficiency and overload: implications for tissue iron uptake in iron-related disorders Haematologica 98 2013 1049 1057
    • (2013) Haematologica , vol.98 , pp. 1049-1057
    • Nam, H.1    Wang, C.Y.2    Zhang, L.3    Zhang, W.4    Hojyo, S.5    Fukada, T.6    Knutson, M.D.7
  • 10
    • 0032104739 scopus 로고    scopus 로고
    • The human Nramp2 gene: Characterization of the gene structure, alternative splicing, promoter region and polymorphisms
    • P.L. Lee, T. Gelbart, C. West, C. Halloran, and E. Beutler The human Nramp2 gene: characterization of the gene structure, alternative splicing, promoter region and polymorphisms Blood Cells Mol. Dis. 24 1998 199 215
    • (1998) Blood Cells Mol. Dis. , vol.24 , pp. 199-215
    • Lee, P.L.1    Gelbart, T.2    West, C.3    Halloran, C.4    Beutler, E.5
  • 11
    • 82155178623 scopus 로고    scopus 로고
    • Iron regulatory protein-1 and -2: Transcriptome-wide definition of binding mRNAs and shaping of the cellular proteome by iron regulatory proteins
    • M. Sanchez, B. Galy, B. Schwanhaeusser, J. Blake, T. Bahr-Ivacevic, V. Benes, M. Selbach, M.U. Muckenthaler, and M.W. Hentze Iron regulatory protein-1 and -2: transcriptome-wide definition of binding mRNAs and shaping of the cellular proteome by iron regulatory proteins Blood 118 2011 e168 e179
    • (2011) Blood , vol.118
    • Sanchez, M.1    Galy, B.2    Schwanhaeusser, B.3    Blake, J.4    Bahr-Ivacevic, T.5    Benes, V.6    Selbach, M.7    Muckenthaler, M.U.8    Hentze, M.W.9
  • 16
    • 20444393434 scopus 로고    scopus 로고
    • Erythrophagocytosis and recycling of heme iron in normal and pathological conditions; Regulation by hepcidin
    • C. Beaumont, and F. Canonne-Hergaux [Erythrophagocytosis and recycling of heme iron in normal and pathological conditions; regulation by hepcidin] Transfus. Clin. Biol. 12 2005 123 130
    • (2005) Transfus. Clin. Biol. , vol.12 , pp. 123-130
    • Beaumont, C.1    Canonne-Hergaux, F.2
  • 18
    • 33746909869 scopus 로고    scopus 로고
    • Regulation of iron acquisition and iron distribution in mammals
    • T. Ganz, and E. Nemeth Regulation of iron acquisition and iron distribution in mammals Biochim. Biophys. Acta 1763 2006 690 699
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 690-699
    • Ganz, T.1    Nemeth, E.2
  • 19
    • 0030886381 scopus 로고    scopus 로고
    • Heme oxygenase 1 is required for mammalian iron reutilization
    • K.D. Poss, and S. Tonegawa Heme oxygenase 1 is required for mammalian iron reutilization Proc. Natl. Acad. Sci. USA 94 1997 10919 10924
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10919-10924
    • Poss, K.D.1    Tonegawa, S.2
  • 20
    • 84876539389 scopus 로고    scopus 로고
    • Role of hepcidin in the setting of hypoferremia during acute inflammation
    • J.C. Deschemin, and S. Vaulont Role of hepcidin in the setting of hypoferremia during acute inflammation PLoS One 8 2013 e61050
    • (2013) PLoS One , vol.8 , pp. 61050
    • Deschemin, J.C.1    Vaulont, S.2
  • 21
    • 34547636893 scopus 로고    scopus 로고
    • Capturing the onset of the common cold and its effects on iron absorption
    • M. Hoppe, and L. Hulthen Capturing the onset of the common cold and its effects on iron absorption Eur. J. Clin. Nutr. 61 2007 1032 1034
    • (2007) Eur. J. Clin. Nutr. , vol.61 , pp. 1032-1034
    • Hoppe, M.1    Hulthen, L.2
  • 25
    • 0035895096 scopus 로고    scopus 로고
    • Characterization of the iron transporter DMT1 (NRAMP2/DCT1) in red blood cells of normal and anemic mk/mk mice
    • F. Canonne-Hergaux, A.S. Zhang, P. Ponka, and P. Gros Characterization of the iron transporter DMT1 (NRAMP2/DCT1) in red blood cells of normal and anemic mk/mk mice Blood 98 2001 3823 3830
    • (2001) Blood , vol.98 , pp. 3823-3830
    • Canonne-Hergaux, F.1    Zhang, A.S.2    Ponka, P.3    Gros, P.4
  • 28
    • 0036800650 scopus 로고    scopus 로고
    • Rare causes of hereditary iron overload
    • P. Ponka Rare causes of hereditary iron overload Semin. Hematol. 39 2002 249 262
    • (2002) Semin. Hematol. , vol.39 , pp. 249-262
    • Ponka, P.1
  • 30
    • 77957783944 scopus 로고    scopus 로고
    • ZRT/IRT-like protein 14 (ZIP14) promotes the cellular assimilation of iron from transferrin
    • N. Zhao, J. Gao, C.A. Enns, and M.D. Knutson ZRT/IRT-like protein 14 (ZIP14) promotes the cellular assimilation of iron from transferrin J. Biol. Chem. 285 2010 32141 32150
    • (2010) J. Biol. Chem. , vol.285 , pp. 32141-32150
    • Zhao, N.1    Gao, J.2    Enns, C.A.3    Knutson, M.D.4
  • 31
    • 84887958462 scopus 로고    scopus 로고
    • Quantitative study of iron metabolism-related genes expression in rat
    • Y.Q. Li, B. Bai, Q.Q. Zheng, H. Yan, and G.H. Zhuang Quantitative study of iron metabolism-related genes expression in rat Biomed. Environ. Sci. 26 2013 808 819
    • (2013) Biomed. Environ. Sci. , vol.26 , pp. 808-819
    • Li, Y.Q.1    Bai, B.2    Zheng, Q.Q.3    Yan, H.4    Zhuang, G.H.5
  • 32
    • 72649093389 scopus 로고    scopus 로고
    • Stoichiometries of transferrin receptors 1 and 2 in human liver
    • M. Chloupkova, A.S. Zhang, and C.A. Enns Stoichiometries of transferrin receptors 1 and 2 in human liver Blood Cells Mol. Dis. 44 2010 28 33
    • (2010) Blood Cells Mol. Dis. , vol.44 , pp. 28-33
    • Chloupkova, M.1    Zhang, A.S.2    Enns, C.A.3
  • 33
    • 0037962795 scopus 로고    scopus 로고
    • The orchestration of body iron intake: How and where do enterocytes receive their cues?
    • D.M. Frazer, and G.J. Anderson The orchestration of body iron intake: how and where do enterocytes receive their cues? Blood Cells Mol. Dis. 30 2003 288 297
    • (2003) Blood Cells Mol. Dis. , vol.30 , pp. 288-297
    • Frazer, D.M.1    Anderson, G.J.2
  • 35
    • 0036174929 scopus 로고    scopus 로고
    • Iron deficiency can upregulate expression of transferrin receptor at both the mRNA and protein level
    • X. Tong, H. Kawabata, and H.P. Koeffler Iron deficiency can upregulate expression of transferrin receptor at both the mRNA and protein level Br. J. Haematol. 116 2002 458 464
    • (2002) Br. J. Haematol. , vol.116 , pp. 458-464
    • Tong, X.1    Kawabata, H.2    Koeffler, H.P.3
  • 36
    • 84875321185 scopus 로고    scopus 로고
    • Iron metabolism: Interactions with normal and disordered erythropoiesis
    • T. Ganz, and E. Nemeth Iron metabolism: interactions with normal and disordered erythropoiesis Cold Spring Harbor Perspect. Med. 2 2012 a011668
    • (2012) Cold Spring Harbor Perspect. Med. , vol.2 , pp. 011668
    • Ganz, T.1    Nemeth, E.2
  • 38
    • 77956795897 scopus 로고    scopus 로고
    • Ferroportin and erythroid cells: An update
    • L. Cianetti, M. Gabbianelli, and N.M. Sposi Ferroportin and erythroid cells: an update Adv. Hematol 2010 2010 404173
    • (2010) Adv. Hematol , vol.2010 , pp. 404173
    • Cianetti, L.1    Gabbianelli, M.2    Sposi, N.M.3
  • 41
    • 78951469267 scopus 로고    scopus 로고
    • Hepatic iron overload or cirrhosis may occur in acquired copper deficiency and is likely mediated by hypoceruloplasminemia
    • E.W. Thackeray, S.O. Sanderson, J.C. Fox, and N. Kumar Hepatic iron overload or cirrhosis may occur in acquired copper deficiency and is likely mediated by hypoceruloplasminemia J. Clin. Gastroenterol. 45 2011 153 158
    • (2011) J. Clin. Gastroenterol. , vol.45 , pp. 153-158
    • Thackeray, E.W.1    Sanderson, S.O.2    Fox, J.C.3    Kumar, N.4
  • 43
    • 0037103195 scopus 로고    scopus 로고
    • Copper deficiency masquerading as myelodysplastic syndrome
    • X.T. Gregg, V. Reddy, and J.T. Prchal Copper deficiency masquerading as myelodysplastic syndrome Blood 100 2002 1493 1495
    • (2002) Blood , vol.100 , pp. 1493-1495
    • Gregg, X.T.1    Reddy, V.2    Prchal, J.T.3
  • 45
    • 77953453474 scopus 로고    scopus 로고
    • Hepcidin biology and therapeutic applications
    • E. Nemeth Hepcidin biology and therapeutic applications Expert Rev. Hematol. 3 2010 153 155
    • (2010) Expert Rev. Hematol. , vol.3 , pp. 153-155
    • Nemeth, E.1
  • 46
    • 79955958017 scopus 로고    scopus 로고
    • Hepcidin and iron regulation, 10 years later
    • T. Ganz Hepcidin and iron regulation, 10 years later Blood 117 2011 4425 4433
    • (2011) Blood , vol.117 , pp. 4425-4433
    • Ganz, T.1
  • 47
    • 84864053080 scopus 로고    scopus 로고
    • Induction of activin B by inflammatory stimuli up-regulates expression of the iron-regulatory peptide hepcidin through Smad1/5/8 signaling
    • C. Besson-Fournier, C. Latour, L. Kautz, J. Bertrand, T. Ganz, M.P. Roth, and H. Coppin Induction of activin B by inflammatory stimuli up-regulates expression of the iron-regulatory peptide hepcidin through Smad1/5/8 signaling Blood 120 2012 431 439
    • (2012) Blood , vol.120 , pp. 431-439
    • Besson-Fournier, C.1    Latour, C.2    Kautz, L.3    Bertrand, J.4    Ganz, T.5    Roth, M.P.6    Coppin, H.7
  • 48
    • 0038662619 scopus 로고    scopus 로고
    • Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein
    • E. Nemeth, E.V. Valore, M. Territo, G. Schiller, A. Lichtenstein, and T. Ganz Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein Blood 101 2003 2461 2463
    • (2003) Blood , vol.101 , pp. 2461-2463
    • Nemeth, E.1    Valore, E.V.2    Territo, M.3    Schiller, G.4    Lichtenstein, A.5    Ganz, T.6
  • 50
    • 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
  • 52
    • 84861357425 scopus 로고    scopus 로고
    • The role of ineffective erythropoiesis in non-transfusion-dependent thalassemia
    • S. Rivella The role of ineffective erythropoiesis in non-transfusion- dependent thalassemia Blood Rev. 26 Suppl. 1 2012 S12 S15
    • (2012) Blood Rev. , vol.26 , Issue.SUPPL. 1
    • Rivella, S.1
  • 54
    • 84883684492 scopus 로고    scopus 로고
    • Transfusion suppresses erythropoiesis and increases hepcidin in adult patients with beta-thalassemia major: A longitudinal study
    • S.R. Pasricha, D.M. Frazer, D.K. Bowden, and G.J. Anderson Transfusion suppresses erythropoiesis and increases hepcidin in adult patients with beta-thalassemia major: a longitudinal study Blood 122 2013 124 133
    • (2013) Blood , vol.122 , pp. 124-133
    • Pasricha, S.R.1    Frazer, D.M.2    Bowden, D.K.3    Anderson, G.J.4
  • 59
    • 77954611973 scopus 로고    scopus 로고
    • Iron loading and overloading due to ineffective erythropoiesis
    • T. Tanno, and J.L. Miller Iron loading and overloading due to ineffective erythropoiesis Adv. Hematol 2010 2010 358283
    • (2010) Adv. Hematol , vol.2010 , pp. 358283
    • Tanno, T.1    Miller, J.L.2
  • 60
    • 38349194098 scopus 로고    scopus 로고
    • Furin-mediated release of soluble hemojuvelin: A new link between hypoxia and iron homeostasis
    • L. Silvestri, A. Pagani, and C. Camaschella Furin-mediated release of soluble hemojuvelin: a new link between hypoxia and iron homeostasis Blood 111 2008 924 931
    • (2008) Blood , vol.111 , pp. 924-931
    • Silvestri, L.1    Pagani, A.2    Camaschella, C.3
  • 61
    • 84899890153 scopus 로고    scopus 로고
    • The erythroid factor erythroferrone and its role in iron homeostasis
    • L. Kautz, G. Jung, E. Nemeth, and T. Ganz The erythroid factor erythroferrone and its role in iron homeostasis Blood 122 21 2013
    • (2013) Blood , vol.122 , Issue.21
    • Kautz, L.1    Jung, G.2    Nemeth, E.3    Ganz, T.4
  • 62
    • 0342264467 scopus 로고    scopus 로고
    • Determination of non-transferrin-bound iron in genetic hemochromatosis using a new HPLC-based method
    • O. Loreal, I. Gosriwatana, D. Guyader, J. Porter, P. Brissot, and R.C. Hider Determination of non-transferrin-bound iron in genetic hemochromatosis using a new HPLC-based method J. Hepatol. 32 2000 727 733
    • (2000) J. Hepatol. , vol.32 , pp. 727-733
    • Loreal, O.1    Gosriwatana, I.2    Guyader, D.3    Porter, J.4    Brissot, P.5    Hider, R.C.6
  • 66
    • 84897930615 scopus 로고    scopus 로고
    • The molecular and cellular basis of iron toxicity in iron overload disorders: Diagnostic and therapeutic approaches
    • Z.I. Cabantchik, Y.S. Sohn, W. Breuer, and B.P. Esposito The molecular and cellular basis of iron toxicity in iron overload disorders: diagnostic and therapeutic approaches Thalassemia Rep. 3 2013 7 13
    • (2013) Thalassemia Rep. , vol.3 , pp. 7-13
    • Cabantchik, Z.I.1    Sohn, Y.S.2    Breuer, W.3    Esposito, B.P.4
  • 68
    • 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
  • 70
    • 0014138218 scopus 로고
    • Hepatic iron deposition in humans. I. First-pass hepatic deposition of intestinally absorbed iron in patients with low plasma latent iron-binding capacity
    • R.A. Fawwaz, H.S. Winchell, M. Pollycove, and T. Sargent Hepatic iron deposition in humans. I. First-pass hepatic deposition of intestinally absorbed iron in patients with low plasma latent iron-binding capacity Blood 30 1967 417 424
    • (1967) Blood , vol.30 , pp. 417-424
    • Fawwaz, R.A.1    Winchell, H.S.2    Pollycove, M.3    Sargent, T.4
  • 71
    • 0027977403 scopus 로고
    • Biliary excretion of plasma non-transferrin-bound iron in rats: Pathogenetic importance in iron-overload disorders
    • P. Brissot, G. Zanninelli, D. Guyader, J. Zeind, and J. Gollan Biliary excretion of plasma non-transferrin-bound iron in rats: pathogenetic importance in iron-overload disorders Am. J. Physiol. 267 1994 G135 G142
    • (1994) Am. J. Physiol. , vol.267
    • Brissot, P.1    Zanninelli, G.2    Guyader, D.3    Zeind, J.4    Gollan, J.5
  • 72
    • 18244399587 scopus 로고    scopus 로고
    • Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver
    • H. Gunshin, Y. Fujiwara, A.O. Custodio, C. Direnzo, S. Robine, and N.C. Andrews Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver J. Clin. Invest. 115 2005 1258 1266
    • (2005) J. Clin. Invest. , vol.115 , pp. 1258-1266
    • Gunshin, H.1    Fujiwara, Y.2    Custodio, A.O.3    Direnzo, C.4    Robine, S.5    Andrews, N.C.6
  • 74
    • 84886264328 scopus 로고    scopus 로고
    • Tissue iron evaluation in chronically transfused children shows significant levels of iron loading at a very young age
    • V. Berdoukas, A. Nord, S. Carson, M. Puliyel, T. Hofstra, J. Wood, and T.D. Coates Tissue iron evaluation in chronically transfused children shows significant levels of iron loading at a very young age Am. J. Hematol. 88 2013 E283 E285
    • (2013) Am. J. Hematol. , vol.88
    • Berdoukas, V.1    Nord, A.2    Carson, S.3    Puliyel, M.4    Hofstra, T.5    Wood, J.6    Coates, T.D.7
  • 75
    • 0842263988 scopus 로고    scopus 로고
    • Localization of iron metabolism-related mRNAs in rat liver indicate that HFE is expressed predominantly in hepatocytes
    • A.S. Zhang, S. Xiong, H. Tsukamoto, and C.A. Enns Localization of iron metabolism-related mRNAs in rat liver indicate that HFE is expressed predominantly in hepatocytes Blood 103 2004 1509 1514
    • (2004) Blood , vol.103 , pp. 1509-1514
    • Zhang, A.S.1    Xiong, S.2    Tsukamoto, H.3    Enns, C.A.4
  • 76
    • 84857373097 scopus 로고    scopus 로고
    • Non-transferrin bound iron: A key role in iron overload and iron toxicity
    • P. Brissot, M. Ropert, C. Le Lan, 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 Lan, C.3    Loreal, O.4
  • 80
    • 0022624950 scopus 로고
    • Ultrastructural evidence for the presence of ferritin-iron in the biliary system of patients with iron overload
    • M.I. Cleton, J.W. Sindram, L.H. Rademakers, F.M. Zuyderhoudt, W.C. De Bruijn, and J.J. Marx Ultrastructural evidence for the presence of ferritin-iron in the biliary system of patients with iron overload Hepatology 6 1986 30 35
    • (1986) Hepatology , vol.6 , pp. 30-35
    • Cleton, M.I.1    Sindram, J.W.2    Rademakers, L.H.3    Zuyderhoudt, F.M.4    De Bruijn, W.C.5    Marx, J.J.6
  • 82
    • 0030913415 scopus 로고    scopus 로고
    • Intestinal absorption and enterohepatic cycling of biliary iron originating from plasma non-transferrin-bound iron in rats
    • P. Brissot, U. Bolder, C.D. Schteingart, J. Arnaud, and A.F. Hofmann Intestinal absorption and enterohepatic cycling of biliary iron originating from plasma non-transferrin-bound iron in rats Hepatology 25 1997 1457 1461
    • (1997) Hepatology , vol.25 , pp. 1457-1461
    • Brissot, P.1    Bolder, U.2    Schteingart, C.D.3    Arnaud, J.4    Hofmann, A.F.5
  • 83
  • 85
    • 0028933888 scopus 로고
    • Modulation by iron loading and chelation of the uptake of non-transferrin-bound iron by human liver cells
    • J.G. Parkes, E.W. Randell, N.F. Olivieri, and D.M. Templeton Modulation by iron loading and chelation of the uptake of non-transferrin-bound iron by human liver cells Biochim. Biophys. Acta 1243 1995 373 380
    • (1995) Biochim. Biophys. Acta , vol.1243 , pp. 373-380
    • Parkes, J.G.1    Randell, E.W.2    Olivieri, N.F.3    Templeton, D.M.4
  • 86
    • 0028244452 scopus 로고
    • Uptake of non-transferrin-bound iron by both reductive and nonreductive processes is modulated by intracellular iron
    • E.W. Randell, J.G. Parkes, N.F. Olivieri, and D.M. Templeton Uptake of non-transferrin-bound iron by both reductive and nonreductive processes is modulated by intracellular iron J. Biol. Chem. 269 1994 16046 16053
    • (1994) J. Biol. Chem. , vol.269 , pp. 16046-16053
    • Randell, E.W.1    Parkes, J.G.2    Olivieri, N.F.3    Templeton, D.M.4
  • 89
    • 84861187773 scopus 로고    scopus 로고
    • T-type calcium channel blockade improves survival and cardiovascular function in thalassemic mice
    • S. Kumfu, S. Chattipakorn, K. Chinda, S. Fucharoen, and N. Chattipakorn T-type calcium channel blockade improves survival and cardiovascular function in thalassemic mice Eur. J. Haematol. 88 2012 535 548
    • (2012) Eur. J. Haematol. , vol.88 , pp. 535-548
    • Kumfu, S.1    Chattipakorn, S.2    Chinda, K.3    Fucharoen, S.4    Chattipakorn, N.5
  • 91
    • 33646548593 scopus 로고    scopus 로고
    • Remodeling the regulation of iron metabolism during erythroid differentiation to ensure efficient heme biosynthesis
    • M. Schranzhofer, M. Schifrer, J.A. Cabrera, S. Kopp, P. Chiba, H. Beug, and E.W. Mullner Remodeling the regulation of iron metabolism during erythroid differentiation to ensure efficient heme biosynthesis Blood 107 2006 4159 4167
    • (2006) Blood , vol.107 , pp. 4159-4167
    • Schranzhofer, M.1    Schifrer, M.2    Cabrera, J.A.3    Kopp, S.4    Chiba, P.5    Beug, H.6    Mullner, E.W.7
  • 92
    • 0027190608 scopus 로고
    • Origin of a soluble truncated transferrin receptor
    • J. Ahn, and R.M. Johnstone Origin of a soluble truncated transferrin receptor Blood 81 1993 2442 2451
    • (1993) Blood , vol.81 , pp. 2442-2451
    • Ahn, J.1    Johnstone, R.M.2
  • 93
    • 0037093531 scopus 로고    scopus 로고
    • The mitochondrial protein frataxin prevents nuclear damage
    • G. Karthikeyan, L.K. Lewis, and M.A. Resnick The mitochondrial protein frataxin prevents nuclear damage Hum. Mol. Genet. 11 2002 1351 1362
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1351-1362
    • Karthikeyan, G.1    Lewis, L.K.2    Resnick, M.A.3
  • 94
    • 67749103803 scopus 로고    scopus 로고
    • Ineffective erythropoiesis and thalassemias
    • S. Rivella Ineffective erythropoiesis and thalassemias Curr. Opin. Hematol. 16 2009 187 194
    • (2009) Curr. Opin. Hematol. , vol.16 , pp. 187-194
    • Rivella, S.1
  • 98
    • 84055190801 scopus 로고    scopus 로고
    • Minihepcidins are rationally designed small peptides that mimic hepcidin activity in mice and may be useful for the treatment of iron overload
    • G.C. Preza, P. Ruchala, R. Pinon, E. Ramos, B. Qiao, M.A. Peralta, S. Sharma, A. Waring, T. Ganz, and E. Nemeth Minihepcidins are rationally designed small peptides that mimic hepcidin activity in mice and may be useful for the treatment of iron overload J. Clin. Invest. 121 2011 4880 4888
    • (2011) J. Clin. Invest. , vol.121 , pp. 4880-4888
    • Preza, G.C.1    Ruchala, P.2    Pinon, R.3    Ramos, E.4    Qiao, B.5    Peralta, M.A.6    Sharma, S.7    Waring, A.8    Ganz, T.9    Nemeth, E.10
  • 104
    • 84877309853 scopus 로고    scopus 로고
    • Pathophysiology and clinical manifestations of the beta-thalassemias
    • A.W. Nienhuis, and D.G. Nathan Pathophysiology and clinical manifestations of the beta-thalassemias Cold Spring Harbor Perspect. Med. 2 2012 a011726
    • (2012) Cold Spring Harbor Perspect. Med. , vol.2 , pp. 011726
    • Nienhuis, A.W.1    Nathan, D.G.2
  • 105
    • 84862573652 scopus 로고    scopus 로고
    • Pathophysiological and clinical aspects of iron chelation therapy in MDS
    • N. Gattermann Pathophysiological and clinical aspects of iron chelation therapy in MDS Curr. Pharm. Des. 18 2012 3222 3234
    • (2012) Curr. Pharm. Des. , vol.18 , pp. 3222-3234
    • Gattermann, N.1
  • 106
    • 84875155964 scopus 로고    scopus 로고
    • Gene therapy for hemoglobinopathies: Progress and challenges
    • A. Dong, S. Rivella, and L. Breda Gene therapy for hemoglobinopathies: progress and challenges Transl. Res. 161 2013 293 306
    • (2013) Transl. Res. , vol.161 , pp. 293-306
    • Dong, A.1    Rivella, S.2    Breda, L.3
  • 108
    • 84858153637 scopus 로고    scopus 로고
    • Congenital sideroblastic anemias: Iron and heme lost in mitochondrial translation
    • M.D. Fleming Congenital sideroblastic anemias: iron and heme lost in mitochondrial translation Hematol. Am. Soc. Hematol. Educ. Program 2011 2011 525 531
    • (2011) Hematol. Am. Soc. Hematol. Educ. Program , vol.2011 , pp. 525-531
    • Fleming, M.D.1
  • 110
    • 27944496081 scopus 로고    scopus 로고
    • Outcome of sickle cell anemia: A 4-decade observational study of 1056 patients
    • D.R. Powars, L.S. Chan, A. Hiti, E. Ramicone, and C. Johnson Outcome of sickle cell anemia: a 4-decade observational study of 1056 patients Medicine (Baltimore) 84 2005 363 376
    • (2005) Medicine (Baltimore) , vol.84 , pp. 363-376
    • Powars, D.R.1    Chan, L.S.2    Hiti, A.3    Ramicone, E.4    Johnson, C.5
  • 111
    • 77951712618 scopus 로고    scopus 로고
    • Improved survival of children and adolescents with sickle cell disease
    • C.T. Quinn, Z.R. Rogers, T.L. McCavit, and G.R. Buchanan Improved survival of children and adolescents with sickle cell disease Blood 115 2010 3447 3452
    • (2010) Blood , vol.115 , pp. 3447-3452
    • Quinn, C.T.1    Rogers, Z.R.2    McCavit, T.L.3    Buchanan, G.R.4
  • 113
    • 27644510463 scopus 로고    scopus 로고
    • Sickle cell disease: Clinical features and management
    • R. Hoffman, B. Furie, E.J. Benz, P. McGlave, L.E. Silberstein, S.J. Shattil, Churchill Livingstone Philadelphia
    • Y. Saunthararajah, and E. Vichinsky Sickle cell disease: clinical features and management R. Hoffman, B. Furie, E.J. Benz, P. McGlave, L.E. Silberstein, S.J. Shattil, Hematology: Basic Principles and Practice 2008 Churchill Livingstone Philadelphia
    • (2008) Hematology: Basic Principles and Practice
    • Saunthararajah, Y.1    Vichinsky, E.2
  • 114
    • 62949245936 scopus 로고    scopus 로고
    • Diamond-Blackfan anemia: Diagnosis, treatment, and molecular pathogenesis
    • J.M. Lipton, and S.R. Ellis Diamond-Blackfan anemia: diagnosis, treatment, and molecular pathogenesis Hematol. Oncol. Clin. North Am. 23 2009 261 282
    • (2009) Hematol. Oncol. Clin. North Am. , vol.23 , pp. 261-282
    • Lipton, J.M.1    Ellis, S.R.2
  • 116
    • 78651287827 scopus 로고    scopus 로고
    • Iron overload in MDS - Pathophysiology, diagnosis, and complications
    • N. Gattermann, and E.A. Rachmilewitz Iron overload in MDS - pathophysiology, diagnosis, and complications Ann. Hematol. 90 2011 1 10
    • (2011) Ann. Hematol. , vol.90 , pp. 1-10
    • Gattermann, N.1    Rachmilewitz, E.A.2
  • 118
    • 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
  • 120
    • 84870777376 scopus 로고    scopus 로고
    • How I manage patients with atypical microcytic anaemia
    • C. Camaschella How I manage patients with atypical microcytic anaemia Br. J. Haematol. 160 2013 12 24
    • (2013) Br. J. Haematol. , vol.160 , pp. 12-24
    • Camaschella, C.1
  • 121
    • 84856292277 scopus 로고    scopus 로고
    • Iron overload in human disease
    • R.E. Fleming, and P. Ponka Iron overload in human disease N. Engl. J. Med. 366 2012 348 359
    • (2012) N. Engl. J. Med. , vol.366 , pp. 348-359
    • Fleming, R.E.1    Ponka, P.2
  • 122
    • 78649634981 scopus 로고    scopus 로고
    • Hepcidin in human iron disorders: Therapeutic implications
    • A. Pietrangelo Hepcidin in human iron disorders: therapeutic implications J. Hepatol. 54 2011 173 181
    • (2011) J. Hepatol. , vol.54 , pp. 173-181
    • Pietrangelo, A.1
  • 123
    • 0035725868 scopus 로고    scopus 로고
    • Practical management of iron overload
    • J.B. Porter Practical management of iron overload Br. J. Haematol. 115 2001 239 252
    • (2001) Br. J. Haematol. , vol.115 , pp. 239-252
    • Porter, J.B.1
  • 126
    • 79960986069 scopus 로고    scopus 로고
    • Thalassemia syndromes
    • R. Hoffman, B. Furie, E.J. Benz, P. McGlave, L.E. Silberstein, S.J. Shattil, Churchill Livingstone Philadelphia
    • P.J. Giardina, and B.G. Forget Thalassemia syndromes R. Hoffman, B. Furie, E.J. Benz, P. McGlave, L.E. Silberstein, S.J. Shattil, Hematology: Basic Principles and Practice 2008 Churchill Livingstone Philadelphia 535 562
    • (2008) Hematology: Basic Principles and Practice , pp. 535-562
    • Giardina, P.J.1    Forget, B.G.2
  • 130
    • 23744459788 scopus 로고    scopus 로고
    • MRI R2 and R2* mapping accurately estimates hepatic iron concentration in transfusion-dependent thalassemia and sickle cell disease patients
    • J.C. Wood, C. Enriquez, N. Ghugre, J.M. Tyzka, S. Carson, M.D. Nelson, and T.D. Coates MRI R2 and R2* mapping accurately estimates hepatic iron concentration in transfusion-dependent thalassemia and sickle cell disease patients Blood 106 2005 1460 1465
    • (2005) Blood , vol.106 , pp. 1460-1465
    • Wood, J.C.1    Enriquez, C.2    Ghugre, N.3    Tyzka, J.M.4    Carson, S.5    Nelson, M.D.6    Coates, T.D.7
  • 131
    • 1442307460 scopus 로고    scopus 로고
    • Myocardial iron loading in transfusion-dependent thalassemia and sickle cell disease
    • J.C. Wood, J.M. Tyszka, S. Carson, M.D. Nelson, and T.D. Coates Myocardial iron loading in transfusion-dependent thalassemia and sickle cell disease Blood 103 2004 1934 1936
    • (2004) Blood , vol.103 , pp. 1934-1936
    • Wood, J.C.1    Tyszka, J.M.2    Carson, S.3    Nelson, M.D.4    Coates, T.D.5
  • 133
    • 77950442762 scopus 로고    scopus 로고
    • Pancreatic iron loading predicts cardiac iron loading in thalassemia major
    • L.J. Noetzli, J. Papudesi, T.D. Coates, and J.C. Wood Pancreatic iron loading predicts cardiac iron loading in thalassemia major Blood 114 2009 4021 4026
    • (2009) Blood , vol.114 , pp. 4021-4026
    • Noetzli, L.J.1    Papudesi, J.2    Coates, T.D.3    Wood, J.C.4
  • 135
    • 60549109901 scopus 로고    scopus 로고
    • Spleen R2 and R2* in iron-overloaded patients with sickle cell disease and thalassemia major
    • C.J. Brewer, T.D. Coates, and J.C. Wood Spleen R2 and R2* in iron-overloaded patients with sickle cell disease and thalassemia major J. Magn. Reson. Imaging 29 2009 357 364
    • (2009) J. Magn. Reson. Imaging , vol.29 , pp. 357-364
    • Brewer, C.J.1    Coates, T.D.2    Wood, J.C.3
  • 145
    • 79951838524 scopus 로고    scopus 로고
    • Relaxivity-iron calibration in hepatic iron overload: Probing underlying biophysical mechanisms using a Monte Carlo model
    • N.R. Ghugre, and J.C. Wood Relaxivity-iron calibration in hepatic iron overload: probing underlying biophysical mechanisms using a Monte Carlo model Magn. Reson. Med. 65 2011 837 847
    • (2011) Magn. Reson. Med. , vol.65 , pp. 837-847
    • Ghugre, N.R.1    Wood, J.C.2
  • 146
    • 0033871140 scopus 로고    scopus 로고
    • Does iron concentration in a liver needle biopsy accurately reflect hepatic iron burden in beta-thalassemia?
    • G. Crisponi, R. Ambu, F. Cristiani, G. Mancosu, V.M. Nurchi, R. Pinna, and G. Faa Does iron concentration in a liver needle biopsy accurately reflect hepatic iron burden in beta-thalassemia? Clin. Chem. 46 2000 1185 1188
    • (2000) Clin. Chem. , vol.46 , pp. 1185-1188
    • Crisponi, G.1    Ambu, R.2    Cristiani, F.3    Mancosu, G.4    Nurchi, V.M.5    Pinna, R.6    Faa, G.7
  • 148
    • 78650392267 scopus 로고    scopus 로고
    • Pancreatic iron loading in chronically transfused sickle cell disease is lower than in thalassaemia major
    • L.J. Noetzli, T.D. Coates, and J.C. Wood Pancreatic iron loading in chronically transfused sickle cell disease is lower than in thalassaemia major Br. J. Haematol. 152 2011 229 233
    • (2011) Br. J. Haematol. , vol.152 , pp. 229-233
    • Noetzli, L.J.1    Coates, T.D.2    Wood, J.C.3
  • 149
    • 7944230624 scopus 로고    scopus 로고
    • Myocardial iron clearance during reversal of siderotic cardiomyopathy with intravenous desferrioxamine: A prospective study using T2* cardiovascular magnetic resonance
    • L.J. Anderson, M.A. Westwood, S. Holden, B. Davis, E. Prescott, B. Wonke, J.B. Porter, J.M. Walker, and D.J. Pennell Myocardial iron clearance during reversal of siderotic cardiomyopathy with intravenous desferrioxamine: a prospective study using T2* cardiovascular magnetic resonance Br. J. Haematol. 127 2004 348 355
    • (2004) Br. J. Haematol. , vol.127 , pp. 348-355
    • Anderson, L.J.1    Westwood, M.A.2    Holden, S.3    Davis, B.4    Prescott, E.5    Wonke, B.6    Porter, J.B.7    Walker, J.M.8    Pennell, D.J.9
  • 150
    • 0011938460 scopus 로고
    • Tissue distribution and clearance kinetics of non-transferrin-bound iron in the hypotransferrinemic mouse: A rodent model for hemochromatosis
    • C.M. Craven, J. Alexander, M. Eldridge, J.P. Kushner, S. Bernstein, and J. Kaplan Tissue distribution and clearance kinetics of non-transferrin-bound iron in the hypotransferrinemic mouse: a rodent model for hemochromatosis Proc. Natl. Acad. Sci. USA 84 1987 3457 3461
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3457-3461
    • Craven, C.M.1    Alexander, J.2    Eldridge, M.3    Kushner, J.P.4    Bernstein, S.5    Kaplan, J.6
  • 151
    • 0023180854 scopus 로고
    • Ultrastructural observations in the carbonyl iron-fed rat, an animal model for hemochromatosis
    • T.C. Iancu, R.J. Ward, and T.J. Peters Ultrastructural observations in the carbonyl iron-fed rat, an animal model for hemochromatosis Virchows Arch. B 53 1987 208 217
    • (1987) Virchows Arch. B , vol.53 , pp. 208-217
    • Iancu, T.C.1    Ward, R.J.2    Peters, T.J.3
  • 152
    • 44949259826 scopus 로고    scopus 로고
    • Onset of cardiac iron loading in pediatric patients with thalassemia major
    • J.C. Wood, R. Origa, A. Agus, G. Matta, T.D. Coates, and R. Galanello Onset of cardiac iron loading in pediatric patients with thalassemia major Haematologica 93 2008 917 920
    • (2008) Haematologica , vol.93 , pp. 917-920
    • Wood, J.C.1    Origa, R.2    Agus, A.3    Matta, G.4    Coates, T.D.5    Galanello, R.6
  • 153
    • 72449151347 scopus 로고    scopus 로고
    • Non-transferrin-bound labile plasma iron and iron overload in sickle-cell disease: A comparative study between sickle-cell disease and beta-thalassemic patients
    • A. Koren, D. Fink, O. Admoni, Y. Tennenbaum-Rakover, and C. Levin Non-transferrin-bound labile plasma iron and iron overload in sickle-cell disease: a comparative study between sickle-cell disease and beta-thalassemic patients Eur. J. Haematol. 84 2010 72 78
    • (2010) Eur. J. Haematol. , vol.84 , pp. 72-78
    • Koren, A.1    Fink, D.2    Admoni, O.3    Tennenbaum-Rakover, Y.4    Levin, C.5
  • 157
    • 77953779950 scopus 로고    scopus 로고
    • The effect of deferasirox on cardiac iron in thalassemia major: Impact of total body iron stores
    • J.C. Wood, B.P. Kang, A. Thompson, P. Giardina, P. Harmatz, T. Glynos, C. Paley, and T.D. Coates The effect of deferasirox on cardiac iron in thalassemia major: impact of total body iron stores Blood 116 2010 537 543
    • (2010) Blood , vol.116 , pp. 537-543
    • Wood, J.C.1    Kang, B.P.2    Thompson, A.3    Giardina, P.4    Harmatz, P.5    Glynos, T.6    Paley, C.7    Coates, T.D.8
  • 158
    • 74049116227 scopus 로고    scopus 로고
    • Normalisation of total body iron load with very intensive combined chelation reverses cardiac and endocrine complications of thalassaemia major
    • K. Farmaki, I. Tzoumari, C. Pappa, G. Chouliaras, and V. Berdoukas Normalisation of total body iron load with very intensive combined chelation reverses cardiac and endocrine complications of thalassaemia major Br. J. Haematol. 148 2010 466 475
    • (2010) Br. J. Haematol. , vol.148 , pp. 466-475
    • Farmaki, K.1    Tzoumari, I.2    Pappa, C.3    Chouliaras, G.4    Berdoukas, V.5
  • 166
    • 0033833865 scopus 로고    scopus 로고
    • Juvenile hemochromatosis associated with B-thalassemia treated by phlebotomy and recombinant human erythropoietin
    • M. De Gobbi, P. Pasquero, F. Brunello, P. Paccotti, U. Mazza, and C. Camaschella Juvenile hemochromatosis associated with B-thalassemia treated by phlebotomy and recombinant human erythropoietin Haematologica 85 2000 865 867
    • (2000) Haematologica , vol.85 , pp. 865-867
    • De Gobbi, M.1    Pasquero, P.2    Brunello, F.3    Paccotti, P.4    Mazza, U.5    Camaschella, C.6
  • 167
    • 0034061096 scopus 로고    scopus 로고
    • Beta-Thalassemia trait might increase the severity of hemochromatosis in subjects with the C282Y mutation in the HFE gene
    • V.R. Arruda, M.F. Agostinho, R. Cancado, F.F. Costa, and S.T.O. Saad beta-Thalassemia trait might increase the severity of hemochromatosis in subjects with the C282Y mutation in the HFE gene Am. J. Hematol. 63 2000 (230-230)
    • (2000) Am. J. Hematol. , vol.63 , pp. 230-230
    • Arruda, V.R.1    Agostinho, M.F.2    Cancado, R.3    Costa, F.F.4    Saad, S.T.O.5
  • 169
    • 84869816833 scopus 로고    scopus 로고
    • Clinical spectrum and severity of hemolytic anemia in glucose 6-phosphate dehydrogenase-deficient children receiving dapsone
    • A. Pamba, N.D. Richardson, N. Carter, S. Duparc, Z. Premji, A.B. Tiono, and L. Luzzatto Clinical spectrum and severity of hemolytic anemia in glucose 6-phosphate dehydrogenase-deficient children receiving dapsone Blood 120 2012 4123 4133
    • (2012) Blood , vol.120 , pp. 4123-4133
    • Pamba, A.1    Richardson, N.D.2    Carter, N.3    Duparc, S.4    Premji, Z.5    Tiono, A.B.6    Luzzatto, L.7
  • 170
    • 79958074832 scopus 로고    scopus 로고
    • Thalassaemia and glucose-6-phosphate dehydrogenase deficiency in sickle-cell disorder patients in Taiz, Yemen
    • H.A. Al-Nood Thalassaemia and glucose-6-phosphate dehydrogenase deficiency in sickle-cell disorder patients in Taiz, Yemen East. Mediterr. Health J. 17 2011 404 408
    • (2011) East. Mediterr. Health J. , vol.17 , pp. 404-408
    • Al-Nood, H.A.1
  • 172
    • 58149143300 scopus 로고    scopus 로고
    • G6PD deficiency, absence of alpha-thalassemia and hemolytic rate at baseline are significant independent risk factors for abnormally high cerebral velocities in patients with sickle cell anemia
    • F. Bernaudin, S. Verlhac, S. Chevret, M. Torres, L. Coic, C. Arnaud, A. Kamdem, I. Hau, M.G. Neonato, and C. Delacourt G6PD deficiency, absence of alpha-thalassemia and hemolytic rate at baseline are significant independent risk factors for abnormally high cerebral velocities in patients with sickle cell anemia Blood 112 2008 4314 4317
    • (2008) Blood , vol.112 , pp. 4314-4317
    • Bernaudin, F.1    Verlhac, S.2    Chevret, S.3    Torres, M.4    Coic, L.5    Arnaud, C.6    Kamdem, A.7    Hau, I.8    Neonato, M.G.9    Delacourt, C.10
  • 174
    • 77951653109 scopus 로고    scopus 로고
    • Analysis of FOXO3 mutation in 114 Chinese women with premature ovarian failure
    • B. Wang, Y. Mu, F. Ni, S. Zhou, J. Wang, Y. Cao, and X. Ma Analysis of FOXO3 mutation in 114 Chinese women with premature ovarian failure Reprod. Biomed. Online 20 2010 499 503
    • (2010) Reprod. Biomed. Online , vol.20 , pp. 499-503
    • Wang, B.1    Mu, Y.2    Ni, F.3    Zhou, S.4    Wang, J.5    Cao, Y.6    Ma, X.7
  • 178
    • 51349117161 scopus 로고    scopus 로고
    • Oxidative stress in the regulation of normal and neoplastic hematopoiesis
    • S. Ghaffari Oxidative stress in the regulation of normal and neoplastic hematopoiesis Antioxid. Redox Signaling 10 2008 1923 1940
    • (2008) Antioxid. Redox Signaling , vol.10 , pp. 1923-1940
    • Ghaffari, S.1
  • 180
    • 84890922670 scopus 로고    scopus 로고
    • The role of iron and reactive oxygen species in cell death
    • S.J. Dixon, and B.R. Stockwell The role of iron and reactive oxygen species in cell death Nat. Chem. Biol. 10 2013 9 17
    • (2013) Nat. Chem. Biol. , vol.10 , pp. 9-17
    • Dixon, S.J.1    Stockwell, B.R.2
  • 181
    • 0032826029 scopus 로고    scopus 로고
    • The influence of hemochromatosis mutations on iron overload of thalassemia major
    • F. Longo, G. Zecchina, L. Sbaiz, R. Fischer, A. Piga, and C. Camaschella The influence of hemochromatosis mutations on iron overload of thalassemia major Haematologica 84 1999 799 803
    • (1999) Haematologica , vol.84 , pp. 799-803
    • Longo, F.1    Zecchina, G.2    Sbaiz, L.3    Fischer, R.4    Piga, A.5    Camaschella, C.6
  • 189
    • 0037222940 scopus 로고    scopus 로고
    • Relationship between hepatocellular injury and transfusional iron overload prior to and during iron chelation with desferrioxamine: A study in adult patients with acquired anemias
    • P.D. Jensen, F.T. Jensen, T. Christensen, J.L. Nielsen, and J. Ellegaard Relationship between hepatocellular injury and transfusional iron overload prior to and during iron chelation with desferrioxamine: a study in adult patients with acquired anemias Blood 101 2003 91 96
    • (2003) Blood , vol.101 , pp. 91-96
    • Jensen, P.D.1    Jensen, F.T.2    Christensen, T.3    Nielsen, J.L.4    Ellegaard, J.5
  • 190
  • 191
    • 33646075753 scopus 로고    scopus 로고
    • Oxidative status of valinomycin-resistant normal, beta-thalassemia and sickle red blood cells
    • J. Amer, Z. Etzion, R.M. Bookchin, and E. Fibach Oxidative status of valinomycin-resistant normal, beta-thalassemia and sickle red blood cells Biochim. Biophys. Acta 1760 2006 793 799
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 793-799
    • Amer, J.1    Etzion, Z.2    Bookchin, R.M.3    Fibach, E.4
  • 192
    • 38549144785 scopus 로고    scopus 로고
    • N-acetylcysteine amide (AD4) attenuates oxidative stress in beta-thalassemia blood cells
    • J. Amer, D. Atlas, and E. Fibach N-acetylcysteine amide (AD4) attenuates oxidative stress in beta-thalassemia blood cells Biochim. Biophys. Acta 1780 2008 249 255
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 249-255
    • Amer, J.1    Atlas, D.2    Fibach, E.3
  • 193
    • 59249091317 scopus 로고    scopus 로고
    • The role of oxidative stress in hemolytic anemia
    • E. Fibach, and E. Rachmilewitz The role of oxidative stress in hemolytic anemia Curr. Mol. Med. 8 2008 609 619
    • (2008) Curr. Mol. Med. , vol.8 , pp. 609-619
    • Fibach, E.1    Rachmilewitz, E.2
  • 194
    • 77955905915 scopus 로고    scopus 로고
    • The role of antioxidants and iron chelators in the treatment of oxidative stress in thalassemia
    • E. Fibach, and E.A. Rachmilewitz The role of antioxidants and iron chelators in the treatment of oxidative stress in thalassemia Ann. N. Y. Acad. Sci. 1202 2010 10 16
    • (2010) Ann. N. Y. Acad. Sci. , vol.1202 , pp. 10-16
    • Fibach, E.1    Rachmilewitz, E.A.2
  • 196
    • 0021093902 scopus 로고
    • Improved survival of iron-deficient patients with sickle erythrocytes
    • O. Castro, and T.B. Haddy Improved survival of iron-deficient patients with sickle erythrocytes N. Engl. J. Med. 308 1983 527
    • (1983) N. Engl. J. Med. , vol.308 , pp. 527
    • Castro, O.1    Haddy, T.B.2
  • 197
    • 0027930702 scopus 로고
    • Improvement of sickle cell anemia by iron-limited erythropoiesis
    • O. Castro, W.N. Poillon, H. Finke, and E. Massac Improvement of sickle cell anemia by iron-limited erythropoiesis Am. J. Hematol. 47 1994 74 81
    • (1994) Am. J. Hematol. , vol.47 , pp. 74-81
    • Castro, O.1    Poillon, W.N.2    Finke, H.3    Massac, E.4
  • 199
    • 0032896230 scopus 로고    scopus 로고
    • Deferiprone therapy in homozygous human beta-thalassemia removes erythrocyte membrane free iron and reduces KCl cotransport activity
    • L. de Franceschi, O. Shalev, A. Piga, M. Collell, O. Olivieri, R. Corrocher, R.P. Hebbel, and C. Brugnara Deferiprone therapy in homozygous human beta-thalassemia removes erythrocyte membrane free iron and reduces KCl cotransport activity J. Lab. Clin. Med. 133 1999 64 69
    • (1999) J. Lab. Clin. Med. , vol.133 , pp. 64-69
    • De Franceschi, L.1    Shalev, O.2    Piga, A.3    Collell, M.4    Olivieri, O.5    Corrocher, R.6    Hebbel, R.P.7    Brugnara, C.8
  • 202
    • 34250789093 scopus 로고    scopus 로고
    • Iron overload in patients with myelodysplastic syndromes
    • P.D. Jensen Iron overload in patients with myelodysplastic syndromes Curr. Hematol. Malig. Rep 2 2007 13 21
    • (2007) Curr. Hematol. Malig. Rep , vol.2 , pp. 13-21
    • Jensen, P.D.1
  • 205
    • 79952607559 scopus 로고    scopus 로고
    • Increased serum hepcidin levels during treatment with deferasirox in iron-overloaded patients with myelodysplastic syndrome
    • H. Ghoti, E. Fibach, M. Westerman, O. Gordana, T. Ganz, and E.A. Rachmilewitz Increased serum hepcidin levels during treatment with deferasirox in iron-overloaded patients with myelodysplastic syndrome Br. J. Haematol. 153 2011 118 120
    • (2011) Br. J. Haematol. , vol.153 , pp. 118-120
    • Ghoti, H.1    Fibach, E.2    Westerman, M.3    Gordana, O.4    Ganz, T.5    Rachmilewitz, E.A.6
  • 206
    • 77954338182 scopus 로고    scopus 로고
    • Iron chelation therapy associated with improvement of hematopoiesis in transfusion-dependent patients
    • E.N. Oliva, F. Ronco, A. Marino, C. Alati, G. Pratico, and F. Nobile Iron chelation therapy associated with improvement of hematopoiesis in transfusion-dependent patients Transfusion 50 2010 1568 1570
    • (2010) Transfusion , vol.50 , pp. 1568-1570
    • Oliva, E.N.1    Ronco, F.2    Marino, A.3    Alati, C.4    Pratico, G.5    Nobile, F.6
  • 207
    • 77953441332 scopus 로고    scopus 로고
    • Red blood cell transfusion independence following the initiation of iron chelation therapy in myelodysplastic syndrome
    • M.A. Badawi, L.M. Vickars, J.M. Chase, and H.A. Leitch Red blood cell transfusion independence following the initiation of iron chelation therapy in myelodysplastic syndrome Adv. Hematol. 2010 2010 164045
    • (2010) Adv. Hematol. , vol.2010 , pp. 164045
    • Badawi, M.A.1    Vickars, L.M.2    Chase, J.M.3    Leitch, H.A.4
  • 208
    • 52649145902 scopus 로고    scopus 로고
    • Deferasirox treatment improved the hemoglobin level and decreased transfusion requirements in four patients with the myelodysplastic syndrome and primary myelofibrosis
    • E. Messa, D. Cilloni, F. Messa, F. Arruga, A. Roetto, and G. Saglio Deferasirox treatment improved the hemoglobin level and decreased transfusion requirements in four patients with the myelodysplastic syndrome and primary myelofibrosis Acta Haematol. 120 2008 70 74
    • (2008) Acta Haematol. , vol.120 , pp. 70-74
    • Messa, E.1    Cilloni, D.2    Messa, F.3    Arruga, F.4    Roetto, A.5    Saglio, G.6
  • 210
    • 80055018836 scopus 로고    scopus 로고
    • Iron chelation therapy with deferasirox results in recovery of hematopoiesis in a child with aplastic anemia
    • J.W. Lee, P.S. Jang, N.G. Chung, B. Cho, D.C. Jeong, and H.K. Kim Iron chelation therapy with deferasirox results in recovery of hematopoiesis in a child with aplastic anemia Pediatr. Hematol. Oncol. 28 2011 718 720
    • (2011) Pediatr. Hematol. Oncol. , vol.28 , pp. 718-720
    • Lee, J.W.1    Jang, P.S.2    Chung, N.G.3    Cho, B.4    Jeong, D.C.5    Kim, H.K.6
  • 211
    • 78349260844 scopus 로고    scopus 로고
    • Restoration of hematopoiesis after iron chelation therapy with deferasirox in 2 children with severe aplastic anemia
    • K.N. Koh, M. Park, B.E. Kim, H.J. Im, and J.J. Seo Restoration of hematopoiesis after iron chelation therapy with deferasirox in 2 children with severe aplastic anemia J. Pediatr. Hematol. Oncol. 32 2010 611 614
    • (2010) J. Pediatr. Hematol. Oncol. , vol.32 , pp. 611-614
    • Koh, K.N.1    Park, M.2    Kim, B.E.3    Im, H.J.4    Seo, J.J.5
  • 212
    • 71049133629 scopus 로고    scopus 로고
    • Remission from transfusion-dependence in a patient with congenital dyserythropoietic anemia (CDA) and increased intensity of iron chelation
    • A.K. Bergmann, H. Tamary, and E.J. Neufeld Remission from transfusion-dependence in a patient with congenital dyserythropoietic anemia (CDA) and increased intensity of iron chelation Pediatr. Blood Cancer 53 2009 1167 1168
    • (2009) Pediatr. Blood Cancer , vol.53 , pp. 1167-1168
    • Bergmann, A.K.1    Tamary, H.2    Neufeld, E.J.3
  • 213
    • 84881669596 scopus 로고    scopus 로고
    • Free iron catalyzes oxidative damage to hematopoietic cells/mesenchymal stem cells in vitro and suppresses hematopoiesis in iron overload patients
    • W. Lu, M. Zhao, S. Rajbhandary, F. Xie, X. Chai, J. Mu, J. Meng, Y. Liu, Y. Jiang, X. Xu, and A. Meng Free iron catalyzes oxidative damage to hematopoietic cells/mesenchymal stem cells in vitro and suppresses hematopoiesis in iron overload patients Eur. J. Haematol. 91 2013 249 261
    • (2013) Eur. J. Haematol. , vol.91 , pp. 249-261
    • Lu, W.1    Zhao, M.2    Rajbhandary, S.3    Xie, F.4    Chai, X.5    Mu, J.6    Meng, J.7    Liu, Y.8    Jiang, Y.9    Xu, X.10    Meng, A.11
  • 216
    • 73149123769 scopus 로고    scopus 로고
    • Iron chelation therapy in MDS: What have we learnt recently?
    • M. Schmid Iron chelation therapy in MDS: what have we learnt recently? Blood Rev. 23 Suppl. 1 2009 S21 S25
    • (2009) Blood Rev. , vol.23 , Issue.SUPPL. 1
    • Schmid, M.1
  • 217
    • 84884950378 scopus 로고    scopus 로고
    • 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
    • T.S. Koskenkorva-Frank, G. Weiss, W.H. Koppenol, and S. Burckhardt 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 Free Radic. Biol. Med. 65 2013 1174 1194
    • (2013) Free Radic. Biol. Med. , vol.65 , pp. 1174-1194
    • Koskenkorva-Frank, T.S.1    Weiss, G.2    Koppenol, W.H.3    Burckhardt, S.4
  • 218
    • 41549136868 scopus 로고    scopus 로고
    • Sickle cell disease vasculopathy: A state of nitric oxide resistance
    • K.C. Wood, L.L. Hsu, and M.T. Gladwin Sickle cell disease vasculopathy: a state of nitric oxide resistance Free Radic. Biol. Med. 44 2008 1506 1528
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 1506-1528
    • Wood, K.C.1    Hsu, L.L.2    Gladwin, M.T.3
  • 219
    • 0029978555 scopus 로고    scopus 로고
    • Kinetics of removal and reappearance of non-transferrin-bound plasma iron with deferoxamine therapy
    • J.B. Porter, R.D. Abeysinghe, L. Marshall, R.C. Hider, and S. Singh Kinetics of removal and reappearance of non-transferrin-bound plasma iron with deferoxamine therapy Blood 88 1996 705 713
    • (1996) Blood , vol.88 , pp. 705-713
    • Porter, J.B.1    Abeysinghe, R.D.2    Marshall, L.3    Hider, R.C.4    Singh, S.5
  • 221
    • 0034651775 scopus 로고    scopus 로고
    • Long-term outcome of continuous 24-hour deferoxamine infusion via indwelling intravenous catheters in high-risk beta-thalassemia
    • B.A. Davis, and J.B. Porter Long-term outcome of continuous 24-hour deferoxamine infusion via indwelling intravenous catheters in high-risk beta-thalassemia Blood 95 2000 1229 1236
    • (2000) Blood , vol.95 , pp. 1229-1236
    • Davis, B.A.1    Porter, J.B.2
  • 223
    • 79951776374 scopus 로고    scopus 로고
    • Iron chelation in thalassemia: Time to reconsider our comfort zones
    • V. Berdoukas, K. Farmaki, J.C. Wood, and T. Coates Iron chelation in thalassemia: time to reconsider our comfort zones Expert Rev. Hematol. 4 2011 17 26
    • (2011) Expert Rev. Hematol. , vol.4 , pp. 17-26
    • Berdoukas, V.1    Farmaki, K.2    Wood, J.C.3    Coates, T.4
  • 224
    • 84896035687 scopus 로고    scopus 로고
    • Combination therapy of deferasirox and deferoxamine shows significant improvements in markers of iron overload in a patient with β-thalassemia major and severe iron burden
    • E. Voskaridou, V. Komninaka, A. Karavas, E. Terpos, V. Akianidis, and D. Christoulas Combination therapy of deferasirox and deferoxamine shows significant improvements in markers of iron overload in a patient with β-thalassemia major and severe iron burden Transfusion 54 2014 646 649
    • (2014) Transfusion , vol.54 , pp. 646-649
    • Voskaridou, E.1    Komninaka, V.2    Karavas, A.3    Terpos, E.4    Akianidis, V.5    Christoulas, D.6
  • 227
    • 79956311461 scopus 로고    scopus 로고
    • Oral chelators in transfusion-dependent thalassemia major patients may prevent or reverse iron overload complications
    • K. Farmaki, I. Tzoumari, and C. Pappa Oral chelators in transfusion-dependent thalassemia major patients may prevent or reverse iron overload complications Blood Cells Mol. Dis. 47 2011 33 40
    • (2011) Blood Cells Mol. Dis. , vol.47 , pp. 33-40
    • Farmaki, K.1    Tzoumari, I.2    Pappa, C.3
  • 228
    • 84890886606 scopus 로고    scopus 로고
    • Epidemiological and nonclinical studies investigating effects of iron in carcinogenesis - A critical review
    • Y. Beguin, M. Aapro, H. Ludwig, L. Mizzen, and A. Osterborg Epidemiological and nonclinical studies investigating effects of iron in carcinogenesis - a critical review Crit. Rev. Oncol./Hematol. 89 2014 1 15
    • (2014) Crit. Rev. Oncol./Hematol. , vol.89 , pp. 1-15
    • Beguin, Y.1    Aapro, M.2    Ludwig, H.3    Mizzen, L.4    Osterborg, A.5
  • 229
    • 84876854791 scopus 로고    scopus 로고
    • Iron and cancer: More ore to be mined
    • S.V. Torti, and F.M. Torti Iron and cancer: more ore to be mined Nat. Rev. Cancer 13 2013 342 355
    • (2013) Nat. Rev. Cancer , vol.13 , pp. 342-355
    • Torti, S.V.1    Torti, F.M.2
  • 233
    • 7044222320 scopus 로고    scopus 로고
    • Hemochromatosis, and hepatocellular carcinoma
    • K.V. Iron Kowdley hemochromatosis, and hepatocellular carcinoma Gastroenterology 127 2004 S79 S86
    • (2004) Gastroenterology , vol.127
    • Kowdley, K.V.I.1
  • 235
    • 84864928828 scopus 로고    scopus 로고
    • Association of projected transfusional iron burden with treatment intensity in childhood cancer survivors
    • K.S. Ruccione, K. Mudambi, R. Sposto, J. Fridey, S. Ghazarossian, and D.R. Freyer Association of projected transfusional iron burden with treatment intensity in childhood cancer survivors Pediatr. Blood Cancer 59 2012 697 702
    • (2012) Pediatr. Blood Cancer , vol.59 , pp. 697-702
    • Ruccione, K.S.1    Mudambi, K.2    Sposto, R.3    Fridey, J.4    Ghazarossian, S.5    Freyer, D.R.6
  • 236
    • 0037108199 scopus 로고    scopus 로고
    • The labile iron pool: Characterization, measurement, and participation in cellular processes
    • O. Kakhlon, and Z.I. Cabantchik The labile iron pool: characterization, measurement, and participation in cellular processes Free Radic. Biol. Med. 33 2002 1037 1046
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1037-1046
    • Kakhlon, O.1    Cabantchik, Z.I.2
  • 239
    • 84896460432 scopus 로고    scopus 로고
    • Combined therapy of iron chelator and antioxidant completely restores brain dysfunction induced by iron toxicity
    • J. Sripetchwandee, N. Pipatpiboon, N. Chattipakorn, and S. Chattipakorn Combined therapy of iron chelator and antioxidant completely restores brain dysfunction induced by iron toxicity PLoS One 9 2014 e85115
    • (2014) PLoS One , vol.9 , pp. 85115
    • Sripetchwandee, J.1    Pipatpiboon, N.2    Chattipakorn, N.3    Chattipakorn, S.4
  • 241
    • 84880356885 scopus 로고    scopus 로고
    • Deferiprone for the treatment of Friedreich's ataxia
    • M. Pandolfo, and L. Hausmann Deferiprone for the treatment of Friedreich's ataxia J. Neurochem. 126 Suppl. 1 2013 142 146
    • (2013) J. Neurochem. , vol.126 , Issue.SUPPL. 1 , pp. 142-146
    • Pandolfo, M.1    Hausmann, L.2
  • 242
    • 84899879296 scopus 로고    scopus 로고
    • Iron chelation for diseases of regional siderosis
    • C. Moreau, and D. Devos Iron chelation for diseases of regional siderosis Blood 122 2013 3435
    • (2013) Blood , vol.122 , pp. 3435
    • Moreau, C.1    Devos, D.2


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