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Volumn 504, Issue , 2020, Pages 180-189

Iron overload: Effects on cellular biochemistry

Author keywords

Antioxidant system; Iron; Membrane enzymes

Indexed keywords

ADENOSINE TRIPHOSPHATASE; HEPCIDIN; IRON REGULATORY FACTOR; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 2; SUPEROXIDE DISMUTASE; TRANSFERRIN RECEPTOR; TRANSFERRIN RECEPTOR 2;

EID: 85076604440     PISSN: 00098981     EISSN: 18733492     Source Type: Journal    
DOI: 10.1016/j.cca.2019.11.029     Document Type: Review
Times cited : (73)

References (208)
  • 1
    • 85042565450 scopus 로고    scopus 로고
    • Absorption mechanisms of iron, copper, and zinc: an overview
    • Nishito, Y., Kambe, T., Absorption mechanisms of iron, copper, and zinc: an overview. J. Nutr. Sci. Vitaminol. (Tokyo) 64:1 (2018), 1–7.
    • (2018) J. Nutr. Sci. Vitaminol. (Tokyo) , vol.64 , Issue.1 , pp. 1-7
    • Nishito, Y.1    Kambe, T.2
  • 2
    • 58049145622 scopus 로고    scopus 로고
    • Metabolismo do ferro: uma revisão sobre os principais mecanismos envolvidos em sua homeostase
    • Grotto, H.Z.W., Metabolismo do ferro: uma revisão sobre os principais mecanismos envolvidos em sua homeostase. Revista Brasileira de Hematologia e Hemoterapia 30 (2008), 390–397.
    • (2008) Revista Brasileira de Hematologia e Hemoterapia , vol.30 , pp. 390-397
    • Grotto, H.Z.W.1
  • 5
    • 0030886054 scopus 로고    scopus 로고
    • Reduced stress defense in heme oxygenase 1-deficient cells
    • Poss, K.D., Tonegawa, S., Reduced stress defense in heme oxygenase 1-deficient cells. Proc. Natl. Acad. Sci. USA 94:20 (1997), 10925–10930.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , Issue.20 , pp. 10925-10930
    • Poss, K.D.1    Tonegawa, S.2
  • 6
    • 0030886381 scopus 로고    scopus 로고
    • Heme oxygenase 1 is required for mammalian iron reutilization
    • Poss, K.D., Tonegawa, S., Heme oxygenase 1 is required for mammalian iron reutilization. PNAS 94:20 (1997), 10919–10924.
    • (1997) PNAS , vol.94 , Issue.20 , pp. 10919-10924
    • Poss, K.D.1    Tonegawa, S.2
  • 8
    • 33645307993 scopus 로고    scopus 로고
    • Complete loss of iron regulatory proteins 1 and 2 prevents viability of murine zygotes beyond the blastocyst stage of embryonic development
    • Smith, S.R., Ghosh, M.C., Ollivierre-Wilson, H., Hang Tong, W., Rouault, T.A., Complete loss of iron regulatory proteins 1 and 2 prevents viability of murine zygotes beyond the blastocyst stage of embryonic development. Blood Cells Mol. Dis. 36:2 (2006), 283–287.
    • (2006) Blood Cells Mol. Dis. , vol.36 , Issue.2 , pp. 283-287
    • Smith, S.R.1    Ghosh, M.C.2    Ollivierre-Wilson, H.3    Hang Tong, W.4    Rouault, T.A.5
  • 9
    • 77956654476 scopus 로고    scopus 로고
    • Interaction of iron regulatory protein-1 (IRP-1) with ATP/ADP maintains a non-IRE-binding state
    • Popovic, Z., Templeton, D.M., Interaction of iron regulatory protein-1 (IRP-1) with ATP/ADP maintains a non-IRE-binding state. Biochem. J. 430:2 (2010), 315–324.
    • (2010) Biochem. J. , vol.430 , Issue.2 , pp. 315-324
    • Popovic, Z.1    Templeton, D.M.2
  • 10
    • 85076603037 scopus 로고    scopus 로고
    • Magnetic Reporter Genes for MRI-Based Stem Cell Tracking
    • University of Liverpool Liverpool
    • Melo, Pereira S., Magnetic Reporter Genes for MRI-Based Stem Cell Tracking. 2015, University of Liverpool, Liverpool.
    • (2015)
    • Melo, P.S.1
  • 11
    • 2342440466 scopus 로고    scopus 로고
    • Disruption of ferroportin 1 regulation causes dynamic alterations in iron homeostasis and erythropoiesis in polycythaemia mice
    • Mok, H., Jelinek, J., Pai, S., Cattanach, B.M., Prchal, J.T., Youssoufian, H., et al. Disruption of ferroportin 1 regulation causes dynamic alterations in iron homeostasis and erythropoiesis in polycythaemia mice. Development 131:8 (2004), 1859–1868.
    • (2004) Development , vol.131 , Issue.8 , pp. 1859-1868
    • Mok, H.1    Jelinek, J.2    Pai, S.3    Cattanach, B.M.4    Prchal, J.T.5    Youssoufian, H.6
  • 13
    • 33646727321 scopus 로고    scopus 로고
    • The ins and outs of iron homeostasis
    • Donovan, A., Roy, C.N., Andrews, N.C., The ins and outs of iron homeostasis. Physiology 21:2 (2006), 115–123.
    • (2006) Physiology , vol.21 , Issue.2 , pp. 115-123
    • Donovan, A.1    Roy, C.N.2    Andrews, N.C.3
  • 14
    • 84984578714 scopus 로고    scopus 로고
    • Possible involvement of membrane lipids peroxidation and oxidation of catalytically essential thiols of the cerebral transmembrane sodium pump as component mechanisms of iron-mediated oxidative stress-linked dysfunction of the pump's activity
    • Omotayo, T.I., Akinyemi, G.S., Omololu, P.A., Ajayi, B.O., Akindahunsi, A.A., Rocha, J.B.T., et al. Possible involvement of membrane lipids peroxidation and oxidation of catalytically essential thiols of the cerebral transmembrane sodium pump as component mechanisms of iron-mediated oxidative stress-linked dysfunction of the pump's activity. Redox Biol. 4 (2015), 234–241.
    • (2015) Redox Biol. , vol.4 , pp. 234-241
    • Omotayo, T.I.1    Akinyemi, G.S.2    Omololu, P.A.3    Ajayi, B.O.4    Akindahunsi, A.A.5    Rocha, J.B.T.6
  • 15
    • 0035824070 scopus 로고    scopus 로고
    • Oxidative stress and p53 mutations in the carcinogenesis of iron overload-associated hepatocellular carcinoma
    • Marrogi, A.J., Khan, M.A., van Gijssel, H.E., Welsh, J.A., Rahim, H., Demetris, A.J., et al. Oxidative stress and p53 mutations in the carcinogenesis of iron overload-associated hepatocellular carcinoma. J. Natl. Cancer Inst. 93:21 (2001), 1652–1655.
    • (2001) J. Natl. Cancer Inst. , vol.93 , Issue.21 , pp. 1652-1655
    • Marrogi, A.J.1    Khan, M.A.2    van Gijssel, H.E.3    Welsh, J.A.4    Rahim, H.5    Demetris, A.J.6
  • 16
    • 33646855159 scopus 로고    scopus 로고
    • Evaluation of erythrocyte na+, k+ -atpase and superoxide dismutase activities and malondialdehyde level alteration in coal miners
    • Gürel, A., Armutçu, F., Damatoğlu, Ş., Unalacak, M., Demircan, N., Evaluation of erythrocyte na+, k+ -atpase and superoxide dismutase activities and malondialdehyde level alteration in coal miners. Eur. J. General Med. 1:4 (2004), 22–28.
    • (2004) Eur. J. General Med. , vol.1 , Issue.4 , pp. 22-28
    • Gürel, A.1    Armutçu, F.2    Damatoğlu, Ş.3    Unalacak, M.4    Demircan, N.5
  • 17
    • 0031032817 scopus 로고    scopus 로고
    • Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress
    • Yakes, F.M., Van Houten, B., Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress. Proc. Natl. Acad. Sci. 94:2 (1997), 514–519.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , Issue.2 , pp. 514-519
    • Yakes, F.M.1    Van Houten, B.2
  • 18
    • 84936120177 scopus 로고    scopus 로고
    • Modulation of Na+/K+ ATPase activity by hydrogen peroxide generated through Heme in L. amazonensis
    • Rocco-Machado, N., Cosentino-Gomes, D., Meyer-Fernandes, J.R., Modulation of Na+/K+ ATPase activity by hydrogen peroxide generated through Heme in L. amazonensis. PLoS ONE, 10(6), 2015, e0129604.
    • (2015) PLoS ONE , vol.10 , Issue.6
    • Rocco-Machado, N.1    Cosentino-Gomes, D.2    Meyer-Fernandes, J.R.3
  • 19
    • 84962949752 scopus 로고    scopus 로고
    • Iron Metabolism and Oxidative Stress
    • T. Miyata K.-U. Eckardt M. Nangaku Humana Press New York City
    • Zarjou, A., Balla, J., Balla, G., Agarwal, A., Iron Metabolism and Oxidative Stress. Miyata, T., Eckardt, K.-U., Nangaku, M., (eds.) Studies on Renal Disorders, 2011, Humana Press, New York City, 205–228.
    • (2011) Studies on Renal Disorders , pp. 205-228
    • Zarjou, A.1    Balla, J.2    Balla, G.3    Agarwal, A.4
  • 20
    • 85049076483 scopus 로고    scopus 로고
    • The effect of different digoxin concentrations on heart tissue and antioxidant status in iron-overloaded rats
    • Shahouzehi, B., Nasri, H.R., Masoumi-Ardakani, Y., The effect of different digoxin concentrations on heart tissue and antioxidant status in iron-overloaded rats. ARYA Atheroscler 14:2 (2018), 46–52.
    • (2018) ARYA Atheroscler , vol.14 , Issue.2 , pp. 46-52
    • Shahouzehi, B.1    Nasri, H.R.2    Masoumi-Ardakani, Y.3
  • 21
    • 0343866914 scopus 로고
    • Competitive inhibition by myoglobin of the reduction of cytochrome c by xanthine oxidase
    • Fridovich, I., Competitive inhibition by myoglobin of the reduction of cytochrome c by xanthine oxidase. J. Biol. Chem. 237 (1962), 584–586.
    • (1962) J. Biol. Chem. , vol.237 , pp. 584-586
    • Fridovich, I.1
  • 22
    • 84867881597 scopus 로고    scopus 로고
    • An in vitro approach to assess the neurotoxicity of valproic acid-induced oxidative stress in cerebellum and cerebral cortex of young rats
    • Chaudhary, S., Parvez, S., An in vitro approach to assess the neurotoxicity of valproic acid-induced oxidative stress in cerebellum and cerebral cortex of young rats. Neuroscience 225 (2012), 258–268.
    • (2012) Neuroscience , vol.225 , pp. 258-268
    • Chaudhary, S.1    Parvez, S.2
  • 23
    • 0030824218 scopus 로고    scopus 로고
    • Bone and joint involvement in genetic hemochromatosis: role of cirrhosis and iron overload
    • Sinigaglia, L., Fargion, S., Fracanzani, A.L., Binelli, L., Battafarano, N., Varenna, M., et al. Bone and joint involvement in genetic hemochromatosis: role of cirrhosis and iron overload. J. Rheumatol. 24:9 (1997), 1809–1813.
    • (1997) J. Rheumatol. , vol.24 , Issue.9 , pp. 1809-1813
    • Sinigaglia, L.1    Fargion, S.2    Fracanzani, A.L.3    Binelli, L.4    Battafarano, N.5    Varenna, M.6
  • 24
    • 0035127525 scopus 로고    scopus 로고
    • Increased cancer risk in a cohort of 230 patients with hereditary hemochromatosis in comparison to matched control patients with non–iron-related chronic liver disease
    • Fracanzani, A.L., Conte, D., Fraquelli, M., Taioli, E., Mattioli, M., Losco, A., et al. Increased cancer risk in a cohort of 230 patients with hereditary hemochromatosis in comparison to matched control patients with non–iron-related chronic liver disease. Hepatology 33:3 (2001), 647–651.
    • (2001) Hepatology , vol.33 , Issue.3 , pp. 647-651
    • Fracanzani, A.L.1    Conte, D.2    Fraquelli, M.3    Taioli, E.4    Mattioli, M.5    Losco, A.6
  • 25
    • 84876854791 scopus 로고    scopus 로고
    • Iron and cancer: more ore to be mined
    • Torti, S.V., Torti, F.M., Iron and cancer: more ore to be mined. Nat. Rev. Cancer 13:5 (2013), 342–355.
    • (2013) Nat. Rev. Cancer , vol.13 , Issue.5 , pp. 342-355
    • Torti, S.V.1    Torti, F.M.2
  • 26
    • 85019186592 scopus 로고    scopus 로고
    • Characterization of ferroptosis in murine models of hemochromatosis
    • Wang, H., An, P., Xie, E., Wu, Q., Fang, X., Gao, H., et al. Characterization of ferroptosis in murine models of hemochromatosis. Hepatology 66:2 (2017), 449–465.
    • (2017) Hepatology , vol.66 , Issue.2 , pp. 449-465
    • Wang, H.1    An, P.2    Xie, E.3    Wu, Q.4    Fang, X.5    Gao, H.6
  • 27
    • 84926387317 scopus 로고    scopus 로고
    • Ferroptosis as a p53-mediated activity during tumour suppression
    • Jiang, L., Kon, N., Li, T., Wang, S.-J., Su, T., Hibshoosh, H., et al. Ferroptosis as a p53-mediated activity during tumour suppression. Nature 520:7545 (2015), 57–62.
    • (2015) Nature , vol.520 , Issue.7545 , pp. 57-62
    • Jiang, L.1    Kon, N.2    Li, T.3    Wang, S.-J.4    Su, T.5    Hibshoosh, H.6
  • 28
    • 84942164064 scopus 로고    scopus 로고
    • Vacuolar-ATPase inhibition blocks iron metabolism to mediate therapeutic effects in breast cancer
    • Schneider, L.S., von Schwarzenberg, K., Lehr, T., Ulrich, M., Kubisch-Dohmen, R., Liebl, J., et al. Vacuolar-ATPase inhibition blocks iron metabolism to mediate therapeutic effects in breast cancer. Cancer Res. 75:14 (2015), 2863–2874.
    • (2015) Cancer Res. , vol.75 , Issue.14 , pp. 2863-2874
    • Schneider, L.S.1    von Schwarzenberg, K.2    Lehr, T.3    Ulrich, M.4    Kubisch-Dohmen, R.5    Liebl, J.6
  • 29
    • 0029555924 scopus 로고
    • Rabbit brain endoplasmic reticulum membranes as target for free radicals. Changes in Ca(2+)-transport and protection by stobadine
    • Racay, P., Kaplán, P., Lehotský, J., Mézesová, V., Rabbit brain endoplasmic reticulum membranes as target for free radicals. Changes in Ca(2+)-transport and protection by stobadine. Biochem. Mol. Biol. Int. 36:3 (1995), 569–577.
    • (1995) Biochem. Mol. Biol. Int. , vol.36 , Issue.3 , pp. 569-577
    • Racay, P.1    Kaplán, P.2    Lehotský, J.3    Mézesová, V.4
  • 30
    • 0030831615 scopus 로고    scopus 로고
    • Iron-induced inhibition of Na+, K+-ATPase and Na+/Ca2+ exchanger in synaptosomes: protection by the pyridoindole stobadine
    • Kaplán, P., Matejovičová, M., Mézešová, V., Iron-induced inhibition of Na+, K+-ATPase and Na+/Ca2+ exchanger in synaptosomes: protection by the pyridoindole stobadine. Neurochem. Res. 22:12 (1997), 1523–1529.
    • (1997) Neurochem. Res. , vol.22 , Issue.12 , pp. 1523-1529
    • Kaplán, P.1    Matejovičová, M.2    Mézešová, V.3
  • 31
    • 0032489095 scopus 로고    scopus 로고
    • Fe2+-induced inhibition of gerbil forebrain microsomal Ca2+-ATPase: effect of stobadine, glutathione and combination of both antioxidants
    • Račay, P., Qteishat, A.W.A., ElKambergy, H.M., Mézešová, V., Lehotský, J., Fe2+-induced inhibition of gerbil forebrain microsomal Ca2+-ATPase: effect of stobadine, glutathione and combination of both antioxidants. Biochim. Biophys. Acta (BBA) – Biomembr. 1370:1 (1998), 119–126.
    • (1998) Biochim. Biophys. Acta (BBA) – Biomembr. , vol.1370 , Issue.1 , pp. 119-126
    • Račay, P.1    Qteishat, A.W.A.2    ElKambergy, H.M.3    Mézešová, V.4    Lehotský, J.5
  • 32
    • 33748528638 scopus 로고    scopus 로고
    • Mitochondrial DNA damage associated with lipid peroxidation of the mitochondrial membrane induced by Fe2+-citrate
    • Almeida, A.M., Bertoncini, C.R., Borecký, J., Souza-Pinto, N.C., Vercesi, A.E., Mitochondrial DNA damage associated with lipid peroxidation of the mitochondrial membrane induced by Fe2+-citrate. An. Acad. Bras Cienc. 78:3 (2006), 505–514.
    • (2006) An. Acad. Bras Cienc. , vol.78 , Issue.3 , pp. 505-514
    • Almeida, A.M.1    Bertoncini, C.R.2    Borecký, J.3    Souza-Pinto, N.C.4    Vercesi, A.E.5
  • 34
    • 78649866553 scopus 로고    scopus 로고
    • Oxidant stress evoked by pacemaking in dopaminergic neurons is attenuated by DJ-1
    • Guzman, J.N., Sanchez-Padilla, J., Wokosin, D., Kondapalli, J., Ilijic, E., Schumacker, P.T., et al. Oxidant stress evoked by pacemaking in dopaminergic neurons is attenuated by DJ-1. Nature 468:7324 (2010), 696–700.
    • (2010) Nature , vol.468 , Issue.7324 , pp. 696-700
    • Guzman, J.N.1    Sanchez-Padilla, J.2    Wokosin, D.3    Kondapalli, J.4    Ilijic, E.5    Schumacker, P.T.6
  • 36
    • 4444274916 scopus 로고    scopus 로고
    • Labile plasma iron (LPI) as an indicator of chelatable plasma redox activity in iron-overloaded β-thalassemia/HbE patients treated with an oral chelator
    • Pootrakul, P., Breuer, W., Sametband, M., Sirankapracha, P., Hershko, C., Cabantchik, Z.I., Labile plasma iron (LPI) as an indicator of chelatable plasma redox activity in iron-overloaded β-thalassemia/HbE patients treated with an oral chelator. Blood 104:5 (2004), 1504–1510.
    • (2004) Blood , vol.104 , Issue.5 , pp. 1504-1510
    • Pootrakul, P.1    Breuer, W.2    Sametband, M.3    Sirankapracha, P.4    Hershko, C.5    Cabantchik, Z.I.6
  • 37
    • 33646351076 scopus 로고    scopus 로고
    • Role of L-type Ca2+ channels in iron transport and iron-overload cardiomyopathy
    • Oudit, G.Y., Trivieri, M.G., Khaper, N., Liu, P.P., Backx, P.H., Role of L-type Ca2+ channels in iron transport and iron-overload cardiomyopathy. J. Mol. Med. 84:5 (2006), 349–364.
    • (2006) J. Mol. Med. , vol.84 , Issue.5 , pp. 349-364
    • Oudit, G.Y.1    Trivieri, M.G.2    Khaper, N.3    Liu, P.P.4    Backx, P.H.5
  • 39
    • 84864312739 scopus 로고    scopus 로고
    • Protein degradation and iron homeostasis
    • Thompson, J.W., Bruick, R.K., Protein degradation and iron homeostasis. BBA 1823:9 (2012), 1484–1490.
    • (2012) BBA , vol.1823 , Issue.9 , pp. 1484-1490
    • Thompson, J.W.1    Bruick, R.K.2
  • 40
    • 85076587720 scopus 로고    scopus 로고
    • Prooxidant mechanisms in iron overload cardiomyopathy
    • Cheng, C.-F., Lian, W.-S., Prooxidant mechanisms in iron overload cardiomyopathy. Biomed. Res. Int., 2013, 2013, 8.
    • (2013) Biomed. Res. Int. , vol.2013 , pp. 8
    • Cheng, C.-F.1    Lian, W.-S.2
  • 41
  • 43
    • 84890922670 scopus 로고    scopus 로고
    • The role of iron and reactive oxygen species in cell death
    • Dixon, S.J., Stockwell, B.R., The role of iron and reactive oxygen species in cell death. Nat. Chem. Biol. 10:1 (2014), 9–17.
    • (2014) Nat. Chem. Biol. , vol.10 , Issue.1 , pp. 9-17
    • Dixon, S.J.1    Stockwell, B.R.2
  • 44
    • 84868109747 scopus 로고    scopus 로고
    • The ubiquity of iron
    • Frey, P.A., Reed, G.H., The ubiquity of iron. ACS Chem. Biol. 7:9 (2012), 1477–1481.
    • (2012) ACS Chem. Biol. , vol.7 , Issue.9 , pp. 1477-1481
    • Frey, P.A.1    Reed, G.H.2
  • 45
    • 84897019491 scopus 로고    scopus 로고
    • Nox enzymes and new thinking on reactive oxygen: a double-edged sword revisited
    • Lambeth, J.D., Neish, A.S., Nox enzymes and new thinking on reactive oxygen: a double-edged sword revisited. Annu. Rev. Pathol. 9 (2014), 119–145.
    • (2014) Annu. Rev. Pathol. , vol.9 , pp. 119-145
    • Lambeth, J.D.1    Neish, A.S.2
  • 46
    • 65449120792 scopus 로고    scopus 로고
    • Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases
    • Kell, D.B., Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases. BMC Med. Genomics., 2, 2009, 2.
    • (2009) BMC Med. Genomics. , vol.2 , pp. 2
    • Kell, D.B.1
  • 48
    • 0024402583 scopus 로고
    • Prevention of postischemic cardiac injury by the orally active iron chelator 1,2-dimethyl-3-hydroxy-4-pyridone (L1) and the antioxidant (+)-cyanidanol-3
    • van der Kraaij, A.M., van Eijk, H.G., Koster, J.F., Prevention of postischemic cardiac injury by the orally active iron chelator 1,2-dimethyl-3-hydroxy-4-pyridone (L1) and the antioxidant (+)-cyanidanol-3. Circulation 80:1 (1989), 158–164.
    • (1989) Circulation , vol.80 , Issue.1 , pp. 158-164
    • van der Kraaij, A.M.1    van Eijk, H.G.2    Koster, J.F.3
  • 49
    • 57249095767 scopus 로고    scopus 로고
    • Lipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids active in physiological and/or pathological conditions
    • Catalá, A., Lipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids active in physiological and/or pathological conditions. Chem. Phys. Lipids 157:1 (2009), 1–11.
    • (2009) Chem. Phys. Lipids , vol.157 , Issue.1 , pp. 1-11
    • Catalá, A.1
  • 51
    • 84866848255 scopus 로고    scopus 로고
    • 4-Hydroxy-2-nonenal, a reactive product of lipid peroxidation, and neurodegenerative diseases: a toxic combination illuminated by redox proteomics studies
    • Perluigi, M., Coccia, R., Butterfield, D.A., 4-Hydroxy-2-nonenal, a reactive product of lipid peroxidation, and neurodegenerative diseases: a toxic combination illuminated by redox proteomics studies. Antioxid. Redox Signal. 17:11 (2012), 1590–1609.
    • (2012) Antioxid. Redox Signal. , vol.17 , Issue.11 , pp. 1590-1609
    • Perluigi, M.1    Coccia, R.2    Butterfield, D.A.3
  • 52
    • 84941357200 scopus 로고    scopus 로고
    • Effects of iron overload on the activity of Na, K-ATPase and lipid profile of the human erythrocyte membrane
    • Sousa, L., Garcia, I.J.P., Costa, T.G.F., Silva, L.N.D., Renó, C.O., Oliveira, E.S., et al. Effects of iron overload on the activity of Na, K-ATPase and lipid profile of the human erythrocyte membrane. PLoS ONE, 10(7), 2015, e0132852.
    • (2015) PLoS ONE , vol.10 , Issue.7
    • Sousa, L.1    Garcia, I.J.P.2    Costa, T.G.F.3    Silva, L.N.D.4    Renó, C.O.5    Oliveira, E.S.6
  • 53
    • 0029932034 scopus 로고    scopus 로고
    • Iron-induced carcinogenesis: the role of redox regulation
    • Toyokuni, S., Iron-induced carcinogenesis: the role of redox regulation. Free Radic. Biol. Med. 20:4 (1996), 553–566.
    • (1996) Free Radic. Biol. Med. , vol.20 , Issue.4 , pp. 553-566
    • Toyokuni, S.1
  • 54
    • 77955938578 scopus 로고    scopus 로고
    • Which is the best way for estimating transferrin saturation?
    • Eleftheriadis, T., Liakopoulos, V., Antoniadi, G., Stefanidis, I., Which is the best way for estimating transferrin saturation?. Ren Fail. 32:8 (2010), 1022–1023.
    • (2010) Ren Fail. , vol.32 , Issue.8 , pp. 1022-1023
    • Eleftheriadis, T.1    Liakopoulos, V.2    Antoniadi, G.3    Stefanidis, I.4
  • 55
    • 0036156028 scopus 로고    scopus 로고
    • Bleomycin-detectable iron assay for non-transferrin-bound iron in hematologic malignancies
    • von Bonsdorff, L., Lindeberg, E., Sahlstedt, L., Lehto, J., Parkkinen, J., Bleomycin-detectable iron assay for non-transferrin-bound iron in hematologic malignancies. Clin. Chem. 48:2 (2002), 307–314.
    • (2002) Clin. Chem. , vol.48 , Issue.2 , pp. 307-314
    • von Bonsdorff, L.1    Lindeberg, E.2    Sahlstedt, L.3    Lehto, J.4    Parkkinen, J.5
  • 56
    • 58149458142 scopus 로고    scopus 로고
    • High nontransferrin bound iron levels and heart disease in thalassemia major
    • Piga, A., Longo, F., Duca, L., Roggero, S., Vinciguerra, T., Calabrese, R., et al. High nontransferrin bound iron levels and heart disease in thalassemia major. Am. J. Hematol. 84:1 (2009), 29–33.
    • (2009) Am. J. Hematol. , vol.84 , Issue.1 , pp. 29-33
    • Piga, A.1    Longo, F.2    Duca, L.3    Roggero, S.4    Vinciguerra, T.5    Calabrese, R.6
  • 58
    • 0005915035 scopus 로고    scopus 로고
    • Membrane fluidity of blood cells
    • Hollán, S., Membrane fluidity of blood cells. Haematologia (Budap). 27:3 (1996), 109–127.
    • (1996) Haematologia (Budap). , vol.27 , Issue.3 , pp. 109-127
    • Hollán, S.1
  • 59
    • 14644406192 scopus 로고    scopus 로고
    • Na, K-ATPase reconstituted in liposomes: effects of lipid composition on hydrolytic activity and enzyme orientation
    • de Lima, Santos H, Lopes, M.L., Maggio, B., Ciancaglini, P., Na, K-ATPase reconstituted in liposomes: effects of lipid composition on hydrolytic activity and enzyme orientation. Colloids Surf. B Biointerfaces 41:4 (2005), 239–248.
    • (2005) Colloids Surf. B Biointerfaces , vol.41 , Issue.4 , pp. 239-248
    • de Lima, S.H.1    Lopes, M.L.2    Maggio, B.3    Ciancaglini, P.4
  • 60
    • 33644996957 scopus 로고    scopus 로고
    • Kinetics behaviors of Na, K-ATPase: comparison of solubilized and DPPC:DPPE-liposome reconstituted enzyme
    • HeL, Santos, Rigos, C.F., Ciancaglini, P., Kinetics behaviors of Na, K-ATPase: comparison of solubilized and DPPC:DPPE-liposome reconstituted enzyme. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 142:3–4 (2006), 309–316.
    • (2006) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.142 , Issue.3-4 , pp. 309-316
    • HeL, S.1    Rigos, C.F.2    Ciancaglini, P.3
  • 61
    • 84876290140 scopus 로고    scopus 로고
    • Disorders of red cell volume regulation
    • Gallagher, P.G., Disorders of red cell volume regulation. Curr. Opin. Hematol. 20:3 (2013), 201–207.
    • (2013) Curr. Opin. Hematol. , vol.20 , Issue.3 , pp. 201-207
    • Gallagher, P.G.1
  • 62
    • 84978823269 scopus 로고    scopus 로고
    • Mechanisms involved in the in vitro contractile dysfunction induced by different concentrations of ferrous iron in the rat myocardium
    • Ávila, R.A., Silva, M.A.S.C., Peixoto, J.V., Kassouf-Silva, I., Fogaça, R.T.H., Dos Santos, L., Mechanisms involved in the in vitro contractile dysfunction induced by different concentrations of ferrous iron in the rat myocardium. Toxicol. In Vitro. 36 (2016), 38–45.
    • (2016) Toxicol. In Vitro. , vol.36 , pp. 38-45
    • Ávila, R.A.1    Silva, M.A.S.C.2    Peixoto, J.V.3    Kassouf-Silva, I.4    Fogaça, R.T.H.5    Dos Santos, L.6
  • 63
    • 0037173578 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of iron homeostasis and toxicity in mammalian cells
    • Crichton, R.R., Wilmet, S., Legssyer, R., Ward, R.J., Molecular and cellular mechanisms of iron homeostasis and toxicity in mammalian cells. J. Inorg. Biochem. 91:1 (2002), 9–18.
    • (2002) J. Inorg. Biochem. , vol.91 , Issue.1 , pp. 9-18
    • Crichton, R.R.1    Wilmet, S.2    Legssyer, R.3    Ward, R.J.4
  • 64
    • 35848942608 scopus 로고    scopus 로고
    • Heme oxygenase-1 in tumors: is it a false friend?
    • Jozkowicz, A., Was, H., Dulak, J., Heme oxygenase-1 in tumors: is it a false friend?. Antioxid. Redox Signal. 9:12 (2007), 2099–2117.
    • (2007) Antioxid. Redox Signal. , vol.9 , Issue.12 , pp. 2099-2117
    • Jozkowicz, A.1    Was, H.2    Dulak, J.3
  • 66
    • 0029002338 scopus 로고
    • Protection by lazaroids of the erythrocyte (Ca2+, Mg2+)-ATPase against iron-induced inhibition
    • Zaidi, A., Marden, M.C., Poyart, C., Leclerc, L., Protection by lazaroids of the erythrocyte (Ca2+, Mg2+)-ATPase against iron-induced inhibition. Eur. J. Pharmacol. 290:2 (1995), 133–139.
    • (1995) Eur. J. Pharmacol. , vol.290 , Issue.2 , pp. 133-139
    • Zaidi, A.1    Marden, M.C.2    Poyart, C.3    Leclerc, L.4
  • 67
    • 0019822476 scopus 로고
    • Acidic phospholipids, unsaturated fatty acids, and limited proteolysis mimic the effect of calmodulin on the purified erythrocyte Ca2+ - ATPase
    • Niggli, V., Adunyah, E.S., Carafoli, E., Acidic phospholipids, unsaturated fatty acids, and limited proteolysis mimic the effect of calmodulin on the purified erythrocyte Ca2+ - ATPase. J. Biol. Chem. 256:16 (1981), 8588–8592.
    • (1981) J. Biol. Chem. , vol.256 , Issue.16 , pp. 8588-8592
    • Niggli, V.1    Adunyah, E.S.2    Carafoli, E.3
  • 68
    • 84928624141 scopus 로고    scopus 로고
    • Differential calcium handling by the cis and trans regions of the Golgi apparatus
    • Aulestia, F.J., Alonso, M.T., García-Sancho, J., Differential calcium handling by the cis and trans regions of the Golgi apparatus. Biochem. J. 466:3 (2015), 455–465.
    • (2015) Biochem. J. , vol.466 , Issue.3 , pp. 455-465
    • Aulestia, F.J.1    Alonso, M.T.2    García-Sancho, J.3
  • 69
    • 20744450586 scopus 로고    scopus 로고
    • The secretory pathway Ca2+/Mn2+-ATPase 2 is a golgi-localized pump with high affinity for Ca2+ ions
    • Vanoevelen, J., Dode, L., Van Baelen, K., Fairclough, R.J., Missiaen, L., Raeymaekers, L., et al. The secretory pathway Ca2+/Mn2+-ATPase 2 is a golgi-localized pump with high affinity for Ca2+ ions. J. Biol. Chem. 280:24 (2005), 22800–22808.
    • (2005) J. Biol. Chem. , vol.280 , Issue.24 , pp. 22800-22808
    • Vanoevelen, J.1    Dode, L.2    Van Baelen, K.3    Fairclough, R.J.4    Missiaen, L.5    Raeymaekers, L.6
  • 70
    • 70349653079 scopus 로고    scopus 로고
    • Calcium pumps in health and disease
    • Brini, M., Carafoli, E., Calcium pumps in health and disease. Physiol. Rev. 89:4 (2009), 1341–1378.
    • (2009) Physiol. Rev. , vol.89 , Issue.4 , pp. 1341-1378
    • Brini, M.1    Carafoli, E.2
  • 71
    • 0025911829 scopus 로고
    • Metal-catalyzed oxidation of proteins. Physiological consequences
    • Stadtman, E.R., Oliver, C.N., Metal-catalyzed oxidation of proteins. Physiological consequences. J. Biol. Chem. 266:4 (1991), 2005–2008.
    • (1991) J. Biol. Chem. , vol.266 , Issue.4 , pp. 2005-2008
    • Stadtman, E.R.1    Oliver, C.N.2
  • 72
    • 0025257164 scopus 로고
    • Ascorbate protects against tert-butyl hydroperoxide inhibition of erythrocyte membrane Ca2+ + Mg2+-ATPase
    • Moore, R.B., Bamberg, A.D., Wilson, L.C., Jenkins, L.D., Mankad, V.N., Ascorbate protects against tert-butyl hydroperoxide inhibition of erythrocyte membrane Ca2+ + Mg2+-ATPase. Arch. Biochem. Biophys. 278:2 (1990), 416–424.
    • (1990) Arch. Biochem. Biophys. , vol.278 , Issue.2 , pp. 416-424
    • Moore, R.B.1    Bamberg, A.D.2    Wilson, L.C.3    Jenkins, L.D.4    Mankad, V.N.5
  • 74
    • 0030012353 scopus 로고    scopus 로고
    • Oxidative damage to sarcoplasmic reticulum Ca2+-pump induced by Fe2+/H2O2/ascorbate is not mediated by lipid peroxidation or thiol oxidation and leads to protein fragmentation
    • Castilho, R.F., Carvalho-Alves, P.C., Vercesi, A.E., Ferreira, S.T., Oxidative damage to sarcoplasmic reticulum Ca2+-pump induced by Fe2+/H2O2/ascorbate is not mediated by lipid peroxidation or thiol oxidation and leads to protein fragmentation. Mol. Cell. Biochem. 159:2 (1996), 105–114.
    • (1996) Mol. Cell. Biochem. , vol.159 , Issue.2 , pp. 105-114
    • Castilho, R.F.1    Carvalho-Alves, P.C.2    Vercesi, A.E.3    Ferreira, S.T.4
  • 75
    • 0027430035 scopus 로고
    • Structure-function relationships of cation binding in the Na+/K+-ATPase
    • Vasilets, L.A., Schwarz, W., Structure-function relationships of cation binding in the Na+/K+-ATPase. Biochim. Biophys. Acta (BBA) – Rev. Biomembr. 1154:2 (1993), 201–222.
    • (1993) Biochim. Biophys. Acta (BBA) – Rev. Biomembr. , vol.1154 , Issue.2 , pp. 201-222
    • Vasilets, L.A.1    Schwarz, W.2
  • 78
    • 0033794991 scopus 로고    scopus 로고
    • Effects of deferoxamine, a chelator of free iron, on Na+, K+-ATPase activity of cortical brain cell membrane during early reperfusion after hypoxia-ischemia in newborn lambs
    • Groenendaal, F., Shadid, M., McGowan, J.E., Mishra, O.P., van Bel, F., Effects of deferoxamine, a chelator of free iron, on Na+, K+-ATPase activity of cortical brain cell membrane during early reperfusion after hypoxia-ischemia in newborn lambs. Pediatr Res. 48:4 (2000), 560–564.
    • (2000) Pediatr Res. , vol.48 , Issue.4 , pp. 560-564
    • Groenendaal, F.1    Shadid, M.2    McGowan, J.E.3    Mishra, O.P.4    van Bel, F.5
  • 79
    • 0030886655 scopus 로고    scopus 로고
    • Fe-catalyzed cleavage of the α subunit of Na/K-ATPase: evidence for conformation-sensitive interactions between cytoplasmic domains
    • Goldshleger, R., Karlish, S.J.D., Fe-catalyzed cleavage of the α subunit of Na/K-ATPase: evidence for conformation-sensitive interactions between cytoplasmic domains. PNAS 94:18 (1997), 9596–9601.
    • (1997) PNAS , vol.94 , Issue.18 , pp. 9596-9601
    • Goldshleger, R.1    Karlish, S.J.D.2
  • 80
    • 0033523099 scopus 로고    scopus 로고
    • The energy transduction mechanism of Na, K-ATPase studied with iron-catalyzed oxidative cleavage
    • Goldshleger, R., Karlish, S.J.D., The energy transduction mechanism of Na, K-ATPase studied with iron-catalyzed oxidative cleavage. J. Biol. Chem. 274:23 (1999), 16213–16221.
    • (1999) J. Biol. Chem. , vol.274 , Issue.23 , pp. 16213-16221
    • Goldshleger, R.1    Karlish, S.J.D.2
  • 81
    • 0037903361 scopus 로고    scopus 로고
    • Investigating the energy transduction mechanism of P-type ATPases with Fe2+-catalyzed oxidative cleavage
    • Karlish, S.J., Investigating the energy transduction mechanism of P-type ATPases with Fe2+-catalyzed oxidative cleavage. Ann. N Y Acad. Sci. 986 (2003), 39–49.
    • (2003) Ann. N Y Acad. Sci. , vol.986 , pp. 39-49
    • Karlish, S.J.1
  • 82
    • 0027305716 scopus 로고
    • Effect of hyperbaric oxygenation on the Na+, K(+)-ATPase and membrane fluidity of cerebrocortical membranes after experimental subarachnoid hemorrhage
    • Yufu, K., Itoh, T., Edamatsu, R., Mori, A., Hirakawa, M., Effect of hyperbaric oxygenation on the Na+, K(+)-ATPase and membrane fluidity of cerebrocortical membranes after experimental subarachnoid hemorrhage. Neurochem. Res. 18:9 (1993), 1033–1039.
    • (1993) Neurochem. Res. , vol.18 , Issue.9 , pp. 1033-1039
    • Yufu, K.1    Itoh, T.2    Edamatsu, R.3    Mori, A.4    Hirakawa, M.5
  • 84
    • 0027364432 scopus 로고
    • Inhibition of the Ca pump of intact red blood cells by t-butyl hydroperoxide: importance of glutathione peroxidase
    • Rohn, T.T., Hinds, T.R., Vincenzi, F.F., Inhibition of the Ca pump of intact red blood cells by t-butyl hydroperoxide: importance of glutathione peroxidase. Biochim. Biophys. Acta (BBA) – Biomembr. 1153:1 (1993), 67–76.
    • (1993) Biochim. Biophys. Acta (BBA) – Biomembr. , vol.1153 , Issue.1 , pp. 67-76
    • Rohn, T.T.1    Hinds, T.R.2    Vincenzi, F.F.3
  • 85
    • 80051588227 scopus 로고    scopus 로고
    • The involvement of Na+, K+-ATPase activity and free radical generation in the susceptibility to pentylenetetrazol-induced seizures after experimental traumatic brain injury
    • Silva, L.F., Hoffmann, M.S., Rambo, L.M., Ribeiro, L.R., Lima, F.D., Furian, A.F., et al. The involvement of Na+, K+-ATPase activity and free radical generation in the susceptibility to pentylenetetrazol-induced seizures after experimental traumatic brain injury. J. Neurol. Sci. 308:1–2 (2011), 35–40.
    • (2011) J. Neurol. Sci. , vol.308 , Issue.1-2 , pp. 35-40
    • Silva, L.F.1    Hoffmann, M.S.2    Rambo, L.M.3    Ribeiro, L.R.4    Lima, F.D.5    Furian, A.F.6
  • 86
    • 0026549248 scopus 로고
    • Sarcolemmal Na(+)-K(+)-ATPase activity in congestive heart failure due to myocardial infarction
    • Dixon, I.M., Hata, T., Dhalla, N.S., Sarcolemmal Na(+)-K(+)-ATPase activity in congestive heart failure due to myocardial infarction. Am. J. Physiol. – Cell Physiol. 262:3 (1992), C664–C671.
    • (1992) Am. J. Physiol. – Cell Physiol. , vol.262 , Issue.3 , pp. C664-C671
    • Dixon, I.M.1    Hata, T.2    Dhalla, N.S.3
  • 87
    • 84880327550 scopus 로고    scopus 로고
    • Cardiovascular function and treatment in β-thalassemia major: a consensus statement from the American Heart Association
    • Pennell, D.J., Udelson, J.E., Arai, A.E., Bozkurt, B., Cohen, A.R., Galanello, R., et al. Cardiovascular function and treatment in β-thalassemia major: a consensus statement from the American Heart Association. Circulation 128:3 (2013), 281–308.
    • (2013) Circulation , vol.128 , Issue.3 , pp. 281-308
    • Pennell, D.J.1    Udelson, J.E.2    Arai, A.E.3    Bozkurt, B.4    Cohen, A.R.5    Galanello, R.6
  • 88
    • 78149284772 scopus 로고    scopus 로고
    • Iron-overload cardiomyopathy: pathophysiology, diagnosis, and treatment
    • Murphy, C.J., Oudit, G.Y., Iron-overload cardiomyopathy: pathophysiology, diagnosis, and treatment. J. Card Fail. 16:11 (2010), 888–900.
    • (2010) J. Card Fail. , vol.16 , Issue.11 , pp. 888-900
    • Murphy, C.J.1    Oudit, G.Y.2
  • 90
    • 84894165975 scopus 로고    scopus 로고
    • Cardiac mitochondria and reactive oxygen species generation
    • Chen, Y.-R., Zweier, J.L., Cardiac mitochondria and reactive oxygen species generation. Circ. Res. 114:3 (2014), 524–537.
    • (2014) Circ. Res. , vol.114 , Issue.3 , pp. 524-537
    • Chen, Y.-R.1    Zweier, J.L.2
  • 91
    • 84924299913 scopus 로고    scopus 로고
    • Cardiac ferroportin regulates cellular iron homeostasis and is important for cardiac function
    • Lakhal-Littleton, S., Wolna, M., Carr, C.A., Miller, J.J.J., Christian, H.C., Ball, V., et al. Cardiac ferroportin regulates cellular iron homeostasis and is important for cardiac function. PNAS 112:10 (2015), 3164–3169.
    • (2015) PNAS , vol.112 , Issue.10 , pp. 3164-3169
    • Lakhal-Littleton, S.1    Wolna, M.2    Carr, C.A.3    Miller, J.J.J.4    Christian, H.C.5    Ball, V.6
  • 92
    • 0018915753 scopus 로고
    • Enzymatic defenses of the mouse heart against reactive oxygen metabolites: alterations produced by doxorubicin
    • Doroshow, J.H., Locker, G.Y., Myers, C.E., Enzymatic defenses of the mouse heart against reactive oxygen metabolites: alterations produced by doxorubicin. J. Clin. Invest. 65:1 (1980), 128–135.
    • (1980) J. Clin. Invest. , vol.65 , Issue.1 , pp. 128-135
    • Doroshow, J.H.1    Locker, G.Y.2    Myers, C.E.3
  • 93
    • 0028244452 scopus 로고
    • Uptake of non-transferrin-bound iron by both reductive and nonreductive processes is modulated by intracellular iron
    • Randell, E.W., Parkes, J.G., Olivieri, N.F., Templeton, D.M., Uptake of non-transferrin-bound iron by both reductive and nonreductive processes is modulated by intracellular iron. J. Biol. Chem. 269:23 (1994), 16046–16053.
    • (1994) J. Biol. Chem. , vol.269 , Issue.23 , pp. 16046-16053
    • Randell, E.W.1    Parkes, J.G.2    Olivieri, N.F.3    Templeton, D.M.4
  • 94
    • 0033546223 scopus 로고    scopus 로고
    • Modulation of iron uptake in heart by L-type Ca2+ channel modifiers: possible implications in iron overload
    • Tsushima, R.G., Wickenden, A.D., Bouchard, R.A., Oudit, G.Y., Liu, P.P., Backx, P.H., Modulation of iron uptake in heart by L-type Ca2+ channel modifiers: possible implications in iron overload. Circ Res. 84:11 (1999), 1302–1309.
    • (1999) Circ Res. , vol.84 , Issue.11 , pp. 1302-1309
    • Tsushima, R.G.1    Wickenden, A.D.2    Bouchard, R.A.3    Oudit, G.Y.4    Liu, P.P.5    Backx, P.H.6
  • 95
    • 0141461407 scopus 로고    scopus 로고
    • L-type Ca2+ channels provide a major pathway for iron entry into cardiomyocytes in iron-overload cardiomyopathy
    • Oudit, G.Y., Sun, H., Trivieri, M.G., Koch, S.E., Dawood, F., Ackerley, C., et al. L-type Ca2+ channels provide a major pathway for iron entry into cardiomyocytes in iron-overload cardiomyopathy. Nat. Med. 9:9 (2003), 1187–1194.
    • (2003) Nat. Med. , vol.9 , Issue.9 , pp. 1187-1194
    • Oudit, G.Y.1    Sun, H.2    Trivieri, M.G.3    Koch, S.E.4    Dawood, F.5    Ackerley, C.6
  • 96
    • 84878962035 scopus 로고    scopus 로고
    • Management of the thalassemias. Cold Spring Harbor perspectives in medicine.3(6):a011767.
    • N.F. Olivieri, Brittenham GM. Management of the thalassemias. Cold Spring Harbor perspectives in medicine.3(6):a011767.
    • Olivieri, N.F.1    Brittenham, G.M.2
  • 99
    • 0032171640 scopus 로고    scopus 로고
    • Oxidative damage to sarcoplasmic reticulum Ca2+-ATPase AT submicromolar iron concentrations: evidence for metal-catalyzed oxidation
    • Moreau, V.H., Castilho, R.F., Ferreira, S.T., Carvalho-Alves, P.C., Oxidative damage to sarcoplasmic reticulum Ca2+-ATPase AT submicromolar iron concentrations: evidence for metal-catalyzed oxidation. Free Radic. Biol. Med. 25:4–5 (1998), 554–560.
    • (1998) Free Radic. Biol. Med. , vol.25 , Issue.4-5 , pp. 554-560
    • Moreau, V.H.1    Castilho, R.F.2    Ferreira, S.T.3    Carvalho-Alves, P.C.4
  • 100
    • 84949502640 scopus 로고    scopus 로고
    • Iron-overload injury and cardiomyopathy in acquired and genetic models is attenuated by resveratrol therapy
    • Das, S.K., Wang, W., Zhabyeyev, P., Basu, R., McLean, B., Fan, D., et al. Iron-overload injury and cardiomyopathy in acquired and genetic models is attenuated by resveratrol therapy. Sci. Rep., 5, 2015, 18132.
    • (2015) Sci. Rep. , vol.5 , pp. 18132
    • Das, S.K.1    Wang, W.2    Zhabyeyev, P.3    Basu, R.4    McLean, B.5    Fan, D.6
  • 102
    • 84974626015 scopus 로고    scopus 로고
    • Association of cardiac injury with iron-increased oxidative and nitrative modifications of the SERCA2a isoform of sarcoplasmic reticulum Ca2+-ATPase in diabetic rats
    • Li, X., Li, W., Gao, Z., Li, H., Association of cardiac injury with iron-increased oxidative and nitrative modifications of the SERCA2a isoform of sarcoplasmic reticulum Ca2+-ATPase in diabetic rats. Biochimie 127 (2016), 144–152.
    • (2016) Biochimie , vol.127 , pp. 144-152
    • Li, X.1    Li, W.2    Gao, Z.3    Li, H.4
  • 103
    • 77954145905 scopus 로고    scopus 로고
    • Mitochondrial dysfunction may explain the cardiomyopathy of chronic iron overload
    • Gao, X., Qian, M., Campian, J.L., Marshall, J., Zhou, Z., Roberts, A.M., et al. Mitochondrial dysfunction may explain the cardiomyopathy of chronic iron overload. Free Radical. Biol. Med. 49:3 (2010), 401–407.
    • (2010) Free Radical. Biol. Med. , vol.49 , Issue.3 , pp. 401-407
    • Gao, X.1    Qian, M.2    Campian, J.L.3    Marshall, J.4    Zhou, Z.5    Roberts, A.M.6
  • 104
    • 0037132637 scopus 로고    scopus 로고
    • Association between increased iron stores and impaired endothelial function in patients with hereditary hemochromatosis
    • Gaenzer, H., Marschang, P., Sturm, W., Gü, Neumayr, Vogel, W., Patsch, J., et al. Association between increased iron stores and impaired endothelial function in patients with hereditary hemochromatosis. J. Am. Coll. Cardiol. 40:12 (2002), 2189–2194.
    • (2002) J. Am. Coll. Cardiol. , vol.40 , Issue.12 , pp. 2189-2194
    • Gaenzer, H.1    Marschang, P.2    Sturm, W.3    Gü, N.4    Vogel, W.5    Patsch, J.6
  • 105
    • 0037159304 scopus 로고    scopus 로고
    • Iron therapy, advanced oxidation protein products, and carotid artery intima-media thickness in end-stage renal disease
    • Drüeke, T., Witko-Sarsat, V., Massy, Z., Descamps-Latscha, B., Guerin, A.P., Marchais, S.J., et al. Iron therapy, advanced oxidation protein products, and carotid artery intima-media thickness in end-stage renal disease. Circulation 106:17 (2002), 2212–2217.
    • (2002) Circulation , vol.106 , Issue.17 , pp. 2212-2217
    • Drüeke, T.1    Witko-Sarsat, V.2    Massy, Z.3    Descamps-Latscha, B.4    Guerin, A.P.5    Marchais, S.J.6
  • 106
    • 23044439090 scopus 로고    scopus 로고
    • Intravenous iron therapy as a possible risk factor for atherosclerosis in end-stage renal disease
    • Reis, K.A., Guz, G., Ozdemir, H., Erten, Y., Atalay, V., Bicik, Z., et al. Intravenous iron therapy as a possible risk factor for atherosclerosis in end-stage renal disease. Int. Heart J. 46:2 (2005), 255–264.
    • (2005) Int. Heart J. , vol.46 , Issue.2 , pp. 255-264
    • Reis, K.A.1    Guz, G.2    Ozdemir, H.3    Erten, Y.4    Atalay, V.5    Bicik, Z.6
  • 107
    • 84964355087 scopus 로고    scopus 로고
    • Iatrogenic iron overload in dialysis patients at the beginning of the 21st century
    • Rostoker, G., Vaziri, N.D., Fishbane, S., Iatrogenic iron overload in dialysis patients at the beginning of the 21st century. Drugs 76:7 (2016), 741–757.
    • (2016) Drugs , vol.76 , Issue.7 , pp. 741-757
    • Rostoker, G.1    Vaziri, N.D.2    Fishbane, S.3
  • 108
    • 84946001626 scopus 로고    scopus 로고
    • Chapter 24 – immune function in chronic kidney disease
    • P.L. Kimmel M.E. Rosenberg Academic Press San Diego
    • Pahl, M.V., Vaziri, N.D., Chapter 24 – immune function in chronic kidney disease. Kimmel, P.L., Rosenberg, M.E., (eds.) Chronic Renal Disease, 2015, Academic Press, San Diego, 285–297.
    • (2015) Chronic Renal Disease , pp. 285-297
    • Pahl, M.V.1    Vaziri, N.D.2
  • 109
    • 70449394604 scopus 로고    scopus 로고
    • Selective modulation of TLR4-activated inflammatory responses by altered iron homeostasis in mice
    • Wang, L., Harrington, L., Trebicka, E., Shi, H.N., Kagan, J.C., Hong, C.C., et al. Selective modulation of TLR4-activated inflammatory responses by altered iron homeostasis in mice. J. Clin. Investig. 119:11 (2009), 3322–3328.
    • (2009) J. Clin. Investig. , vol.119 , Issue.11 , pp. 3322-3328
    • Wang, L.1    Harrington, L.2    Trebicka, E.3    Shi, H.N.4    Kagan, J.C.5    Hong, C.C.6
  • 110
    • 79960681867 scopus 로고    scopus 로고
    • Low hepcidin accounts for the proinflammatory status associated with iron deficiency
    • Pagani, A., Nai, A., Corna, G., Bosurgi, L., Rovere-Querini, P., Camaschella, C., et al. Low hepcidin accounts for the proinflammatory status associated with iron deficiency. Blood 118:3 (2011), 736–746.
    • (2011) Blood , vol.118 , Issue.3 , pp. 736-746
    • Pagani, A.1    Nai, A.2    Corna, G.3    Bosurgi, L.4    Rovere-Querini, P.5    Camaschella, C.6
  • 112
    • 84865960840 scopus 로고    scopus 로고
    • Effect of iron overload on endocrinopathies in patients with beta-thalassaemia major and intermedia
    • Kurtoglu, A.U., Kurtoglu, E., Temizkan, A.K., Effect of iron overload on endocrinopathies in patients with beta-thalassaemia major and intermedia. Endokrynol Pol. 63:4 (2012), 260–263.
    • (2012) Endokrynol Pol. , vol.63 , Issue.4 , pp. 260-263
    • Kurtoglu, A.U.1    Kurtoglu, E.2    Temizkan, A.K.3
  • 113
    • 84925321769 scopus 로고    scopus 로고
    • Endocrine and bone complications in β-thalassemia intermedia: current understanding and treatment
    • Inati, A., Noureldine, M.A., Mansour, A., Abbas, H.A., Endocrine and bone complications in β-thalassemia intermedia: current understanding and treatment. Biomed. Res. Int., 2015, 2015, 813098-.
    • (2015) Biomed. Res. Int. , vol.2015 , pp. 813098-
    • Inati, A.1    Noureldine, M.A.2    Mansour, A.3    Abbas, H.A.4
  • 114
    • 9244230038 scopus 로고    scopus 로고
    • Oxidative stress, beta-cell apoptosis, and decreased insulin secretory capacity in mouse models of hemochromatosis
    • Cooksey, R.C., Jouihan, H.A., Ajioka, R.S., Hazel, M.W., Jones, D.L., Kushner, J.P., et al. Oxidative stress, beta-cell apoptosis, and decreased insulin secretory capacity in mouse models of hemochromatosis. Endocrinology 145:11 (2004), 5305–5312.
    • (2004) Endocrinology , vol.145 , Issue.11 , pp. 5305-5312
    • Cooksey, R.C.1    Jouihan, H.A.2    Ajioka, R.S.3    Hazel, M.W.4    Jones, D.L.5    Kushner, J.P.6
  • 115
    • 84889675405 scopus 로고    scopus 로고
    • At pharmacologically relevant concentrations intravenous iron preparations cause pancreatic beta cell death
    • Masuda, Y., Ichii, H., Vaziri, N.D., At pharmacologically relevant concentrations intravenous iron preparations cause pancreatic beta cell death. Am. J. Transl. Res. 6:1 (2013), 64–70.
    • (2013) Am. J. Transl. Res. , vol.6 , Issue.1 , pp. 64-70
    • Masuda, Y.1    Ichii, H.2    Vaziri, N.D.3
  • 116
    • 84901603732 scopus 로고    scopus 로고
    • Effects of iron overload on chronic metabolic diseases
    • Fernández-Real, J.M., Manco, M., Effects of iron overload on chronic metabolic diseases. Lancet Diabetes Endocrinol. 2:6 (2014), 513–526.
    • (2014) Lancet Diabetes Endocrinol. , vol.2 , Issue.6 , pp. 513-526
    • Fernández-Real, J.M.1    Manco, M.2
  • 118
    • 0027279232 scopus 로고
    • Diabetes mellitus and free radicals. Free radicals, transition metals and oxidative stress in the aetiology of diabetes mellitus and complications
    • Wolff, S.P., Diabetes mellitus and free radicals. Free radicals, transition metals and oxidative stress in the aetiology of diabetes mellitus and complications. Br. Med. Bull. 49:3 (1993), 642–652.
    • (1993) Br. Med. Bull. , vol.49 , Issue.3 , pp. 642-652
    • Wolff, S.P.1
  • 119
    • 35048833703 scopus 로고    scopus 로고
    • Non-transferrin-bound iron reaches mitochondria by a chelator-inaccessible mechanism: biological and clinical implications
    • Shvartsman, M., Kikkeri, R., Shanzer, A., Cabantchik, Z.I., Non-transferrin-bound iron reaches mitochondria by a chelator-inaccessible mechanism: biological and clinical implications. Am. J. Physiol. Cell Physiol. 293:4 (2007), C1383–C1394.
    • (2007) Am. J. Physiol. Cell Physiol. , vol.293 , Issue.4 , pp. C1383-C1394
    • Shvartsman, M.1    Kikkeri, R.2    Shanzer, A.3    Cabantchik, Z.I.4
  • 120
    • 1442314640 scopus 로고    scopus 로고
    • Body iron stores in relation to risk of type 2 diabetes in apparently healthy women
    • Jiang, R., Manson, J.E., Meigs, J.B., Ma, J., Rifai, N., Hu, F.B., Body iron stores in relation to risk of type 2 diabetes in apparently healthy women. JAMA 291:6 (2004), 711–717.
    • (2004) JAMA , vol.291 , Issue.6 , pp. 711-717
    • Jiang, R.1    Manson, J.E.2    Meigs, J.B.3    Ma, J.4    Rifai, N.5    Hu, F.B.6
  • 121
    • 85014181915 scopus 로고    scopus 로고
    • Clinical impact and cellular mechanisms of iron overload-associated bone loss
    • Jeney, V., Clinical impact and cellular mechanisms of iron overload-associated bone loss. Front. Pharmacol., 8, 2017, 77-.
    • (2017) Front. Pharmacol. , vol.8 , pp. 77-
    • Jeney, V.1
  • 122
    • 70349282987 scopus 로고    scopus 로고
    • Iron overload alters iron-regulatory genes and proteins, down-regulates osteoblastic phenotype, and is associated with apoptosis in fetal rat calvaria cultures
    • Messer, J.G., Kilbarger, A.K., Erikson, K.M., Kipp, D.E., Iron overload alters iron-regulatory genes and proteins, down-regulates osteoblastic phenotype, and is associated with apoptosis in fetal rat calvaria cultures. Bone 45:5 (2009), 972–979.
    • (2009) Bone , vol.45 , Issue.5 , pp. 972-979
    • Messer, J.G.1    Kilbarger, A.K.2    Erikson, K.M.3    Kipp, D.E.4
  • 124
    • 84861357425 scopus 로고    scopus 로고
    • The role of ineffective erythropoiesis in non-transfusion-dependent thalassemia
    • Rivella, S., The role of ineffective erythropoiesis in non-transfusion-dependent thalassemia. Blood Rev. 26:Suppl 1 (2012), S12–S15.
    • (2012) Blood Rev. , vol.26 , pp. S12-S15
    • Rivella, S.1
  • 126
    • 0024554054 scopus 로고
    • Osteoporosis in hemochromatosis: iron excess, gonadal deficiency, or other factors?
    • Diamond, T., Stiel, D., Posen, S., Osteoporosis in hemochromatosis: iron excess, gonadal deficiency, or other factors?. Ann. Int. Med. 110:6 (1989), 430–436.
    • (1989) Ann. Int. Med. , vol.110 , Issue.6 , pp. 430-436
    • Diamond, T.1    Stiel, D.2    Posen, S.3
  • 128
    • 29144461958 scopus 로고    scopus 로고
    • Tolis G. Osteoporosis in HFE2 juvenile hemochromatosis. A case report and review of the literature
    • Angelopoulos, N.G., Goula, A.K., Papanikolaou, G., Tolis G. Osteoporosis in HFE2 juvenile hemochromatosis. A case report and review of the literature. Osteoporos Int. 17:1 (2006), 150–155.
    • (2006) Osteoporos Int. , vol.17 , Issue.1 , pp. 150-155
    • Angelopoulos, N.G.1    Goula, A.K.2    Papanikolaou, G.3
  • 130
    • 0027051824 scopus 로고
    • Iron accumulation in human chronic renal disease
    • Nankivell, B.J., Boadle, R.A., Harris, D.C., Iron accumulation in human chronic renal disease. Am. J. Kidney Dis. 20:6 (1992), 580–584.
    • (1992) Am. J. Kidney Dis. , vol.20 , Issue.6 , pp. 580-584
    • Nankivell, B.J.1    Boadle, R.A.2    Harris, D.C.3
  • 131
    • 0034748257 scopus 로고    scopus 로고
    • Iron deposition in renal biopsy specimens from patients with kidney diseases
    • Wang, H., Nishiya, K., Ito, H., Hosokawa, T., Hashimoto, K., Moriki, T., Iron deposition in renal biopsy specimens from patients with kidney diseases. Am. J. Kidney Dis. 38:5 (2001), 1038–1044.
    • (2001) Am. J. Kidney Dis. , vol.38 , Issue.5 , pp. 1038-1044
    • Wang, H.1    Nishiya, K.2    Ito, H.3    Hosokawa, T.4    Hashimoto, K.5    Moriki, T.6
  • 132
    • 84885094738 scopus 로고    scopus 로고
    • Increased renal iron accumulation in hypertensive nephropathy of salt-loaded hypertensive rats
    • Naito, Y., Sawada, H., Oboshi, M., Fujii, A., Hirotani, S., Iwasaku, T., et al. Increased renal iron accumulation in hypertensive nephropathy of salt-loaded hypertensive rats. PLoS ONE, 8(10), 2013, e75906.
    • (2013) PLoS ONE , vol.8 , Issue.10
    • Naito, Y.1    Sawada, H.2    Oboshi, M.3    Fujii, A.4    Hirotani, S.5    Iwasaku, T.6
  • 133
    • 85005976093 scopus 로고    scopus 로고
    • Renal iron overload in rats with diabetic nephropathy
    • Dominguez, J.H., Liu, Y., Kelly, K.J., Renal iron overload in rats with diabetic nephropathy. Physiol. Rep., 3(12), 2015, e12654.
    • (2015) Physiol. Rep. , vol.3 , Issue.12
    • Dominguez, J.H.1    Liu, Y.2    Kelly, K.J.3
  • 136
    • 84937979950 scopus 로고    scopus 로고
    • Hepcidin mitigates renal ischemia-reperfusion injury by modulating systemic iron homeostasis
    • Scindia, Y., Dey, P., Thirunagari, A., Liping, H., Rosin, D.L., Floris, M., et al. Hepcidin mitigates renal ischemia-reperfusion injury by modulating systemic iron homeostasis. J. Am. Soc. Nephrol.: JASN 26:11 (2015), 2800–2814.
    • (2015) J. Am. Soc. Nephrol.: JASN , vol.26 , Issue.11 , pp. 2800-2814
    • Scindia, Y.1    Dey, P.2    Thirunagari, A.3    Liping, H.4    Rosin, D.L.5    Floris, M.6
  • 137
  • 138
    • 84952802841 scopus 로고    scopus 로고
    • Iron and the liver
    • Pietrangelo, A., Iron and the liver. Liver Int. 36:S1 (2016), 116–123.
    • (2016) Liver Int. , vol.36 , Issue.S1 , pp. 116-123
    • Pietrangelo, A.1
  • 139
    • 84956923279 scopus 로고    scopus 로고
    • Ineffective erythropoiesis and regulation of iron status in iron loading anaemias
    • Camaschella, C., Nai, A., Ineffective erythropoiesis and regulation of iron status in iron loading anaemias. Br. J. Haematol. 172:4 (2016), 512–523.
    • (2016) Br. J. Haematol. , vol.172 , Issue.4 , pp. 512-523
    • Camaschella, C.1    Nai, A.2
  • 140
    • 85006288786 scopus 로고    scopus 로고
    • Hepatocellular carcinoma as an emerging morbidity in the thalassemia syndromes: a comprehensive review
    • Moukhadder, H.M., Halawi, R., Cappellini, M.D., Taher, A.T., Hepatocellular carcinoma as an emerging morbidity in the thalassemia syndromes: a comprehensive review. Cancer 123:5 (2017), 751–758.
    • (2017) Cancer , vol.123 , Issue.5 , pp. 751-758
    • Moukhadder, H.M.1    Halawi, R.2    Cappellini, M.D.3    Taher, A.T.4
  • 144
    • 84892559263 scopus 로고    scopus 로고
    • Transcription factor NRF2 protects mice against dietary iron-induced liver injury by preventing hepatocytic cell death
    • Silva-Gomes, S., Santos, A.G., Caldas, C., Silva, C.M., Neves, J.V., Lopes, J., et al. Transcription factor NRF2 protects mice against dietary iron-induced liver injury by preventing hepatocytic cell death. J. Hepatol. 60:2 (2014), 354–361.
    • (2014) J. Hepatol. , vol.60 , Issue.2 , pp. 354-361
    • Silva-Gomes, S.1    Santos, A.G.2    Caldas, C.3    Silva, C.M.4    Neves, J.V.5    Lopes, J.6
  • 146
    • 84896470468 scopus 로고    scopus 로고
    • A randomized trial of iron depletion in patients with nonalcoholic fatty liver disease and hyperferritinemia
    • Valenti, L., Fracanzani, A.L., Dongiovanni, P., Rovida, S., Rametta, R., Fatta, E., et al. A randomized trial of iron depletion in patients with nonalcoholic fatty liver disease and hyperferritinemia. World J. Gastroenterol. 20:11 (2014), 3002–3010.
    • (2014) World J. Gastroenterol. , vol.20 , Issue.11 , pp. 3002-3010
    • Valenti, L.1    Fracanzani, A.L.2    Dongiovanni, P.3    Rovida, S.4    Rametta, R.5    Fatta, E.6
  • 147
    • 84929301137 scopus 로고    scopus 로고
    • ROS-mediated iron overload injures the hematopoiesis of bone marrow by damaging hematopoietic stem/progenitor cells in mice
    • Chai, X., Li, D., Cao, X., Zhang, Y., Mu, J., Lu, W., et al. ROS-mediated iron overload injures the hematopoiesis of bone marrow by damaging hematopoietic stem/progenitor cells in mice. Sci. Rep., 5, 2015, 10181.
    • (2015) Sci. Rep. , vol.5 , pp. 10181
    • Chai, X.1    Li, D.2    Cao, X.3    Zhang, Y.4    Mu, J.5    Lu, W.6
  • 148
    • 84862650577 scopus 로고    scopus 로고
    • The effect of iron overload and chelation on erythroid differentiation
    • Taoka, K., Kumano, K., Nakamura, F., Hosoi, M., Goyama, S., Imai, Y., et al. The effect of iron overload and chelation on erythroid differentiation. Int. J. Hematol. 95:2 (2012), 149–159.
    • (2012) Int. J. Hematol. , vol.95 , Issue.2 , pp. 149-159
    • Taoka, K.1    Kumano, K.2    Nakamura, F.3    Hosoi, M.4    Goyama, S.5    Imai, Y.6
  • 149
    • 0035103932 scopus 로고    scopus 로고
    • Iron, neuromelanin and ferritin content in the substantia nigra of normal subjects at different ages: consequences for iron storage and neurodegenerative processes
    • Zecca, L., Gallorini, M., Schünemann, V., Trautwein, A.X., Gerlach, M., Riederer, P., et al. Iron, neuromelanin and ferritin content in the substantia nigra of normal subjects at different ages: consequences for iron storage and neurodegenerative processes. J. Neurochem. 76:6 (2001), 1766–1773.
    • (2001) J. Neurochem. , vol.76 , Issue.6 , pp. 1766-1773
    • Zecca, L.1    Gallorini, M.2    Schünemann, V.3    Trautwein, A.X.4    Gerlach, M.5    Riederer, P.6
  • 150
    • 3042793602 scopus 로고    scopus 로고
    • The role of iron and copper molecules in the neuronal vulnerability of locus coeruleus and substantia nigra during aging
    • Zecca, L., Stroppolo, A., Gatti, A., Tampellini, D., Toscani, M., Gallorini, M., et al. The role of iron and copper molecules in the neuronal vulnerability of locus coeruleus and substantia nigra during aging. PNAS 101:26 (2004), 9843–9848.
    • (2004) PNAS , vol.101 , Issue.26 , pp. 9843-9848
    • Zecca, L.1    Stroppolo, A.2    Gatti, A.3    Tampellini, D.4    Toscani, M.5    Gallorini, M.6
  • 152
    • 84876361328 scopus 로고    scopus 로고
    • Role of brain iron accumulation in cognitive dysfunction: evidence from animal models and human studies
    • Schröder, N., Figueiredo, L.S., de Lima, M.N., Role of brain iron accumulation in cognitive dysfunction: evidence from animal models and human studies. J. Alzheimers Dis. 34:4 (2013), 797–812.
    • (2013) J. Alzheimers Dis. , vol.34 , Issue.4 , pp. 797-812
    • Schröder, N.1    Figueiredo, L.S.2    de Lima, M.N.3
  • 153
    • 84988380551 scopus 로고    scopus 로고
    • Metallo-pathways to Alzheimer's disease: lessons from genetic disorders of copper trafficking
    • Greenough, M.A., Ramírez Munoz, A., Bush, A.I., Opazo, C.M., Metallo-pathways to Alzheimer's disease: lessons from genetic disorders of copper trafficking. Metallomics 8:9 (2016), 831–839.
    • (2016) Metallomics , vol.8 , Issue.9 , pp. 831-839
    • Greenough, M.A.1    Ramírez Munoz, A.2    Bush, A.I.3    Opazo, C.M.4
  • 154
    • 37349032828 scopus 로고    scopus 로고
    • Iron toxicity as a potential factor in amd
    • Wong, R.W., Richa, D.C., Hahn, P., Green, W.R., Dunaief, J.L., Iron toxicity as a potential factor in amd. Retina 27:8 (2007), 997–1003.
    • (2007) Retina , vol.27 , Issue.8 , pp. 997-1003
    • Wong, R.W.1    Richa, D.C.2    Hahn, P.3    Green, W.R.4    Dunaief, J.L.5
  • 155
    • 84907999177 scopus 로고    scopus 로고
    • The role of iron in brain ageing and neurodegenerative disorders
    • Ward, R.J., Zucca, F.A., Duyn, J.H., Crichton, R.R., Zecca, L., The role of iron in brain ageing and neurodegenerative disorders. Lancet Neurol. 13:10 (2014), 1045–1060.
    • (2014) Lancet Neurol. , vol.13 , Issue.10 , pp. 1045-1060
    • Ward, R.J.1    Zucca, F.A.2    Duyn, J.H.3    Crichton, R.R.4    Zecca, L.5
  • 156
    • 84894475785 scopus 로고    scopus 로고
    • Brain iron homeostasis: from molecular mechanisms to clinical significance and therapeutic opportunities
    • Singh, N., Haldar, S., Tripathi, A.K., Horback, K., Wong, J., Sharma, D., et al. Brain iron homeostasis: from molecular mechanisms to clinical significance and therapeutic opportunities. Antioxid. Redox Signal. 20:8 (2014), 1324–1363.
    • (2014) Antioxid. Redox Signal. , vol.20 , Issue.8 , pp. 1324-1363
    • Singh, N.1    Haldar, S.2    Tripathi, A.K.3    Horback, K.4    Wong, J.5    Sharma, D.6
  • 158
    • 84880805523 scopus 로고    scopus 로고
    • Iron metabolism in the CNS: implications for neurodegenerative diseases
    • Rouault, T.A., Iron metabolism in the CNS: implications for neurodegenerative diseases. Nat. Rev. Neurosci. 14:8 (2013), 551–564.
    • (2013) Nat. Rev. Neurosci. , vol.14 , Issue.8 , pp. 551-564
    • Rouault, T.A.1
  • 159
    • 77954249308 scopus 로고    scopus 로고
    • Two to tango: regulation of mammalian iron metabolism
    • Hentze, M.W., Muckenthaler, M.U., Galy, B., Camaschella, C., Two to tango: regulation of mammalian iron metabolism. Cell 142:1 (2010), 24–38.
    • (2010) Cell , vol.142 , Issue.1 , pp. 24-38
    • Hentze, M.W.1    Muckenthaler, M.U.2    Galy, B.3    Camaschella, C.4
  • 160
    • 79952162002 scopus 로고    scopus 로고
    • Regulation of cellular iron metabolism
    • Wang, J., Pantopoulos, K., Regulation of cellular iron metabolism. Biochem. J. 434:3 (2011), 365–381.
    • (2011) Biochem. J. , vol.434 , Issue.3 , pp. 365-381
    • Wang, J.1    Pantopoulos, K.2
  • 162
    • 58549098084 scopus 로고    scopus 로고
    • Blood–brain barrier: ageing and microvascular disease – systematic review and meta-analysis
    • Farrall, A.J., Wardlaw, J.M., Blood–brain barrier: ageing and microvascular disease – systematic review and meta-analysis. Neurobiol. Aging 30:3 (2009), 337–352.
    • (2009) Neurobiol. Aging , vol.30 , Issue.3 , pp. 337-352
    • Farrall, A.J.1    Wardlaw, J.M.2
  • 163
    • 83855163999 scopus 로고    scopus 로고
    • Pathogenic implications of iron accumulation in multiple sclerosis
    • Williams, R., Buchheit, C.L., Berman, N.E.J., LeVine, S.M., Pathogenic implications of iron accumulation in multiple sclerosis. J. Neurochem. 120:1 (2012), 7–25.
    • (2012) J. Neurochem. , vol.120 , Issue.1 , pp. 7-25
    • Williams, R.1    Buchheit, C.L.2    Berman, N.E.J.3    LeVine, S.M.4
  • 165
    • 84885953717 scopus 로고    scopus 로고
    • Inflammation alters the expression of DMT1, FPN1 and hepcidin, and it causes iron accumulation in central nervous system cells
    • Urrutia, P., Aguirre, P., Esparza, A., Tapia, V., Mena, N.P., Arredondo, M., et al. Inflammation alters the expression of DMT1, FPN1 and hepcidin, and it causes iron accumulation in central nervous system cells. J. Neurochem. 126:4 (2013), 541–549.
    • (2013) J. Neurochem. , vol.126 , Issue.4 , pp. 541-549
    • Urrutia, P.1    Aguirre, P.2    Esparza, A.3    Tapia, V.4    Mena, N.P.5    Arredondo, M.6
  • 166
    • 0033947467 scopus 로고    scopus 로고
    • Sequestration of iron by Lewy bodies in Parkinson's disease
    • Castellani, R.J., Siedlak, S.L., Perry, G., Smith, M.A., Sequestration of iron by Lewy bodies in Parkinson's disease. Acta Neuropathol. 100:2 (2000), 111–114.
    • (2000) Acta Neuropathol. , vol.100 , Issue.2 , pp. 111-114
    • Castellani, R.J.1    Siedlak, S.L.2    Perry, G.3    Smith, M.A.4
  • 167
    • 0042433192 scopus 로고    scopus 로고
    • Neuromelanin associated redox-active iron is increased in the substantia nigra of patients with Parkinson's disease
    • Faucheux, B.A., Martin, M.-E., Beaumont, C., Hauw, J.-J., Agid, Y., Hirsch, E.C., Neuromelanin associated redox-active iron is increased in the substantia nigra of patients with Parkinson's disease. J. Neurochem. 86:5 (2003), 1142–1148.
    • (2003) J. Neurochem. , vol.86 , Issue.5 , pp. 1142-1148
    • Faucheux, B.A.1    Martin, M.-E.2    Beaumont, C.3    Hauw, J.-J.4    Agid, Y.5    Hirsch, E.C.6
  • 168
  • 169
    • 0026746512 scopus 로고
    • Neuromelanin-containing neurons of the substantia nigra accumulate iron and aluminum in Parkinson's disease: a LAMMA study
    • Good, P.F., Olanow, C.W., Perl, D.P., Neuromelanin-containing neurons of the substantia nigra accumulate iron and aluminum in Parkinson's disease: a LAMMA study. Brain Res. 593:2 (1992), 343–346.
    • (1992) Brain Res. , vol.593 , Issue.2 , pp. 343-346
    • Good, P.F.1    Olanow, C.W.2    Perl, D.P.3
  • 170
    • 84856708923 scopus 로고    scopus 로고
    • Tau deficiency induces parkinsonism with dementia by impairing APP-mediated iron export
    • Lei, P., Ayton, S., Finkelstein, D.I., Spoerri, L., Ciccotosto, G.D., Wright, D.K., et al. Tau deficiency induces parkinsonism with dementia by impairing APP-mediated iron export. Nat. Med. 18:2 (2012), 291–295.
    • (2012) Nat. Med. , vol.18 , Issue.2 , pp. 291-295
    • Lei, P.1    Ayton, S.2    Finkelstein, D.I.3    Spoerri, L.4    Ciccotosto, G.D.5    Wright, D.K.6
  • 171
    • 77956647381 scopus 로고    scopus 로고
    • Iron-export ferroxidase activity of β-amyloid precursor protein is inhibited by zinc in Alzheimer's disease
    • Duce, J.A., Tsatsanis, A., Cater, M.A., James, S.A., Robb, E., Wikhe, K., et al. Iron-export ferroxidase activity of β-amyloid precursor protein is inhibited by zinc in Alzheimer's disease. Cell 142:6 (2010), 857–867.
    • (2010) Cell , vol.142 , Issue.6 , pp. 857-867
    • Duce, J.A.1    Tsatsanis, A.2    Cater, M.A.3    James, S.A.4    Robb, E.5    Wikhe, K.6
  • 172
    • 0242684415 scopus 로고    scopus 로고
    • Genetic or pharmacological iron chelation prevents MPTP-induced neurotoxicity in vivo: a novel therapy for Parkinson's disease
    • Kaur, D., Yantiri, F., Rajagopalan, S., Kumar, J., Mo, J.Q., Boonplueang, R., et al. Genetic or pharmacological iron chelation prevents MPTP-induced neurotoxicity in vivo: a novel therapy for Parkinson's disease. Neuron 37:6 (2003), 899–909.
    • (2003) Neuron , vol.37 , Issue.6 , pp. 899-909
    • Kaur, D.1    Yantiri, F.2    Rajagopalan, S.3    Kumar, J.4    Mo, J.Q.5    Boonplueang, R.6
  • 173
    • 0026015052 scopus 로고
    • Catechol oxidation by peroxidase-positive astrocytes in primary culture: an electron spin resonance study
    • Schipper, H., Kotake, Y., Janzen, E., Catechol oxidation by peroxidase-positive astrocytes in primary culture: an electron spin resonance study. J. Neurosci. 11:7 (1991), 2170–2176.
    • (1991) J. Neurosci. , vol.11 , Issue.7 , pp. 2170-2176
    • Schipper, H.1    Kotake, Y.2    Janzen, E.3
  • 174
    • 0001672745 scopus 로고    scopus 로고
    • Intraneuronal dopamine-quinone synthesis: a review
    • Sulzer, D., Zecca, L., Intraneuronal dopamine-quinone synthesis: a review. Neurotox Res. 1:3 (2000), 181–195.
    • (2000) Neurotox Res. , vol.1 , Issue.3 , pp. 181-195
    • Sulzer, D.1    Zecca, L.2
  • 176
    • 85015193487 scopus 로고    scopus 로고
    • Overview of iron metabolism in health and disease. Hemodialysis international International Symposium on Home Hemodialysis 21 (Suppl 1), S6–S20.
    • S. Dev, J.L. Babitt, Overview of iron metabolism in health and disease. Hemodialysis international International Symposium on Home Hemodialysis, 2017, 21 (Suppl 1), S6–S20.
    • (2017)
    • Dev, S.1    Babitt, J.L.2
  • 178
    • 85042114202 scopus 로고    scopus 로고
    • Iron overload accelerates the progression of diabetic retinopathy in association with increased retinal renin expression
    • Chaudhary, K., Promsote, W., Ananth, S., Veeranan-Karmegam, R., Tawfik, A., Arjunan, P., et al. Iron overload accelerates the progression of diabetic retinopathy in association with increased retinal renin expression. Sci. Rep., 8(1), 2018, 3025.
    • (2018) Sci. Rep. , vol.8 , Issue.1 , pp. 3025
    • Chaudhary, K.1    Promsote, W.2    Ananth, S.3    Veeranan-Karmegam, R.4    Tawfik, A.5    Arjunan, P.6
  • 179
    • 0141671890 scopus 로고    scopus 로고
    • Unusual susceptibility of heme proteins to damage by glucose during non-enzymatic glycation
    • Cussimanio, B.L., Booth, A.A., Todd, P., Hudson, B.G., Khalifah, R.G., Unusual susceptibility of heme proteins to damage by glucose during non-enzymatic glycation. Biophys. Chem. 105:2–3 (2003), 743–755.
    • (2003) Biophys. Chem. , vol.105 , Issue.2-3 , pp. 743-755
    • Cussimanio, B.L.1    Booth, A.A.2    Todd, P.3    Hudson, B.G.4    Khalifah, R.G.5
  • 180
    • 70450209180 scopus 로고    scopus 로고
    • Absence of iron-regulatory protein Hfe results in hyperproliferation of retinal pigment epithelium: role of cystine/glutamate exchanger
    • Gnana-Prakasam, J.P., Thangaraju, M., Liu, K., Ha, Y., Martin, P.M., Smith, S.B., et al. Absence of iron-regulatory protein Hfe results in hyperproliferation of retinal pigment epithelium: role of cystine/glutamate exchanger. Biochem. J. 424:2 (2009), 243–252.
    • (2009) Biochem. J. , vol.424 , Issue.2 , pp. 243-252
    • Gnana-Prakasam, J.P.1    Thangaraju, M.2    Liu, K.3    Ha, Y.4    Martin, P.M.5    Smith, S.B.6
  • 182
    • 12244262242 scopus 로고    scopus 로고
    • Increased content of zinc and iron in human cataractous lenses
    • Dawczynski, J., Blum, M., Winnefeld, K., Strobel, J., Increased content of zinc and iron in human cataractous lenses. Biol. Trace Elem. Res. 90:1–3 (2002), 15–23.
    • (2002) Biol. Trace Elem. Res. , vol.90 , Issue.1-3 , pp. 15-23
    • Dawczynski, J.1    Blum, M.2    Winnefeld, K.3    Strobel, J.4
  • 184
    • 80051924706 scopus 로고    scopus 로고
    • The 'incessant menstruation' hypothesis: a mechanistic ovarian cancer model with implications for prevention
    • Vercellini, P., Crosignani, P., Somigliana, E., Viganò, P., Buggio, L., Bolis, G., et al. The 'incessant menstruation' hypothesis: a mechanistic ovarian cancer model with implications for prevention. Hum. Reprod. 26:9 (2011), 2262–2273.
    • (2011) Hum. Reprod. , vol.26 , Issue.9 , pp. 2262-2273
    • Vercellini, P.1    Crosignani, P.2    Somigliana, E.3    Viganò, P.4    Buggio, L.5    Bolis, G.6
  • 185
    • 40749162395 scopus 로고    scopus 로고
    • Contents of endometriotic cysts, especially the high concentration of free iron, are a possible cause of carcinogenesis in the cysts through the iron-induced persistent oxidative stress
    • Yamaguchi, K., Mandai, M., Toyokuni, S., Hamanishi, J., Higuchi, T., Takakura, K., et al. Contents of endometriotic cysts, especially the high concentration of free iron, are a possible cause of carcinogenesis in the cysts through the iron-induced persistent oxidative stress. Clin. Cancer Res. 14:1 (2008), 32–40.
    • (2008) Clin. Cancer Res. , vol.14 , Issue.1 , pp. 32-40
    • Yamaguchi, K.1    Mandai, M.2    Toyokuni, S.3    Hamanishi, J.4    Higuchi, T.5    Takakura, K.6
  • 186
    • 84883447571 scopus 로고    scopus 로고
    • The presence of mucosal iron in the fallopian tube supports the “incessant menstruation hypothesis” for ovarian carcinoma
    • Seidman, J.D., The presence of mucosal iron in the fallopian tube supports the “incessant menstruation hypothesis” for ovarian carcinoma. Int. J. Gynecol. Pathol. 32:5 (2013), 454–458.
    • (2013) Int. J. Gynecol. Pathol. , vol.32 , Issue.5 , pp. 454-458
    • Seidman, J.D.1
  • 187
    • 0031441858 scopus 로고    scopus 로고
    • Preferential mitochondrial DNA injury caused by glucose oxidase as a steady generator of hydrogen peroxide in human fibroblasts
    • Salazar, J.J., Van Houten, B., Preferential mitochondrial DNA injury caused by glucose oxidase as a steady generator of hydrogen peroxide in human fibroblasts. Mutation Res./DNA Repair 385:2 (1997), 139–149.
    • (1997) Mutation Res./DNA Repair , vol.385 , Issue.2 , pp. 139-149
    • Salazar, J.J.1    Van Houten, B.2
  • 188
    • 84878537085 scopus 로고    scopus 로고
    • Oxidative DNA damage and nucleotide excision repair
    • Melis, J.P.M., van Steeg, H., Luijten, M., Oxidative DNA damage and nucleotide excision repair. Antioxid. Redox Signal. 18:18 (2013), 2409–2419.
    • (2013) Antioxid. Redox Signal. , vol.18 , Issue.18 , pp. 2409-2419
    • Melis, J.P.M.1    van Steeg, H.2    Luijten, M.3
  • 189
    • 77954474798 scopus 로고    scopus 로고
    • Transferrin-iron routing to the cytosol and mitochondria as studied by live and real-time fluorescence
    • Shvartsman, M., Fibach, E., Cabantchik, Z.I., Transferrin-iron routing to the cytosol and mitochondria as studied by live and real-time fluorescence. Biochem. J. 429:1 (2010), 185–193.
    • (2010) Biochem. J. , vol.429 , Issue.1 , pp. 185-193
    • Shvartsman, M.1    Fibach, E.2    Cabantchik, Z.I.3
  • 191
    • 84858017083 scopus 로고    scopus 로고
    • Heme induces programmed necrosis on macrophages through autocrine TNF and ROS production
    • Fortes, G.B., Alves, L.S., de Oliveira, R., Dutra, F.F., Rodrigues, D., Fernandez, P.L., et al. Heme induces programmed necrosis on macrophages through autocrine TNF and ROS production. Blood 119:10 (2012), 2368–2375.
    • (2012) Blood , vol.119 , Issue.10 , pp. 2368-2375
    • Fortes, G.B.1    Alves, L.S.2    de Oliveira, R.3    Dutra, F.F.4    Rodrigues, D.5    Fernandez, P.L.6
  • 192
  • 194
    • 34250372956 scopus 로고    scopus 로고
    • RAS-RAF-MEK-dependent oxidative cell death involving voltage-dependent anion channels
    • Yagoda, N., von Rechenberg, M., Zaganjor, E., Bauer, A.J., Yang, W.S., Fridman, D.J., et al. RAS-RAF-MEK-dependent oxidative cell death involving voltage-dependent anion channels. Nature 447:7146 (2007), 864–868.
    • (2007) Nature , vol.447 , Issue.7146 , pp. 864-868
    • Yagoda, N.1    von Rechenberg, M.2    Zaganjor, E.3    Bauer, A.J.4    Yang, W.S.5    Fridman, D.J.6
  • 195
    • 40849085503 scopus 로고    scopus 로고
    • Synthetic lethal screening identifies compounds activating iron-dependent, nonapoptotic cell death in oncogenic-RAS-harboring cancer cells
    • Yang, W.S., Stockwell, B.R., Synthetic lethal screening identifies compounds activating iron-dependent, nonapoptotic cell death in oncogenic-RAS-harboring cancer cells. Chem. Biol. 15:3 (2008), 234–245.
    • (2008) Chem. Biol. , vol.15 , Issue.3 , pp. 234-245
    • Yang, W.S.1    Stockwell, B.R.2
  • 196
    • 84952639010 scopus 로고    scopus 로고
    • Activation of the p62-Keap1-NRF2 pathway protects against ferroptosis in hepatocellular carcinoma cells
    • Sun, X., Ou, Z., Chen, R., Niu, X., Chen, D., Kang, R., et al. Activation of the p62-Keap1-NRF2 pathway protects against ferroptosis in hepatocellular carcinoma cells. Hepatology 63:1 (2016), 173–184.
    • (2016) Hepatology , vol.63 , Issue.1 , pp. 173-184
    • Sun, X.1    Ou, Z.2    Chen, R.3    Niu, X.4    Chen, D.5    Kang, R.6
  • 197
    • 84978997718 scopus 로고    scopus 로고
    • Metallothionein-1G facilitates sorafenib resistance through inhibition of ferroptosis
    • Sun, X., Niu, X., Chen, R., He, W., Chen, D., Kang, R., et al. Metallothionein-1G facilitates sorafenib resistance through inhibition of ferroptosis. Hepatology 64:2 (2016), 488–500.
    • (2016) Hepatology , vol.64 , Issue.2 , pp. 488-500
    • Sun, X.1    Niu, X.2    Chen, R.3    He, W.4    Chen, D.5    Kang, R.6
  • 198
    • 84937525519 scopus 로고    scopus 로고
    • Glutaminolysis and Transferrin Regulate Ferroptosis
    • Gao, M., Monian, P., Quadri, N., Ramasamy, R., Jiang, X., Glutaminolysis and Transferrin Regulate Ferroptosis. Mol Cell. 59:2 (2015), 298–308.
    • (2015) Mol Cell. , vol.59 , Issue.2 , pp. 298-308
    • Gao, M.1    Monian, P.2    Quadri, N.3    Ramasamy, R.4    Jiang, X.5
  • 199
    • 84943390843 scopus 로고    scopus 로고
    • Heme oxygenase-1 accelerates erastin-induced ferroptotic cell death
    • Kwon, M.Y., Park, E., Lee, S.J., Chung, S.W., Heme oxygenase-1 accelerates erastin-induced ferroptotic cell death. Oncotarget 6:27 (2015), 24393–24403.
    • (2015) Oncotarget , vol.6 , Issue.27 , pp. 24393-24403
    • Kwon, M.Y.1    Park, E.2    Lee, S.J.3    Chung, S.W.4
  • 200
    • 0029887959 scopus 로고    scopus 로고
    • The environment of the lipoxygenase iron binding site explored with novel hydroxypyridinone iron chelators
    • Abeysinghe, R.D., Roberts, P.J., Cooper, C.E., MacLean, K.H., Hider, R.C., Porter, J.B., The environment of the lipoxygenase iron binding site explored with novel hydroxypyridinone iron chelators. J. Biol. Chem. 271:14 (1996), 7965–7972.
    • (1996) J. Biol. Chem. , vol.271 , Issue.14 , pp. 7965-7972
    • Abeysinghe, R.D.1    Roberts, P.J.2    Cooper, C.E.3    MacLean, K.H.4    Hider, R.C.5    Porter, J.B.6
  • 201
    • 84897059782 scopus 로고    scopus 로고
    • Ferrostatins inhibit oxidative lipid damage and cell death in diverse disease models
    • Skouta, R., Dixon, S.J., Wang, J., Dunn, D.E., Orman, M., Shimada, K., et al. Ferrostatins inhibit oxidative lipid damage and cell death in diverse disease models. J. Am. Chem. Soc. 136:12 (2014), 4551–4556.
    • (2014) J. Am. Chem. Soc. , vol.136 , Issue.12 , pp. 4551-4556
    • Skouta, R.1    Dixon, S.J.2    Wang, J.3    Dunn, D.E.4    Orman, M.5    Shimada, K.6
  • 202
    • 0037932865 scopus 로고    scopus 로고
    • Identification of genotype-selective antitumor agents using synthetic lethal chemical screening in engineered human tumor cells
    • Dolma, S., Lessnick, S.L., Hahn, W.C., Stockwell, B.R., Identification of genotype-selective antitumor agents using synthetic lethal chemical screening in engineered human tumor cells. Cancer Cell 3:3 (2003), 285–296.
    • (2003) Cancer Cell , vol.3 , Issue.3 , pp. 285-296
    • Dolma, S.1    Lessnick, S.L.2    Hahn, W.C.3    Stockwell, B.R.4
  • 203
    • 84965008627 scopus 로고    scopus 로고
    • Cell-line selectivity improves the predictive power of pharmacogenomic analyses and helps identify NADPH as biomarker for ferroptosis sensitivity
    • Shimada, K., Hayano, M., Pagano, N.C., Stockwell, B.R., Cell-line selectivity improves the predictive power of pharmacogenomic analyses and helps identify NADPH as biomarker for ferroptosis sensitivity. Cell Chem. Biol. 23:2 (2016), 225–235.
    • (2016) Cell Chem. Biol. , vol.23 , Issue.2 , pp. 225-235
    • Shimada, K.1    Hayano, M.2    Pagano, N.C.3    Stockwell, B.R.4
  • 204
    • 84913582286 scopus 로고    scopus 로고
    • Synchronized renal tubular cell death involves ferroptosis
    • Linkermann, A., Skouta, R., Himmerkus, N., Mulay, S.R., Dewitz, C., De Zen, F., et al. Synchronized renal tubular cell death involves ferroptosis. PNAS 111:47 (2014), 16836–16841.
    • (2014) PNAS , vol.111 , Issue.47 , pp. 16836-16841
    • Linkermann, A.1    Skouta, R.2    Himmerkus, N.3    Mulay, S.R.4    Dewitz, C.5    De Zen, F.6
  • 205
    • 84958103915 scopus 로고    scopus 로고
    • Ferroptosis: death by lipid peroxidation
    • Yang, W.S., Stockwell, B.R., Ferroptosis: death by lipid peroxidation. Trends Cell Biol. 26:3 (2016), 165–176.
    • (2016) Trends Cell Biol. , vol.26 , Issue.3 , pp. 165-176
    • Yang, W.S.1    Stockwell, B.R.2
  • 206
    • 85018960248 scopus 로고    scopus 로고
    • Ferroptosis: bug or feature?
    • Dixon, S.J., Ferroptosis: bug or feature?. Immunol. Rev. 277:1 (2017), 150–157.
    • (2017) Immunol. Rev. , vol.277 , Issue.1 , pp. 150-157
    • Dixon, S.J.1
  • 207
    • 0032534748 scopus 로고    scopus 로고
    • Redox Regulation of caspase-3(-like) protease activity: regulatory roles of thioredoxin and Cytochrome c
    • Ueda, S., Nakamura, H., Masutani, H., Sasada, T., Yonehara, S., Takabayashi, A., et al. Redox Regulation of caspase-3(-like) protease activity: regulatory roles of thioredoxin and Cytochrome c. J. Immunol., 161(12), 1998, 6689.
    • (1998) J. Immunol. , vol.161 , Issue.12 , pp. 6689
    • Ueda, S.1    Nakamura, H.2    Masutani, H.3    Sasada, T.4    Yonehara, S.5    Takabayashi, A.6
  • 208
    • 85063738581 scopus 로고    scopus 로고
    • Ferroptosis, a new form of cell death: opportunities and challenges in cancer
    • Mou, Y., Wang, J., Wu, J., He, D., Zhang, C., Duan, C., et al. Ferroptosis, a new form of cell death: opportunities and challenges in cancer. J Hematol Oncol., 12(1), 2019, 34.
    • (2019) J Hematol Oncol. , vol.12 , Issue.1 , pp. 34
    • Mou, Y.1    Wang, J.2    Wu, J.3    He, D.4    Zhang, C.5    Duan, C.6


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