메뉴 건너뛰기




Volumn 60, Issue , 2013, Pages 85-128

Protein Antioxidants in Thalassemia

Author keywords

Albumin; Antioxidative proteins; Ceruloplasmin; Ferroxidase; Glutathione; Haptoglobin; Iron overload; Oxidative stress; Thalassemia

Indexed keywords


EID: 84875118880     PISSN: 00652423     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-407681-5.00003-9     Document Type: Chapter
Times cited : (19)

References (237)
  • 1
    • 84948984545 scopus 로고    scopus 로고
    • The molecular pathology of the thalassaemias
    • Blackwell Science, Oxford, England, D.J. Weatherall, B. Clegg (Eds.)
    • Higgs D.R., Thein S.L., Woods W.G. The molecular pathology of the thalassaemias. The Thalassaemia Syndromes 2001, 133-191. Blackwell Science, Oxford, England. fourth ed. D.J. Weatherall, B. Clegg (Eds.).
    • (2001) The Thalassaemia Syndromes , pp. 133-191
    • Higgs, D.R.1    Thein, S.L.2    Woods, W.G.3
  • 2
    • 0034889014 scopus 로고    scopus 로고
    • Inherited hemoglobin disorders: an increasing global health problem
    • Weatherall D.J., Clegg J.B. Inherited hemoglobin disorders: an increasing global health problem. Bull. World Health Organ. 2001, 79:704-712.
    • (2001) Bull. World Health Organ. , vol.79 , pp. 704-712
    • Weatherall, D.J.1    Clegg, J.B.2
  • 3
    • 0031855380 scopus 로고    scopus 로고
    • Global epidemiology of hemoglobin disorders
    • Angastiniotis M., Modell B. Global epidemiology of hemoglobin disorders. Ann. N. Y. Acad. Sci. 1998, 850:251-269.
    • (1998) Ann. N. Y. Acad. Sci. , vol.850 , pp. 251-269
    • Angastiniotis, M.1    Modell, B.2
  • 5
    • 33644701423 scopus 로고    scopus 로고
    • Changes in the epidemiology of thalassemia in North America: a new minority disease
    • Vichinsky E.P., MacKlin E.A., Waye J.S., Lorey F., Olivieri N.F. Changes in the epidemiology of thalassemia in North America: a new minority disease. Pediatrics 2005, 116:e818-e825.
    • (2005) Pediatrics , vol.116
    • Vichinsky, E.P.1    MacKlin, E.A.2    Waye, J.S.3    Lorey, F.4    Olivieri, N.F.5
  • 8
    • 0037305250 scopus 로고    scopus 로고
    • Hemoglobin H disease: not necessarily a benign disorder
    • Chui D.H., Fucharoen S., Chan V. Hemoglobin H disease: not necessarily a benign disorder. Blood 2003, 101:791-800.
    • (2003) Blood , vol.101 , pp. 791-800
    • Chui, D.H.1    Fucharoen, S.2    Chan, V.3
  • 9
    • 70350287853 scopus 로고    scopus 로고
    • Clinical features and molecular analysis in Thai patients with HbH disease
    • Laosombat V., Viprakasit V., Chotsampancharoen T., et al. Clinical features and molecular analysis in Thai patients with HbH disease. Ann. Hematol. 2009, 88:1185-1192.
    • (2009) Ann. Hematol. , vol.88 , pp. 1185-1192
    • Laosombat, V.1    Viprakasit, V.2    Chotsampancharoen, T.3
  • 11
    • 0842308839 scopus 로고    scopus 로고
    • Genetic insights into the clinical diversity of β-thalassaemia
    • Thein S.L. Genetic insights into the clinical diversity of β-thalassaemia. Br. J. Haematol. 2004, 124:264-274.
    • (2004) Br. J. Haematol. , vol.124 , pp. 264-274
    • Thein, S.L.1
  • 14
    • 0036180342 scopus 로고    scopus 로고
    • Pathophysiology of thalassaemia
    • Schrier S.L. Pathophysiology of thalassaemia. Curr. Opin. Hematol. 2002, 9:123-126.
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 123-126
    • Schrier, S.L.1
  • 15
    • 0027181636 scopus 로고
    • Accelerated programmed cell death (apoptosis) in erythroid precursors of patients with severe β-thalassemia (Cooley's anemia)
    • Yuan J., Angelucci E., Lucarelli G., et al. Accelerated programmed cell death (apoptosis) in erythroid precursors of patients with severe β-thalassemia (Cooley's anemia). Blood 1993, 82:374-377.
    • (1993) Blood , vol.82 , pp. 374-377
    • Yuan, J.1    Angelucci, E.2    Lucarelli, G.3
  • 16
    • 0034669951 scopus 로고    scopus 로고
    • The importance of erythroid expansion in determining the extent of apoptosis in erythroid precursors in patients with β-thalassemia major
    • Centis F., Tabellini L., Lucarelli G., et al. The importance of erythroid expansion in determining the extent of apoptosis in erythroid precursors in patients with β-thalassemia major. Blood 2000, 96:3624-3629.
    • (2000) Blood , vol.96 , pp. 3624-3629
    • Centis, F.1    Tabellini, L.2    Lucarelli, G.3
  • 17
    • 0034538786 scopus 로고    scopus 로고
    • Ineffective erythropoiesis in b-thalassemia major is due to apoptosis at the polychromatophilic normoblast stage
    • Mathias L.A., Fisher T.C., Zeng L., et al. Ineffective erythropoiesis in b-thalassemia major is due to apoptosis at the polychromatophilic normoblast stage. Exp. Hematol. 2000, 28:1343-1353.
    • (2000) Exp. Hematol. , vol.28 , pp. 1343-1353
    • Mathias, L.A.1    Fisher, T.C.2    Zeng, L.3
  • 18
    • 0034324594 scopus 로고    scopus 로고
    • Introduction to the problem of hemoglobin EB thalassemia
    • Weatherall D.J. Introduction to the problem of hemoglobin EB thalassemia. J. Pediatr. Hematol. Oncol. 2000, 22:551.
    • (2000) J. Pediatr. Hematol. Oncol. , vol.22 , pp. 551
    • Weatherall, D.J.1
  • 20
    • 0033953189 scopus 로고    scopus 로고
    • Clinical and hematologic aspects of hemoglobin E beta-thalassemia
    • Fucharoen S., Winichagoon P. Clinical and hematologic aspects of hemoglobin E beta-thalassemia. Curr. Opin. Hematol. 2000, 7:106-112.
    • (2000) Curr. Opin. Hematol. , vol.7 , pp. 106-112
    • Fucharoen, S.1    Winichagoon, P.2
  • 22
    • 34247171870 scopus 로고    scopus 로고
    • Normal iron metabolism and the physiopathology of iron overload disorders
    • Siah C.W., Ombiga J., Adams L.A., et al. Normal iron metabolism and the physiopathology of iron overload disorders. Clin. Biochem. Rev. 2006, 27:5-16.
    • (2006) Clin. Biochem. Rev. , vol.27 , pp. 5-16
    • Siah, C.W.1    Ombiga, J.2    Adams, L.A.3
  • 23
    • 0036669942 scopus 로고    scopus 로고
    • Molecular evidence for the role of a ferric reductase in iron transport
    • McKie A.T., Latunde-Dada G.O., Miret S., et al. Molecular evidence for the role of a ferric reductase in iron transport. Biochem. Soc. Trans. 2002, 30:722-724.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 722-724
    • McKie, A.T.1    Latunde-Dada, G.O.2    Miret, S.3
  • 24
    • 34249740700 scopus 로고    scopus 로고
    • The role of transporters in cellular heme and porphyrin homeostasis
    • Krishnamurthy P., Xie T., Schuetz J.D. The role of transporters in cellular heme and porphyrin homeostasis. Pharmacol. Ther. 2007, 114:345-358.
    • (2007) Pharmacol. Ther. , vol.114 , pp. 345-358
    • Krishnamurthy, P.1    Xie, T.2    Schuetz, J.D.3
  • 25
    • 27744603887 scopus 로고    scopus 로고
    • Structure/function overview of proteins involved in iron storage and transport
    • Sargent P.J., Farnaud S., Evans R.W. Structure/function overview of proteins involved in iron storage and transport. Curr. Med. Chem. 2005, 12:2683-2693.
    • (2005) Curr. Med. Chem. , vol.12 , pp. 2683-2693
    • Sargent, P.J.1    Farnaud, S.2    Evans, R.W.3
  • 26
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization
    • Nemeth E., Tuttle M.S., Powelson J., et al. Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science 2004, 306:2090-2093.
    • (2004) Science , vol.306 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3
  • 27
    • 0031816970 scopus 로고    scopus 로고
    • Aceruloplasminemia
    • Gitlin J.D. Aceruloplasminemia. Pediatr. Res. 1998, 44:271-276.
    • (1998) Pediatr. Res. , vol.44 , pp. 271-276
    • Gitlin, J.D.1
  • 28
    • 0035843134 scopus 로고    scopus 로고
    • Identification of the haemoglobin scavenger receptor
    • Kristiansen M., Graversen J.H., Jacobsen C., et al. Identification of the haemoglobin scavenger receptor. Nature 2001, 409:198-201.
    • (2001) Nature , vol.409 , pp. 198-201
    • Kristiansen, M.1    Graversen, J.H.2    Jacobsen, C.3
  • 29
    • 30144435054 scopus 로고    scopus 로고
    • CD163 is the macrophage scavenger receptor for native and chemically modified hemoglobins in the absence of haptoglobin
    • Schaer D.J., Schaer C.A., Buehler P.W., et al. CD163 is the macrophage scavenger receptor for native and chemically modified hemoglobins in the absence of haptoglobin. Blood 2006, 107:373-380.
    • (2006) Blood , vol.107 , pp. 373-380
    • Schaer, D.J.1    Schaer, C.A.2    Buehler, P.W.3
  • 32
    • 34250800318 scopus 로고    scopus 로고
    • Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin
    • De Domenico I., Ward D.M., di Patti M.C., et al. Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin. EMBO J. 2007, 26:2823-2831.
    • (2007) EMBO J. , vol.26 , pp. 2823-2831
    • De Domenico, I.1    Ward, D.M.2    di Patti, M.C.3
  • 34
    • 79953078598 scopus 로고    scopus 로고
    • Disorders of iron metabolism. Part 1: molecular basis of iron homoeostasis
    • Munoz M., Garci{dotless}a-Erce J.A., Remacha A.F. Disorders of iron metabolism. Part 1: molecular basis of iron homoeostasis. J. Clin. Pathol. 2011, 64:281-286.
    • (2011) J. Clin. Pathol. , vol.64 , pp. 281-286
    • Munoz, M.1    Garcia-Erce, J.A.2    Remacha, A.F.3
  • 35
    • 0035896642 scopus 로고    scopus 로고
    • Hepcidin, a urinary antimicrobial peptide synthesized in the liver
    • Park C.H., Valore E.V., Waring A.J., Ganz T. Hepcidin, a urinary antimicrobial peptide synthesized in the liver. J. Biol. Chem. 2001, 276:7806-7810.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7806-7810
    • Park, C.H.1    Valore, E.V.2    Waring, A.J.3    Ganz, T.4
  • 36
    • 0037007064 scopus 로고    scopus 로고
    • Severe iron deficiency anemia in transgenic mice expressing liver hepcidin
    • Nicolas G., Bennoun M., Porteu A., et al. Severe iron deficiency anemia in transgenic mice expressing liver hepcidin. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:4596-4601.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 4596-4601
    • Nicolas, G.1    Bennoun, M.2    Porteu, A.3
  • 37
    • 79551583056 scopus 로고    scopus 로고
    • Hepcidin and disorders of iron metabolism
    • Ganz T., Nemeth E. Hepcidin and disorders of iron metabolism. Annu. Rev. Med. 2011, 62:347-360.
    • (2011) Annu. Rev. Med. , vol.62 , pp. 347-360
    • Ganz, T.1    Nemeth, E.2
  • 38
    • 77949687937 scopus 로고    scopus 로고
    • Hepcidin targets ferroportin for degradation in hepatocytes
    • Ramey G., Deschemin J.C., Durel B., et al. Hepcidin targets ferroportin for degradation in hepatocytes. Haematologica 2010, 95:501-504.
    • (2010) Haematologica , vol.95 , pp. 501-504
    • Ramey, G.1    Deschemin, J.C.2    Durel, B.3
  • 40
    • 67349211785 scopus 로고    scopus 로고
    • Iron overload following red blood cell transfusion and its impact on disease severity
    • Ozment C.P., Turi J.L. Iron overload following red blood cell transfusion and its impact on disease severity. Biochim. Biophys. Acta 2009, 1790:694-701.
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 694-701
    • Ozment, C.P.1    Turi, J.L.2
  • 41
    • 77953372767 scopus 로고    scopus 로고
    • Future alternative therapies for β-thalassemia
    • Rivella S., Rachmilewitz E. Future alternative therapies for β-thalassemia. Expert Rev. Hematol. 2009, 2:685.
    • (2009) Expert Rev. Hematol. , vol.2 , pp. 685
    • Rivella, S.1    Rachmilewitz, E.2
  • 43
    • 0041672570 scopus 로고    scopus 로고
    • Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation
    • Ganz T. Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation. Blood 2003, 102:783-788.
    • (2003) Blood , vol.102 , pp. 783-788
    • Ganz, T.1
  • 44
    • 0036791486 scopus 로고    scopus 로고
    • The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation
    • Nicolas G., Chauvet C., Viatte L., et al. The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation. J. Clin. Invest. 2002, 110:1037-1044.
    • (2002) J. Clin. Invest. , vol.110 , pp. 1037-1044
    • Nicolas, G.1    Chauvet, C.2    Viatte, L.3
  • 45
    • 66149145303 scopus 로고    scopus 로고
    • Regulation of hepcidin and iron-overload disease
    • Lee P.L., Beutler E. Regulation of hepcidin and iron-overload disease. Annu. Rev. Pathol. 2009, 4:489-515.
    • (2009) Annu. Rev. Pathol. , vol.4 , pp. 489-515
    • Lee, P.L.1    Beutler, E.2
  • 46
    • 33745755350 scopus 로고    scopus 로고
    • The effects of erythropoetic activity and iron burden on hepcidin expression in patients with thalassemia major
    • Kattamis A., Papassotiriou I., Palaiologou D., et al. The effects of erythropoetic activity and iron burden on hepcidin expression in patients with thalassemia major. Haematologica 2006, 91:809-812.
    • (2006) Haematologica , vol.91 , pp. 809-812
    • Kattamis, A.1    Papassotiriou, I.2    Palaiologou, D.3
  • 47
    • 34447306076 scopus 로고    scopus 로고
    • Liver iron concentrations and urinary hepcidin in β-thalassemia
    • Origa R., Galanello R., Ganz T., et al. Liver iron concentrations and urinary hepcidin in β-thalassemia. Haematologica 2007, 92:583-588.
    • (2007) Haematologica , vol.92 , pp. 583-588
    • Origa, R.1    Galanello, R.2    Ganz, T.3
  • 48
    • 34249658982 scopus 로고    scopus 로고
    • Ineffective erythropoiesis in β-thalassemia is characterized by increased iron absorption mediated by down-regulation of hepcidin and upregulation of ferroportin
    • Gardenghi S., Marongiu M.F., Ramos P., et al. Ineffective erythropoiesis in β-thalassemia is characterized by increased iron absorption mediated by down-regulation of hepcidin and upregulation of ferroportin. Blood 2007, 109:5027-5035.
    • (2007) Blood , vol.109 , pp. 5027-5035
    • Gardenghi, S.1    Marongiu, M.F.2    Ramos, P.3
  • 49
    • 33745684771 scopus 로고    scopus 로고
    • MRNA expression of iron regulatory genes in β-thalassemia intermedia and β-thalassemia major mouse models
    • Weizer-Stern O., Adamsky K., Amariglio N., et al. mRNA expression of iron regulatory genes in β-thalassemia intermedia and β-thalassemia major mouse models. Am. J. Hematol. 2006, 81:479-483.
    • (2006) Am. J. Hematol. , vol.81 , pp. 479-483
    • Weizer-Stern, O.1    Adamsky, K.2    Amariglio, N.3
  • 50
    • 33745743014 scopus 로고    scopus 로고
    • Hepcidin and iron-loading anemias
    • Nemeth E., Ganz T. Hepcidin and iron-loading anemias. Haematologica 2006, 91:727-732.
    • (2006) Haematologica , vol.91 , pp. 727-732
    • Nemeth, E.1    Ganz, T.2
  • 51
    • 33646370235 scopus 로고    scopus 로고
    • Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression
    • Babitt J.L., Huang F.W., Wrighting D.M., et al. Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression. Nat. Genet. 2006, 38:531-539.
    • (2006) Nat. Genet. , vol.38 , pp. 531-539
    • Babitt, J.L.1    Huang, F.W.2    Wrighting, D.M.3
  • 52
    • 34948904750 scopus 로고    scopus 로고
    • High levels of GDF15 in thalassemia suppress expression of the iron regulatory protein hepcidin
    • Tanno T., Bhanu N.V., Oneal P.A., et al. High levels of GDF15 in thalassemia suppress expression of the iron regulatory protein hepcidin. Nat. Med. 2007, 13:1096-1101.
    • (2007) Nat. Med. , vol.13 , pp. 1096-1101
    • Tanno, T.1    Bhanu, N.V.2    Oneal, P.A.3
  • 53
    • 33748370295 scopus 로고    scopus 로고
    • Downregulation of hepcidin and haemojuvelin expression in the hepatocyte cell-line HepG2 induced by thalassaemic sera
    • Weizer-Stern O., Adamsky K., Amariglio N., et al. Downregulation of hepcidin and haemojuvelin expression in the hepatocyte cell-line HepG2 induced by thalassaemic sera. Br. J. Haematol. 2006, 135:129-138.
    • (2006) Br. J. Haematol. , vol.135 , pp. 129-138
    • Weizer-Stern, O.1    Adamsky, K.2    Amariglio, N.3
  • 54
    • 0033774945 scopus 로고    scopus 로고
    • The haptoglobin 2-2 phenotype affects serum markers of iron status in healthy males
    • Langlois M.R., Martin M.-E., Boelaert J.R., et al. The haptoglobin 2-2 phenotype affects serum markers of iron status in healthy males. Clin. Chem. 2000, 46:1619-1625.
    • (2000) Clin. Chem. , vol.46 , pp. 1619-1625
    • Langlois, M.R.1    Martin, M.-E.2    Boelaert, J.R.3
  • 55
    • 63849094585 scopus 로고    scopus 로고
    • Haptoglobin preserves the CD163 hemoglobin scavenger pathway by shielding hemoglobin from peroxidative modification
    • Buehler P.W., Abraham B., Vallelian F., et al. Haptoglobin preserves the CD163 hemoglobin scavenger pathway by shielding hemoglobin from peroxidative modification. Blood 2009, 113:2578-2586.
    • (2009) Blood , vol.113 , pp. 2578-2586
    • Buehler, P.W.1    Abraham, B.2    Vallelian, F.3
  • 56
    • 0034836428 scopus 로고    scopus 로고
    • LRP: a multifunctional scavenger and signaling receptor
    • Herz J., Strickland D.K. LRP: a multifunctional scavenger and signaling receptor. J. Clin. Invest. 2001, 108:779-784.
    • (2001) J. Clin. Invest. , vol.108 , pp. 779-784
    • Herz, J.1    Strickland, D.K.2
  • 57
    • 0034806977 scopus 로고    scopus 로고
    • Hemopexin: a review of biological aspects and the role in laboratory medicine
    • Delanghe J.R., Langlois M.R. Hemopexin: a review of biological aspects and the role in laboratory medicine. Clin. Chim. Acta 2001, 312:13-23.
    • (2001) Clin. Chim. Acta , vol.312 , pp. 13-23
    • Delanghe, J.R.1    Langlois, M.R.2
  • 58
    • 0014408353 scopus 로고
    • Exchange of heme among hemoglobins and between hemoglobin and albumin
    • Bunn H.F., Jandl J.H. Exchange of heme among hemoglobins and between hemoglobin and albumin. J. Biol. Chem. 1968, 243:465-475.
    • (1968) J. Biol. Chem. , vol.243 , pp. 465-475
    • Bunn, H.F.1    Jandl, J.H.2
  • 59
    • 0037108199 scopus 로고    scopus 로고
    • The labile iron pool: characterization, measurement, and participation in cellular processes
    • Kakhlon O., Cabantchik Z.I. The labile iron pool: characterization, measurement, and participation in cellular processes. Free Radic. Biol. Med. 2002, 33:1037-1046.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1037-1046
    • Kakhlon, O.1    Cabantchik, Z.I.2
  • 60
    • 0033677772 scopus 로고    scopus 로고
    • The importance of nontransferrin bound iron in disorders of iron metabolism
    • Breuer W., Hershko C., Cabantchik Z.I. The importance of nontransferrin bound iron in disorders of iron metabolism. Transfus. Sci. 2000, 23:185-192.
    • (2000) Transfus. Sci. , vol.23 , pp. 185-192
    • Breuer, W.1    Hershko, C.2    Cabantchik, Z.I.3
  • 63
    • 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. 1994, 269:16046-16053.
    • (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
  • 64
    • 84155180765 scopus 로고    scopus 로고
    • Non-transferrin bound iron in Thalassemia: differential detection of redox active forms in children and older patients
    • Breuer W., Ghoti H., Shattat A., et al. Non-transferrin bound iron in Thalassemia: differential detection of redox active forms in children and older patients. Am. J. Hematol. 2012, 87:55-61.
    • (2012) Am. J. Hematol. , vol.87 , pp. 55-61
    • Breuer, W.1    Ghoti, H.2    Shattat, A.3
  • 65
    • 37049096853 scopus 로고
    • Computer-simulation of metal-ion equilibria in biofluids-models for low-molecular-weight complex distribution of calcium (II), magnesium(II), manganese(II), iron(III), copper (II), zinc(II) and lead(II) ions in human-blood plasma
    • May P.M., Linder P.W., Williams D.R. Computer-simulation of metal-ion equilibria in biofluids-models for low-molecular-weight complex distribution of calcium (II), magnesium(II), manganese(II), iron(III), copper (II), zinc(II) and lead(II) ions in human-blood plasma. J. Chem. Soc. Dalton Trans. 1977, 6:588-595.
    • (1977) J. Chem. Soc. Dalton Trans. , vol.6 , pp. 588-595
    • May, P.M.1    Linder, P.W.2    Williams, D.R.3
  • 66
    • 0024564712 scopus 로고
    • Nontransferrin-bound iron in plasma or serum from patients with idiopathic hemochromatosis: characterization by high-performance liquid-chromatography and nuclear magnetic-resonance spectroscopy
    • Grootveld M., Bell J.D., Halliwell B., Aruoma O.I., Bomford A., Sadler P.J. Nontransferrin-bound iron in plasma or serum from patients with idiopathic hemochromatosis: characterization by high-performance liquid-chromatography and nuclear magnetic-resonance spectroscopy. J. Biol. Chem. 1989, 15:4417-4422.
    • (1989) J. Biol. Chem. , vol.15 , pp. 4417-4422
    • Grootveld, M.1    Bell, J.D.2    Halliwell, B.3    Aruoma, O.I.4    Bomford, A.5    Sadler, P.J.6
  • 67
    • 17944388628 scopus 로고    scopus 로고
    • Nature of nontransferrin-bound iron
    • Hider R.C. Nature of nontransferrin-bound iron. Eur. J. Clin. Invest. 2002, 32:50-54.
    • (2002) Eur. J. Clin. Invest. , vol.32 , pp. 50-54
    • Hider, R.C.1
  • 68
    • 69449101913 scopus 로고    scopus 로고
    • Influence of non-enzymatic post-translation modifications on the ability of human serum albumin to bind iron. Implications for non-transferrin-bound iron speciation
    • Silva A.M.N., Hider R.C. Influence of non-enzymatic post-translation modifications on the ability of human serum albumin to bind iron. Implications for non-transferrin-bound iron speciation. Biochim. Biophys. Acta 2009, 1794:1449-1458.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 1449-1458
    • Silva, A.M.N.1    Hider, R.C.2
  • 69
    • 36649038516 scopus 로고    scopus 로고
    • Nature of non-transferrin-bound iron: studies on iron citrate complexes and thalassemic sera
    • Evans R.W., Rafique R., Zarea A., et al. Nature of non-transferrin-bound iron: studies on iron citrate complexes and thalassemic sera. J. Biol. Inorg. Chem. 2008, 13:57-74.
    • (2008) J. Biol. Inorg. Chem. , vol.13 , pp. 57-74
    • Evans, R.W.1    Rafique, R.2    Zarea, A.3
  • 70
    • 68949212139 scopus 로고    scopus 로고
    • Levels of nontransferrin-bound iron as an index of iron overload in patients with thalassaemia intermedia
    • Taher A., Musallam K.M., Rassi F., et al. Levels of nontransferrin-bound iron as an index of iron overload in patients with thalassaemia intermedia. Br. J. Haematol. 2009, 146:569-572.
    • (2009) Br. J. Haematol. , vol.146 , pp. 569-572
    • Taher, A.1    Musallam, K.M.2    Rassi, F.3
  • 71
    • 77955379581 scopus 로고    scopus 로고
    • Mechanisms for the shuttling of plasma non-transferrin bound iron (NTBI) onto deferoxamine by deferiprone
    • Evans P., Kayyali R., Hider R.C., Eccleston J., Porter J.B. Mechanisms for the shuttling of plasma non-transferrin bound iron (NTBI) onto deferoxamine by deferiprone. Transl. Res. 2010, 156:55-67.
    • (2010) Transl. Res. , vol.156 , pp. 55-67
    • Evans, P.1    Kayyali, R.2    Hider, R.C.3    Eccleston, J.4    Porter, J.B.5
  • 72
    • 33748749961 scopus 로고    scopus 로고
    • Oxidative stress and inflammation in iron-overloaded patients with beta-thalassaemia or sickle cell disease
    • Walter P.B., Fung E.B., Killilea D.W., et al. Oxidative stress and inflammation in iron-overloaded patients with beta-thalassaemia or sickle cell disease. Br. J. Haematol. 2006, 135:254-263.
    • (2006) Br. J. Haematol. , vol.135 , pp. 254-263
    • Walter, P.B.1    Fung, E.B.2    Killilea, D.W.3
  • 73
    • 3242780446 scopus 로고    scopus 로고
    • Oxidative status and malondialdehyde in beta-thalassaemia patients
    • Cighetti G., Duca L., Bortone L., et al. Oxidative status and malondialdehyde in beta-thalassaemia patients. Eur. J. Clin. Invest. 2002, 32(Suppl. 1):55-60.
    • (2002) Eur. J. Clin. Invest. , vol.32 , Issue.SUPPL. 1 , pp. 55-60
    • Cighetti, G.1    Duca, L.2    Bortone, L.3
  • 74
    • 58149458142 scopus 로고    scopus 로고
    • High nontransferrin bound iron levels and heart disease in thalassemia major
    • Piga A., Longo F., Duca L., et al. High nontransferrin bound iron levels and heart disease in thalassemia major. Am. J. Hematol. 2009, 84:29-33.
    • (2009) Am. J. Hematol. , vol.84 , pp. 29-33
    • Piga, A.1    Longo, F.2    Duca, L.3
  • 75
    • 42649091793 scopus 로고    scopus 로고
    • Increased urinary 1, N6-ethenodeoxyadenosine and 3, N4-ethenodeoxycytidine excretion in thalassemia patients: markers for lipid peroxidation-induced DNA damage
    • Meerang M., Nair J., Sirankapracha P., et al. Increased urinary 1, N6-ethenodeoxyadenosine and 3, N4-ethenodeoxycytidine excretion in thalassemia patients: markers for lipid peroxidation-induced DNA damage. Free Radic. Biol. Med. 2008, 44:1863-1868.
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 1863-1868
    • Meerang, M.1    Nair, J.2    Sirankapracha, P.3
  • 76
    • 33646692249 scopus 로고    scopus 로고
    • The reduction of cholesteryl linoleate in lipoproteins: an index of clinical severity in beta-thalassemia/Hb E
    • Luechapudiporn R., Morales N.P., Fucharoen S., Chantharaksri U. The reduction of cholesteryl linoleate in lipoproteins: an index of clinical severity in beta-thalassemia/Hb E. Clin. Chem. Lab. Med. 2006, 44:574-581.
    • (2006) Clin. Chem. Lab. Med. , vol.44 , pp. 574-581
    • Luechapudiporn, R.1    Morales, N.P.2    Fucharoen, S.3    Chantharaksri, U.4
  • 77
    • 0032810030 scopus 로고    scopus 로고
    • Blood antioxidant status and urinary levels of catecholamine metabolites in beta-thalassemia
    • De Luca C., Filosa A., Grandinetti M., Maggio F., Lamba M., Passi S. Blood antioxidant status and urinary levels of catecholamine metabolites in beta-thalassemia. Free Radic. Res. 1999, 30:453-462.
    • (1999) Free Radic. Res. , vol.30 , pp. 453-462
    • De Luca, C.1    Filosa, A.2    Grandinetti, M.3    Maggio, F.4    Lamba, M.5    Passi, S.6
  • 78
    • 0016660866 scopus 로고
    • Formation of superoxide in the autoxidation of the isolated α and β chains of human hemoglobin and its involvement in hemichrome precipitation
    • Brunori M., Falcioni G., Fioretti E., Giardina B., Rotilio G. Formation of superoxide in the autoxidation of the isolated α and β chains of human hemoglobin and its involvement in hemichrome precipitation. Eur. J. Biochem. 1975, 53:99-104.
    • (1975) Eur. J. Biochem. , vol.53 , pp. 99-104
    • Brunori, M.1    Falcioni, G.2    Fioretti, E.3    Giardina, B.4    Rotilio, G.5
  • 79
    • 0020577135 scopus 로고
    • Increased sensitivity of isolated alpha subunits of normal human hemoglobin to oxidative damage and crosslinkage with spectrin
    • Joshi W., Leb L., Piotrowski J., Fortier N., Snyder L.M. Increased sensitivity of isolated alpha subunits of normal human hemoglobin to oxidative damage and crosslinkage with spectrin. J. Lab. Clin. Med. 1983, 102:46-52.
    • (1983) J. Lab. Clin. Med. , vol.102 , pp. 46-52
    • Joshi, W.1    Leb, L.2    Piotrowski, J.3    Fortier, N.4    Snyder, L.M.5
  • 80
    • 0024990715 scopus 로고
    • Entrapment of purified α-hemoglobin chains in normal erythrocytes: a model for β-thalassemia
    • Scott M.D., Rouyer-Fessard P., Lubin B.H., Beuzard Y. Entrapment of purified α-hemoglobin chains in normal erythrocytes: a model for β-thalassemia. J. Biol. Chem. 1990, 265:17953-17959.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17953-17959
    • Scott, M.D.1    Rouyer-Fessard, P.2    Lubin, B.H.3    Beuzard, Y.4
  • 81
    • 0023508190 scopus 로고
    • Inhibition of red blood cell enzymes by hemin: a mechanism for hemolysis in hemoglobinopathies
    • Zerez C.R., Hseih J.W., Tanaka K.R. Inhibition of red blood cell enzymes by hemin: a mechanism for hemolysis in hemoglobinopathies. Trans. Assoc. Am. Physicians 1988, 100:329-338.
    • (1988) Trans. Assoc. Am. Physicians , vol.100 , pp. 329-338
    • Zerez, C.R.1    Hseih, J.W.2    Tanaka, K.R.3
  • 82
    • 0344879576 scopus 로고
    • Membrane deposition of heme and non-heme iron in model thalassemic erythrocytes
    • Scott M.D., Repka T., Hebbel R.P., van den Berg J.J.M., Wagner T.C., Lubin B.H. Membrane deposition of heme and non-heme iron in model thalassemic erythrocytes. Blood 1991, 78(Suppl. 1):771.
    • (1991) Blood , vol.78 , Issue.SUPPL. 1 , pp. 771
    • Scott, M.D.1    Repka, T.2    Hebbel, R.P.3    van den Berg, J.J.M.4    Wagner, T.C.5    Lubin, B.H.6
  • 83
    • 0013471415 scopus 로고
    • 'Loose' iron: an important element in the pathogenesis of damage within β thalassemic erythrocytes
    • Scott M.D., Wagner T.C., Lubin B.H., Eaton J.W. 'Loose' iron: an important element in the pathogenesis of damage within β thalassemic erythrocytes. Blood 1991, 78(Suppl. 1):772.
    • (1991) Blood , vol.78 , Issue.SUPPL. 1 , pp. 772
    • Scott, M.D.1    Wagner, T.C.2    Lubin, B.H.3    Eaton, J.W.4
  • 84
    • 0034307683 scopus 로고    scopus 로고
    • A correlation of erythrokinetics, ineffective erythropoiesis, and erythroid precursor apoptosis in thai patients with thalassemia
    • Pootrakul P., Sirankapracha P., Hemsorach S., et al. A correlation of erythrokinetics, ineffective erythropoiesis, and erythroid precursor apoptosis in thai patients with thalassemia. Blood 2000, 96:2606-2612.
    • (2000) Blood , vol.96 , pp. 2606-2612
    • Pootrakul, P.1    Sirankapracha, P.2    Hemsorach, S.3
  • 85
    • 0027232102 scopus 로고
    • Effect of excess α-hemoglobin chains on cellular and membrane oxidation in model β-thalassemic erythrocytes
    • Scott M.D., van den Berg J.J.M., Repka T., et al. Effect of excess α-hemoglobin chains on cellular and membrane oxidation in model β-thalassemic erythrocytes. J. Clin. Invest. 1993, 91:1706-1712.
    • (1993) J. Clin. Invest. , vol.91 , pp. 1706-1712
    • Scott, M.D.1    van den Berg, J.J.M.2    Repka, T.3
  • 86
    • 33644907169 scopus 로고    scopus 로고
    • H2O2 injury in β thalassemic erythrocytes: protective role of catalase and the prooxidant effects of GSH
    • Scott M.D. H2O2 injury in β thalassemic erythrocytes: protective role of catalase and the prooxidant effects of GSH. Free Radic. Biol. Med. 2006, 40:1264-1272.
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 1264-1272
    • Scott, M.D.1
  • 87
    • 0023463529 scopus 로고
    • Relationship of serum vitamin E, erythrocyte nonheme iron, and malonyldialdehyde (lipid membrane peroxidation product) in thalassemia
    • Vatanavicharn S., Anuwatanakulchai M., Yenchitsomanus P., Siddhikol C. Relationship of serum vitamin E, erythrocyte nonheme iron, and malonyldialdehyde (lipid membrane peroxidation product) in thalassemia. Birth Defects Orig. Artic. Ser. 1987, 23:207-211.
    • (1987) Birth Defects Orig. Artic. Ser. , vol.23 , pp. 207-211
    • Vatanavicharn, S.1    Anuwatanakulchai, M.2    Yenchitsomanus, P.3    Siddhikol, C.4
  • 88
    • 0035007589 scopus 로고    scopus 로고
    • Oral supplements of vitamin E improve measures of oxidative stress in plasma and reduce oxidative damage to LDL and erythrocytes in beta-thalassemia intermedia patients
    • Tesoriere L., D'Arpa D., Butera D., et al. Oral supplements of vitamin E improve measures of oxidative stress in plasma and reduce oxidative damage to LDL and erythrocytes in beta-thalassemia intermedia patients. Free Radic. Res. 2001, 34:529-540.
    • (2001) Free Radic. Res. , vol.34 , pp. 529-540
    • Tesoriere, L.1    D'Arpa, D.2    Butera, D.3
  • 90
    • 0036432879 scopus 로고    scopus 로고
    • Enhanced erythrocyte apoptosis in sickle cell anemia, thalassemia and glucose-6-phosphate dehydrogenase deficiency
    • Lang K.S., Roll B., Myssina S., et al. Enhanced erythrocyte apoptosis in sickle cell anemia, thalassemia and glucose-6-phosphate dehydrogenase deficiency. Cell. Physiol. Biochem. 2002, 12:365-372.
    • (2002) Cell. Physiol. Biochem. , vol.12 , pp. 365-372
    • Lang, K.S.1    Roll, B.2    Myssina, S.3
  • 92
    • 67650065532 scopus 로고    scopus 로고
    • Accumulation of lipid peroxidation-derived DNA lesions in iron-overloaded thalassemic mouse livers: comparison with levels in the lymphocytes of thalassemia patients
    • Meerang M., Nair J., Sirankapracha P., et al. Accumulation of lipid peroxidation-derived DNA lesions in iron-overloaded thalassemic mouse livers: comparison with levels in the lymphocytes of thalassemia patients. Int. J. Cancer 2009, 125:759-766.
    • (2009) Int. J. Cancer , vol.125 , pp. 759-766
    • Meerang, M.1    Nair, J.2    Sirankapracha, P.3
  • 93
  • 95
    • 0032533264 scopus 로고    scopus 로고
    • Oxidative modification of low-density lipoprotein and atherogenetic risk in beta-thalassemia
    • Livrea M.A., Tesoriere L., Maggio A., D'Arpa D., Pintaudi A.M., Pedone E. Oxidative modification of low-density lipoprotein and atherogenetic risk in beta-thalassemia. Blood 1998, 92:3936-3942.
    • (1998) Blood , vol.92 , pp. 3936-3942
    • Livrea, M.A.1    Tesoriere, L.2    Maggio, A.3    D'Arpa, D.4    Pintaudi, A.M.5    Pedone, E.6
  • 96
    • 0032055035 scopus 로고    scopus 로고
    • Oxidation resistance of LDL is correlated with vitamin E status in beta-thalassemia intermedia
    • Tesoriere L., D'Arpa D., Maggio A., Giaccone V., Pedone E., Livrea M.A. Oxidation resistance of LDL is correlated with vitamin E status in beta-thalassemia intermedia. Atherosclerosis 1998, 137:429-435.
    • (1998) Atherosclerosis , vol.137 , pp. 429-435
    • Tesoriere, L.1    D'Arpa, D.2    Maggio, A.3    Giaccone, V.4    Pedone, E.5    Livrea, M.A.6
  • 97
    • 0029959755 scopus 로고    scopus 로고
    • Oxidative stress and antioxidant status in beta-thalassemia major: iron overload and depletion of lipid-soluble antioxidants
    • Livrea M.A., Tesoriere L., Pintaudi A.M., et al. Oxidative stress and antioxidant status in beta-thalassemia major: iron overload and depletion of lipid-soluble antioxidants. Blood 1996, 88:3608-3614.
    • (1996) Blood , vol.88 , pp. 3608-3614
    • Livrea, M.A.1    Tesoriere, L.2    Pintaudi, A.M.3
  • 99
    • 84873861592 scopus 로고    scopus 로고
    • The antioxidant effect of erythropoietin on thalassemic blood cells
    • Amer J., Dana M., Fibach E. The antioxidant effect of erythropoietin on thalassemic blood cells. Anemia 2010, 2010:978710.
    • (2010) Anemia , vol.2010 , pp. 978710
    • Amer, J.1    Dana, M.2    Fibach, E.3
  • 100
    • 9144261634 scopus 로고    scopus 로고
    • In vivo reduction of erythrocyte oxidant stress in a murine model of beta-thalassemia
    • de Franceschi L., Turrini F., Honczarenko M., et al. In vivo reduction of erythrocyte oxidant stress in a murine model of beta-thalassemia. Haematologica 2004, 89:1287-1298.
    • (2004) Haematologica , vol.89 , pp. 1287-1298
    • de Franceschi, L.1    Turrini, F.2    Honczarenko, M.3
  • 101
    • 46849096278 scopus 로고    scopus 로고
    • Fermented papaya preparation as redox regulator in blood cells of beta-thalassemic mice and patients
    • Amer J., Goldfarb A., Rachmilewitz E.A., Fibach E. Fermented papaya preparation as redox regulator in blood cells of beta-thalassemic mice and patients. Phytother. Res. 2008, 22:820-828.
    • (2008) Phytother. Res. , vol.22 , pp. 820-828
    • Amer, J.1    Goldfarb, A.2    Rachmilewitz, E.A.3    Fibach, E.4
  • 102
    • 77955867065 scopus 로고    scopus 로고
    • Amelioration of oxidative stress in red blood cells from patients with beta-thalassemia major and intermedia and E-beta-thalassemia following administration of a fermented papaya preparation
    • Fibach E., Tan E.S., Jamuar S., Ng I., Amer J., Rachmilewitz E.A. Amelioration of oxidative stress in red blood cells from patients with beta-thalassemia major and intermedia and E-beta-thalassemia following administration of a fermented papaya preparation. Phytother. Res. 2010, 24:1334-1338.
    • (2010) Phytother. Res. , vol.24 , pp. 1334-1338
    • Fibach, E.1    Tan, E.S.2    Jamuar, S.3    Ng, I.4    Amer, J.5    Rachmilewitz, E.A.6
  • 103
    • 0027161045 scopus 로고
    • Phosphatidylserine in the outer leaflet of red blood cells from beta-thalassemia patients may explain the chronic hypercoagulable state and thrombotic episodes
    • Borenstain-Ben Yashar V., Barenholz Y., Hy-Am E., Rachmilewitz E.A., Eldor A. Phosphatidylserine in the outer leaflet of red blood cells from beta-thalassemia patients may explain the chronic hypercoagulable state and thrombotic episodes. Am. J. Hematol. 1993, 44:63-65.
    • (1993) Am. J. Hematol. , vol.44 , pp. 63-65
    • Borenstain-Ben Yashar, V.1    Barenholz, Y.2    Hy-Am, E.3    Rachmilewitz, E.A.4    Eldor, A.5
  • 104
    • 0036265634 scopus 로고    scopus 로고
    • Comparison of mechanisms of anemia in mice with sickle cell disease and beta-thalassemia: peripheral destruction, ineffective erythropoiesis, and phospholipid scramblase-mediated phosphatidylserine exposure
    • Kean L.S., Brown L.E., Nichols J.W., Mohandas N., Archer D.R., Hsu L.L. Comparison of mechanisms of anemia in mice with sickle cell disease and beta-thalassemia: peripheral destruction, ineffective erythropoiesis, and phospholipid scramblase-mediated phosphatidylserine exposure. Exp. Hematol. 2002, 30:394-402.
    • (2002) Exp. Hematol. , vol.30 , pp. 394-402
    • Kean, L.S.1    Brown, L.E.2    Nichols, J.W.3    Mohandas, N.4    Archer, D.R.5    Hsu, L.L.6
  • 105
    • 0033057033 scopus 로고    scopus 로고
    • Metabolic indicators of oxidative stress correlate with haemichrome attachment to membrane, band 3 aggregation and erythrophagocytosis in beta-thalassaemia intermedia
    • Cappellini M.D., Tavazzi D., Duca L., et al. Metabolic indicators of oxidative stress correlate with haemichrome attachment to membrane, band 3 aggregation and erythrophagocytosis in beta-thalassaemia intermedia. Br. J. Haematol. 1999, 104:504-512.
    • (1999) Br. J. Haematol. , vol.104 , pp. 504-512
    • Cappellini, M.D.1    Tavazzi, D.2    Duca, L.3
  • 106
    • 0029165258 scopus 로고
    • Role of hemichrome binding to erythrocyte membrane in the generation of band-3 alterations in beta-thalassemia intermedia erythrocytes
    • Mannu F., Arese P., Cappellini M.D., et al. Role of hemichrome binding to erythrocyte membrane in the generation of band-3 alterations in beta-thalassemia intermedia erythrocytes. Blood 1995, 86:2014-2020.
    • (1995) Blood , vol.86 , pp. 2014-2020
    • Mannu, F.1    Arese, P.2    Cappellini, M.D.3
  • 107
    • 35948929823 scopus 로고    scopus 로고
    • Quantitative determination of ortho- and meta-tyrosine as biomarkers of protein oxidative damage in beta-thalassemia
    • Matayatsuk C., Poljak A., Bustamante S., et al. Quantitative determination of ortho- and meta-tyrosine as biomarkers of protein oxidative damage in beta-thalassemia. Redox Rep. 2007, 12:219-228.
    • (2007) Redox Rep. , vol.12 , pp. 219-228
    • Matayatsuk, C.1    Poljak, A.2    Bustamante, S.3
  • 108
    • 84858618285 scopus 로고    scopus 로고
    • Ischemia modified albumin: an oxidative stress marker in β-thalassemia major
    • Awadallah S.M., Atoum M.F., Nimer N.A., Saleh S.A. Ischemia modified albumin: an oxidative stress marker in β-thalassemia major. Clin. Chim. Acta 2012, 413:907-910.
    • (2012) Clin. Chim. Acta , vol.413 , pp. 907-910
    • Awadallah, S.M.1    Atoum, M.F.2    Nimer, N.A.3    Saleh, S.A.4
  • 109
    • 0027181636 scopus 로고
    • Accelerated programmed cell death (apoptosis) in erythroid precursors of patients with severe beta-thalassemia (Cooley's anemia)
    • Yuan J., Angelucci E., Lucarelli G., et al. Accelerated programmed cell death (apoptosis) in erythroid precursors of patients with severe beta-thalassemia (Cooley's anemia). Blood 1993, 82:374-377.
    • (1993) Blood , vol.82 , pp. 374-377
    • Yuan, J.1    Angelucci, E.2    Lucarelli, G.3
  • 110
    • 0036867895 scopus 로고    scopus 로고
    • Oxidation of biological systems: oxidative stress phenomena, antioxidants, redox reactions, and methods for their quantification
    • Kohen R., Nyska A. Oxidation of biological systems: oxidative stress phenomena, antioxidants, redox reactions, and methods for their quantification. Toxicol. Pathol. 2002, 30:620-650.
    • (2002) Toxicol. Pathol. , vol.30 , pp. 620-650
    • Kohen, R.1    Nyska, A.2
  • 112
    • 76749103354 scopus 로고    scopus 로고
    • Improvement in oxidative stress and antioxidant parameters in beta-thalassemia/Hb E patients treated with curcuminoids
    • Kalpravidh R.W., Siritanaratkul N., Insain P., et al. Improvement in oxidative stress and antioxidant parameters in beta-thalassemia/Hb E patients treated with curcuminoids. Clin. Biochem. 2010, 43:424-429.
    • (2010) Clin. Biochem. , vol.43 , pp. 424-429
    • Kalpravidh, R.W.1    Siritanaratkul, N.2    Insain, P.3
  • 113
    • 33750034922 scopus 로고    scopus 로고
    • Lipid peroxidation and antioxidative status in beta-thalassemia major patients with or without hepatitis C virus infection
    • Chiou S.S., Chang T.T., Tsai S.P., et al. Lipid peroxidation and antioxidative status in beta-thalassemia major patients with or without hepatitis C virus infection. Clin. Chem. Lab. Med. 2006, 44:1226-1233.
    • (2006) Clin. Chem. Lab. Med. , vol.44 , pp. 1226-1233
    • Chiou, S.S.1    Chang, T.T.2    Tsai, S.P.3
  • 114
    • 33746093499 scopus 로고    scopus 로고
    • Effect of coenzyme Q10 as an antioxidant in beta-thalassemia/Hb E patients
    • Kalpravidh R.W., Wichit A., Siritanaratkul N., Fucharoen S. Effect of coenzyme Q10 as an antioxidant in beta-thalassemia/Hb E patients. Biofactors 2005, 25:225-234.
    • (2005) Biofactors , vol.25 , pp. 225-234
    • Kalpravidh, R.W.1    Wichit, A.2    Siritanaratkul, N.3    Fucharoen, S.4
  • 116
    • 1942517014 scopus 로고    scopus 로고
    • Attenuation of oxidative stress-induced changes in thalassemic erythrocytes by vitamin E
    • Das N., Das Chowdhury T., Chattopadhyay A., Datta A.G. Attenuation of oxidative stress-induced changes in thalassemic erythrocytes by vitamin E. Pol. J. Pharmacol. 2004, 56:85-96.
    • (2004) Pol. J. Pharmacol. , vol.56 , pp. 85-96
    • Das, N.1    Das Chowdhury, T.2    Chattopadhyay, A.3    Datta, A.G.4
  • 117
    • 0345017140 scopus 로고    scopus 로고
    • Oxidant, antioxidant status and metabolic data in patients with beta-thalassemia
    • Kassab-Chekir A., Laradi S., Ferchichi S., et al. Oxidant, antioxidant status and metabolic data in patients with beta-thalassemia. Clin. Chim. Acta 2003, 338:79-86.
    • (2003) Clin. Chim. Acta , vol.338 , pp. 79-86
    • Kassab-Chekir, A.1    Laradi, S.2    Ferchichi, S.3
  • 118
    • 0035105069 scopus 로고    scopus 로고
    • Antioxidant defense status of red blood cells of patients with beta-thalassemia and Ebeta-thalassemia
    • Chakraborty D., Bhattacharyya M. Antioxidant defense status of red blood cells of patients with beta-thalassemia and Ebeta-thalassemia. Clin. Chim. Acta 2001, 305:123-129.
    • (2001) Clin. Chim. Acta , vol.305 , pp. 123-129
    • Chakraborty, D.1    Bhattacharyya, M.2
  • 119
    • 0023273618 scopus 로고
    • Antioxidant system and serum trace elements in alpha-thalassaemia and Hb Lepore trait
    • Gerli G.C., Mongiat R., Sandri M.T., et al. Antioxidant system and serum trace elements in alpha-thalassaemia and Hb Lepore trait. Eur. J. Haematol. 1987, 39:23-27.
    • (1987) Eur. J. Haematol. , vol.39 , pp. 23-27
    • Gerli, G.C.1    Mongiat, R.2    Sandri, M.T.3
  • 120
    • 0022889356 scopus 로고
    • Comparison of erythrocyte antioxidative enzyme activities between two types of haemoglobin H disease
    • Prasartkaew S., Bunyaratvej A., Fucharoen S., Wasi P. Comparison of erythrocyte antioxidative enzyme activities between two types of haemoglobin H disease. J. Clin. Pathol. 1986, 39:1299-1303.
    • (1986) J. Clin. Pathol. , vol.39 , pp. 1299-1303
    • Prasartkaew, S.1    Bunyaratvej, A.2    Fucharoen, S.3    Wasi, P.4
  • 121
    • 0020693690 scopus 로고
    • Increased erythrocyte superoxide dismutase activities in beta 0-thalassaemia/haemoglobin E and in haemoglobin H diseases
    • Yenchitsomanus P., Wasi P. Increased erythrocyte superoxide dismutase activities in beta 0-thalassaemia/haemoglobin E and in haemoglobin H diseases. J. Clin. Pathol. 1983, 36:329-333.
    • (1983) J. Clin. Pathol. , vol.36 , pp. 329-333
    • Yenchitsomanus, P.1    Wasi, P.2
  • 122
    • 0018942275 scopus 로고
    • Erythrocyte superoxide dismutase, catalase and glutathione peroxidase activities in beta-thalassaemia (major and minor)
    • Gerli G.C., Beretta L., Bianchi M., Pellegatta A., Agostoni A. Erythrocyte superoxide dismutase, catalase and glutathione peroxidase activities in beta-thalassaemia (major and minor). Scand. J. Haematol. 1980, 25:87-92.
    • (1980) Scand. J. Haematol. , vol.25 , pp. 87-92
    • Gerli, G.C.1    Beretta, L.2    Bianchi, M.3    Pellegatta, A.4    Agostoni, A.5
  • 123
    • 0028839146 scopus 로고
    • Increased susceptibility of microcytic red blood cells to in vitro oxidative stress
    • Vives Corrons J.L., Miguel-García A., Pujades M.A., et al. Increased susceptibility of microcytic red blood cells to in vitro oxidative stress. Eur. J. Haematol. 1995, 55:327-331.
    • (1995) Eur. J. Haematol. , vol.55 , pp. 327-331
    • Vives Corrons, J.L.1    Miguel-García, A.2    Pujades, M.A.3
  • 124
    • 0027704968 scopus 로고
    • Vitamin E status, glutathione peroxidase activity and the effect of vitamin E supplementation in children with thalassemia
    • Suthutvoravut U., Hathirat P., Sirichakwal P., Sasanakul W., Tassaneeyakul A., Feungpean B. Vitamin E status, glutathione peroxidase activity and the effect of vitamin E supplementation in children with thalassemia. J. Med. Assoc. Thai. 1993, 76(Suppl. 2):146-152.
    • (1993) J. Med. Assoc. Thai. , vol.76 , Issue.SUPPL. 2 , pp. 146-152
    • Suthutvoravut, U.1    Hathirat, P.2    Sirichakwal, P.3    Sasanakul, W.4    Tassaneeyakul, A.5    Feungpean, B.6
  • 125
    • 84943133829 scopus 로고
    • Enzymes of the pentose phosphate pathway in glutathione-regulated membrane protection in beta-thalassaemia
    • Ponnazhagan S., Sarkar R. Enzymes of the pentose phosphate pathway in glutathione-regulated membrane protection in beta-thalassaemia. Eur. J. Clin. Chem. Clin. Biochem. 1992, 30:481-484.
    • (1992) Eur. J. Clin. Chem. Clin. Biochem. , vol.30 , pp. 481-484
    • Ponnazhagan, S.1    Sarkar, R.2
  • 126
    • 0019505812 scopus 로고
    • Glutathione peroxidase activity in whole blood of patients with sickle cell anaemia
    • Zimmerman C.P., Natta C. Glutathione peroxidase activity in whole blood of patients with sickle cell anaemia. Scand. J. Haematol. 1981, 26:177-181.
    • (1981) Scand. J. Haematol. , vol.26 , pp. 177-181
    • Zimmerman, C.P.1    Natta, C.2
  • 127
    • 0017663106 scopus 로고
    • Increased glutathione peroxidase activity in alpha-thalassemia
    • Beutler E., Matsumoto F., Powars D., Warner J. Increased glutathione peroxidase activity in alpha-thalassemia. Blood 1977, 50:647-655.
    • (1977) Blood , vol.50 , pp. 647-655
    • Beutler, E.1    Matsumoto, F.2    Powars, D.3    Warner, J.4
  • 128
    • 12744268394 scopus 로고    scopus 로고
    • Antioxidant deficit and enhanced susceptibility to oxidative damage in individuals with different forms of alpha-thalassaemia
    • Cheng M.L., Ho H.Y., Tseng H.C., Lee C.H., Shih L.Y., Chiu D.T. Antioxidant deficit and enhanced susceptibility to oxidative damage in individuals with different forms of alpha-thalassaemia. Br. J. Haematol. 2005, 128:119-127.
    • (2005) Br. J. Haematol. , vol.128 , pp. 119-127
    • Cheng, M.L.1    Ho, H.Y.2    Tseng, H.C.3    Lee, C.H.4    Shih, L.Y.5    Chiu, D.T.6
  • 129
    • 84864613582 scopus 로고    scopus 로고
    • A simple method for examination of polymorphisms of catalase exon 9: rs769217 in Hungarian microcytic anemia and beta-thalassemia patients
    • Nagy T., Csordás M., Kósa Z., Góth L. A simple method for examination of polymorphisms of catalase exon 9: rs769217 in Hungarian microcytic anemia and beta-thalassemia patients. Arch. Biochem. Biophys. 2012, 525:201-206.
    • (2012) Arch. Biochem. Biophys. , vol.525 , pp. 201-206
    • Nagy, T.1    Csordás, M.2    Kósa, Z.3    Góth, L.4
  • 130
    • 84857441824 scopus 로고    scopus 로고
    • Decreased blood catalase activity is not related to specific beta-thalassemia mutations in Hungary
    • Kósa Z., Nagy T., Nagy E., Fazakas F., Góth L. Decreased blood catalase activity is not related to specific beta-thalassemia mutations in Hungary. Int. J. Lab. Hematol. 2012, 34:172-178.
    • (2012) Int. J. Lab. Hematol. , vol.34 , pp. 172-178
    • Kósa, Z.1    Nagy, T.2    Nagy, E.3    Fazakas, F.4    Góth, L.5
  • 131
    • 75749139735 scopus 로고    scopus 로고
    • Non-haem iron-mediated oxidative stress in haemoglobin E beta-thalassaemia
    • Chakraborty I., Mitra S., Gachhui R., Kar M. Non-haem iron-mediated oxidative stress in haemoglobin E beta-thalassaemia. Ann. Acad. Med. Singapore 2010, 39:13-16.
    • (2010) Ann. Acad. Med. Singapore , vol.39 , pp. 13-16
    • Chakraborty, I.1    Mitra, S.2    Gachhui, R.3    Kar, M.4
  • 132
    • 38549144785 scopus 로고    scopus 로고
    • N-acetylcysteine amide (AD4) attenuates oxidative stress in beta-thalassemia blood cells
    • Amer J., Atlas D., Fibach E. N-acetylcysteine amide (AD4) attenuates oxidative stress in beta-thalassemia blood cells. Biochim. Biophys. Acta 2008, 1780:249-255.
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 249-255
    • Amer, J.1    Atlas, D.2    Fibach, E.3
  • 133
    • 18444400585 scopus 로고    scopus 로고
    • Chronic oxidative stress reduces the respiratory burst response of neutrophils from beta-thalassaemia patients
    • Amer J., Fibach E. Chronic oxidative stress reduces the respiratory burst response of neutrophils from beta-thalassaemia patients. Br. J. Haematol. 2005, 129:435-441.
    • (2005) Br. J. Haematol. , vol.129 , pp. 435-441
    • Amer, J.1    Fibach, E.2
  • 134
    • 9144245631 scopus 로고    scopus 로고
    • Oxidative status of platelets in normal and thalassemic blood
    • Amer J., Fibach E. Oxidative status of platelets in normal and thalassemic blood. Thromb. Haemost. 2004, 92:1052-1059.
    • (2004) Thromb. Haemost. , vol.92 , pp. 1052-1059
    • Amer, J.1    Fibach, E.2
  • 135
    • 3042779559 scopus 로고    scopus 로고
    • Flow cytometric analysis of the oxidative status of normal and thalassemic red blood cells
    • Amer J., Goldfarb A., Fibach E. Flow cytometric analysis of the oxidative status of normal and thalassemic red blood cells. Cytometry A 2004, 60:73-80.
    • (2004) Cytometry A , vol.60 , pp. 73-80
    • Amer, J.1    Goldfarb, A.2    Fibach, E.3
  • 137
    • 33646854927 scopus 로고    scopus 로고
    • The benefits of vitamin C and vitamin E in children with beta-thalassemia with high oxidative stress
    • Dissayabutra T., Tosukhowwong P., Seksan P. The benefits of vitamin C and vitamin E in children with beta-thalassemia with high oxidative stress. J. Med. Assoc. Thai. 2005, 88(Suppl. 4):S317-S321.
    • (2005) J. Med. Assoc. Thai. , vol.88 , Issue.SUPPL. 4
    • Dissayabutra, T.1    Tosukhowwong, P.2    Seksan, P.3
  • 138
    • 0345392519 scopus 로고    scopus 로고
    • The effects of vitamin E on platelet activity in beta-thalassaemia patients
    • Unchern S., Laoharuangpanya N., Phumala N., et al. The effects of vitamin E on platelet activity in beta-thalassaemia patients. Br. J. Haematol. 2003, 123:738-744.
    • (2003) Br. J. Haematol. , vol.123 , pp. 738-744
    • Unchern, S.1    Laoharuangpanya, N.2    Phumala, N.3
  • 139
    • 0020346751 scopus 로고
    • Vitamin E deficiency due to increased consumption in beta-thalassemia and in Gaucher's disease
    • Rachmilewitz E.A., Kornberg A., Acker M. Vitamin E deficiency due to increased consumption in beta-thalassemia and in Gaucher's disease. Ann. N. Y. Acad. Sci. 1982, 393:336-347.
    • (1982) Ann. N. Y. Acad. Sci. , vol.393 , pp. 336-347
    • Rachmilewitz, E.A.1    Kornberg, A.2    Acker, M.3
  • 140
    • 0017256126 scopus 로고
    • Alterations in the red blood cell membrane and the effect of vitamin E on osmotic fragility in beta-thalassemia major
    • Kahane I., Rachmilewitz E.A. Alterations in the red blood cell membrane and the effect of vitamin E on osmotic fragility in beta-thalassemia major. Isr. J. Med. Sci. 1976, 12:11-15.
    • (1976) Isr. J. Med. Sci. , vol.12 , pp. 11-15
    • Kahane, I.1    Rachmilewitz, E.A.2
  • 141
    • 0016475349 scopus 로고
    • High dose ascorbic acid in the management of thalassaemia leg ulcers-a pilot study
    • Afifi A.M., Ellis L., Huntsman R.G., Said M.I. High dose ascorbic acid in the management of thalassaemia leg ulcers-a pilot study. Br. J. Dermatol. 1975, 92:339-341.
    • (1975) Br. J. Dermatol. , vol.92 , pp. 339-341
    • Afifi, A.M.1    Ellis, L.2    Huntsman, R.G.3    Said, M.I.4
  • 142
    • 67149141758 scopus 로고    scopus 로고
    • Combined therapy of silymarin and desferrioxamine in patients with beta-thalassemia major: a randomized double-blind clinical trial
    • Gharagozloo M., Moayedi B., Zakerinia M., et al. Combined therapy of silymarin and desferrioxamine in patients with beta-thalassemia major: a randomized double-blind clinical trial. Fundam. Clin. Pharmacol. 2009, 23:359-365.
    • (2009) Fundam. Clin. Pharmacol. , vol.23 , pp. 359-365
    • Gharagozloo, M.1    Moayedi, B.2    Zakerinia, M.3
  • 143
    • 33744980639 scopus 로고    scopus 로고
    • Effects of silymarin on the proliferation and glutathione levels of peripheral blood mononuclear cells from beta-thalassemia major patients
    • Alidoost F., Gharagozloo M., et al. Effects of silymarin on the proliferation and glutathione levels of peripheral blood mononuclear cells from beta-thalassemia major patients. Int. Immunopharmacol. 2006, 6:1305-1310.
    • (2006) Int. Immunopharmacol. , vol.6 , pp. 1305-1310
    • Alidoost, F.1    Gharagozloo, M.2
  • 144
    • 0029044458 scopus 로고
    • Sustained increase in haemoglobin and RBC following long-term administration of recombinant human erythropoietin to patients with homozygous beta-thalassaemia
    • Rachmilewitz E.A., Aker M., Perry D., Dover G. Sustained increase in haemoglobin and RBC following long-term administration of recombinant human erythropoietin to patients with homozygous beta-thalassaemia. Br. J. Haematol. 1995, 90:341-345.
    • (1995) Br. J. Haematol. , vol.90 , pp. 341-345
    • Rachmilewitz, E.A.1    Aker, M.2    Perry, D.3    Dover, G.4
  • 145
    • 33644845747 scopus 로고    scopus 로고
    • In vitro effects of vitamin C and selenium on NK activity of patients with beta-thalassemia major
    • Atasever B., Ertan N.Z., Erdem-Kuruca S., Karakas Z. In vitro effects of vitamin C and selenium on NK activity of patients with beta-thalassemia major. Pediatr. Hematol. Oncol. 2006, 23:187-197.
    • (2006) Pediatr. Hematol. Oncol. , vol.23 , pp. 187-197
    • Atasever, B.1    Ertan, N.Z.2    Erdem-Kuruca, S.3    Karakas, Z.4
  • 146
    • 33749319474 scopus 로고    scopus 로고
    • Cytoprotective effects of the antioxidant phytochemical indicaxanthin in beta-thalassemia red blood cells
    • Tesoriere L., Allegra M., Butera D., Gentile C., Livrea M.A. Cytoprotective effects of the antioxidant phytochemical indicaxanthin in beta-thalassemia red blood cells. Free Radic. Res. 2006, 40:753-761.
    • (2006) Free Radic. Res. , vol.40 , pp. 753-761
    • Tesoriere, L.1    Allegra, M.2    Butera, D.3    Gentile, C.4    Livrea, M.A.5
  • 147
    • 70349142708 scopus 로고    scopus 로고
    • Efficacy of curcuminoids in alleviation of iron overload and lipid peroxidation in thalassemic mice
    • Thephinlap C., Phisalaphong C., Fucharoen S., Porter J.B., Srichairatanakool S. Efficacy of curcuminoids in alleviation of iron overload and lipid peroxidation in thalassemic mice. Med. Chem. 2009, 5:474-482.
    • (2009) Med. Chem. , vol.5 , pp. 474-482
    • Thephinlap, C.1    Phisalaphong, C.2    Fucharoen, S.3    Porter, J.B.4    Srichairatanakool, S.5
  • 148
    • 84856365960 scopus 로고    scopus 로고
    • Antioxidant status in beta thalassemia major: a single-center study
    • Waseem F., Khemomal K.A., Sajid R. Antioxidant status in beta thalassemia major: a single-center study. Indian J. Pathol. Microbiol. 2011, 54:761-763.
    • (2011) Indian J. Pathol. Microbiol. , vol.54 , pp. 761-763
    • Waseem, F.1    Khemomal, K.A.2    Sajid, R.3
  • 149
    • 33644689756 scopus 로고    scopus 로고
    • Antioxidant status in children with homozygous thalassemia
    • Dhawan V., Kumar Kh.R., Marwaha R.K., Ganguly N.K. Antioxidant status in children with homozygous thalassemia. Indian Pediatr. 2005, 42:1141-1145.
    • (2005) Indian Pediatr. , vol.42 , pp. 1141-1145
    • Dhawan, V.1    Kumar, K.2    Marwaha, R.K.3    Ganguly, N.K.4
  • 150
    • 0035348724 scopus 로고    scopus 로고
    • Selenium and glutathione peroxidase with beta-thalassemia major
    • Bartfay W.J., Bartfay E. Selenium and glutathione peroxidase with beta-thalassemia major. Nurs. Res. 2001, 50:178-183.
    • (2001) Nurs. Res. , vol.50 , pp. 178-183
    • Bartfay, W.J.1    Bartfay, E.2
  • 151
    • 80155198934 scopus 로고    scopus 로고
    • Chelation therapy with desferrioxamine does not normalize ferritin level but attenuates oxidative damage and improves total antioxidant level in Malaysian Chinese beta-thalassaemia major patients
    • Kuppusamy U.R., Tan J.A. Chelation therapy with desferrioxamine does not normalize ferritin level but attenuates oxidative damage and improves total antioxidant level in Malaysian Chinese beta-thalassaemia major patients. West Indian Med. J. 2011, 60:3-8.
    • (2011) West Indian Med. J. , vol.60 , pp. 3-8
    • Kuppusamy, U.R.1    Tan, J.A.2
  • 152
    • 0027216574 scopus 로고
    • Inactivation of glutathione peroxidase following entrapment of purified alpha or beta hemoglobin chains in human erythrocytes
    • Grelloni F., Gabbianelli R., Santroni A.M., Falcioni G. Inactivation of glutathione peroxidase following entrapment of purified alpha or beta hemoglobin chains in human erythrocytes. Clin. Chim. Acta 1993, 217:187-192.
    • (1993) Clin. Chim. Acta , vol.217 , pp. 187-192
    • Grelloni, F.1    Gabbianelli, R.2    Santroni, A.M.3    Falcioni, G.4
  • 153
    • 1542376929 scopus 로고    scopus 로고
    • Glutathione metabolism and its implications for health
    • Wu G., Fang Y.Z., Yang S., Lupton J.R., Turner N.D. Glutathione metabolism and its implications for health. J. Nutr. 2004, 134:489-492.
    • (2004) J. Nutr. , vol.134 , pp. 489-492
    • Wu, G.1    Fang, Y.Z.2    Yang, S.3    Lupton, J.R.4    Turner, N.D.5
  • 154
    • 0015954510 scopus 로고
    • Generation of superoxide free radical during the autoxidation of thiols
    • Misra H.P. Generation of superoxide free radical during the autoxidation of thiols. J. Biol. Chem. 1974, 249:2151-2155.
    • (1974) J. Biol. Chem. , vol.249 , pp. 2151-2155
    • Misra, H.P.1
  • 155
    • 0017758983 scopus 로고
    • Role of vitamin E in glutathione-induced oxidant stress: methemoglobin, lipid peroxidation, and hemolysis
    • Brownlee N.R., Huttner J.J., Panganamala R.V., Cornwell D.G. Role of vitamin E in glutathione-induced oxidant stress: methemoglobin, lipid peroxidation, and hemolysis. J. Lipid Res. 1977, 18:635-644.
    • (1977) J. Lipid Res. , vol.18 , pp. 635-644
    • Brownlee, N.R.1    Huttner, J.J.2    Panganamala, R.V.3    Cornwell, D.G.4
  • 157
    • 0025327523 scopus 로고
    • Ubiquinol-10 is an effective lipid soluble antioxidant at physiological concentrations
    • Frie B., Kim B.C., Ames B.N. Ubiquinol-10 is an effective lipid soluble antioxidant at physiological concentrations. Proc. Natl. Acad. Sci. U.S.A. 1990, 87:4879-4883.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 4879-4883
    • Frie, B.1    Kim, B.C.2    Ames, B.N.3
  • 158
    • 0025979077 scopus 로고
    • Ubiquinol-10 protects human low density lipoprotein more efficiently against lipid peroxidation than does alpha-tocopherol
    • Stocker R., Bowry V.W., Frie B. Ubiquinol-10 protects human low density lipoprotein more efficiently against lipid peroxidation than does alpha-tocopherol. Proc. Natl. Acad. Sci. U.S.A. 1991, 88:1646-1651.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 1646-1651
    • Stocker, R.1    Bowry, V.W.2    Frie, B.3
  • 159
    • 0025358550 scopus 로고
    • Stopped-flow kinetic study of regeneration reaction of tocopheroxyl radical by reduced ubiquinone-10 in solution
    • Mukai K., Kikuchi S., Urano S. Stopped-flow kinetic study of regeneration reaction of tocopheroxyl radical by reduced ubiquinone-10 in solution. Biochim. Biophys. Acta 1990, 1035:77-83.
    • (1990) Biochim. Biophys. Acta , vol.1035 , pp. 77-83
    • Mukai, K.1    Kikuchi, S.2    Urano, S.3
  • 160
    • 33746093499 scopus 로고    scopus 로고
    • Effect of coenzyme Q10 as an antioxidant in β-thalassemia/Hb E patients
    • Kalpravidha R.W., Wichit A., Siritanaratkul N., Fucharoen S. Effect of coenzyme Q10 as an antioxidant in β-thalassemia/Hb E patients. Biofactors 2005, 25:225-234.
    • (2005) Biofactors , vol.25 , pp. 225-234
    • Kalpravidha, R.W.1    Wichit, A.2    Siritanaratkul, N.3    Fucharoen, S.4
  • 161
    • 0034672639 scopus 로고    scopus 로고
    • The physiopathological significance of caeruloplasmin
    • Floris G., Medda R., Padiglia A., Musci G. The physiopathological significance of caeruloplasmin. Biochem. Pharmacol. 2000, 60:1735-1741.
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 1735-1741
    • Floris, G.1    Medda, R.2    Padiglia, A.3    Musci, G.4
  • 162
    • 0024576159 scopus 로고
    • Inhibition of superoxide and ferritin dependent lipid peroxidation by ceruloplasmin
    • Samokyszyn V.M., Miller D., Reif D., Aust S. Inhibition of superoxide and ferritin dependent lipid peroxidation by ceruloplasmin. J. Biol. Chem. 1989, 264:21-26.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21-26
    • Samokyszyn, V.M.1    Miller, D.2    Reif, D.3    Aust, S.4
  • 163
    • 0020529963 scopus 로고
    • Antioxidant properties of caeruloplasmin towards iron- and copper-dependent oxygen radical formation
    • Gutteridge J.M. Antioxidant properties of caeruloplasmin towards iron- and copper-dependent oxygen radical formation. FEBS Lett. 1983, 157:37-40.
    • (1983) FEBS Lett. , vol.157 , pp. 37-40
    • Gutteridge, J.M.1
  • 164
    • 0025788446 scopus 로고
    • Effects of ceruloplasmin on superoxide-dependent iron release from ferritin and lipid peroxidation
    • Samokyszyn V.M., Reif D.W., Miller D.M., Aust S.D. Effects of ceruloplasmin on superoxide-dependent iron release from ferritin and lipid peroxidation. Free Radic. Res. Commun. 1991, 1:153-159.
    • (1991) Free Radic. Res. Commun. , vol.1 , pp. 153-159
    • Samokyszyn, V.M.1    Reif, D.W.2    Miller, D.M.3    Aust, S.D.4
  • 165
    • 0030854755 scopus 로고    scopus 로고
    • Ceruloplasmin, transferrin and apotransferrin facilitate iron release from human liver cells
    • Young S.P., Fahmy M., Golding S. Ceruloplasmin, transferrin and apotransferrin facilitate iron release from human liver cells. FEBS Lett. 1997, 411:93-96.
    • (1997) FEBS Lett. , vol.411 , pp. 93-96
    • Young, S.P.1    Fahmy, M.2    Golding, S.3
  • 166
    • 0033534589 scopus 로고    scopus 로고
    • Ceruloplasmin ferroxidase activity stimulates cellular iron uptake by a trivalent cation-specific transport mechanism
    • Attieh Z.K., Mukhopadhyay C.K., Seshadri V., Tripoulas N.A., Fox P.L. Ceruloplasmin ferroxidase activity stimulates cellular iron uptake by a trivalent cation-specific transport mechanism. J. Biol. Chem. 1999, 274:1116-1123.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1116-1123
    • Attieh, Z.K.1    Mukhopadhyay, C.K.2    Seshadri, V.3    Tripoulas, N.A.4    Fox, P.L.5
  • 167
    • 0031981976 scopus 로고    scopus 로고
    • Aceruloplasminemia: an inherited neurodegenerative disease with impairment of iron homeostasis
    • Harris Z.L., Klomp L.W., Gitlin J.D. Aceruloplasminemia: an inherited neurodegenerative disease with impairment of iron homeostasis. Am. J. Clin. Nutr. 1998, 67(Suppl.):972S-977S.
    • (1998) Am. J. Clin. Nutr. , vol.67 , Issue.SUPPL.
    • Harris, Z.L.1    Klomp, L.W.2    Gitlin, J.D.3
  • 168
    • 0034656236 scopus 로고    scopus 로고
    • Increased lipid peroxidation in the brains of aceruloplasminemia patients
    • Yoshida K., Kaneko K., Miyajima H., et al. Increased lipid peroxidation in the brains of aceruloplasminemia patients. J. Neurol. Sci. 2000, 175:91-95.
    • (2000) J. Neurol. Sci. , vol.175 , pp. 91-95
    • Yoshida, K.1    Kaneko, K.2    Miyajima, H.3
  • 169
    • 0032875387 scopus 로고    scopus 로고
    • Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux
    • Harris Z.L., Durley A.P., Man T.K., Gitlin J.D. Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux. Proc. Natl. Acad. Sci. U.S.A. 1999, 96:10812-10817.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 10812-10817
    • Harris, Z.L.1    Durley, A.P.2    Man, T.K.3    Gitlin, J.D.4
  • 170
    • 79955048479 scopus 로고    scopus 로고
    • Association of haptoglobin phenotypes with ceruloplasmin ferroxidase activity in β-thalassemia major
    • Awadallah S.M., Nimer N.A., Atoum M.F., Saleh S.A. Association of haptoglobin phenotypes with ceruloplasmin ferroxidase activity in β-thalassemia major. Clin. Chim. Acta 2011, 412:975-979.
    • (2011) Clin. Chim. Acta , vol.412 , pp. 975-979
    • Awadallah, S.M.1    Nimer, N.A.2    Atoum, M.F.3    Saleh, S.A.4
  • 171
    • 0029854812 scopus 로고    scopus 로고
    • Biological and clinical significance of haptoglobin polymorphism in humans
    • Langlois M.R., Delanghe J.R. Biological and clinical significance of haptoglobin polymorphism in humans. Clin. Chem. 1996, 42:1589-1600.
    • (1996) Clin. Chem. , vol.42 , pp. 1589-1600
    • Langlois, M.R.1    Delanghe, J.R.2
  • 172
    • 0014360531 scopus 로고
    • Plasma concentrations of hemopexin, haptoglobin and heme in patients with various hemolytic diseases
    • Muller-Eberhard U., Javid J., Liem H.H., Hanstein A., Hanna M. Plasma concentrations of hemopexin, haptoglobin and heme in patients with various hemolytic diseases. Blood 1968, 32:811-815.
    • (1968) Blood , vol.32 , pp. 811-815
    • Muller-Eberhard, U.1    Javid, J.2    Liem, H.H.3    Hanstein, A.4    Hanna, M.5
  • 173
    • 0016257586 scopus 로고
    • Serum concentrations of haptoglobin and hemopexin in favism and thalassemia
    • Cutillo S., Meloni T. Serum concentrations of haptoglobin and hemopexin in favism and thalassemia. Acta Haematol. 1974, 52:65-69.
    • (1974) Acta Haematol. , vol.52 , pp. 65-69
    • Cutillo, S.1    Meloni, T.2
  • 174
    • 84875089596 scopus 로고    scopus 로고
    • Proteomic analysis of plasma protein in β-thalassemia/HbE patients treated with curcumin
    • 858.1
    • Kalpravidh R., Weeraphan C., Srisomsap C., Siritanaratkul N., Svasti M.R.J. Proteomic analysis of plasma protein in β-thalassemia/HbE patients treated with curcumin. FASEB J. 2009, 23(Suppl.). 858.1.
    • (2009) FASEB J. , vol.23 , Issue.SUPPL.
    • Kalpravidh, R.1    Weeraphan, C.2    Srisomsap, C.3    Siritanaratkul, N.4    Svasti, M.R.J.5
  • 175
    • 0032079491 scopus 로고    scopus 로고
    • Congenital anhaptoglobinemia versus acquired hypohaptoglobinemia
    • Delanghe J.R., Langlois M.R., De Buyzere M.L. Congenital anhaptoglobinemia versus acquired hypohaptoglobinemia. Blood 1998, 91:3524.
    • (1998) Blood , vol.91 , pp. 3524
    • Delanghe, J.R.1    Langlois, M.R.2    De Buyzere, M.L.3
  • 176
    • 20244371687 scopus 로고    scopus 로고
    • Plasma protein haptoglobin modulates renal iron loading
    • Fagoonee S., Gburek J., Hirsch E., et al. Plasma protein haptoglobin modulates renal iron loading. Am. J. Pathol. 2005, 166:973-983.
    • (2005) Am. J. Pathol. , vol.166 , pp. 973-983
    • Fagoonee, S.1    Gburek, J.2    Hirsch, E.3
  • 177
    • 34848925133 scopus 로고    scopus 로고
    • Lack of haptoglobin affects iron transport across duodenum by modulating ferroportin expression
    • Marro S., Barisani D., Chiabrando D., et al. Lack of haptoglobin affects iron transport across duodenum by modulating ferroportin expression. Gastroenterology 2007, 133:1261-1271.
    • (2007) Gastroenterology , vol.133 , pp. 1261-1271
    • Marro, S.1    Barisani, D.2    Chiabrando, D.3
  • 178
    • 2942542718 scopus 로고    scopus 로고
    • Haptoglobin polymorphisms and iron homeostasis in health and in disease
    • Van Vlierberghe H., Langlois M., Delanghe J. Haptoglobin polymorphisms and iron homeostasis in health and in disease. Clin. Chim. Acta 2004, 345:35-42.
    • (2004) Clin. Chim. Acta , vol.345 , pp. 35-42
    • Van Vlierberghe, H.1    Langlois, M.2    Delanghe, J.3
  • 179
    • 0036893006 scopus 로고    scopus 로고
    • Haptoglobin polymorphism and iron homeostasis
    • Beutler E., Gelbart T., Lee P. Haptoglobin polymorphism and iron homeostasis. Clin. Chem. 2002, 48:2232-2235.
    • (2002) Clin. Chem. , vol.48 , pp. 2232-2235
    • Beutler, E.1    Gelbart, T.2    Lee, P.3
  • 180
    • 33646687754 scopus 로고    scopus 로고
    • Influence of human haptoglobin polymorphism on oxidative stress induced by free hemoglobin on red blood cells
    • Gueye P.M., Glasser N., Ferard G., Lessinger J.M. Influence of human haptoglobin polymorphism on oxidative stress induced by free hemoglobin on red blood cells. Clin. Chem. Lab. Med. 2006, 44:542-547.
    • (2006) Clin. Chem. Lab. Med. , vol.44 , pp. 542-547
    • Gueye, P.M.1    Glasser, N.2    Ferard, G.3    Lessinger, J.M.4
  • 181
    • 0027358877 scopus 로고
    • Endothelial-cell heme uptake from heme proteins: induction of sensitization and desensitization to oxidant damage
    • Balla J., Jacob H.S., Balla G., Nath K., Eaton J.W., Vercellotti G.M. Endothelial-cell heme uptake from heme proteins: induction of sensitization and desensitization to oxidant damage. Proc. Natl. Acad. Sci. U.S.A. 1993, 90:9285-9289.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 9285-9289
    • Balla, J.1    Jacob, H.S.2    Balla, G.3    Nath, K.4    Eaton, J.W.5    Vercellotti, G.M.6
  • 182
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • Hentze M., Kuhn L.C. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc. Natl. Acad. Sci. U.S.A. 1996, 93:8175-8182.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 8175-8182
    • Hentze, M.1    Kuhn, L.C.2
  • 183
    • 46749135674 scopus 로고    scopus 로고
    • Hemopexin prevents endothelial damage and liver congestion in a mouse model of heme overload
    • Vinchi F., Gastaldi S., Silengo L., Altruda F., Tolosano E. Hemopexin prevents endothelial damage and liver congestion in a mouse model of heme overload. Am. J. Pathol. 2008, 173:289-299.
    • (2008) Am. J. Pathol. , vol.173 , pp. 289-299
    • Vinchi, F.1    Gastaldi, S.2    Silengo, L.3    Altruda, F.4    Tolosano, E.5
  • 184
    • 0036893587 scopus 로고    scopus 로고
    • Enhanced splenomegaly and severe liver inflammation in haptoglobin/hemopexin double-null mice after acute hemolysis
    • Tolosano E., Fagoonee S., Hirsch E., et al. Enhanced splenomegaly and severe liver inflammation in haptoglobin/hemopexin double-null mice after acute hemolysis. Blood 2002, 100:4201-4208.
    • (2002) Blood , vol.100 , pp. 4201-4208
    • Tolosano, E.1    Fagoonee, S.2    Hirsch, E.3
  • 186
    • 0035009582 scopus 로고    scopus 로고
    • The importance of proteins in defense against oxidation
    • Bourdon E., Blache D. The importance of proteins in defense against oxidation. Antioxid. Redox Signal. 2001, 3:293-311.
    • (2001) Antioxid. Redox Signal. , vol.3 , pp. 293-311
    • Bourdon, E.1    Blache, D.2
  • 187
    • 14644412955 scopus 로고    scopus 로고
    • Differential effects of cysteine and methionine residues in the antioxidant activity of human serum albumin
    • Bourdon E., Loreau N., Lagrost L., Blache D. Differential effects of cysteine and methionine residues in the antioxidant activity of human serum albumin. Free Radic. Res. 2005, 39:15-20.
    • (2005) Free Radic. Res. , vol.39 , pp. 15-20
    • Bourdon, E.1    Loreau, N.2    Lagrost, L.3    Blache, D.4
  • 188
    • 33846945770 scopus 로고    scopus 로고
    • Impairments of the biological properties of serum albumin in patients on haemodialysis
    • Lim P.S., Cheng Y.M., Yang S.M. Impairments of the biological properties of serum albumin in patients on haemodialysis. Nephrology (Carlton) 2007, 12:18-24.
    • (2007) Nephrology (Carlton) , vol.12 , pp. 18-24
    • Lim, P.S.1    Cheng, Y.M.2    Yang, S.M.3
  • 189
    • 0034815784 scopus 로고    scopus 로고
    • An analog of the human albumin N-terminus (Asp-Ala-His-Lys) prevents formation of copper-induced reactive oxygen species
    • Bar-Or D., Rael L.T., Lau E.P., et al. An analog of the human albumin N-terminus (Asp-Ala-His-Lys) prevents formation of copper-induced reactive oxygen species. Biochem. Biophys. Res. Commun. 2001, 284:856-862.
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 856-862
    • Bar-Or, D.1    Rael, L.T.2    Lau, E.P.3
  • 190
    • 0022657588 scopus 로고
    • Antioxidant properties of the proteins caeruloplasmin, albumin and transferrin. A study of their activity in serum and synovial fluid from patients with rheumatoid arthritis
    • Gutteridge J.M. Antioxidant properties of the proteins caeruloplasmin, albumin and transferrin. A study of their activity in serum and synovial fluid from patients with rheumatoid arthritis. Biochim. Biophys. Acta 1986, 869:119-127.
    • (1986) Biochim. Biophys. Acta , vol.869 , pp. 119-127
    • Gutteridge, J.M.1
  • 191
    • 0042974241 scopus 로고    scopus 로고
    • Sulfenic acid formation in human serum albumin by hydrogen peroxide and peroxynitrite
    • Carballal S., Radi R., Kirk M.C., Barnes S., Freeman B.A., Alvarez B. Sulfenic acid formation in human serum albumin by hydrogen peroxide and peroxynitrite. Biochemistry 2003, 42:9906-9914.
    • (2003) Biochemistry , vol.42 , pp. 9906-9914
    • Carballal, S.1    Radi, R.2    Kirk, M.C.3    Barnes, S.4    Freeman, B.A.5    Alvarez, B.6
  • 192
    • 0027490428 scopus 로고
    • Bilirubin attenuates radical-mediated damage to serum albumin
    • Neuzil J., Stocker R. Bilirubin attenuates radical-mediated damage to serum albumin. FEBS Lett. 1993, 331:281-284.
    • (1993) FEBS Lett. , vol.331 , pp. 281-284
    • Neuzil, J.1    Stocker, R.2
  • 193
    • 0028239795 scopus 로고
    • Free and albumin-bound bilirubin are efficient co-antioxidants for alpha-tocopherol, inhibiting plasma and low density lipoprotein lipid peroxidation
    • Neuzil J., Stocker R. Free and albumin-bound bilirubin are efficient co-antioxidants for alpha-tocopherol, inhibiting plasma and low density lipoprotein lipid peroxidation. J. Biol. Chem. 1994, 269:16712-16719.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16712-16719
    • Neuzil, J.1    Stocker, R.2
  • 195
    • 0035173354 scopus 로고    scopus 로고
    • Characterization of the Co(2+) and Ni(2+) binding amino-acid residues of the N-terminus of human albumin
    • Bar-Or D., Curtis G., Rao N., Bampos N., Lau E. Characterization of the Co(2+) and Ni(2+) binding amino-acid residues of the N-terminus of human albumin. Eur. J. Biochem. 2001, 268:42-47.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 42-47
    • Bar-Or, D.1    Curtis, G.2    Rao, N.3    Bampos, N.4    Lau, E.5
  • 196
    • 0033765993 scopus 로고    scopus 로고
    • Novel assay for cobalt-albumin binding and its potential as a marker for myocardial ischemia-a preliminary report
    • Bar-Or D., Lau E., Winkler J.V. Novel assay for cobalt-albumin binding and its potential as a marker for myocardial ischemia-a preliminary report. J. Emerg. Med. 2000, 19:311-315.
    • (2000) J. Emerg. Med. , vol.19 , pp. 311-315
    • Bar-Or, D.1    Lau, E.2    Winkler, J.V.3
  • 197
    • 29644446462 scopus 로고    scopus 로고
    • Role of reactive oxygen species on the formation of the novel diagnostic marker ischaemia modified albumin
    • Roy D., Quiles J., Gaze D.C., Collinson P., Kaski J.C., Baxter G.F. Role of reactive oxygen species on the formation of the novel diagnostic marker ischaemia modified albumin. Heart 2006, 92:113-114.
    • (2006) Heart , vol.92 , pp. 113-114
    • Roy, D.1    Quiles, J.2    Gaze, D.C.3    Collinson, P.4    Kaski, J.C.5    Baxter, G.F.6
  • 198
    • 0030797118 scopus 로고    scopus 로고
    • Antioxidant status in patients with uncomplicated insulin-dependent and non-insulin-dependent diabetes mellitus
    • Maxwell S.R., Thomason H., Sandler D., et al. Antioxidant status in patients with uncomplicated insulin-dependent and non-insulin-dependent diabetes mellitus. Eur. J. Clin. Invest. 1997, 27:484-490.
    • (1997) Eur. J. Clin. Invest. , vol.27 , pp. 484-490
    • Maxwell, S.R.1    Thomason, H.2    Sandler, D.3
  • 199
    • 0019787519 scopus 로고
    • Uric acid provides an antioxidant defense in humans against oxidant- and radical-caused aging and cancer: a hypothesis
    • Ames B.N., Cathcart R., Schwiers E., Hochstein P. Uric acid provides an antioxidant defense in humans against oxidant- and radical-caused aging and cancer: a hypothesis. Proc. Natl. Acad. Sci. U.S.A. 1981, 78:6858-6862.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 6858-6862
    • Ames, B.N.1    Cathcart, R.2    Schwiers, E.3    Hochstein, P.4
  • 200
    • 0034655982 scopus 로고    scopus 로고
    • Reaction of uric acid with peroxynitrite and implications for the mechanism of neuroprotection by uric acid
    • Squadrito G.L., Cueto R., Splenser A.E., et al. Reaction of uric acid with peroxynitrite and implications for the mechanism of neuroprotection by uric acid. Arch. Biochem. Biophys. 2000, 376:333-337.
    • (2000) Arch. Biochem. Biophys. , vol.376 , pp. 333-337
    • Squadrito, G.L.1    Cueto, R.2    Splenser, A.E.3
  • 202
    • 0022510621 scopus 로고
    • Uric acid-iron ion complexes: a new aspect of the antioxidant functions of uric acid
    • Davies K.J.A., Sevanian A., Mukkassah-Kelly S.F., Hochstein P. Uric acid-iron ion complexes: a new aspect of the antioxidant functions of uric acid. Biochem. J. 1986, 235:747-754.
    • (1986) Biochem. J. , vol.235 , pp. 747-754
    • Davies, K.J.A.1    Sevanian, A.2    Mukkassah-Kelly, S.F.3    Hochstein, P.4
  • 204
    • 0016616098 scopus 로고
    • Electron spin resonance study on peroxidase and oxidase-reactions of horse radish peroxidase and methemoglobin
    • Shiga T., Imaizumi K. Electron spin resonance study on peroxidase and oxidase-reactions of horse radish peroxidase and methemoglobin. Arch. Biochem. Biophys. 1975, 167:469-479.
    • (1975) Arch. Biochem. Biophys. , vol.167 , pp. 469-479
    • Shiga, T.1    Imaizumi, K.2
  • 205
    • 0023132858 scopus 로고
    • Bilirubin is an antioxidant of possible physiological importance
    • Stocker R., Yamamoto Y., McDonagh A.F., Glazer A.N., Ames B.N. Bilirubin is an antioxidant of possible physiological importance. Science 1987, 235:1043-1046.
    • (1987) Science , vol.235 , pp. 1043-1046
    • Stocker, R.1    Yamamoto, Y.2    McDonagh, A.F.3    Glazer, A.N.4    Ames, B.N.5
  • 207
    • 0032897558 scopus 로고    scopus 로고
    • Antioxidant and cytotoxic effects of bilirubin on neonatal erythrocytes
    • Mireles L.C., Lum M.A., Dennery P.A. Antioxidant and cytotoxic effects of bilirubin on neonatal erythrocytes. Pediatr. Res. 1999, 45:355-362.
    • (1999) Pediatr. Res. , vol.45 , pp. 355-362
    • Mireles, L.C.1    Lum, M.A.2    Dennery, P.A.3
  • 208
    • 0027978986 scopus 로고
    • Bilirubin and ascorbate antioxidant activity in neonatal plasma
    • Gopinathan V., Miller N.J., Milner A.D., Rice-Evans C.A. Bilirubin and ascorbate antioxidant activity in neonatal plasma. FEBS Lett. 1994, 349:197-200.
    • (1994) FEBS Lett. , vol.349 , pp. 197-200
    • Gopinathan, V.1    Miller, N.J.2    Milner, A.D.3    Rice-Evans, C.A.4
  • 209
    • 53149091267 scopus 로고    scopus 로고
    • Evaluation of oxidant and antioxidant status in term neonates: a plausible protective role of bilirubin
    • Shekeeb Shahab M., Kumar P., Sharma N., Narang A., Prasad R. Evaluation of oxidant and antioxidant status in term neonates: a plausible protective role of bilirubin. Mol. Cell. Biochem. 2008, 317:51-59.
    • (2008) Mol. Cell. Biochem. , vol.317 , pp. 51-59
    • Shekeeb Shahab, M.1    Kumar, P.2    Sharma, N.3    Narang, A.4    Prasad, R.5
  • 210
    • 77952386398 scopus 로고    scopus 로고
    • In vitro antioxidant activity of tocopherols and tocotrienols and comparison of vitamin E concentration and lipophilic antioxidant capacity in human plasma
    • Muller L., Theile K., Bohm V. In vitro antioxidant activity of tocopherols and tocotrienols and comparison of vitamin E concentration and lipophilic antioxidant capacity in human plasma. Mol. Nutr. Food Res. 2010, 54:731-742.
    • (2010) Mol. Nutr. Food Res. , vol.54 , pp. 731-742
    • Muller, L.1    Theile, K.2    Bohm, V.3
  • 211
    • 59349116817 scopus 로고    scopus 로고
    • Vitamin E: the shrew waiting to be tamed
    • Brigelius-Flohe R. Vitamin E: the shrew waiting to be tamed. Free Radic. Biol. Med. 2009, 46:543-554.
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 543-554
    • Brigelius-Flohe, R.1
  • 212
    • 0027251053 scopus 로고
    • The pecking order of free radicals and antioxidants: lipid peroxidation, alpha-tocopherol, and ascorbate
    • Buettner G.R. The pecking order of free radicals and antioxidants: lipid peroxidation, alpha-tocopherol, and ascorbate. Arch. Biochem. Biophys. 1993, 300:535-543.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 535-543
    • Buettner, G.R.1
  • 213
    • 0030641128 scopus 로고    scopus 로고
    • Requirement for, promotion, or inhibition by alpha-tocopherol of radical-induced initiation of plasma lipoprotein lipid peroxidation
    • Neuzil J., Thomas S.R., Stocker R. Requirement for, promotion, or inhibition by alpha-tocopherol of radical-induced initiation of plasma lipoprotein lipid peroxidation. Free Radic. Biol. Med. 1997, 22:57-71.
    • (1997) Free Radic. Biol. Med. , vol.22 , pp. 57-71
    • Neuzil, J.1    Thomas, S.R.2    Stocker, R.3
  • 215
    • 80051668513 scopus 로고    scopus 로고
    • Vitamins C and E: beneficial effects from a mechanistic perspective
    • Traber M.G., Stevens J.F. Vitamins C and E: beneficial effects from a mechanistic perspective. Free Radic. Biol. Med. 2011, 5:1000-1013.
    • (2011) Free Radic. Biol. Med. , vol.5 , pp. 1000-1013
    • Traber, M.G.1    Stevens, J.F.2
  • 216
    • 0027304737 scopus 로고
    • Ascorbic acid recycling in human neutrophils
    • Washko P.W., Wang Y., Levine M. Ascorbic acid recycling in human neutrophils. J. Biol. Chem. 1993, 268:15531-15535.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15531-15535
    • Washko, P.W.1    Wang, Y.2    Levine, M.3
  • 217
    • 0033042677 scopus 로고    scopus 로고
    • Is ascorbic acid an antioxidant for the plasma membrane?
    • May J.M. Is ascorbic acid an antioxidant for the plasma membrane?. FASEB J. 1999, 13:995-1006.
    • (1999) FASEB J. , vol.13 , pp. 995-1006
    • May, J.M.1
  • 218
    • 34548489878 scopus 로고    scopus 로고
    • 2-induced damage and iron homeostasis in human cells
    • 2-induced damage and iron homeostasis in human cells. Free Radic. Biol. Med. 2007, 43:1165-1175.
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 1165-1175
    • Duarte, T.L.1    Jones, G.D.2
  • 219
    • 0029868538 scopus 로고    scopus 로고
    • Vitamin C-driven free radical generation from iron
    • Herbert V., Shaw S., Jayatilleke E. Vitamin C-driven free radical generation from iron. J. Nutr. 1996, 126:1213S-1220S.
    • (1996) J. Nutr. , vol.126
    • Herbert, V.1    Shaw, S.2    Jayatilleke, E.3
  • 221
    • 0025239795 scopus 로고
    • The physiological role of zinc as an antioxidant
    • Bray T.M., Bettger W.J. The physiological role of zinc as an antioxidant. Free Radic. Biol. Med. 1990, 8:281-291.
    • (1990) Free Radic. Biol. Med. , vol.8 , pp. 281-291
    • Bray, T.M.1    Bettger, W.J.2
  • 222
    • 2642579266 scopus 로고    scopus 로고
    • New evidence of iron and zinc interplay at the enterocyte and neural tissues
    • Kordas K., Stoltzfus R.J. New evidence of iron and zinc interplay at the enterocyte and neural tissues. J. Nutr. 2004, 134:1295-1298.
    • (2004) J. Nutr. , vol.134 , pp. 1295-1298
    • Kordas, K.1    Stoltzfus, R.J.2
  • 223
    • 33846407277 scopus 로고    scopus 로고
    • Efficacy of zinc treatment against iron-induced toxicity in rat hepatoma cell line H4-II-E-C3
    • Formigari A., Santon A., Irato P. Efficacy of zinc treatment against iron-induced toxicity in rat hepatoma cell line H4-II-E-C3. Liver Int. 2007, 27:120-127.
    • (2007) Liver Int. , vol.27 , pp. 120-127
    • Formigari, A.1    Santon, A.2    Irato, P.3
  • 224
    • 34848877207 scopus 로고    scopus 로고
    • Zinc, antioxidant systems and metallothionein in metal mediated-apoptosis: biochemical and cytochemical aspects
    • Formigari A., Irato P., Santon A. Zinc, antioxidant systems and metallothionein in metal mediated-apoptosis: biochemical and cytochemical aspects. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 2007, 146:443-459.
    • (2007) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.146 , pp. 443-459
    • Formigari, A.1    Irato, P.2    Santon, A.3
  • 225
    • 0024416630 scopus 로고
    • Oxidative damage to human red cells induced by copper and iron complexes in the presence of ascorbate
    • Shinar E., Rachmilewitz E.A., Shifter A., Rahamim E., Saltman P. Oxidative damage to human red cells induced by copper and iron complexes in the presence of ascorbate. Biochim. Biophys. Acta 1989, 1014:66-72.
    • (1989) Biochim. Biophys. Acta , vol.1014 , pp. 66-72
    • Shinar, E.1    Rachmilewitz, E.A.2    Shifter, A.3    Rahamim, E.4    Saltman, P.5
  • 226
    • 50949093099 scopus 로고    scopus 로고
    • Zinc supplementation decreases oxidative stress, incidence of infection, and generation of inflammatory cytokines in sickle cell disease patients
    • Bao B., Prasad A.S., Beck F.W., et al. Zinc supplementation decreases oxidative stress, incidence of infection, and generation of inflammatory cytokines in sickle cell disease patients. Transl. Res. 2008, 152:67-80.
    • (2008) Transl. Res. , vol.152 , pp. 67-80
    • Bao, B.1    Prasad, A.S.2    Beck, F.W.3
  • 228
    • 2442686700 scopus 로고    scopus 로고
    • Metabolic and endocrinologic complications in beta-thalassemia major: a multicenter study in Tehran
    • Shamshirsaz A., Bekheirnia1 M.R., Kamgar M. Metabolic and endocrinologic complications in beta-thalassemia major: a multicenter study in Tehran. BMC Endocr. Disord. 2003, 3:4.
    • (2003) BMC Endocr. Disord. , vol.3 , pp. 4
    • Shamshirsaz, A.1    Bekheirnia1, M.R.2    Kamgar, M.3
  • 229
    • 12144287429 scopus 로고    scopus 로고
    • Serum zinc and its relation to bone mineral density in beta-thalassemic adolescents
    • Bekheiia M.R., Abdollah Shahirsaz A., Kamgar M., et al. Serum zinc and its relation to bone mineral density in beta-thalassemic adolescents. Biol. Trace Elem. Res. 2004, 97:215-224.
    • (2004) Biol. Trace Elem. Res. , vol.97 , pp. 215-224
    • Bekheiia, M.R.1    Abdollah Shahirsaz, A.2    Kamgar, M.3
  • 230
    • 0035217499 scopus 로고    scopus 로고
    • Serum zinc levels and zinc binding capacity in thalassemia
    • Arcasoy A., Canata D., Sinav B., et al. Serum zinc levels and zinc binding capacity in thalassemia. J. Trace Elem. Med. Biol. 2001, 15:85-87.
    • (2001) J. Trace Elem. Med. Biol. , vol.15 , pp. 85-87
    • Arcasoy, A.1    Canata, D.2    Sinav, B.3
  • 231
    • 0021345271 scopus 로고
    • Zinc levels of serum, hair and urine in homozygous beta-thalassemic subjects under hypertransfusional treatment
    • Rea F., Perrone L., Mastrobuono A., et al. Zinc levels of serum, hair and urine in homozygous beta-thalassemic subjects under hypertransfusional treatment. Acta Haematol. 1984, 71:139-142.
    • (1984) Acta Haematol. , vol.71 , pp. 139-142
    • Rea, F.1    Perrone, L.2    Mastrobuono, A.3
  • 233
    • 0032759637 scopus 로고    scopus 로고
    • Urinary zinc excretion and zinc status of patients with beta-thalassemia major
    • Aydinok Y., Coker C., Kavakli K., et al. Urinary zinc excretion and zinc status of patients with beta-thalassemia major. Biol. Trace Elem. Res. 1999, 70:165-172.
    • (1999) Biol. Trace Elem. Res. , vol.70 , pp. 165-172
    • Aydinok, Y.1    Coker, C.2    Kavakli, K.3
  • 234
    • 0027218506 scopus 로고
    • Desferrioxamine and urinary zinc excretion in beta-thalassemia major
    • Uysal Z., Akar N., Kemahli S., et al. Desferrioxamine and urinary zinc excretion in beta-thalassemia major. Pediatr. Hematol. Oncol. 1993, 10:257-260.
    • (1993) Pediatr. Hematol. Oncol. , vol.10 , pp. 257-260
    • Uysal, Z.1    Akar, N.2    Kemahli, S.3
  • 235
    • 67650805623 scopus 로고    scopus 로고
    • The human selenoproteome: recent insights into functions and regulation
    • Reeves M.A., Hoffmann P.R. The human selenoproteome: recent insights into functions and regulation. Cell. Mol. Life Sci. 2009, 66:2457-2478.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2457-2478
    • Reeves, M.A.1    Hoffmann, P.R.2
  • 236
    • 66849102130 scopus 로고    scopus 로고
    • Nutritional deficiencies in iron overloaded patients with hemoglobinopathies
    • Claster S., Wood J.C., Noetzli L., et al. Nutritional deficiencies in iron overloaded patients with hemoglobinopathies. Am. J. Hematol. 2009, 84:344-348.
    • (2009) Am. J. Hematol. , vol.84 , pp. 344-348
    • Claster, S.1    Wood, J.C.2    Noetzli, L.3
  • 237
    • 33644845747 scopus 로고    scopus 로고
    • In vitro effects of vitamin C and selenium on NK activity of patients with β-thalassemia major
    • Atasever Belkis, Ertan Nesrin Zeynep, Erdem-Kuruca Serap In vitro effects of vitamin C and selenium on NK activity of patients with β-thalassemia major. Pediatr. Hematol. Oncol. 2006, 23:187-197.
    • (2006) Pediatr. Hematol. Oncol. , vol.23 , pp. 187-197
    • Atasever, B.1    Ertan, N.Z.2    Erdem-Kuruca, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.