메뉴 건너뛰기




Volumn 48, Issue 2, 2011, Pages 103-106

Iron regulation by hepatocytes and free radicals

Author keywords

Free radicals; Hepatocyte; Hepcidin; Iron; Transferrin

Indexed keywords

CD71 ANTIGEN; CELL PROTEIN; FERRITIN; FERROPORTIN; FREE RADICAL; HEPCIDIN; IRON; IRON REGULATORY PROTEIN 1; IRON REGULATORY PROTEIN 2; NUCLEIC ACID; TRANSFERRIN; TRANSFERRIN RECEPTOR 2;

EID: 79952384324     PISSN: 09120009     EISSN: None     Source Type: Journal    
DOI: 10.3164/jcbn.10-76     Document Type: Review
Times cited : (47)

References (61)
  • 1
    • 37349059256 scopus 로고    scopus 로고
    • Oxygen-binding haem proteins
    • DOI 10.1113/expphysiol.2007.039735
    • Wilson MT, Reeder BJ. Oxygen-binding haem proteins. Exp Physiol 2008; 93: 128-132. (Pubitemid 350293981)
    • (2008) Experimental Physiology , vol.93 , Issue.1 , pp. 128-132
    • Wilson, M.T.1    Reeder, B.J.2
  • 2
    • 17144378216 scopus 로고    scopus 로고
    • Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis
    • DOI 10.1038/nrm1620
    • Rouault TA, Tong WH. Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis. Nat Rev Mol Cell Biol 2005; 6: 345-351. (Pubitemid 40516901)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.4 , pp. 345-351
    • Rouault, T.A.1    Tong, W.-H.2
  • 3
    • 33751177803 scopus 로고    scopus 로고
    • Iron-sulfur protein biogenesis in eukaryotes: Components and mechanisms
    • Lill R, Mühlenhoff U. Iron-sulfur protein biogenesis in eukaryotes: components and mechanisms. Annu Rev Cell Dev Biol 2006; 22: 457-486.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 457-486
    • Lill, R.1    Mühlenhoff, U.2
  • 4
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • DOI 10.1016/0005-2728(96)00022-9
    • Harrison PM, Arosio P. The ferritins: molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta 1996; 1275: 161-203. (Pubitemid 26248989)
    • (1996) Biochimica et Biophysica Acta - Bioenergetics , vol.1275 , Issue.3 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 5
    • 34249686049 scopus 로고    scopus 로고
    • Ferritin and ferritin isoforms I: Structure-function relationships, synthesis, degradation and secretion
    • Koorts AM, Viljoen M. Ferritin and ferritin isoforms I: structure-function relationships, synthesis, degradation and secretion. Arch Physiol Biochem 2007; 113: 30-54.
    • (2007) Arch Physiol Biochem , vol.113 , pp. 30-54
    • Koorts, A.M.1    Viljoen, M.2
  • 6
    • 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 AM, Hider RC. 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.1    Hider, R.C.2
  • 8
    • 0033597780 scopus 로고    scopus 로고
    • Molecular cloning of transferrin receptor 2. A new member of the transferrin receptor-like family
    • Kawabata H, Yang R, Hirama T, and et al. Molecular cloning of transferrin receptor 2. A new member of the transferrin receptor-like family. J Biol Chem 1999; 274: 20826-20832.
    • (1999) J Biol Chem , vol.274 , pp. 20826-20832
    • Kawabata, H.1    Yang, R.2    Hirama, T.3
  • 9
    • 0036439587 scopus 로고    scopus 로고
    • Effective binding of free iron by a single intravenous dose of human apotransferrin in haematological stem cell transplant patients
    • DOI 10.1046/j.1365-2141.2002.03836.x
    • Sahlstedt L, von Bonsdorff L, Ebeling F, Ruutu T, Parkkinen J. Effective binding of free iron by a single intravenous dose of human apotransferrin in haematological stem cell transplant patients. Br J Haematol 2002; 119: 547-553. (Pubitemid 35365512)
    • (2002) British Journal of Haematology , vol.119 , Issue.2 , pp. 547-553
    • Sahlstedt, L.1    Von Bonsdorff, L.2    Ebeling, F.3    Ruutu, T.4    Parkkinen, J.5
  • 11
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • DOI 10.1016/S0092-8674(04)00343-5, PII S0092867404003435
    • Hentze MW, Muckenthaler MU, Andrews NC. Balancing acts: molecular control of mammalian iron metabolism. Cell 2004; 117: 285-297. (Pubitemid 38534536)
    • (2004) Cell , vol.117 , Issue.3 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 12
    • 0344845282 scopus 로고    scopus 로고
    • Recycling, degradation and sensitivity to the synergistic anion of transferrin in the receptor-independent route of iron uptake by human hepatoma (HuH-7) cells
    • DOI 10.1016/S1357-2725(03)00258-9
    • Ikuta K, Zak O, Aisen P. Recycling, degradation and sensitivity to the synergistic anion of transferrin in the receptor-independent route of iron uptake by human hepatoma (HuH-7) cells. Int J Biochem Cell Biol 2004; 36: 340-352. (Pubitemid 37487768)
    • (2004) International Journal of Biochemistry and Cell Biology , vol.36 , Issue.2 , pp. 340-352
    • Ikuta, K.1    Zak, O.2    Aisen, P.3
  • 13
    • 33745727879 scopus 로고    scopus 로고
    • Functional role of DMT1 in transferrin-independent iron uptake by human hepatocyte and hepatocellular carcinoma cell, HLF
    • Shindo M, Torimoto Y, Saito H, and et al. Functional role of DMT1 in transferrin-independent iron uptake by human hepatocyte and hepatocellular carcinoma cell, HLF. Hepatol Res 2006; 35: 152-162.
    • (2006) Hepatol Res , vol.35 , pp. 152-162
    • Shindo, M.1    Torimoto, Y.2    Saito, H.3
  • 14
    • 0020550999 scopus 로고
    • Kinetics of internalization and recycling of transferrin and the transferrin receptor in a human hepatoma cell line. Effect of lysosomotropic agents
    • Ciechanover A, Schwartz AL, Dautry-Varsat A, Lodish HF. Kinetics of internalization and recycling of transferrin and the transferrin receptor in a human hepatoma cell line. Effect of lysosomotropic agents. J Biol Chem 1983; 258: 9681-9689. (Pubitemid 13049101)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.16 , pp. 9681-9689
    • Ciechanover, A.1    Schwartz, A.L.2    Dautry, V.A.3    Lodish, H.F.4
  • 15
    • 0032959574 scopus 로고    scopus 로고
    • Transferrin receptor is necessary for development of erythrocytes and the nervous system
    • DOI 10.1038/7727
    • Levy JE, Jin O, Fujiwara Y, Kuo F, Andrews NC. Transferrin receptor is necessary for development of erythrocytes and the nervous system. Nat Genet 1999; 21: 396-399. (Pubitemid 29159576)
    • (1999) Nature Genetics , vol.21 , Issue.4 , pp. 396-399
    • Levy, J.E.1    Jin, O.2    Fujiwara, Y.3    Kuo, F.4    Andrews, N.C.5
  • 16
    • 1842608845 scopus 로고    scopus 로고
    • Iron metabolism and the IRE/IRP regulatory system: An update
    • DOI 10.1196/annals.1306.001
    • Pantopoulos K. Iron metabolism and the IRE/IRP regulatory system: an update. Ann NY Acad Sci 2004; 1012: 1-13. (Pubitemid 38453511)
    • (2004) Annals of the New York Academy of Sciences , vol.1012 , pp. 1-13
    • Pantopoulos, K.1
  • 17
    • 33746361251 scopus 로고    scopus 로고
    • The role of iron regulatory proteins in mammalian iron homeostasis and disease
    • DOI 10.1038/nchembio807, PII NCHEMBIO807
    • Rouault TA. The role of iron regulatory proteins in mammalian iron homeostasis and disease. Nat Chem Biol 2006; 2: 406-414. (Pubitemid 44114917)
    • (2006) Nature Chemical Biology , vol.2 , Issue.8 , pp. 406-414
    • Rouault, T.A.1
  • 18
    • 38449094356 scopus 로고    scopus 로고
    • Iron-regulatory proteins: Molecular biology and pathophysiological implications
    • DOI 10.1017/S1462399407000531, PII S1462399407000531
    • Cairo G, Recalcati S. Iron-regulatory proteins: molecular biology and pathophysiological implications. Expert Rev Mol Med 2007; 9: 1-13. (Pubitemid 351698602)
    • (2007) Expert Reviews in Molecular Medicine , vol.9 , Issue.33 , pp. 1-13
    • Cairo, G.1    Recalcati, S.2
  • 26
    • 0035339557 scopus 로고    scopus 로고
    • Escherichia coli Nth and human hNTH1 DNA glycosylases are involved in removal of 8-oxoguanine from 8-oxoguanine/guanine mispairs in DNA
    • Matsumoto Y, Zhang QM, Takao M, Yasui A, Yonei S. Escherichia coli Nth and human hNTH1 DNA glycosylases are involved in removal of 8-oxoguanine from 8-oxoguanine/guanine mispairs in DNA. Nucleic Acids Res 2001; 29: 1975-1981. (Pubitemid 32433283)
    • (2001) Nucleic Acids Research , vol.29 , Issue.9 , pp. 1975-1981
    • Matsumoto, Y.1    Zhang, Q.-M.2    Takao, M.3    Yasui, A.4    Yonei, S.5
  • 29
    • 0034595856 scopus 로고    scopus 로고
    • Transferrin receptor 2-alpha supports cell growth both in iron-chelated cultured cells and in vivo
    • DOI 10.1074/jbc.M908846199
    • Kawabata H, Germain RS, Vuong PT, Nakamaki T, Said JW, Koeffler HP. Transferrin receptor 2-alpha supports cell growth both in iron-chelated cultured cells and in vivo. J Biol Chem 2000; 275: 16618-16625. (Pubitemid 30398888)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.22 , pp. 16618-16625
    • Kawabata, H.1    Germain, R.S.2    Vuong, P.T.3    Nakamaki, T.4    Said, J.W.5    Koeffler, H.P.6
  • 30
    • 10244265904 scopus 로고    scopus 로고
    • Diferric transferrin regulates transferrin receptor 2 protein stability
    • DOI 10.1182/blood-2004-06-2477
    • Johnson MB, Enns CA. Diferric transferrin regulates transferrin receptor 2 protein stability. Blood 2004; 104: 4287-4293. (Pubitemid 39620184)
    • (2004) Blood , vol.104 , Issue.13 , pp. 4287-4293
    • Johnson, M.B.1    Enns, C.A.2
  • 31
    • 33947111426 scopus 로고    scopus 로고
    • Transferrin receptor 2: Evidence for ligand-induced stabilization and redirection to a recycling pathway
    • DOI 10.1091/mbc.E06-09-0798
    • Johnson MB, Chen J, Murchison N, Green FA, Enns CA. Transferrin receptor 2: evidence for ligand-induced stabilization and redirection to a recycling pathway. Mol Biol Cell 2007; 18: 743-754. (Pubitemid 46399482)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.3 , pp. 743-754
    • Johnson, M.B.1    Chen, J.2    Murchison, N.3    Green, F.A.4    Enns, C.A.5
  • 32
    • 0025231790 scopus 로고
    • Characterization of a transferrin-independent uptake system for iron in HeLa cells
    • Sturrock A, Alexander J, Lamb J, Craven CM, Kaplan J. Characterization of a transferrin-independent uptake system for iron in HeLa cells. J Biol Chem 1990; 265: 3139-3145.
    • (1990) J Biol Chem , vol.265 , pp. 3139-3145
    • Sturrock, A.1    Alexander, J.2    Lamb, J.3    Craven, C.M.4    Kaplan, J.5
  • 35
    • 0025059348 scopus 로고
    • Iron regulation of ferritin gene expression
    • Munro HN. Iron regulation of ferritin gene expression. J Cell Biochem 1990; 44: 107-115. (Pubitemid 20350940)
    • (1990) Journal of Cellular Biochemistry , vol.44 , Issue.2 , pp. 107-115
    • Munro, H.N.1
  • 37
    • 0038670716 scopus 로고    scopus 로고
    • Ferritin: At the crossroads of iron and oxygen metabolism
    • Theil EC. Ferritin: at the crossroads of iron and oxygen metabolism. J Nutr 2003; 133: 1549S-1553S.
    • (2003) J Nutr , vol.133
    • Theil, E.C.1
  • 39
    • 0023430885 scopus 로고    scopus 로고
    • A cis-acting element is necessary and sufficient for translational regulation of human ferritin expression in response to iron
    • Hentze MW, Rouault TA, Caughman SW, and et al. A cis-acting element is necessary and sufficient for translational regulation of human ferritin expression in response to iron. Proc Natl Acad Sci USA 1987; 84: 6730-6734.
    • Proc Natl Acad Sci USA 1987 , vol.84 , pp. 6730-6734
    • Hentze, M.W.1    Rouault, T.A.2    Caughman, S.W.3
  • 40
    • 0035498850 scopus 로고    scopus 로고
    • The end of the beginning for pluripotent stem cells
    • Donovan PJ, Gearhart J. The end of the beginning for pluripotent stem cells. Nature 2001; 414: 92-97.
    • (2001) Nature , vol.414 , pp. 92-97
    • Donovan, P.J.1    Gearhart, J.2
  • 41
  • 43
    • 0035896642 scopus 로고    scopus 로고
    • Hepcidin, a urinary antimicrobial peptide synthesized in the liver
    • Park CH, Valore EV, Waring AJ, 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, Ch.1    Valore, E.V.2    Waring, A.J.3    Ganz, T.4
  • 45
    • 0036698323 scopus 로고    scopus 로고
    • Hepcidin: The Grail of iron metabolism
    • Loréal O, Brissot P. Hepcidin: the Grail of iron metabolism. Gastroenterol Clin Biol 2002; 26: 805-807.
    • (2002) Gastroenterol Clin Biol , vol.26 , pp. 805-807
    • Loréal, O.1    Brissot, P.2
  • 46
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization
    • DOI 10.1126/science.1104742
    • Nemeth E, Tuttle MS, Powelson J, and et al. Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science 2004; 306: 2090-2093. (Pubitemid 40007660)
    • (2004) Science , vol.306 , Issue.5704 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3    Vaughn, M.D.4    Donovan, A.5    Ward, D.M.6    Ganz, T.7    Kaplan, J.8
  • 47
    • 0035896581 scopus 로고    scopus 로고
    • A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin, is overexpressed during iron overload
    • Pigeon C, Ilyin G, Courselaud B, and et al. A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin, is overexpressed during iron overload. J Biol Chem 2001; 276: 7811-7819.
    • (2001) J Biol Chem , vol.276 , pp. 7811-7819
    • Pigeon, C.1    Ilyin, G.2    Courselaud, B.3
  • 48
    • 62649135982 scopus 로고    scopus 로고
    • Hepcidin-induced internalization of ferroportin requires binding and cooperative interaction with Jak2
    • De Domenico I, Lo E, Ward DM, Kaplan J. Hepcidin-induced internalization of ferroportin requires binding and cooperative interaction with Jak2. Proc Natl Acad Sci USA 2009; 106: 3800-3805.
    • Proc Natl Acad Sci USA 2009 , vol.106 , pp. 3800-3805
    • De Domenico, I.1    Lo, E.2    Ward, D.M.3    Kaplan, J.4
  • 49
    • 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, and 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
  • 50
    • 2342425296 scopus 로고    scopus 로고
    • Changes in the expression of intestinal iron transport and hepatic regulatory molecules explain the enhanced iron absorption associated with pregnancy in the rat
    • DOI 10.1136/gut.2003.031153
    • Millard KN, Frazer DM, Wilkins SJ, Anderson GJ. Changes in the expression of intestinal iron transport and hepatic regulatory molecules explain the enhanced iron absorption associated with pregnancy in the rat. Gut 2004; 53: 655-660. (Pubitemid 38561442)
    • (2004) Gut , vol.53 , Issue.5 , pp. 655-660
    • Millard, K.N.1    Frazer, D.M.2    Wilkins, S.J.3    Anderson, G.J.4
  • 52
    • 0036182252 scopus 로고    scopus 로고
    • Denatured H-ferritin subunit is a major constituent of haemosiderin in the liver of patients with iron overload
    • DOI 10.1136/gut.50.3.413
    • Miyazaki E, Kato J, Kobune M, and et al. Denatured H-ferritin subunit is a major constituent of haemosiderin in the liver of patients with iron overload. Gut 2002; 50: 413-419. (Pubitemid 34161061)
    • (2002) Gut , vol.50 , Issue.3 , pp. 413-419
    • Miyazaki, E.1    Kato, J.2    Kobune, M.3    Okumura, K.4    Sasaki, K.5    Shintani, N.6    Arosio, P.7    Niitsu, Y.8
  • 53
    • 0029946043 scopus 로고    scopus 로고
    • Fas mediates apoptosis in human monocytes by a reactive oxygen intermediate dependent pathway
    • Um HD, Orenstein JM, Wahl SM. Fas mediates apoptosis in human monocytes by a reactive oxygen intermediate dependent pathway. J Immunol 1996; 156: 3469-3477. (Pubitemid 26123563)
    • (1996) Journal of Immunology , vol.156 , Issue.9 , pp. 3469-3477
    • Um, H.-D.1    Orenstein, J.M.2    Wahl, S.M.3
  • 54
    • 0025238656 scopus 로고
    • Autophagic degradation of protein generates a pool of ferric iron required for the killing of cultured hepatocytes by an oxidative stress
    • Sakaida I, Kyle ME, Farber JL. Autophagic degradation of protein generates a pool of ferric iron required for the killing of cultured hepatocytes by an oxidative stress. Mol Pharmacol 1990; 37: 435-442. (Pubitemid 20115603)
    • (1990) Molecular Pharmacology , vol.37 , Issue.3 , pp. 435-442
    • Sakaida, I.1    Kyle, M.E.2    Farber, J.L.3
  • 55
    • 0025964030 scopus 로고
    • Increases in cytosolic calcium ion concentration can be dissociated from the killing of cultured hepatocytes by tert-butyl hydroperoxide
    • Sakaida I, Thomas AP, Farber JL. Increases in cytosolic calcium ion concentration can be dissociated from the killing of cultured hepatocytes by tertbutyl hydroperoxide. J Biol Chem 1991; 266: 717-722. (Pubitemid 21907173)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.2 , pp. 717-722
    • Sakaida, I.1    Thomas, A.P.2    Farber, J.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.