메뉴 건너뛰기




Volumn 26, Issue 4, 2005, Pages 315-324

Advances in iron metabolism: A transition state;Données récentes sur le métabolisme du fer: Un état de transition

Author keywords

Haemochromatosis; Hepcidin; Iron metabolism; Regulation

Indexed keywords

DNA MICROARRAY; GENE CONTROL; GENE EXPRESSION; HOMEOSTASIS; HUMAN; INTESTINE ABSORPTION; IRON METABOLISM; IRON TRANSPORT; NONHUMAN; PROTEIN FUNCTION; REGULATORY MECHANISM; REVIEW;

EID: 17044369245     PISSN: 02488663     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.revmed.2004.09.024     Document Type: Short Survey
Times cited : (16)

References (93)
  • 2
    • 17044416307 scopus 로고    scopus 로고
    • Regulation of mammalian iron metabolism: Current state and need for further knowledge
    • H.A. Goldenberg Regulation of mammalian iron metabolism: current state and need for further knowledge Crit. Rev. Clin. Lab. Sci. 51 1997 S4 S8
    • (1997) Crit. Rev. Clin. Lab. Sci. , vol.51
    • Goldenberg, H.A.1
  • 3
    • 0642287958 scopus 로고    scopus 로고
    • Mechanisms and regulation of intestinal iron absorption
    • E.H. Morgan, and P.S. Oates Mechanisms and regulation of intestinal iron absorption Blood Cells Mol. Dis. 29 2002 384 399
    • (2002) Blood Cells Mol. Dis. , vol.29 , pp. 384-399
    • Morgan, E.H.1    Oates, P.S.2
  • 4
    • 0023554542 scopus 로고
    • Small intestinal regulation of ion absorption in the rat
    • M.E. Conrad, R.T. Parmley, and K. Osterloh Small intestinal regulation of ion absorption in the rat J. Lab. Clin. Med. 110 1987 418 426
    • (1987) J. Lab. Clin. Med. , vol.110 , pp. 418-426
    • Conrad, M.E.1    Parmley, R.T.2    Osterloh, K.3
  • 5
    • 0030959086 scopus 로고    scopus 로고
    • Regulation of intestinal non-haem iron absorption
    • M. Lombard, E. Chua, and P. O'Toole Regulation of intestinal non-haem iron absorption Gut 40 1997 435 439
    • (1997) Gut , vol.40 , pp. 435-439
    • Lombard, M.1    Chua, E.2    O'Toole, P.3
  • 8
    • 0030755366 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian proton-coupled-metal-iron transporter
    • H. Gunshin, B. Mackenzie, U.V. Berger, Y. Gunshin, M.G. Romera, and W.F. Boron Cloning and characterization of a mammalian proton-coupled-metal-iron transporter Nature 388 1997 482 488
    • (1997) Nature , vol.388 , pp. 482-488
    • Gunshin, H.1    MacKenzie, B.2    Berger, U.V.3    Gunshin, Y.4    Romera, M.G.5    Boron, W.F.6
  • 9
    • 0026637274 scopus 로고
    • Investigation of a role for reduction in ferric iron uptake by mouse duodenum
    • K.B. Raja, R.J. Simpson, and T.J. Peters Investigation of a role for reduction in ferric iron uptake by mouse duodenum Biochim. Biophys. Acta. 1135 1992 141 146 Erratum in Biochim. Biophys. Acta. 1993;1176:197
    • (1992) Biochim. Biophys. Acta. , vol.1135 , pp. 141-146
    • Raja, K.B.1    Simpson, R.J.2    Peters, T.J.3
  • 10
    • 0035793856 scopus 로고    scopus 로고
    • An iron-regulated ferric reductase associated with the absorption of dietary iron
    • A.T. McKie, D. Barrow, G.O. Latunde-Dada, A. Rolfs, G. Sager, and M. Mudaly An iron-regulated ferric reductase associated with the absorption of dietary iron Science 291 2001 1755 1759
    • (2001) Science , vol.291 , pp. 1755-1759
    • McKie, A.T.1    Barrow, D.2    Latunde-Dada, G.O.3    Rolfs, A.4    Sager, G.5    Mudaly, M.6
  • 12
    • 0032530922 scopus 로고    scopus 로고
    • The G185R mutation disrupts function of iron transporter Nramp2
    • M.A. Su, C.C. Trenor, J.C. Fleming, M.D. Fleming, and N.C. Andrews The G185R mutation disrupts function of iron transporter Nramp2 Blood 92 1998 2157 2163
    • (1998) Blood , vol.92 , pp. 2157-2163
    • Su, M.A.1    Trenor, C.C.2    Fleming, J.C.3    Fleming, M.D.4    Andrews, N.C.5
  • 13
    • 0027396615 scopus 로고
    • Iron absorption - The mucin-mobilferrin-integrin pathway. A competitive pathway for metal absorption
    • M.E. Conrad, and J.N. Umbreit Iron absorption - the mucin-mobilferrin- integrin pathway. A competitive pathway for metal absorption Am. J. Hematol. 42 1993 67 73
    • (1993) Am. J. Hematol. , vol.42 , pp. 67-73
    • Conrad, M.E.1    Umbreit, J.N.2
  • 14
    • 0025228853 scopus 로고
    • A newly identified iron binding protein in duodenal mucosa of rats: Purification and characterization of mobilferrin
    • M.E. Conrad, J.N. Umbreit, E.G. Moore, R.D.A. Peterson, and M.B. Jones A newly identified iron binding protein in duodenal mucosa of rats: purification and characterization of mobilferrin J. Biol. Chem. 265 1990 5273 5279
    • (1990) J. Biol. Chem. , vol.265 , pp. 5273-5279
    • Conrad, M.E.1    Umbreit, J.N.2    Moore, E.G.3    Peterson, R.D.A.4    Jones, M.B.5
  • 15
    • 0026586391 scopus 로고
    • Newly identified iron-binding protein in human duodenal mucosa
    • M.E. Conrad, J.N. Umbreit, E.G. Moore, and C.R. Rodning Newly identified iron-binding protein in human duodenal mucosa Blood 79 1992 244 247
    • (1992) Blood , vol.79 , pp. 244-247
    • Conrad, M.E.1    Umbreit, J.N.2    Moore, E.G.3    Rodning, C.R.4
  • 16
    • 0030004758 scopus 로고    scopus 로고
    • Paraferritin: A protein complex with ferrireductase activity is associated with iron absorption in rats
    • J.N. Umbreit, M.E. Conrad, E.G. Moore, M.P. Desai, and J. Turrens Paraferritin: a protein complex with ferrireductase activity is associated with iron absorption in rats Biochemistry 35 1996 6460 6469
    • (1996) Biochemistry , vol.35 , pp. 6460-6469
    • Umbreit, J.N.1    Conrad, M.E.2    Moore, E.G.3    Desai, M.P.4    Turrens, J.5
  • 17
    • 0142222530 scopus 로고    scopus 로고
    • The ceruloplasmin homolog hephaestin and the control of intestinal iron absorption
    • G.J. Anderson, D.M. Frazer, A.T. McKie, and C.D. Vulpe The ceruloplasmin homolog hephaestin and the control of intestinal iron absorption Blood Cells Mol. Dis. 29 2002 367 375
    • (2002) Blood Cells Mol. Dis. , vol.29 , pp. 367-375
    • Anderson, G.J.1    Frazer, D.M.2    McKie, A.T.3    Vulpe, C.D.4
  • 18
    • 0037962795 scopus 로고    scopus 로고
    • The orchestration of body iron intake: How and where do enterocytes receive their cues?
    • D.M. Frazer, and G.J. Anderson The orchestration of body iron intake: how and where do enterocytes receive their cues? Blood Cells Mol. Dis. 30 2003 288 297
    • (2003) Blood Cells Mol. Dis. , vol.30 , pp. 288-297
    • Frazer, D.M.1    Anderson, G.J.2
  • 19
    • 0031964395 scopus 로고    scopus 로고
    • Iron absorption and cellular transport: The mobilferrin/paraferritin paradigm
    • J.N. Umbreit, M.E. Conrad, E.G. Moore, and L.F. Latour Iron absorption and cellular transport: the mobilferrin/paraferritin paradigm Semin. Hematol. 35 1998 13 26
    • (1998) Semin. Hematol. , vol.35 , pp. 13-26
    • Umbreit, J.N.1    Conrad, M.E.2    Moore, E.G.3    Latour, L.F.4
  • 20
    • 0034677467 scopus 로고    scopus 로고
    • Positional cloning of zebrafish ferroportin 1 identifies a conserved vertebrate iron exporter
    • A. Donovan, A. Brownlie, Y. Zhou, J. Shepard, S.J. Pratt, and J. Moynihan Positional cloning of zebrafish ferroportin 1 identifies a conserved vertebrate iron exporter Nature 403 2000 776 781
    • (2000) Nature , vol.403 , pp. 776-781
    • Donovan, A.1    Brownlie, A.2    Zhou, Y.3    Shepard, J.4    Pratt, S.J.5    Moynihan, J.6
  • 21
    • 0033861745 scopus 로고    scopus 로고
    • A novel duodenal iron-regulated transporter, IREG1, implicated in the basolateral transfer of iron to the circulation
    • A.T. McKie, P. Marciani, A. Rolfs, K. Brennan, K. Wehr, and D. Barrow A novel duodenal iron-regulated transporter, IREG1, implicated in the basolateral transfer of iron to the circulation Mol. Cell 5 2000 299 309
    • (2000) Mol. Cell , vol.5 , pp. 299-309
    • McKie, A.T.1    Marciani, P.2    Rolfs, A.3    Brennan, K.4    Wehr, K.5    Barrow, D.6
  • 22
    • 0032909207 scopus 로고    scopus 로고
    • Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse
    • C.D. Vulpe, Y.M. Kuo, T.L. Murphy, L. Cowley, C. Askwith, and N. Libina Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse Nat. Genet. 21 1999 195 199
    • (1999) Nat. Genet. , vol.21 , pp. 195-199
    • Vulpe, C.D.1    Kuo, Y.M.2    Murphy, T.L.3    Cowley, L.4    Askwith, C.5    Libina, N.6
  • 25
    • 0037100517 scopus 로고    scopus 로고
    • Novel mutation in ferroportin 1 is associated with autosomal dominant hemochromatosis
    • D.F. Wallace, P. Pedersen, J.L. Dixon, P. Stephenson, J.W. Searle, and L.W. Powell Novel mutation in ferroportin 1 is associated with autosomal dominant hemochromatosis Blood 100 2002 692 694
    • (2002) Blood , vol.100 , pp. 692-694
    • Wallace, D.F.1    Pedersen, P.2    Dixon, J.L.3    Stephenson, P.4    Searle, J.W.5    Powell, L.W.6
  • 27
  • 28
    • 0014866334 scopus 로고
    • Hereditary defect of intestinal iron transport in mice with sex-linked anemia
    • J.A. Edwards, and R.M. Bannerman Hereditary defect of intestinal iron transport in mice with sex-linked anemia J. Clin. Invest. 49 1970 1869 1871
    • (1970) J. Clin. Invest. , vol.49 , pp. 1869-1871
    • Edwards, J.A.1    Bannerman, R.M.2
  • 29
    • 0014005552 scopus 로고
    • Sex-linked anemia: A hypochromic anemia of mice
    • R.M. Bannerman, and R.G. Cooper Sex-linked anemia: a hypochromic anemia of mice Science 151 1966 581 582
    • (1966) Science , vol.151 , pp. 581-582
    • Bannerman, R.M.1    Cooper, R.G.2
  • 30
    • 0033599057 scopus 로고    scopus 로고
    • Disorders of iron metabolism
    • N.C. Andrews Disorders of iron metabolism N. Engl. J. Med. 341 1999 1986 1995
    • (1999) N. Engl. J. Med. , vol.341 , pp. 1986-1995
    • Andrews, N.C.1
  • 31
    • 0022345593 scopus 로고
    • Efficient clearance of non-transferrin-bound iron by rat liver. Implications for hepatic iron loading in iron overload states
    • P. Brissot, T.L. Wright, W.L. Ma, and R.A. Weisiger Efficient clearance of non-transferrin-bound iron by rat liver. Implications for hepatic iron loading in iron overload states J. Clin. Invest. 76 1985 1463 1470
    • (1985) J. Clin. Invest. , vol.76 , pp. 1463-1470
    • Brissot, P.1    Wright, T.L.2    Ma, W.L.3    Weisiger, R.A.4
  • 32
    • 0021910539 scopus 로고
    • Low-molecular-weight iron complexes and oxygen radical reactions in idiopathic haemochromatosis
    • J.M. Gutteridge, D.A. Rowley, E. Griffiths, and B. Halliwell Low-molecular-weight iron complexes and oxygen radical reactions in idiopathic haemochromatosis Clin Sci (Colch) 68 1985 463 467
    • (1985) Clin Sci (Colch) , vol.68 , pp. 463-467
    • Gutteridge, J.M.1    Rowley, D.A.2    Griffiths, E.3    Halliwell, B.4
  • 33
    • 0023430885 scopus 로고
    • A cis-acting element is necessary and sufficient for translational regulation of human ferritin expression in response to iron
    • M.W. Hentze, T.A. Rouault, S.W. Caughman, A. Dancis, J.B. Harford, and R.D. Klausner A cis-acting element is necessary and sufficient for translational regulation of human ferritin expression in response to iron Proc. Natl. Acad. Sci. USA 84 1987 6730 6734
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6730-6734
    • Hentze, M.W.1    Rouault, T.A.2    Caughman, S.W.3    Dancis, A.4    Harford, J.B.5    Klausner, R.D.6
  • 35
    • 0000683220 scopus 로고
    • Iron absorption: The effect of an iron deficient diet
    • S. Pollack, R.M. Kaufman, and W.H. Crosby Iron absorption: the effect of an iron deficient diet Science 144 1964 1015 1016
    • (1964) Science , vol.144 , pp. 1015-1016
    • Pollack, S.1    Kaufman, R.M.2    Crosby, W.H.3
  • 36
    • 0016325705 scopus 로고
    • Origin, differentiation and renewal of the four main epithelial cell types in the mouse small intestine
    • H. Cheng, and C.F. Leblond Origin, differentiation and renewal of the four main epithelial cell types in the mouse small intestine Am. J. Anat. 141 1974 537 562
    • (1974) Am. J. Anat. , vol.141 , pp. 537-562
    • Cheng, H.1    Leblond, C.F.2
  • 37
    • 0001537486 scopus 로고
    • Radioactive iron absorption by the gastro-intestinal tract: Influence of anemia, anoxia, and antecedent feeding distribution in growing dogs
    • P.F. Hahn, W.F. Bale, J.F. Ross, W.M. Balfour, and G.H. Whipple Radioactive iron absorption by the gastro-intestinal tract: influence of anemia, anoxia, and antecedent feeding distribution in growing dogs J. Exp. Med. 78 1943 169 188
    • (1943) J. Exp. Med. , vol.78 , pp. 169-188
    • Hahn, P.F.1    Bale, W.F.2    Ross, J.F.3    Balfour, W.M.4    Whipple, G.H.5
  • 38
    • 0028049495 scopus 로고
    • Regulators of iron balance in humans
    • C. Finch Regulators of iron balance in humans Blood 84 1994 1697 1702
    • (1994) Blood , vol.84 , pp. 1697-1702
    • Finch, C.1
  • 39
    • 0027997958 scopus 로고
    • Capacity of the store-regulator in maintaining iron balance
    • M.H. Sayers, G. English, and C. Finch Capacity of the store-regulator in maintaining iron balance Am. J. Hematol. 1994 194 197
    • (1994) Am. J. Hematol. , pp. 194-197
    • Sayers, M.H.1    English, G.2    Finch, C.3
  • 40
    • 0037020241 scopus 로고    scopus 로고
    • The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis
    • H.N. Hunter, D.B. Fulton, T. Ganz, and H.J. Vogel The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis J. Biol. Chem. 277 2002 37597 37603
    • (2002) J. Biol. Chem. , vol.277 , pp. 37597-37603
    • Hunter, H.N.1    Fulton, D.B.2    Ganz, T.3    Vogel, H.J.4
  • 41
    • 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
    • C. Pigeon, G. Ilyin, B. Courselaud, P. Leroyer, B. Turlin, and P. Brissot A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin, is overexpressed during iron overload J. Biol. Chem. 276 2001 7811 7819
    • (2001) J. Biol. Chem. , vol.276 , pp. 7811-7819
    • Pigeon, C.1    Ilyin, G.2    Courselaud, B.3    Leroyer, P.4    Turlin, B.5    Brissot, P.6
  • 42
    • 0035902605 scopus 로고    scopus 로고
    • Lack of hepcidin gene expression and severe tissue iron overload in Upstream Stimulator Factor 2 (USF2) knockout mice
    • G. Nicolas, M. Bennoun, I. Devaux, C. Beaumont, B. Grandchamp, and A. Kahn Lack of hepcidin gene expression and severe tissue iron overload in Upstream Stimulator Factor 2 (USF2) knockout mice Proc. Natl. Acad. Sci. USA 98 2001 8780 8785
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8780-8785
    • Nicolas, G.1    Bennoun, M.2    Devaux, I.3    Beaumont, C.4    Grandchamp, B.5    Kahn, A.6
  • 44
    • 0037111732 scopus 로고    scopus 로고
    • Inappropriate expression of hepcidin is associated with iron refractory anemia: Implications for the anemia of chronic disease
    • D.A. Weinstein, C.N. Roy, M.D. Fleming, M.F. Loda, J.I. Wolfsdorf, and N.C. Andrews Inappropriate expression of hepcidin is associated with iron refractory anemia: implications for the anemia of chronic disease Blood 100 2002 3776 3781
    • (2002) Blood , vol.100 , pp. 3776-3781
    • Weinstein, D.A.1    Roy, C.N.2    Fleming, M.D.3    Loda, M.F.4    Wolfsdorf, J.I.5    Andrews, N.C.6
  • 47
    • 0035902586 scopus 로고    scopus 로고
    • Hepcidin: A putative iron-regulatory hormone relevant to hereditary hemochromatosis and the anemia of chronic disease
    • R.E. Fleming, and W.S. Sly Hepcidin: a putative iron-regulatory hormone relevant to hereditary hemochromatosis and the anemia of chronic disease Proc. Natl. Acad. Sci. USA 98 2001 8160 8162
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8160-8162
    • Fleming, R.E.1    Sly, W.S.2
  • 48
    • 0036727925 scopus 로고    scopus 로고
    • Hepcidin expression inversely correlates with the expression of duodenal iron transporters and iron absorption in rats
    • D.M. Frazer, S.J. Wilkins, E.M. Becker, C.D. Vulpe, A.T. McKie, and D. Trinder Hepcidin expression inversely correlates with the expression of duodenal iron transporters and iron absorption in rats Gastroenterology 123 2002 835 844
    • (2002) Gastroenterology , vol.123 , pp. 835-844
    • Frazer, D.M.1    Wilkins, S.J.2    Becker, E.M.3    Vulpe, C.D.4    McKie, A.T.5    Trinder, D.6
  • 51
    • 0036791486 scopus 로고    scopus 로고
    • The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation
    • G. Nicolas, C. Chauvet, L. Viatte, J.L. Danan, X. Bigard, and I. Devaux The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation J. Clin. Invest. 110 2002 1037 1044
    • (2002) J. Clin. Invest. , vol.110 , pp. 1037-1044
    • Nicolas, G.1    Chauvet, C.2    Viatte, L.3    Danan, J.L.4    Bigard, X.5    Devaux, I.6
  • 53
    • 0038662619 scopus 로고    scopus 로고
    • Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein
    • E. Nemeth, E.V. Valore, M. Territo, G. Schiller, A. Lichtenstein, and T. Ganz Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein Blood 101 2003 2461 2463
    • (2003) Blood , vol.101 , pp. 2461-2463
    • Nemeth, E.1    Valore, E.V.2    Territo, M.3    Schiller, G.4    Lichtenstein, A.5    Ganz, T.6
  • 55
    • 0037847496 scopus 로고    scopus 로고
    • Constitutive hepcidin expression prevents iron overload in a mouse model of hemochromatosis
    • G. Nicolas, L. Viatte, D.Q. Lou, M. Bennoun, C. Beaumont, and A. Kahn Constitutive hepcidin expression prevents iron overload in a mouse model of hemochromatosis Nat. Genet. 34 2003 97 101
    • (2003) Nat. Genet. , vol.34 , pp. 97-101
    • Nicolas, G.1    Viatte, L.2    Lou, D.Q.3    Bennoun, M.4    Beaumont, C.5    Kahn, A.6
  • 56
    • 0037460697 scopus 로고    scopus 로고
    • Disrupted hepcidin regulation in HFE-associated haemochromatosis and the liver as a regulator of body iron homoeostasis
    • K.R. Bridle, D.M. Frazer, S.J. Wilkins, J.L. Dixon, D.M. Purdie, and D.H.G. Crawford Disrupted hepcidin regulation in HFE-associated haemochromatosis and the liver as a regulator of body iron homoeostasis Lancet 361 2003 669 673
    • (2003) Lancet , vol.361 , pp. 669-673
    • Bridle, K.R.1    Frazer, D.M.2    Wilkins, S.J.3    Dixon, J.L.4    Purdie, D.M.5    Crawford, D.H.G.6
  • 57
    • 0037509928 scopus 로고    scopus 로고
    • Regulatory defects in liver and intestine implicate abnormal hepcidin and Cybrd1 expression in mouse hemochromatosis
    • M. Muckenthaler, C.N. Roy, A.O. Custodio, B. Minana, J. De Graaf, and L.K. Montross Regulatory defects in liver and intestine implicate abnormal hepcidin and Cybrd1 expression in mouse hemochromatosis Nat. Genet. 34 2003 102 107
    • (2003) Nat. Genet. , vol.34 , pp. 102-107
    • Muckenthaler, M.1    Roy, C.N.2    Custodio, A.O.3    Minana, B.4    De Graaf, J.5    Montross, L.K.6
  • 58
    • 0036800592 scopus 로고    scopus 로고
    • A genetic view of iron homeostasis
    • N.C. Andrews A genetic view of iron homeostasis Semin. Hematol. 39 2002 227 234
    • (2002) Semin. Hematol. , vol.39 , pp. 227-234
    • Andrews, N.C.1
  • 60
    • 0032478524 scopus 로고    scopus 로고
    • Crystal structure of the hemochromatosis protein HFE and characterisation of its interaction with transferrin receptor
    • J.A. Lebrón, M.J. Bennett, D.E. Vaughn, A.J. Chirino, P.M. Snow, and G.A. Mintier Crystal structure of the hemochromatosis protein HFE and characterisation of its interaction with transferrin receptor Cell 93 1998 111 123
    • (1998) Cell , vol.93 , pp. 111-123
    • Lebrón, J.A.1    Bennett, M.J.2    Vaughn, D.E.3    Chirino, A.J.4    Snow, P.M.5    Mintier, G.A.6
  • 61
    • 17644434333 scopus 로고    scopus 로고
    • The hemochromatosis founder mutation in HLA-H disrupts beta-2-microglobulin interaction and cell surface expression
    • J.N. Feder, Z. Tsuchihashi, A. Irrinki, V.K. Lee, F.A. Mapa, and E. Morikang The hemochromatosis founder mutation in HLA-H disrupts beta-2-microglobulin interaction and cell surface expression J. Biol. Chem. 272 1997 14025 14028
    • (1997) J. Biol. Chem. , vol.272 , pp. 14025-14028
    • Feder, J.N.1    Tsuchihashi, Z.2    Irrinki, A.3    Lee, V.K.4    Mapa, F.A.5    Morikang, E.6
  • 62
    • 0032555601 scopus 로고    scopus 로고
    • Co-trafficking of HFE, a non-classical major histocompatibility complex class I protein, with the transferrin receptor implies a role in intracellular iron regulation
    • C.N. Gross, A. Irrinki, J.N. Feder, and C.A. Enns Co-trafficking of HFE, a non-classical major histocompatibility complex class I protein, with the transferrin receptor implies a role in intracellular iron regulation J. Biol. Chem. 273 1998 22068 22074
    • (1998) J. Biol. Chem. , vol.273 , pp. 22068-22074
    • Gross, C.N.1    Irrinki, A.2    Feder, J.N.3    Enns, C.A.4
  • 64
    • 0037103357 scopus 로고    scopus 로고
    • Regulation of iron absorption in Hfe mutant mice
    • R.S. Ajioka, J.E. Levy, N.C. Andrews, and J.P. Kushner Regulation of iron absorption in Hfe mutant mice Blood 100 2002 1465 1469
    • (2002) Blood , vol.100 , pp. 1465-1469
    • Ajioka, R.S.1    Levy, J.E.2    Andrews, N.C.3    Kushner, J.P.4
  • 65
    • 0842263988 scopus 로고    scopus 로고
    • Localization of iron metabolism-related mRNAs in rat liver indicate that HFE is expressed predominantly in hepatocytes
    • A.S. Zhang, S. Xiong, H. Tsukamoto, and C.A. Enns Localization of iron metabolism-related mRNAs in rat liver indicate that HFE is expressed predominantly in hepatocytes Blood 103 2004 1509 1514
    • (2004) Blood , vol.103 , pp. 1509-1514
    • Zhang, A.S.1    Xiong, S.2    Tsukamoto, H.3    Enns, C.A.4
  • 66
    • 0033597780 scopus 로고    scopus 로고
    • Molecular cloning of transferrin receptor 2. A new member of the transferrin receptor-like family
    • H. Kawabata, R. Yang, T. Hirama, P.T. Vuong, S. Kawano, and A.F. Gombart Molecular cloning of transferrin receptor 2. A new member of the transferrin receptor-like family J. Biol. Chem. 274 1999 20826 20832
    • (1999) J. Biol. Chem. , vol.274 , pp. 20826-20832
    • Kawabata, H.1    Yang, R.2    Hirama, T.3    Vuong, P.T.4    Kawano, S.5    Gombart, A.F.6
  • 67
    • 0034007995 scopus 로고    scopus 로고
    • Transferrin receptor 2: Continued expression in mouse liver in the face of iron overload and in hereditary hemochromatosis
    • R.E. Fleming, M.C. Migas, C.C. Holden, A. Waheed, R.S. Britton, and S. Tomatsu Transferrin receptor 2: continued expression in mouse liver in the face of iron overload and in hereditary hemochromatosis Proc. Natl. Acad. Sci. USA 97 2000 2214 2219
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2214-2219
    • Fleming, R.E.1    Migas, M.C.2    Holden, C.C.3    Waheed, A.4    Britton, R.S.5    Tomatsu, S.6
  • 68
    • 0034595856 scopus 로고    scopus 로고
    • Transferrin receptor 2-α supports cell growth both in iron-chelated cultured cells and in vivo
    • H. Kawabata, R.S. Germain, P.T. Vuong, T. Nakamaki, J.W. Said, and H.P. Koeffler Transferrin receptor 2-α supports cell growth both in iron-chelated cultured cells and in vivo J. Biol. Chem. 275 2000 16618 16625
    • (2000) J. Biol. Chem. , vol.275 , 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
  • 69
    • 0034623930 scopus 로고    scopus 로고
    • Comparison of the interactions of transferrin receptor and transferrin receptor 2 with transferrin and the hereditary hemochromatosis protein HFE
    • A.P. West Jr., M.J. Bennett, V.M. Sellers, N.C. Andrews, C.A. Enns, and P.J. Bjorkman Comparison of the interactions of transferrin receptor and transferrin receptor 2 with transferrin and the hereditary hemochromatosis protein HFE J. Biol. Chem. 275 2000 38135 38138
    • (2000) J. Biol. Chem. , vol.275 , pp. 38135-38138
    • West Jr., A.P.1    Bennett, M.J.2    Sellers, V.M.3    Andrews, N.C.4    Enns, C.A.5    Bjorkman, P.J.6
  • 70
    • 0034022636 scopus 로고    scopus 로고
    • The gene encoding transferrin receptor 2 is mutated in a new type of hemochromatosis mapping to 7q22
    • C. Camaschella, A. Roetto, A. Cali, M. De Gobbi, G. Garozzo, and M. Carella The gene encoding transferrin receptor 2 is mutated in a new type of hemochromatosis mapping to 7q22 Nat. Genet. 25 2000 14 15
    • (2000) Nat. Genet. , vol.25 , pp. 14-15
    • Camaschella, C.1    Roetto, A.2    Cali, A.3    De Gobbi, M.4    Garozzo, G.5    Carella, M.6
  • 71
    • 0035353167 scopus 로고    scopus 로고
    • New mutations inactivating transferrin receptor 2 in hemochromatosis type 3
    • A. Roetto, A. Totaro, A. Piperno, A. Piga, F. Longo, and G. Garozzo New mutations inactivating transferrin receptor 2 in hemochromatosis type 3 Blood 97 2001 2555 2560
    • (2001) Blood , vol.97 , pp. 2555-2560
    • Roetto, A.1    Totaro, A.2    Piperno, A.3    Piga, A.4    Longo, F.5    Garozzo, G.6
  • 72
    • 0036242163 scopus 로고    scopus 로고
    • Clinical and pathologic findings in hemochromatosis type 3 due to a novel mutation in transferrin receptor 2 gene
    • D. Girelli, C. Bozzini, A. Roetto, F. Alberti, F. Daraio, and R. Colombari Clinical and pathologic findings in hemochromatosis type 3 due to a novel mutation in transferrin receptor 2 gene Gastroenterology 122 2002 1295 1302
    • (2002) Gastroenterology , vol.122 , pp. 1295-1302
    • Girelli, D.1    Bozzini, C.2    Roetto, A.3    Alberti, F.4    Daraio, F.5    Colombari, R.6
  • 73
    • 0037111572 scopus 로고    scopus 로고
    • Structural, functional, and tissue distribution analysis of human transferrin receptor-2 by murine monoclonal antibodies and a polyclonal antiserum
    • S. Deaglio, A. Capobianco, A. Cali, F. Bellora, F. Alberti, and L. Righi Structural, functional, and tissue distribution analysis of human transferrin receptor-2 by murine monoclonal antibodies and a polyclonal antiserum Blood 100 2002 3782 3789
    • (2002) Blood , vol.100 , pp. 3782-3789
    • Deaglio, S.1    Capobianco, A.2    Cali, A.3    Bellora, F.4    Alberti, F.5    Righi, L.6
  • 74
    • 0037006654 scopus 로고    scopus 로고
    • Role of HFE in iron metabolism, hereditary haemochromatosis, anaemia of chronic disease, and secondary iron overload
    • A. Townsend, and H. Drakesmith Role of HFE in iron metabolism, hereditary haemochromatosis, anaemia of chronic disease, and secondary iron overload Lancet 359 2002 786 790
    • (2002) Lancet , vol.359 , pp. 786-790
    • Townsend, A.1    Drakesmith, H.2
  • 75
    • 0037406254 scopus 로고    scopus 로고
    • Colocalization of the mammalian hemochromatosis gene product (HFE) and a newly identified transferrin receptor (TfR2) in intestinal tissue and cells
    • W.J.H. Griffiths, and T.M. Cox Colocalization of the mammalian hemochromatosis gene product (HFE) and a newly identified transferrin receptor (TfR2) in intestinal tissue and cells J. Histochem. Cytochem. 51 2003 613 623
    • (2003) J. Histochem. Cytochem. , vol.51 , pp. 613-623
    • Griffiths, W.J.H.1    Cox, T.M.2
  • 77
    • 0023476064 scopus 로고
    • Iron regulates ferritin mRNA translation through a segment of its 5'untranslated region
    • N. Aziz, and H.N. Munro Iron regulates ferritin mRNA translation through a segment of its 5'untranslated region Proc. Natl. Acad. Sci. USA 87 1987 8478 8482
    • (1987) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8478-8482
    • Aziz, N.1    Munro, H.N.2
  • 78
    • 0023612118 scopus 로고
    • Identification of the iron-responsive element for the translational regulation of human ferritin mRNA
    • M.W. Hentze, S.W. Caughman, T.A. Rouault, J.G. Barriocanal, A. Dancis, and J.B. Harford Identification of the iron-responsive element for the translational regulation of human ferritin mRNA Science 238 1987 1570 1573
    • (1987) Science , vol.238 , pp. 1570-1573
    • Hentze, M.W.1    Caughman, S.W.2    Rouault, T.A.3    Barriocanal, J.G.4    Dancis, A.5    Harford, J.B.6
  • 79
    • 0023336087 scopus 로고
    • Non-coding 3' sequences of the transferrin receptor gene are required for mRNA regulation by iron
    • D. Owen, and L.C. Kühn Non-coding 3' sequences of the transferrin receptor gene are required for mRNA regulation by iron EMBO J. 6 1987 1287 1293
    • (1987) EMBO J. , vol.6 , pp. 1287-1293
    • Owen, D.1    Kühn, L.C.2
  • 80
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: MRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • M.W. Hentze, and L.C. Kühn Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress Proc. Natl. Acad. Sci. USA 93 1996 8175 8182
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kühn, L.C.2
  • 81
    • 0030624029 scopus 로고    scopus 로고
    • Regulation of iron metabolism in eukaryotes
    • T. Rouault, and R. Klausner Regulation of iron metabolism in eukaryotes Curr. Top. Cell. Regul. 35 1997 1 19
    • (1997) Curr. Top. Cell. Regul. , vol.35 , pp. 1-19
    • Rouault, T.1    Klausner, R.2
  • 82
    • 0027300938 scopus 로고
    • The putative iron-responsive element in the human erythroid 5-aminolevulinate synthase mRNA mediates translational control
    • C.R. Bhasker, G. Burgiel, B. Neupert, A. Emery-Goodman, L.C. Kuhn, and B.K. May The putative iron-responsive element in the human erythroid 5-aminolevulinate synthase mRNA mediates translational control J. Biol. Chem. 268 1993 12699 12705
    • (1993) J. Biol. Chem. , vol.268 , pp. 12699-12705
    • Bhasker, C.R.1    Burgiel, G.2    Neupert, B.3    Emery-Goodman, A.4    Kuhn, L.C.5    May, B.K.6
  • 83
    • 0025811624 scopus 로고
    • Human erythroid 5-aminolevulinate synthase: Promoter analysis and identification of an iron-responsive element in the mRNA
    • T.C. Cox, M.J. Bawden, A. Martin, and B.K. May Human erythroid 5-aminolevulinate synthase: promoter analysis and identification of an iron-responsive element in the mRNA EMBO J. 10 1994 1891 1902
    • (1994) EMBO J. , vol.10 , pp. 1891-1902
    • Cox, T.C.1    Bawden, M.J.2    Martin, A.3    May, B.K.4
  • 84
    • 0029899154 scopus 로고    scopus 로고
    • Translational regulation of mammalian and drosophila citric acid cycle enzymes via iron-responsive elements
    • N.K. Gray, K. Pantopoulous, T. Dandekar, B.A. Ackrell, and M.W. Hentze Translational regulation of mammalian and drosophila citric acid cycle enzymes via iron-responsive elements Proc. Natl. Acad. Sci. USA 93 1996 4925 4930
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4925-4930
    • Gray, N.K.1    Pantopoulous, K.2    Dandekar, T.3    Ackrell, B.A.4    Hentze, M.W.5
  • 85
    • 0029793466 scopus 로고    scopus 로고
    • Identification of a conserved and functional iron-responsive element in the 5' untranslated region of mammalian mitochondrial aconitase
    • H.Y. Kim, T. La Vaute, K. Iwai, R.D. Klausner, and T.A. Rouault Identification of a conserved and functional iron-responsive element in the 5' untranslated region of mammalian mitochondrial aconitase J. Biol. Chem. 271 1996 24226 24230
    • (1996) J. Biol. Chem. , vol.271 , pp. 24226-24230
    • Kim, H.Y.1    La Vaute, T.2    Iwai, K.3    Klausner, R.D.4    Rouault, T.A.5
  • 86
    • 0024276911 scopus 로고
    • A stem-loop in the 3' untranslated region mediates iron-dependent regulation of transferrin receptor mRNA stability in the cytoplasm
    • E.W. Mullner, and L.C. Kühn A stem-loop in the 3' untranslated region mediates iron-dependent regulation of transferrin receptor mRNA stability in the cytoplasm Cell 53 1988 815 825
    • (1988) Cell , vol.53 , pp. 815-825
    • Mullner, E.W.1    Kühn, L.C.2
  • 87
    • 0032104739 scopus 로고    scopus 로고
    • The human Nramp2 gene: Characterization of the gene structure, alternative splicing, promoter region and polymorphisms
    • P. Lee, T. Gelbart, C. West, C. Halloran, and E. Beutler The human Nramp2 gene: characterization of the gene structure, alternative splicing, promoter region and polymorphisms Blood Cells Mol. Dis. 24 1998 199 215
    • (1998) Blood Cells Mol. Dis. , vol.24 , pp. 199-215
    • Lee, P.1    Gelbart, T.2    West, C.3    Halloran, C.4    Beutler, E.5
  • 89
    • 0030894809 scopus 로고    scopus 로고
    • Inappropriately high iron regulatory protein activity in monocytes of patients with genetic hemochromatosis
    • G. Cairo, S. Recalcati, G. Montosi, E. Castrusini, D. Conte, and A. Pietrangelo Inappropriately high iron regulatory protein activity in monocytes of patients with genetic hemochromatosis Blood 89 1997 2546 2553
    • (1997) Blood , vol.89 , pp. 2546-2553
    • Cairo, G.1    Recalcati, S.2    Montosi, G.3    Castrusini, E.4    Conte, D.5    Pietrangelo, A.6
  • 90
    • 0032875387 scopus 로고    scopus 로고
    • Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux
    • Z.L. Harris, A.P. Durley, T.K. Man, and J.D. Gitlin Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux Proc. Natl. Acad. Sci. USA 96 1999 10812 10817
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10812-10817
    • Harris, Z.L.1    Durley, A.P.2    Man, T.K.3    Gitlin, J.D.4
  • 91
    • 0034733635 scopus 로고    scopus 로고
    • A novel mammalian iron-regulated protein involved in intracellular iron metabolism
    • S. Abboud, and D.J. Haile A novel mammalian iron-regulated protein involved in intracellular iron metabolism J. Biol. Chem. 26 2000 19906 19912
    • (2000) J. Biol. Chem. , vol.26 , pp. 19906-19912
    • Abboud, S.1    Haile, D.J.2
  • 93
    • 0028895749 scopus 로고
    • A mutation in the ceruloplasmin gene is associated with systemic hemosiderosis in humans
    • K. Yoshida, K. Furihata, S. Takeda, A. Nakamura, K. Yamamoto, and H. Morita A mutation in the ceruloplasmin gene is associated with systemic hemosiderosis in humans Nat. Genet. 9 1995 267 272
    • (1995) Nat. Genet. , vol.9 , pp. 267-272
    • Yoshida, K.1    Furihata, K.2    Takeda, S.3    Nakamura, A.4    Yamamoto, K.5    Morita, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.