메뉴 건너뛰기




Volumn 1762, Issue 4, 2006, Pages 414-423

Animal models with enhanced erythropoiesis and iron absorption

Author keywords

Erythropoiesis; Hepcidin; Hypotransferrinaemic mice; Phenylhydrazine induced anaemia

Indexed keywords

HEMOJUVELIN; HEPCIDIN; HFE PROTEIN; PHENYLHYDRAZINE; TRANSFERRIN; TRANSFERRIN RECEPTOR 2;

EID: 33644772206     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2005.12.007     Document Type: Review
Times cited : (38)

References (139)
  • 3
    • 0031963449 scopus 로고    scopus 로고
    • Function and regulation of transferrin and ferritin
    • P. Ponka, C. Beaumont, and D.R. Richardson Function and regulation of transferrin and ferritin Semin. Hematol. 35 1998 35 54
    • (1998) Semin. Hematol. , vol.35 , pp. 35-54
    • Ponka, P.1    Beaumont, C.2    Richardson, D.R.3
  • 4
    • 0033968052 scopus 로고    scopus 로고
    • Discovery of the ceruloplasmin homologue hephaestin: New insight into the copper/iron connection
    • R.S. Eisenstein Discovery of the ceruloplasmin homologue hephaestin: new insight into the copper/iron connection Nutr. Rev. 58 2000 22 26
    • (2000) Nutr. Rev. , vol.58 , pp. 22-26
    • Eisenstein, R.S.1
  • 6
    • 50349143880 scopus 로고
    • Absorption and excretion of iron
    • R.A. McCance, and E.M. Widdowson Absorption and excretion of iron Lancet 2 1937 680 684
    • (1937) Lancet , vol.2 , pp. 680-684
    • McCance, R.A.1    Widdowson, E.M.2
  • 9
    • 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
  • 10
    • 0034672236 scopus 로고    scopus 로고
    • Iron homeostasis: New tales from the crypt
    • C.N. Roy, and C.A. Enns Iron homeostasis: new tales from the crypt Blood 96 2000 4020 4027
    • (2000) Blood , vol.96 , pp. 4020-4027
    • Roy, C.N.1    Enns, C.A.2
  • 12
    • 0042866137 scopus 로고    scopus 로고
    • Physiology and molecular biology of dietary iron absorption
    • S. Miret, R.J. Simpson, and A.T. Mckie Physiology and molecular biology of dietary iron absorption Annu. Rev. Nutr. 23 2003 283 301
    • (2003) Annu. Rev. Nutr. , vol.23 , pp. 283-301
    • Miret, S.1    Simpson, R.J.2    McKie, A.T.3
  • 13
    • 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, P. Brissot, and O. Loreal 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    Loreal, O.7
  • 15
    • 14644407428 scopus 로고    scopus 로고
    • Advances in understanding the molecular basis for the regulation of dietary iron absorption
    • R.E. Fleming Advances in understanding the molecular basis for the regulation of dietary iron absorption Curr. Opin. Gastroenterol. 21 2005 201 206
    • (2005) Curr. Opin. Gastroenterol. , vol.21 , pp. 201-206
    • Fleming, R.E.1
  • 17
    • 0023848532 scopus 로고
    • Age related changes in the kinetics of iron absorption across the guinea pig proximal small intestine in vivo
    • S.K.S. Srai, S. Debnam, M. Boss, and O. Epstein Age related changes in the kinetics of iron absorption across the guinea pig proximal small intestine in vivo Biol. Neonate 53 1988 53 59
    • (1988) Biol. Neonate , vol.53 , pp. 53-59
    • Srai, S.K.S.1    Debnam, S.2    Boss, M.3    Epstein, O.4
  • 19
    • 0006908586 scopus 로고
    • Influence of altitude change on intestinal iron absorption
    • C. Reynafarje, and J. Ramos Influence of altitude change on intestinal iron absorption J. Lab. Clin. Med. 57 1961 848 855
    • (1961) J. Lab. Clin. Med. , vol.57 , pp. 848-855
    • Reynafarje, C.1    Ramos, J.2
  • 20
    • 0014979572 scopus 로고
    • The influence of hypoxia on iron absorption in the rat
    • M.K.S. Hathorn The influence of hypoxia on iron absorption in the rat Gastroenterology 60 1971 76 81
    • (1971) Gastroenterology , vol.60 , pp. 76-81
    • Hathorn, M.K.S.1
  • 21
    • 0023897841 scopus 로고
    • In vivo studies of the relationship between intestinal iron (Fe3+) absorption, hypoxia and erythropoiesis in the mouse
    • K.B. Raja, R.J. Simpson, M.J. Pippard, and T.J. Peters In vivo studies of the relationship between intestinal iron (Fe3+) absorption, hypoxia and erythropoiesis in the mouse Br. J. Haematol. 68 1988 373 378
    • (1988) Br. J. Haematol. , vol.68 , pp. 373-378
    • Raja, K.B.1    Simpson, R.J.2    Pippard, M.J.3    Peters, T.J.4
  • 22
    • 0024378623 scopus 로고
    • Effect of exchange transfusion of reticulocytes on in vitro and in vivo intestinal iron (Fe3+) absorption in mice
    • K.B. Raja, R.J. Simpson, and T.J. Peters Effect of exchange transfusion of reticulocytes on in vitro and in vivo intestinal iron (Fe3+) absorption in mice Br. J. Haematol. 73 1989 254 259
    • (1989) Br. J. Haematol. , vol.73 , pp. 254-259
    • Raja, K.B.1    Simpson, R.J.2    Peters, T.J.3
  • 24
    • 0000723465 scopus 로고
    • Studies on iron absorption: I. the relationship between the rate of erythropoiesis, hypoxia and iron absorption
    • G.A. Mendel Studies on iron absorption: I. The relationship between the rate of erythropoiesis, hypoxia and iron absorption Blood 18 1961 727 736
    • (1961) Blood , vol.18 , pp. 727-736
    • Mendel, G.A.1
  • 25
    • 0023024955 scopus 로고
    • Relationship between erythropoiesis and the enhanced intestinal uptake of ferric iron in hypoxia
    • K.B. Raja, M. Pippard, R.J. Simpson, and T.J. Peters Relationship between erythropoiesis and the enhanced intestinal uptake of ferric iron in hypoxia Br. J. Haematol. 64 1986 587 593
    • (1986) Br. J. Haematol. , vol.64 , pp. 587-593
    • Raja, K.B.1    Pippard, M.2    Simpson, R.J.3    Peters, T.J.4
  • 26
    • 0027051271 scopus 로고
    • Effect of hypoxic exposure on iron absorption in heterozygous hypotransferrinaemic mice
    • R.J. Simpson Effect of hypoxic exposure on iron absorption in heterozygous hypotransferrinaemic mice Ann. Haematol. 65 1992 260 264
    • (1992) Ann. Haematol. , vol.65 , pp. 260-264
    • Simpson, R.J.1
  • 28
    • 0030015514 scopus 로고    scopus 로고
    • Dietary iron levels and hypoxia independently affect iron absorption in mice
    • R.J. Simpson Dietary iron levels and hypoxia independently affect iron absorption in mice J. Nutr. 126 1996 1858 1864
    • (1996) J. Nutr. , vol.126 , pp. 1858-1864
    • Simpson, R.J.1
  • 29
    • 0141573094 scopus 로고
    • In vitro and in vivo studies on Fe3+ absorption by mouse duodenum. Effect of iron loading on adaptive response to chronic hypoxia
    • K.B. Raja, P.E. Duane, R.J. Ward, T.C. Iancu, R.J. Simpson, and T.J. Peters In vitro and in vivo studies on Fe3+ absorption by mouse duodenum. Effect of iron loading on adaptive response to chronic hypoxia Biochem. Pharmacol. (Life Sci. Adv.) 9 9 1990 107 117
    • (1990) Biochem. Pharmacol. (Life Sci. Adv.) , vol.9 , Issue.9 , pp. 107-117
    • Raja, K.B.1    Duane, P.E.2    Ward, R.J.3    Iancu, T.C.4    Simpson, R.J.5    Peters, T.J.6
  • 30
    • 0028282990 scopus 로고
    • Absorption of non-haem iron from food during normal pregnancy
    • J.F. Barrett, P.G. Whittaker, J.G. Williams, and T. Lind Absorption of non-haem iron from food during normal pregnancy BMJ 309 1994 79 82
    • (1994) BMJ , vol.309 , pp. 79-82
    • Barrett, J.F.1    Whittaker, P.G.2    Williams, J.G.3    Lind, T.4
  • 31
    • 3542999567 scopus 로고
    • Sexual differences in the storage and metabolism of iron
    • E.M. Widdowson, and R.A. McCance Sexual differences in the storage and metabolism of iron Biochem. J. 42 1948 577 581
    • (1948) Biochem. J. , vol.42 , pp. 577-581
    • Widdowson, E.M.1    McCance, R.A.2
  • 33
    • 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
  • 34
    • 0026482871 scopus 로고
    • Effect of enhanced erythropoiesis on iron absorption
    • B.S. Skikne, and J.D. Cook Effect of enhanced erythropoiesis on iron absorption J. Lab. Clin. Med. 120 1992 746 751
    • (1992) J. Lab. Clin. Med. , vol.120 , pp. 746-751
    • Skikne, B.S.1    Cook, J.D.2
  • 36
    • 0042810742 scopus 로고    scopus 로고
    • Animal models of hereditary iron transport disorders
    • N.C. Andrews Animal models of hereditary iron transport disorders Adv. Exp. Med. Biol. 509 2002 1 17
    • (2002) Adv. Exp. Med. Biol. , vol.509 , pp. 1-17
    • Andrews, N.C.1
  • 37
    • 0019412848 scopus 로고
    • Induction of porphobilinogen oxygenase and porphobilinogen deaminase in rat blood under conditions of erythropoietic stress
    • M.L. Tomaro, R.B. Frydman, A. Gutnisky, and A. Sburlati Induction of porphobilinogen oxygenase and porphobilinogen deaminase in rat blood under conditions of erythropoietic stress Biochim. Biophys. Acta 676 1981 31 42
    • (1981) Biochim. Biophys. Acta , vol.676 , pp. 31-42
    • Tomaro, M.L.1    Frydman, R.B.2    Gutnisky, A.3    Sburlati, A.4
  • 38
    • 0016821308 scopus 로고
    • Mechanism of induction of haemolytic anaemia by phenylhydrazine
    • K. H.A.Itano, and K. Hirota Mechanism of induction of haemolytic anaemia by phenylhydrazine Nature 256 1975 665 667
    • (1975) Nature , vol.256 , pp. 665-667
    • H.a.itano, K.1    Hirota, K.2
  • 39
    • 0020315925 scopus 로고
    • N-Phenylprotoporphyrin IX formation in the hemoglobin-phenylhydrazine reaction. Evidence for a protein-stabilized iron-phenyl intermediate
    • O. Augusto, K.L. Kunze, and P.R. Ortiz de Montellano N- Phenylprotoporphyrin IX formation in the hemoglobin-phenylhydrazine reaction. Evidence for a protein-stabilized iron-phenyl intermediate J. Biol. Chem. 257 1982 6231 6241
    • (1982) J. Biol. Chem. , vol.257 , pp. 6231-6241
    • Augusto, O.1    Kunze, K.L.2    Ortiz De Montellano, P.R.3
  • 40
    • 0021056052 scopus 로고
    • Inactivation of catalase by phenylhydrazine. Formation of a stable aryl-iron heme complex
    • P.R. Ortiz de Montellano, and D.E. Kerr Inactivation of catalase by phenylhydrazine. Formation of a stable aryl-iron heme complex J. Biol. Chem. 258 1983 10558 10563
    • (1983) J. Biol. Chem. , vol.258 , pp. 10558-10563
    • Ortiz De Montellano, P.R.1    Kerr, D.E.2
  • 41
    • 0019872977 scopus 로고
    • Isolation of the phagocytosis-inducing IgG-binding antigen on senescent somatic cells
    • M.M. Kay Isolation of the phagocytosis-inducing IgG-binding antigen on senescent somatic cells Nature 289 1981 491 494
    • (1981) Nature , vol.289 , pp. 491-494
    • Kay, M.M.1
  • 42
    • 0020334281 scopus 로고
    • Erythropoiesis, erythropoietin and iron
    • C.A. Finch Erythropoiesis, erythropoietin and iron Blood 60 1982 1241 1246
    • (1982) Blood , vol.60 , pp. 1241-1246
    • Finch, C.A.1
  • 44
    • 0022001840 scopus 로고
    • Erythropoietin concentration during the development and recovery from iron deficiency in the rat
    • L.T. Jansson, M.V. Perkkio, G. Clemons, C.J. Refino, and P.R. Dallman Erythropoietin concentration during the development and recovery from iron deficiency in the rat Blood 65 1985 959 963
    • (1985) Blood , vol.65 , pp. 959-963
    • Jansson, L.T.1    Perkkio, M.V.2    Clemons, G.3    Refino, C.J.4    Dallman, P.R.5
  • 45
    • 4644309964 scopus 로고    scopus 로고
    • Tissue-specific changes in iron metabolism genes in mice following phenylhydrazine-induced haemolysis
    • G.O. Latunde-Dada, C.D. Vulpe, G.J. Anderson, R.J. Simpson, and A.T. Mckie Tissue-specific changes in iron metabolism genes in mice following phenylhydrazine-induced haemolysis Biochim. Biophys. Acta 1690 2004 169 176
    • (2004) Biochim. Biophys. Acta , vol.1690 , pp. 169-176
    • Latunde-Dada, G.O.1    Vulpe, C.D.2    Anderson, G.J.3    Simpson, R.J.4    McKie, A.T.5
  • 48
    • 0006461193 scopus 로고
    • Effect of hemolysis on excretion and accumulation of iron in the rat
    • R.M. Kaufman, S. Pollack, P. Anderson, and W.H. Crosby Effect of hemolysis on excretion and accumulation of iron in the rat Am. J. Physiol. 207 1964 1041 1043
    • (1964) Am. J. Physiol. , vol.207 , pp. 1041-1043
    • Kaufman, R.M.1    Pollack, S.2    Anderson, P.3    Crosby, W.H.4
  • 50
    • 0008352084 scopus 로고
    • Iron metabolism in rats with phenylhydrazine-induced hemolytic disease
    • M.E. Conrad, L.R. Weintraub, and W.H. Crosby Iron metabolism in rats with phenylhydrazine-induced hemolytic disease Blood 25 1965 990 998
    • (1965) Blood , vol.25 , pp. 990-998
    • Conrad, M.E.1    Weintraub, L.R.2    Crosby, W.H.3
  • 53
    • 0021326333 scopus 로고
    • Phenylhydrazine-mediated induction of haem oxygenase activity in rat liver and kidney and development of hyperbilirubinaemia. Inhibition by zinc-protoporphyrin
    • M.D. Maines, and J.C. Veltman Phenylhydrazine-mediated induction of haem oxygenase activity in rat liver and kidney and development of hyperbilirubinaemia. Inhibition by zinc-protoporphyrin Biochem. J. 217 1984 409 417
    • (1984) Biochem. J. , vol.217 , pp. 409-417
    • Maines, M.D.1    Veltman, J.C.2
  • 55
    • 0035895096 scopus 로고    scopus 로고
    • Characterization of the iron transporter DMT1 (NRAMP2/DCT1) in red blood cells of normal and anemic mk/mk mice
    • F. CanonneHergaux, A.S. Zhang, P. Ponka, and P. Gros Characterization of the iron transporter DMT1 (NRAMP2/DCT1) in red blood cells of normal and anemic mk/mk mice Blood 98 2001 3823 3830
    • (2001) Blood , vol.98 , pp. 3823-3830
    • Canonnehergaux, F.1    Zhang, A.S.2    Ponka, P.3    Gros, P.4
  • 56
    • 0023707817 scopus 로고
    • Regulation of the distribution of tissue iron. Lessons learned from the hypotransferrinemic mouse
    • J. Kaplan, C. Craven, J. Alexander, J. Kushner, J. Lamb, and S. Bernstein Regulation of the distribution of tissue iron. Lessons learned from the hypotransferrinemic mouse Ann. N.Y. Acad. Sci. 526 1988 124 135
    • (1988) Ann. N.Y. Acad. Sci. , vol.526 , pp. 124-135
    • Kaplan, J.1    Craven, C.2    Alexander, J.3    Kushner, J.4    Lamb, J.5    Bernstein, S.6
  • 57
    • 0000605253 scopus 로고
    • Role of transferrin in iron absorption
    • M.S. Wheby, and L.G. Jones Role of transferrin in iron absorption J. Clin. Invest. 42 1963 1007 1016
    • (1963) J. Clin. Invest. , vol.42 , pp. 1007-1016
    • Wheby, M.S.1    Jones, L.G.2
  • 58
    • 0033485566 scopus 로고    scopus 로고
    • Defective recovery and severe renal damage after acute hemolysis in hemopexin-deficient mice
    • E. Tolosano, E. Hirsch, E. Patrucco, C. Camaschella, R. Navone, L. Silengo, and F. Altruda Defective recovery and severe renal damage after acute hemolysis in hemopexin-deficient mice Blood 94 1999 3906 3914
    • (1999) Blood , vol.94 , pp. 3906-3914
    • Tolosano, E.1    Hirsch, E.2    Patrucco, E.3    Camaschella, C.4    Navone, R.5    Silengo, L.6    Altruda, F.7
  • 61
    • 0001369958 scopus 로고
    • Studies on congenital hemolytic syndromes: IV. Gastrointestinal absorption of iron
    • M.E. Erlandson, B. Walden, G. Stern, M.W. Higartner, J. Wehman, and C.H. Smith Studies on congenital hemolytic syndromes: IV. Gastrointestinal absorption of iron Blood 19 1962 359 378
    • (1962) Blood , vol.19 , pp. 359-378
    • Erlandson, M.E.1    Walden, B.2    Stern, G.3    Higartner, M.W.4    Wehman, J.5    Smith, C.H.6
  • 62
    • 0014449479 scopus 로고
    • The role of oxygen supply in the regulation of erythropoiesis in compensated anaemia
    • E. Necas, and J. Neuwirt The role of oxygen supply in the regulation of erythropoiesis in compensated anaemia Scand. J. Haematol. 6 1969 179 185
    • (1969) Scand. J. Haematol. , vol.6 , pp. 179-185
    • Necas, E.1    Neuwirt, J.2
  • 63
    • 0019486898 scopus 로고
    • Factors affecting iron balance
    • M.E. Conrad, and J.C. Barton Factors affecting iron balance Am. J. Hematol. 10 1981 199 225
    • (1981) Am. J. Hematol. , vol.10 , pp. 199-225
    • Conrad, M.E.1    Barton, J.C.2
  • 64
    • 0028858571 scopus 로고
    • Cellular mechanisms underlying the increased duodenal iron absorption in rats in response to phenylhydrazine-induced haemolytic anaemia [see comments]
    • D.K. O'Riordan, P. Sharp, R.M. Sykes, S.K. Srai, O. Epstein, and E.S. Debnam Cellular mechanisms underlying the increased duodenal iron absorption in rats in response to phenylhydrazine-induced haemolytic anaemia [see comments] Eur. J. Clin. Invest. 25 1995 722 727
    • (1995) Eur. J. Clin. Invest. , vol.25 , pp. 722-727
    • O'Riordan, D.K.1    Sharp, P.2    Sykes, R.M.3    Srai, S.K.4    Epstein, O.5    Debnam, E.S.6
  • 65
    • 0020074170 scopus 로고
    • Effect of transfused reticulocytes on iron exchange
    • C.A. Finch, H. Huebers, M. Eng, and L. Miller Effect of transfused reticulocytes on iron exchange Blood 59 1982 364 369
    • (1982) Blood , vol.59 , pp. 364-369
    • Finch, C.A.1    Huebers, H.2    Eng, M.3    Miller, L.4
  • 66
    • 3442875926 scopus 로고    scopus 로고
    • Increased hepcidin expression and hypoferraemia associated with an acute phase response are not affected by inactivation of HFE
    • D.M. Frazer, S.J. Wilkins, K.N. Millard, A.T. Mckie, C.D. Vulpe, and G.J. Anderson Increased hepcidin expression and hypoferraemia associated with an acute phase response are not affected by inactivation of HFE Br. J. Haematol. 126 2004 434 436
    • (2004) Br. J. Haematol. , vol.126 , pp. 434-436
    • Frazer, D.M.1    Wilkins, S.J.2    Millard, K.N.3    McKie, A.T.4    Vulpe, C.D.5    Anderson, G.J.6
  • 68
    • 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
    • K.N. Millard, D.M. Frazer, S.J. Wilkins, and G.J. Anderson Changes in the expression of intestinal iron transport and hepatic regulatory molecules explain the enhanced iron absorption associated with pregnancy in the rat Gut 53 2004 655 660
    • (2004) Gut , vol.53 , pp. 655-660
    • Millard, K.N.1    Frazer, D.M.2    Wilkins, S.J.3    Anderson, G.J.4
  • 70
    • 0025228001 scopus 로고
    • Effects of turpentine-induced inflammation on the hypoxic stimulation of intestinal Fe3+ absorption in mice
    • K.B. Raja, P. Duane, and T.J. Peters Effects of turpentine-induced inflammation on the hypoxic stimulation of intestinal Fe3+ absorption in mice Int. J. Exp. Pathol. 71 1990 785 789
    • (1990) Int. J. Exp. Pathol. , vol.71 , pp. 785-789
    • Raja, K.B.1    Duane, P.2    Peters, T.J.3
  • 71
    • 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
  • 73
    • 0024317279 scopus 로고
    • Hepatic iron in the control of iron absorption in a rat liver transplantation model
    • P.C. Adams, A.S. Reece, L.W. Powell, and J.W. Halliday Hepatic iron in the control of iron absorption in a rat liver transplantation model Transplantation 48 1989 19 21
    • (1989) Transplantation , vol.48 , pp. 19-21
    • Adams, P.C.1    Reece, A.S.2    Powell, L.W.3    Halliday, J.W.4
  • 74
    • 23444439528 scopus 로고    scopus 로고
    • Systemic regulation of intestinal iron absorption
    • T.M. Steele, D.M. Frazer, and G.J. Anderson Systemic regulation of intestinal iron absorption IUBMB Life 57 2005 499 503
    • (2005) IUBMB Life , vol.57 , pp. 499-503
    • Steele, T.M.1    Frazer, D.M.2    Anderson, G.J.3
  • 76
    • 23644444316 scopus 로고    scopus 로고
    • Hemojuvelin is essential for dietary iron sensing, and its mutation leads to severe iron overload
    • V. Niederkofler, R. Salie, and S. Arber Hemojuvelin is essential for dietary iron sensing, and its mutation leads to severe iron overload J. Clin. Invest. 115 2005 2180 2186
    • (2005) J. Clin. Invest. , vol.115 , pp. 2180-2186
    • Niederkofler, V.1    Salie, R.2    Arber, S.3
  • 77
    • 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
  • 78
    • 0037372606 scopus 로고    scopus 로고
    • A rapid decrease in the expression of DMT1 and Dcytb but not Ireg1 or hephaestin explains the mucosal block phenomenon of iron absorption
    • D.M. Frazer, S.J. Wilkins, E.M. Becker, T.L. Murphy, C.D. Vulpe, A.T. Mckie, and G.J. Anderson A rapid decrease in the expression of DMT1 and Dcytb but not Ireg1 or hephaestin explains the mucosal block phenomenon of iron absorption Gut 52 2003 340 346
    • (2003) Gut , vol.52 , pp. 340-346
    • Frazer, D.M.1    Wilkins, S.J.2    Becker, E.M.3    Murphy, T.L.4    Vulpe, C.D.5    McKie, A.T.6    Anderson, G.J.7
  • 79
    • 0041438849 scopus 로고    scopus 로고
    • Systemic regulation of HEPHAESTIN and IREG1 revealed in studies of genetic and nutritional iron deficiency
    • H. Chen, T. Su, Z.K. Attieh, T.C. Fox, A.T. Mckie, G.J. Anderson, and C.D. Vulpe Systemic regulation of HEPHAESTIN and IREG1 revealed in studies of genetic and nutritional iron deficiency Blood 102 2003 1893 1899
    • (2003) Blood , vol.102 , pp. 1893-1899
    • Chen, H.1    Su, T.2    Attieh, Z.K.3    Fox, T.C.4    McKie, A.T.5    Anderson, G.J.6    Vulpe, C.D.7
  • 80
    • 0033072214 scopus 로고    scopus 로고
    • Kinetic analysis of 59Fe movement across the intestinal wall in duodenal rat segments ex vivo
    • K. Schumann, B. Elsenhans, and W. Forth Kinetic analysis of 59Fe movement across the intestinal wall in duodenal rat segments ex vivo Am. J. Phyisol. 276 1999 G431 G440
    • (1999) Am. J. Phyisol. , vol.276
    • Schumann, K.1    Elsenhans, B.2    Forth, W.3
  • 81
    • 0042866137 scopus 로고    scopus 로고
    • Physiology and molecular biology of dietary iron absorption
    • S. Miret, R.J. Simpson, and A.T. Mckie Physiology and molecular biology of dietary iron absorption Annu. Rev. Nutr. 23 2003 283 301
    • (2003) Annu. Rev. Nutr. , vol.23 , pp. 283-301
    • Miret, S.1    Simpson, R.J.2    McKie, A.T.3
  • 83
    • 0020035215 scopus 로고
    • Perspectives in iron metabolism
    • C.A. Finch, and H. Huebers Perspectives in iron metabolism N. Engl. J. Med. 306 1982 1520 1528
    • (1982) N. Engl. J. Med. , vol.306 , pp. 1520-1528
    • Finch, C.A.1    Huebers, H.2
  • 85
    • 0033231035 scopus 로고    scopus 로고
    • Importance of anaemia and transferrin levels in the regulation of intestinal iron absorption in hypotransferrinaemic mice
    • K.B. Raja, D.J. Pountney, R.J. Simpson, and T.J. Peters Importance of anaemia and transferrin levels in the regulation of intestinal iron absorption in hypotransferrinaemic mice Blood 94 1999 3185 3192
    • (1999) Blood , vol.94 , pp. 3185-3192
    • Raja, K.B.1    Pountney, D.J.2    Simpson, R.J.3    Peters, T.J.4
  • 88
    • 0023522698 scopus 로고
    • Hereditary hypotransferrinaemia with hemosiderosis. a murine disorder resembling human atransferrinemia
    • S.E. Bernstein Hereditary hypotransferrinaemia with hemosiderosis. A murine disorder resembling human atransferrinemia J. Lab. Clin. Med. 110 1987 690 705
    • (1987) J. Lab. Clin. Med. , vol.110 , pp. 690-705
    • Bernstein, S.E.1
  • 91
    • 0023707817 scopus 로고
    • Regulation of the distribution of tissue iron. Lessons learned from the hypotransferrinaemic mouse
    • J. Kaplan, C. Craven, J. Alexander, J. Kushner, J. Lamb, and S. Bernstein Regulation of the distribution of tissue iron. Lessons learned from the hypotransferrinaemic mouse Ann. N. Y. Acad. Sci. 526 1988 124 135
    • (1988) Ann. N. Y. Acad. Sci. , vol.526 , pp. 124-135
    • Kaplan, J.1    Craven, C.2    Alexander, J.3    Kushner, J.4    Lamb, J.5    Bernstein, S.6
  • 93
    • 0028957804 scopus 로고
    • Plasma clearance of transferrin in control and hypotransferrinaemic mice: Implications for regulation of transferrin turnover
    • K.B. Raja, R.J. Simpson, and T.J. Peters Plasma clearance of transferrin in control and hypotransferrinaemic mice: implications for regulation of transferrin turnover Br. J. Haematol. 89 1995 177 180
    • (1995) Br. J. Haematol. , vol.89 , pp. 177-180
    • Raja, K.B.1    Simpson, R.J.2    Peters, T.J.3
  • 94
    • 0030725150 scopus 로고    scopus 로고
    • Time-course of iron overload and biochemical, histopathological and ultrastructural evidence of pancreatic damage in hypotransferrinaemic mice
    • R.J. Simpson, J. Deenmamode, A.T. Mckie, K.B. Raja, J.R. Salisbury, T.C. Iancu, and T.J. Peters Time-course of iron overload and biochemical, histopathological and ultrastructural evidence of pancreatic damage in hypotransferrinaemic mice Clin. Sci. 93 1997 453 462
    • (1997) Clin. Sci. , vol.93 , pp. 453-462
    • Simpson, R.J.1    Deenmamode, J.2    McKie, A.T.3    Raja, K.B.4    Salisbury, J.R.5    Iancu, T.C.6    Peters, T.J.7
  • 95
    • 0029065064 scopus 로고
    • Cellular distribution of iron, transferrin, and ferritin in the hypotransferrinemic (Hp) mouse brain
    • T.K. Dickinson, and J.R. Connor Cellular distribution of iron, transferrin, and ferritin in the hypotransferrinemic (Hp) mouse brain J. Comp. Neurol. 355 1995 67 80
    • (1995) J. Comp. Neurol. , vol.355 , pp. 67-80
    • Dickinson, T.K.1    Connor, J.R.2
  • 96
    • 0011938460 scopus 로고
    • Tissue distribution and clearance kinetics of non-transferrin-bound iron in the hypotransferrinaemic mouse: A rodent model for hemochromatosis
    • C.M. Craven, J. Alexander, M. Eldridge, J.P. Kushner, S. Bernstein, and J. Kaplan Tissue distribution and clearance kinetics of non-transferrin-bound iron in the hypotransferrinaemic mouse: a rodent model for hemochromatosis Proc. Natl. Acad. Sci. 84 1987 3457 3461
    • (1987) Proc. Natl. Acad. Sci. , vol.84 , pp. 3457-3461
    • Craven, C.M.1    Alexander, J.2    Eldridge, M.3    Kushner, J.P.4    Bernstein, S.5    Kaplan, J.6
  • 97
    • 0027339568 scopus 로고
    • Rate of 59Fe uptake into brain and cerebrospinal fluid and the influence thereon of antibodies against the transferrin receptor
    • F. Ueda, K.B. Raja, I.S. Trowbridge, R.J. Simpson, and M.W.B. Bradbury Rate of 59Fe uptake into brain and cerebrospinal fluid and the influence thereon of antibodies against the transferrin receptor J. Neurochem. 60 1993 106 113
    • (1993) J. Neurochem. , vol.60 , pp. 106-113
    • Ueda, F.1    Raja, K.B.2    Trowbridge, I.S.3    Simpson, R.J.4    Bradbury, M.W.B.5
  • 98
    • 0030230223 scopus 로고    scopus 로고
    • Distribution of injected iron 59 and manganese 54 in hypotransferrinemic mice
    • T.K. Dickinson, A.G. Devenyi, and J.R. Connor Distribution of injected iron 59 and manganese 54 in hypotransferrinemic mice J. Lab. Clin. Med. 128 1996 270 278
    • (1996) J. Lab. Clin. Med. , vol.128 , pp. 270-278
    • Dickinson, T.K.1    Devenyi, A.G.2    Connor, J.R.3
  • 99
    • 0028305332 scopus 로고
    • Intestinal iron absorption studies in mouse models of iron-overload
    • K.B. Raja, R.J. Simpson, and T.J. Peters Intestinal iron absorption studies in mouse models of iron-overload Br. J. Haematol. 86 1994 156 162
    • (1994) Br. J. Haematol. , vol.86 , pp. 156-162
    • Raja, K.B.1    Simpson, R.J.2    Peters, T.J.3
  • 104
    • 0031047394 scopus 로고    scopus 로고
    • Iron metabolism in transgenic mice with hypoplastic anaemia due to incomplete deficiency of erythropoietin
    • K.B. Raja, P.H. Maxwell, P.J. Ratcliffe, J.R. Salisbury, R.J. Simpson, and T.J. Peters Iron metabolism in transgenic mice with hypoplastic anaemia due to incomplete deficiency of erythropoietin Br. J. Haematol. 96 1997 248 253
    • (1997) Br. J. Haematol. , vol.96 , pp. 248-253
    • Raja, K.B.1    Maxwell, P.H.2    Ratcliffe, P.J.3    Salisbury, J.R.4    Simpson, R.J.5    Peters, T.J.6
  • 107
    • 85117737568 scopus 로고    scopus 로고
    • Iron metabolism in the hemoglobin deficit mouse: Correlation of diferric transferrin with hepcidin expression
    • (in press).
    • S.J. Wilkins, D.M. Frazer, K.N. Millard, G.D. McLaren, G.J. Anderson, Iron metabolism in the hemoglobin deficit mouse: correlation of diferric transferrin with hepcidin expression, Blood (in press).
    • Blood
    • Wilkins, S.J.1    Frazer, D.M.2    Millard, K.N.3    McLaren, G.D.4    Anderson, G.J.5
  • 109
    • 21044434748 scopus 로고    scopus 로고
    • First phenotypic description of transferrin receptor 2 knockout mouse, and the role of hepcidin
    • D.F. Wallace, L. Summerville, P.E. Lusby, and V.N. Subramaniam First phenotypic description of transferrin receptor 2 knockout mouse, and the role of hepcidin Gut 54 2005 980 986
    • (2005) Gut , vol.54 , pp. 980-986
    • Wallace, D.F.1    Summerville, L.2    Lusby, P.E.3    Subramaniam, V.N.4
  • 112
    • 0038627974 scopus 로고    scopus 로고
    • The role of hypoxia and nitrogen monoxide in the regulation of cellular iron metabolism
    • D.R. Richardson The role of hypoxia and nitrogen monoxide in the regulation of cellular iron metabolism J. Lab. Clin. Med. 141 2003 289 291
    • (2003) J. Lab. Clin. Med. , vol.141 , pp. 289-291
    • Richardson, D.R.1
  • 113
    • 0036374378 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor 1 in enterocytic cells
    • D.J. Bertges, S. Berg, M.P. Fink, and R.L. Delude Regulation of hypoxia-inducible factor 1 in enterocytic cells J. Surg. Res. 106 2002 157 165
    • (2002) J. Surg. Res. , vol.106 , pp. 157-165
    • Bertges, D.J.1    Berg, S.2    Fink, M.P.3    Delude, R.L.4
  • 114
    • 4344618718 scopus 로고    scopus 로고
    • Tumour necrosis factor alpha regulates iron transport and transporter expression in human intestinal epithelial cells
    • D. Johnson, H. Bayele, K. Johnston, J. Tennant, S.K. Srai, and P. Sharp Tumour necrosis factor alpha regulates iron transport and transporter expression in human intestinal epithelial cells FEBS Lett. 573 2004 195 201
    • (2004) FEBS Lett. , vol.573 , pp. 195-201
    • Johnson, D.1    Bayele, H.2    Johnston, K.3    Tennant, J.4    Srai, S.K.5    Sharp, P.6
  • 115
  • 117
    • 4143075777 scopus 로고    scopus 로고
    • Identification of dietary copper- and iron-regulated genes in rat intestine
    • L. Marzullo, A. Tosco, R. Capone, H.S. Andersen, A. Capasso, and A. Leone Identification of dietary copper- and iron-regulated genes in rat intestine Gene 338 2004 225 233
    • (2004) Gene , vol.338 , pp. 225-233
    • Marzullo, L.1    Tosco, A.2    Capone, R.3    Andersen, H.S.4    Capasso, A.5    Leone, A.6
  • 119
    • 2342510407 scopus 로고    scopus 로고
    • IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin
    • E. Nemeth, S. Rivera, V. Gabayan, C. Keller, S. Taudorf, B.K. Pedersen, and T. Ganz IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin J. Clin. Invest. 113 2004 1271 1276
    • (2004) J. Clin. Invest. , vol.113 , pp. 1271-1276
    • Nemeth, E.1    Rivera, S.2    Gabayan, V.3    Keller, C.4    Taudorf, S.5    Pedersen, B.K.6    Ganz, T.7
  • 122
  • 123
    • 0030045543 scopus 로고    scopus 로고
    • Isoenzyme-specific regulation of genes involved in energy metabolism by hypoxia: Similarities with the regulation of erythropoietin
    • B.L. Ebert, J.M. Gleadle, J.F. O'Rourke, S.M. Bartlett, J. Poulton, and P.J. Ratcliffe Isoenzyme-specific regulation of genes involved in energy metabolism by hypoxia: similarities with the regulation of erythropoietin Biochem. J. 313 1996 809 814
    • (1996) Biochem. J. , vol.313 , pp. 809-814
    • Ebert, B.L.1    Gleadle, J.M.2    O'Rourke, J.F.3    Bartlett, S.M.4    Poulton, J.5    Ratcliffe, P.J.6
  • 124
    • 0015763693 scopus 로고
    • Storage iron kinetics: V. Iron exchange in the rat
    • J.D. Cook, C. Hershko, and C.A. Finch Storage iron kinetics: V. Iron exchange in the rat Br. J. Haematol. 25 1973 695 706
    • (1973) Br. J. Haematol. , vol.25 , pp. 695-706
    • Cook, J.D.1    Hershko, C.2    Finch, C.A.3
  • 126
    • 0015307895 scopus 로고
    • Iron deficiency anemia and physical performance and activity of rats
    • V.R. Edgerton, S.L. Bryant, C.A. Gillespie, and G.W. Gardner Iron deficiency anemia and physical performance and activity of rats J. Nutr. 102 1972 381 399
    • (1972) J. Nutr. , vol.102 , pp. 381-399
    • Edgerton, V.R.1    Bryant, S.L.2    Gillespie, C.A.3    Gardner, G.W.4
  • 127
    • 0344903376 scopus 로고
    • Iron deficiency in rats: Changes in body and organ weights, plasma proteins, hemoglobins, myoglobins, and catalase
    • R.P. Cusack, and W.D. Brown Iron deficiency in rats: changes in body and organ weights, plasma proteins, hemoglobins, myoglobins, and catalase J. Nutr. 86 1965 383 393
    • (1965) J. Nutr. , vol.86 , pp. 383-393
    • Cusack, R.P.1    Brown, W.D.2
  • 128
    • 0015422849 scopus 로고
    • Iron transport by rat small intestine in vitro: Effect of body iron status
    • J. Howard, and A. Jacobs Iron transport by rat small intestine in vitro: effect of body iron status Br. J. Haematol. 23 1972 595 603
    • (1972) Br. J. Haematol. , vol.23 , pp. 595-603
    • Howard, J.1    Jacobs, A.2
  • 129
    • 0033991142 scopus 로고    scopus 로고
    • Genetic variation of basal iron status, ferritin and iron regulatory protein in mice: Potential for modulation of oxidative stress
    • B. Clothier, S. Robinson, R.A. Akhtar, J.E. Francis, T.J. Peters, K. Raja, and A.G. Smith Genetic variation of basal iron status, ferritin and iron regulatory protein in mice: potential for modulation of oxidative stress Biochem. Pharmacol. 59 2000 115 122
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 115-122
    • Clothier, B.1    Robinson, S.2    Akhtar, R.A.3    Francis, J.E.4    Peters, T.J.5    Raja, K.6    Smith, A.G.7
  • 130
    • 0345268705 scopus 로고    scopus 로고
    • Duodenal mucosal reductase in wild type and HFE knock-out mice on iron-adequate, iron -deficient and iron-rich feeding
    • R.J. Simpson, E. Debnam, N. Beaumont, S. Bahram, K. Schumann, and S. Srai Duodenal mucosal reductase in wild type and HFE knock-out mice on iron-adequate, iron -deficient and iron-rich feeding Gut 52 2003 510 513
    • (2003) Gut , vol.52 , pp. 510-513
    • Simpson, R.J.1    Debnam, E.2    Beaumont, N.3    Bahram, S.4    Schumann, K.5    Srai, S.6
  • 131
    • 0033168767 scopus 로고    scopus 로고
    • The C282Y mutation causing hereditary hemochromatosis does not produce a null allele
    • J.E. Levy, L.K. Montross, D.E. Cohen, M.D. Fleming, and N.C. Andrews The C282Y mutation causing hereditary hemochromatosis does not produce a null allele Blood 94 1999 9 11
    • (1999) Blood , vol.94 , pp. 9-11
    • Levy, J.E.1    Montross, L.K.2    Cohen, D.E.3    Fleming, M.D.4    Andrews, N.C.5
  • 134
    • 0029842459 scopus 로고    scopus 로고
    • Oxygen sensing and molecular adaptation to hypoxia
    • H.F. Bunn, and R.O. Poyton Oxygen sensing and molecular adaptation to hypoxia Physiol. Rev. 76 1996 839 885
    • (1996) Physiol. Rev. , vol.76 , pp. 839-885
    • Bunn, H.F.1    Poyton, R.O.2
  • 135
    • 33644754867 scopus 로고
    • Organ weights in three forms of experimental obesity in the mouse
    • N.B. Marshall, S.B. Andrus, and J. Mayer Organ weights in three forms of experimental obesity in the mouse Am. J. Physiol. 189 1957 343 346
    • (1957) Am. J. Physiol. , vol.189 , pp. 343-346
    • Marshall, N.B.1    Andrus, S.B.2    Mayer, J.3
  • 137
    • 0004733051 scopus 로고
    • The effect of growth and development on the composition of mammals
    • C.M. Spray, and E.M. Widdowson The effect of growth and development on the composition of mammals Br. J. Nutr. 4 1950 332 353
    • (1950) Br. J. Nutr. , vol.4 , pp. 332-353
    • Spray, C.M.1    Widdowson, E.M.2
  • 138
    • 0015257563 scopus 로고
    • Red cell and plasma volume development in newborn rats measured with double label
    • A.M. Masters, A.J. Leslie, and I. Kaldor Red cell and plasma volume development in newborn rats measured with double label Am. J. Physiol. 222 1972 49 54
    • (1972) Am. J. Physiol. , vol.222 , pp. 49-54
    • Masters, A.M.1    Leslie, A.J.2    Kaldor, I.3
  • 139
    • 0020523478 scopus 로고
    • Synergism of iron and hexachlorobenzene inhibits hepatic uroporphyrinogen decarboxylase in inbred mice
    • A.G. Smith, and J.E. Francis Synergism of iron and hexachlorobenzene inhibits hepatic uroporphyrinogen decarboxylase in inbred mice Biochem. J. 214 1983 909 913
    • (1983) Biochem. J. , vol.214 , pp. 909-913
    • Smith, A.G.1    Francis, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.