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Volumn , Issue , 2012, Pages 101-116

Intestinal iron absorption

Author keywords

Dcytb; DMT1; Duodenum; Ferroportin; HCP1; Heme; Hepcidin; Hephaestin; HIF2 alpha; Iron; IRP1; IRP2; Regulation

Indexed keywords


EID: 84906738627     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-60327-485-2_6     Document Type: Chapter
Times cited : (9)

References (108)
  • 1
    • 50349143880 scopus 로고
    • Absorption and excretion of iron
    • McCance RA, Widdowson EM. Absorption and excretion of iron. Lancet. 1937;2:680-4.
    • (1937) Lancet. , vol.2 , pp. 680-684
    • McCance, R.A.1    Widdowson, E.M.2
  • 5
  • 6
    • 0016326163 scopus 로고
    • Intestinal absorption of hemoglobin iron-heme cleavage by mucosal heme oxygenase
    • Raffin SB, Woo CH, Roost KT, Price DC, Schmid R. Intestinal absorption of hemoglobin iron-heme cleavage by mucosal heme oxygenase. J Clin Invest. 1974;54:1344-52.
    • (1974) J Clin Invest. , vol.54 , pp. 1344-1352
    • Raffin, S.B.1    Woo, C.H.2    Roost, K.T.3    Price, D.C.4    Schmid, R.5
  • 7
    • 33845497171 scopus 로고    scopus 로고
    • Haem carrier protein 1 (HCP1): expression and functional studies in cultured cells
    • Latunde-Dada GO, Takeuchi K, Simpson RJ, McKie AT. Haem carrier protein 1 (HCP1): expression and functional studies in cultured cells. FEBS Lett. 2006;580:6865-70.
    • (2006) FEBS Lett. , vol.580 , pp. 6865-6870
    • Latunde-Dada, G.O.1    Takeuchi, K.2    Simpson, R.J.3    McKie, A.T.4
  • 9
    • 33751244559 scopus 로고    scopus 로고
    • Identification of an intestinal folate transporter and the molecular basis for hereditary folate malabsorption
    • Qiu A, Jansen M, Sakaris A, Min SH, Chattopadhyay S, Tsai E, et al. Identification of an intestinal folate transporter and the molecular basis for hereditary folate malabsorption. Cell. 2006;127:917-28.
    • (2006) Cell. , vol.127 , pp. 917-928
    • Qiu, A.1    Jansen, M.2    Sakaris, A.3    Min, S.H.4    Chattopadhyay, S.5    Tsai, E.6
  • 10
    • 34548026299 scopus 로고    scopus 로고
    • The spectrum of mutations in the PCFT gene, coding for an intestinal folate transporter, that are the basis for hereditary folate malabsorption
    • Zhao R, Min SH, Qiu A, Sakaris A, Goldberg GL, Sandoval C, et al. The spectrum of mutations in the PCFT gene, coding for an intestinal folate transporter, that are the basis for hereditary folate malabsorption. Blood. 2007;110:1147-52.
    • (2007) Blood. , vol.110 , pp. 1147-1152
    • Zhao, R.1    Min, S.H.2    Qiu, A.3    Sakaris, A.4    Goldberg, G.L.5    Sandoval, C.6
  • 11
    • 0035133172 scopus 로고    scopus 로고
    • Effect of hemochromatosis genotype and lifestyle factors on iron and red cell indices in a community population
    • Rossi E, Bulsara MK, Olynyk JK, Cullen DJ, Summerville L, Powell LW. Effect of hemochromatosis genotype and lifestyle factors on iron and red cell indices in a community population. Clin Chem. 2001;47:202-8.
    • (2001) Clin Chem. , vol.47 , pp. 202-208
    • Rossi, E.1    Bulsara, M.K.2    Olynyk, J.K.3    Cullen, D.J.4    Summerville, L.5    Powell, L.W.6
  • 15
    • 78651019148 scopus 로고
    • Reduction of iron in the human stomach
    • Bergheim O, Kirch ER. Reduction of iron in the human stomach. J Biol Chem. 1949;177:591-6.
    • (1949) J Biol Chem. , vol.177 , pp. 591-596
    • Bergheim, O.1    Kirch, E.R.2
  • 16
    • 0025141461 scopus 로고
    • Forms of soluble iron in mouse stomach and duodenal lumen: significance for mucosal uptake
    • Simpson RJ, Peters TJ. Forms of soluble iron in mouse stomach and duodenal lumen: significance for mucosal uptake. Br J Nutr. 1990;63:79-89.
    • (1990) Br J Nutr. , vol.63 , pp. 79-89
    • Simpson, R.J.1    Peters, T.J.2
  • 17
    • 0025767641 scopus 로고
    • Inhibition of iron absorption by omeprazole in rat model
    • Golubov J, Flanagan P, Adams P. Inhibition of iron absorption by omeprazole in rat model. Dig Dis Sci. 1991;36:405-8.
    • (1991) Dig Dis Sci. , vol.36 , pp. 405-408
    • Golubov, J.1    Flanagan, P.2    Adams, P.3
  • 18
    • 0042866137 scopus 로고    scopus 로고
    • Physiology and molecular biology of dietary iron absorption
    • Miret S, Simpson RJ, McKie AT. Physiology and molecular biology of dietary iron absorption. Annu Rev Nutr. 2003;23:283-301.
    • (2003) Annu Rev Nutr. , vol.23 , pp. 283-301
    • Miret, S.1    Simpson, R.J.2    McKie, A.T.3
  • 21
    • 0002379389 scopus 로고
    • Active transport of iron by intestine: features of the two-step mechanism
    • Manis JG, Schachter D. Active transport of iron by intestine: features of the two-step mechanism. Am J Physiol. 1962;203:73-80.
    • (1962) Am J Physiol. , vol.203 , pp. 73-80
    • Manis, J.G.1    Schachter, D.2
  • 22
    • 0043005309 scopus 로고    scopus 로고
    • Basolateral transport of iron in mammalian intestine: from physiology to molecules
    • In: Templeton DM, editor. New York: Marcel Dekker
    • McKie AT, Simpson RJ. Basolateral transport of iron in mammalian intestine: from physiology to molecules. In: Templeton DM, editor. Molecular and cellular iron transport. New York: Marcel Dekker; 2002. p. 175-88.
    • (2002) Molecular and cellular iron transport , pp. 175-188
    • McKie, A.T.1    Simpson, R.J.2
  • 23
    • 0030755366 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian proton-coupled metal-ion transporter
    • Gunshin H, Mackenzie B, Berger UV, Gunshin Y, Romero MF, Boron WF, et al. Cloning and characterization of a mammalian proton-coupled metal-ion transporter. Nature. 1997;388:482-8.
    • (1997) Nature. , vol.388 , pp. 482-488
    • Gunshin, H.1    Mackenzie, B.2    Berger, U.V.3    Gunshin, Y.4    Romero, M.F.5    Boron, W.F.6
  • 24
    • 0033984237 scopus 로고    scopus 로고
    • Nramp2 expression is associated with pH-dependent iron uptake across the apical membrane of human intestinal Caco-2 cells
    • Tandy S, Williams M, Leggett A, Lopez-Jimenez M, Dedes M, Ramesh B, et al. Nramp2 expression is associated with pH-dependent iron uptake across the apical membrane of human intestinal Caco-2 cells. J Biol Chem. 2000;275:1023-9.
    • (2000) J Biol Chem. , vol.275 , pp. 1023-1029
    • Tandy, S.1    Williams, M.2    Leggett, A.3    Lopez-Jimenez, M.4    Dedes, M.5    Ramesh, B.6
  • 28
    • 18244399587 scopus 로고    scopus 로고
    • Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver
    • Gunshin H, Fujiwara Y, Custodio AO, Direnzo C, Robine S, Andrews NC. Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver. J Clin Invest. 2005;115:1258-66.
    • (2005) J Clin Invest. , vol.115 , pp. 1258-1266
    • Gunshin, H.1    Fujiwara, Y.2    Custodio, A.O.3    Direnzo, C.4    Robine, S.5    Andrews, N.C.6
  • 29
    • 12844260664 scopus 로고    scopus 로고
    • Identification of a human mutation of DMT1 in a patient with microcytic anemia and iron overload
    • Mims MP, Guan Y, Pospisilova D, Priwitzerova M, Indrak K, Ponka P, et al. Identification of a human mutation of DMT1 in a patient with microcytic anemia and iron overload. Blood. 2005;105:1337-42.
    • (2005) Blood. , vol.105 , pp. 1337-1342
    • Mims, M.P.1    Guan, Y.2    Pospisilova, D.3    Priwitzerova, M.4    Indrak, K.5    Ponka, P.6
  • 30
    • 30144443274 scopus 로고    scopus 로고
    • Microcytic anemia and hepatic iron overload in a child with compound heterozygous mutations in DMT1 (SCL11A2)
    • Iolascon A, d'Apolito M, Servedio V, Cimmino F, Piga A, Camaschella C. Microcytic anemia and hepatic iron overload in a child with compound heterozygous mutations in DMT1 (SCL11A2). Blood. 2006;107:349-54.
    • (2006) Blood. , vol.107 , pp. 349-354
    • Iolascon, A.1    d'Apolito, M.2    Servedio, V.3    Cimmino, F.4    Piga, A.5    Camaschella, C.6
  • 31
    • 33646537173 scopus 로고    scopus 로고
    • Two new human DMT1 gene mutations in a patient with microcytic anemia, low ferritinemia, and liver iron overload
    • Beaumont C, Delaunay J, Hetet G, Grandchamp B, de Montalembert M, Tchernia G. Two new human DMT1 gene mutations in a patient with microcytic anemia, low ferritinemia, and liver iron overload. Blood. 2006;107:4168-70.
    • (2006) Blood. , vol.107 , pp. 4168-4170
    • Beaumont, C.1    Delaunay, J.2    Hetet, G.3    Grandchamp, B.4    de Montalembert, M.5    Tchernia, G.6
  • 33
    • 67650050211 scopus 로고    scopus 로고
    • Mammalian zinc transporters: nutritional and physiologic regulation
    • Lichten LA, Cousins RJ. Mammalian zinc transporters: nutritional and physiologic regulation. Annu Rev Nutr. 2009;29:153-76.
    • (2009) Annu Rev Nutr. , vol.29 , pp. 153-176
    • Lichten, L.A.1    Cousins, R.J.2
  • 35
    • 0031194722 scopus 로고    scopus 로고
    • Manganese metabolism is impaired in the Belgrade laboratory rat
    • Chua AC, Morgan EH. Manganese metabolism is impaired in the Belgrade laboratory rat. J Comp Physiol B. 1997;167:361-9.
    • (1997) J Comp Physiol B. , vol.167 , pp. 361-369
    • Chua, A.C.1    Morgan, E.H.2
  • 36
    • 54349109848 scopus 로고    scopus 로고
    • Increased hepatic accumulation of ingested Cd is associated with upregulation of several intestinal transporters in mice fed diets deficient in essential metals
    • Min KS, Ueda H, Kihara T, Tanaka K. Increased hepatic accumulation of ingested Cd is associated with upregulation of several intestinal transporters in mice fed diets deficient in essential metals. Toxicol Sci. 2008;106:284-9.
    • (2008) Toxicol Sci. , vol.106 , pp. 284-289
    • Min, K.S.1    Ueda, H.2    Kihara, T.3    Tanaka, K.4
  • 37
    • 33747881027 scopus 로고    scopus 로고
    • Iron and cadmium uptake by duodenum of hypotransferrinaemic mice
    • Raja K, Jafri S, Peters T, Simpson R. Iron and cadmium uptake by duodenum of hypotransferrinaemic mice. Biometals. 2006;19:547-53.
    • (2006) Biometals. , vol.19 , pp. 547-553
    • Raja, K.1    Jafri, S.2    Peters, T.3    Simpson, R.4
  • 38
    • 39849085963 scopus 로고    scopus 로고
    • Normal cadmium uptake in microcytic anemia mk/mk mice suggests that DMT1 is not the only cadmium transporter in vivo
    • Suzuki T, Momoi K, Hosoyamada M, Kimura M, Shibasaki T. Normal cadmium uptake in microcytic anemia mk/mk mice suggests that DMT1 is not the only cadmium transporter in vivo. Toxicol Appl Pharmacol. 2008;227:462-7.
    • (2008) Toxicol Appl Pharmacol. , vol.227 , pp. 462-467
    • Suzuki, T.1    Momoi, K.2    Hosoyamada, M.3    Kimura, M.4    Shibasaki, T.5
  • 39
    • 0035955440 scopus 로고    scopus 로고
    • Zinc regulates the function and expression of the iron transporters DMT1 and IREG1 in human intestinal Caco-2 cells
    • Yamaji S, Tennant J, Tandy S, Williams M, Singh Srai SK, Sharp P. Zinc regulates the function and expression of the iron transporters DMT1 and IREG1 in human intestinal Caco-2 cells. FEBS Lett. 2001;507:137-41.
    • (2001) FEBS Lett. , vol.507 , pp. 137-141
    • Yamaji, S.1    Tennant, J.2    Tandy, S.3    Williams, M.4    Singh Srai, S.K.5    Sharp, P.6
  • 40
    • 0037063360 scopus 로고    scopus 로고
    • Effects of copper on the expression of metal transporters in human intestinal Caco-2 cells
    • Tennant J, Stansfield M, Yamaji S, Srai S, Sharp P. Effects of copper on the expression of metal transporters in human intestinal Caco-2 cells. FEBS Lett. 2002;527:239.
    • (2002) FEBS Lett. , vol.527 , pp. 239
    • Tennant, J.1    Stansfield, M.2    Yamaji, S.3    Srai, S.4    Sharp, P.5
  • 42
    • 0026637274 scopus 로고
    • Investigation of a role for reduction in ferric iron uptake by mouse duodenum (published erratum appears in Biochim Biophys Acta 1993; 1176: 197)
    • Raja KB, Simpson RJ, Peters TJ. Investigation of a role for reduction in ferric iron uptake by mouse duodenum (published erratum appears in Biochim Biophys Acta 1993; 1176: 197). Biochim Biophys Acta. 1992;1135:141-6.
    • (1992) Biochim Biophys Acta. , vol.1135 , pp. 141-146
    • Raja, K.B.1    Simpson, R.J.2    Peters, T.J.3
  • 43
    • 0033013832 scopus 로고    scopus 로고
    • The ferric-reducing activity of duodenal brush-border membrane vesicles is associated with a b-type haem
    • Pountney DJ, Raja KB, Simpson RJ, Wrigglesworth JM. The ferric-reducing activity of duodenal brush-border membrane vesicles is associated with a b-type haem. Biometals. 1999;12:53-62.
    • (1999) Biometals. , vol.12 , pp. 53-62
    • Pountney, D.J.1    Raja, K.B.2    Simpson, R.J.3    Wrigglesworth, J.M.4
  • 45
    • 0035793856 scopus 로고    scopus 로고
    • An iron-regulated ferric reductase associated with the absorption of dietary iron
    • McKie AT, Barrow D, Latunde-Dada GO, Rolfs A, Sager G, Mudaly E, et al. An iron-regulated ferric reductase associated with the absorption of dietary iron. Science. 2001;291:1755-9.
    • (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, E.6
  • 46
    • 0021287589 scopus 로고
    • Cytochrome b561 catalyzes transmembrane electron transfer
    • Srivastava M, Duong LT, Fleming PJ. Cytochrome b561 catalyzes transmembrane electron transfer. J Biol Chem. 1984;259:8072-5.
    • (1984) J Biol Chem. , vol.259 , pp. 8072-8075
    • Srivastava, M.1    Duong, L.T.2    Fleming, P.J.3
  • 47
    • 0021289369 scopus 로고
    • An identical cytochrome b561 is present in bovine adrenal chromaffin vesicles and posterior pituitary neurosecretory vesicles
    • Duong LT, Fleming PJ, Russell JT. An identical cytochrome b561 is present in bovine adrenal chromaffin vesicles and posterior pituitary neurosecretory vesicles. J Biol Chem. 1984;259:4885-9.
    • (1984) J Biol Chem. , vol.259 , pp. 4885-4889
    • Duong, L.T.1    Fleming, P.J.2    Russell, J.T.3
  • 48
    • 0023062602 scopus 로고
    • Secretory vesicle cytochrome b561: a transmembrane electron transporter
    • Fleming PJ, Kent UM. Secretory vesicle cytochrome b561: a transmembrane electron transporter. Ann N Y Acad Sci. 1987;493:101-7.
    • (1987) Ann N Y Acad Sci. , vol.493 , pp. 101-107
    • Fleming, P.J.1    Kent, U.M.2
  • 49
    • 0028318199 scopus 로고
    • Purification and physical properties of a novel type of cytochrome b from rabbit peritoneal neutrophils
    • Escriou V, Laporte F, Garin J, Brandolin G, Vignais PV. Purification and physical properties of a novel type of cytochrome b from rabbit peritoneal neutrophils. J Biol Chem. 1994;269:14007-14.
    • (1994) J Biol Chem. , vol.269 , pp. 14007-14014
    • Escriou, V.1    Laporte, F.2    Garin, J.3    Brandolin, G.4    Vignais, P.V.5
  • 50
    • 0030968065 scopus 로고    scopus 로고
    • Differential characterization of neutrophil cytochrome p30 and cytochrome b-558 by low-temperature absorption and resonance Raman spectroscopies
    • Escriou V, Laporte F, Vignais PV, Desbois A. Differential characterization of neutrophil cytochrome p30 and cytochrome b-558 by low-temperature absorption and resonance Raman spectroscopies. Eur J Biochem. 1997;245:505-11.
    • (1997) Eur J Biochem. , vol.245 , pp. 505-511
    • Escriou, V.1    Laporte, F.2    Vignais, P.V.3    Desbois, A.4
  • 51
    • 33845979527 scopus 로고    scopus 로고
    • Human erythrocyte membranes contain a cytochrome b561 that may be involved in extracellular ascorbate recycling
    • Su D, May JM, Koury MJ, Asard H. Human erythrocyte membranes contain a cytochrome b561 that may be involved in extracellular ascorbate recycling. J Biol Chem. 2006;281:39852-9.
    • (2006) J Biol Chem. , vol.281 , pp. 39852-39859
    • Su, D.1    May, J.M.2    Koury, M.J.3    Asard, H.4
  • 52
    • 27144507493 scopus 로고    scopus 로고
    • Cybrd1 (duodenal cytochrome b) is not necessary for dietary iron absorption in mice
    • Gunshin H, Starr CN, Direnzo C, Fleming MD, Jin J, Greer EL, et al. Cybrd1 (duodenal cytochrome b) is not necessary for dietary iron absorption in mice. Blood. 2005;106:2879-83.
    • (2005) Blood. , vol.106 , pp. 2879-2883
    • Gunshin, H.1    Starr, C.N.2    Direnzo, C.3    Fleming, M.D.4    Jin, J.5    Greer, E.L.6
  • 53
    • 28844447007 scopus 로고    scopus 로고
    • The role of duodenal cytochrome b in intestinal iron absorption remains unclear
    • Frazer DM, Wilkins SJ, Vulpe CD, Anderson GJ. The role of duodenal cytochrome b in intestinal iron absorption remains unclear. Blood. 2005;106:4413.
    • (2005) Blood. , vol.106 , pp. 4413
    • Frazer, D.M.1    Wilkins, S.J.2    Vulpe, C.D.3    Anderson, G.J.4
  • 54
    • 0033861745 scopus 로고    scopus 로고
    • A novel duodenal iron-regulated transporter, IREG1, implicated in the basolateral transfer of iron to the circulation
    • McKie AT, Marciani P, Rolfs A, Brennan K, Wehr K, Barrow D, et al. A novel duodenal iron-regulated transporter, IREG1, implicated in the basolateral transfer of iron to the circulation. Mol Cell. 2000;5:299-309.
    • (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
  • 55
    • 0034677467 scopus 로고    scopus 로고
    • Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter
    • Donovan A, Brownlie A, Zhou Y, Shepard J, Pratt SJ, Moynihan J, et al. Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter. Nature. 2000;403:776-81.
    • (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
  • 56
    • 0034733635 scopus 로고    scopus 로고
    • A novel mammalian iron-regulated protein involved in intracellular iron metabolism
    • Abboud S, Haile DJ. A novel mammalian iron-regulated protein involved in intracellular iron metabolism. J Biol Chem. 2000;275:19906-12.
    • (2000) J Biol Chem. , vol.275 , pp. 19906-19912
    • Abboud, S.1    Haile, D.J.2
  • 57
    • 65349126484 scopus 로고    scopus 로고
    • A ferroportin transcript that lacks an iron-responsive element enables duodenal and erythroid precursor cells to evade translational repression
    • Zhang DL, Hughes RM, Ollivierre-Wilson H, Ghosh MC, Rouault TA. A ferroportin transcript that lacks an iron-responsive element enables duodenal and erythroid precursor cells to evade translational repression. Cell Metab. 2009;9:461-73.
    • (2009) Cell Metab. , vol.9 , pp. 461-473
    • Zhang, D.L.1    Hughes, R.M.2    Ollivierre-Wilson, H.3    Ghosh, M.C.4    Rouault, T.A.5
  • 59
    • 17944380796 scopus 로고    scopus 로고
    • Autosomal-dominant hemochromatosis is associated with a mutation in the ferroportin (SLC11A3) gene
    • Montosi G, Donovan A, Totaro A, Garuti C, Pignatti E, Cassanelli S, et al. Autosomal-dominant hemochromatosis is associated with a mutation in the ferroportin (SLC11A3) gene. J Clin Invest. 2001;108:619-23.
    • (2001) J Clin Invest. , vol.108 , pp. 619-623
    • Montosi, G.1    Donovan, A.2    Totaro, A.3    Garuti, C.4    Pignatti, E.5    Cassanelli, S.6
  • 60
    • 0037100382 scopus 로고    scopus 로고
    • Autosomal dominant reticuloendothelial iron overload associated with a 3-base pair deletion in the ferroportin 1 gene (SLC11A3)
    • Devalia V, Carter K, Walker AP, Perkins SJ, Worwood M, May A, et al. Autosomal dominant reticuloendothelial iron overload associated with a 3-base pair deletion in the ferroportin 1 gene (SLC11A3). Blood. 2002;100:695-7.
    • (2002) Blood. , vol.100 , pp. 695-697
    • Devalia, V.1    Carter, K.2    Walker, A.P.3    Perkins, S.J.4    Worwood, M.5    May, A.6
  • 64
    • 0014005552 scopus 로고
    • Sex-linked anemia: a hypochromic anemia of mice
    • Bannerman RM, Cooper RG. Sex-linked anemia: a hypochromic anemia of mice. Science. 1966;151:581-2.
    • (1966) Science. , vol.151 , pp. 581-582
    • Bannerman, R.M.1    Cooper, R.G.2
  • 65
    • 0019971267 scopus 로고
    • The kinetics of iron uptake by isolated intestinal cells from normal mice and mice with sex-linked anemia
    • Peppriell JE, Edwards JA, Bannerman RM. The kinetics of iron uptake by isolated intestinal cells from normal mice and mice with sex-linked anemia. Blood. 1982;60:635-41.
    • (1982) Blood. , vol.60 , pp. 635-641
    • Peppriell, J.E.1    Edwards, J.A.2    Bannerman, R.M.3
  • 66
    • 0032909207 scopus 로고    scopus 로고
    • Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse
    • Vulpe CD, Kuo YM, Murphy TL, Cowley L, Askwith C, Libina N, et al. Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse. Nat Genet. 1999;21:195-9.
    • (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
  • 67
    • 1642451921 scopus 로고    scopus 로고
    • Mislocalisation of hephaestin, a multicopper ferroxidase involved in basolateral intestinal iron transport, in the sex linked anaemia mouse
    • Kuo YM, Su T, Chen H, Attieh Z, Syed BA, McKie AT, et al. Mislocalisation of hephaestin, a multicopper ferroxidase involved in basolateral intestinal iron transport, in the sex linked anaemia mouse. Gut. 2004;53:201-6.
    • (2004) Gut. , vol.53 , pp. 201-206
    • Kuo, Y.M.1    Su, T.2    Chen, H.3    Attieh, Z.4    Syed, B.A.5    McKie, A.T.6
  • 69
    • 0026468180 scopus 로고
    • A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation
    • Semenza GL, Wang GL. A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation. Mol Cell Biol. 1992;12:5447-54.
    • (1992) Mol Cell Biol. , vol.12 , pp. 5447-5454
    • Semenza, G.L.1    Wang, G.L.2
  • 70
    • 38349111676 scopus 로고    scopus 로고
    • Role of the hypoxia inducible factors HIF in iron metabolism
    • Peyssonnaux C, Nizet V, Johnson RS. Role of the hypoxia inducible factors HIF in iron metabolism. Cell Cycle. 2008;7:28-32.
    • (2008) Cell Cycle. , vol.7 , pp. 28-32
    • Peyssonnaux, C.1    Nizet, V.2    Johnson, R.S.3
  • 71
    • 33646175288 scopus 로고    scopus 로고
    • The hypoxia-inducible-factor hydroxylases bring fresh air into hypoxia signalling
    • Berra E, Ginouves A, Pouyssegur J. The hypoxia-inducible-factor hydroxylases bring fresh air into hypoxia signalling. EMBO Rep. 2006;7:41-5.
    • (2006) EMBO Rep. , vol.7 , pp. 41-45
    • Berra, E.1    Ginouves, A.2    Pouyssegur, J.3
  • 72
    • 58749094789 scopus 로고    scopus 로고
    • Intestinal hypoxia-inducible transcription factors are essential for iron absorption following iron deficiency
    • Shah YM, Matsubara T, Ito S, Yim SH, Gonzalez FJ. Intestinal hypoxia-inducible transcription factors are essential for iron absorption following iron deficiency. Cell Metab. 2009;9:152-64.
    • (2009) Cell Metab. , vol.9 , pp. 152-164
    • Shah, Y.M.1    Matsubara, T.2    Ito, S.3    Yim, S.H.4    Gonzalez, F.J.5
  • 74
    • 0014979572 scopus 로고
    • The influence of hypoxia on iron absorption in the rat
    • Hathorn MK. The influence of hypoxia on iron absorption in the rat. Gastroenterology. 1971;60:76-81.
    • (1971) Gastroenterology. , vol.60 , pp. 76-81
    • Hathorn, M.K.1
  • 75
    • 0023897841 scopus 로고
    • In vivo studies on the relationship between intestinal iron (Fe3+) absorption, hypoxia and erythropoiesis in the mouse
    • Raja KB, Simpson RJ, Pippard MJ, Peters TJ. In vivo studies on the relationship between intestinal iron (Fe3+) absorption, hypoxia and erythropoiesis in the mouse. Br J Haematol. 1988;68:373-8.
    • (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
  • 76
    • 37449009448 scopus 로고    scopus 로고
    • Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum
    • Galy B, Ferring-Appel D, Kaden S, Grone HJ, Hentze MW. Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum. Cell Metab. 2008;7:79-85.
    • (2008) Cell Metab. , vol.7 , pp. 79-85
    • Galy, B.1    Ferring-Appel, D.2    Kaden, S.3    Grone, H.J.4    Hentze, M.W.5
  • 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
    • Frazer DM, Wilkins SJ, Becker EM, Murphy TL, Vulpe CD, McKie AT, et al. A rapid decrease in the expression of DMT1 and Dcytb but not Ireg1 or hephaestin explains the mucosal block phenomenon of iron absorption. Gut. 2003;52:340-6.
    • (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
  • 79
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization
    • Nemeth E, Tuttle MS, Powelson J, Vaughn MB, Donovan A, Ward DM, et al. Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science. 2004;306:2090-3.
    • (2004) Science. , vol.306 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3    Vaughn, M.B.4    Donovan, A.5    Ward, D.M.6
  • 80
    • 0022341540 scopus 로고
    • The effects of cytoskeletal inhibitors on intestinal iron absorption in the rat
    • Johnson G, Jacobs P, Purves LR. The effects of cytoskeletal inhibitors on intestinal iron absorption in the rat. Biochim Biophys Acta. 1985;843:83-91.
    • (1985) Biochim Biophys Acta. , vol.843 , pp. 83-91
    • Johnson, G.1    Jacobs, P.2    Purves, L.R.3
  • 81
    • 0022899231 scopus 로고
    • Studies on the role of transferrin and endocytosis in the uptake of Fe3+ from Fe-nitrilotriacetate by mouse duodenum
    • Simpson RJ, Osterloh KRS, Raja KB, Snape SD, Peters TJ. Studies on the role of transferrin and endocytosis in the uptake of Fe3+ from Fe-nitrilotriacetate by mouse duodenum. Biochim Biophys Acta. 1986; 884:166-71.
    • (1986) Biochim Biophys Acta. , vol.884 , pp. 166-171
    • Simpson, R.J.1    Osterloh, K.R.S.2    Raja, K.B.3    Snape, S.D.4    Peters, T.J.5
  • 83
    • 33644869168 scopus 로고    scopus 로고
    • Vesicular transport and apotransferrin in intestinal iron absorption, as shown in the Caco-2 cell model
    • Moriya M, Linder MC. Vesicular transport and apotransferrin in intestinal iron absorption, as shown in the Caco-2 cell model. Am J Physiol Gastrointest Liver Physiol. 2006;290:G301-9.
    • (2006) Am J Physiol Gastrointest Liver Physiol. , vol.290 , pp. G301-G309
    • Moriya, M.1    Linder, M.C.2
  • 84
    • 34648828230 scopus 로고    scopus 로고
    • Molecular mechanisms involved in intestinal iron absorption
    • Sharp P, Srai SK. Molecular mechanisms involved in intestinal iron absorption. World J Gastroenterol. 2007;13:4716-24.
    • (2007) World J Gastroenterol. , vol.13 , pp. 4716-4724
    • Sharp, P.1    Srai, S.K.2
  • 87
    • 0344587188 scopus 로고
    • On the kinetics of iron absorption in mice
    • Gitlin D, Cruchard A. On the kinetics of iron absorption in mice. J Clin Invest. 1962;41:344-50.
    • (1962) J Clin Invest. , vol.41 , pp. 344-350
    • Gitlin, D.1    Cruchard, A.2
  • 89
    • 0025285912 scopus 로고
    • Subcellular localization of recently-absorbed iron in mouse duodenal enterocytes: identification of a basolateral membrane iron-binding site
    • Snape S, Simpson RJ, Peters TJ. Subcellular localization of recently-absorbed iron in mouse duodenal enterocytes: identification of a basolateral membrane iron-binding site. Cell Biochem Funct. 1990;8:107-15.
    • (1990) Cell Biochem Funct. , vol.8 , pp. 107-115
    • Snape, S.1    Simpson, R.J.2    Peters, T.J.3
  • 90
    • 0023886346 scopus 로고
    • Subcellular distribution of recently absorbed iron and of transferrin in the mouse duodenal mucosa
    • Osterloh K, Snape S, Simpson RJ, Grindley H, Peters TJ. Subcellular distribution of recently absorbed iron and of transferrin in the mouse duodenal mucosa. Biochim Biophys Acta. 1988;969:166-75.
    • (1988) Biochim Biophys Acta. , vol.969 , pp. 166-175
    • Osterloh, K.1    Snape, S.2    Simpson, R.J.3    Grindley, H.4    Peters, T.J.5
  • 91
    • 27144467097 scopus 로고    scopus 로고
    • Altered body iron distribution and microcytosis in mice deficient in iron regulatory protein 2 (IRP2)
    • Galy B, Ferring D, Minana B, Bell O, Janser HG, Muckenthaler M, et al. Altered body iron distribution and microcytosis in mice deficient in iron regulatory protein 2 (IRP2). Blood. 2005;106:2580-9.
    • (2005) Blood. , vol.106 , pp. 2580-2589
    • Galy, B.1    Ferring, D.2    Minana, B.3    Bell, O.4    Janser, H.G.5    Muckenthaler, M.6
  • 92
    • 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, Leroyer P, Turlin B, Brissot P, 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;276:7811-9.
    • (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
  • 93
    • 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, Danan JL, Bigard X, Devaux I, et al. The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation. J Clin Invest. 2002;110:1037-44.
    • (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
  • 94
    • 0037962795 scopus 로고    scopus 로고
    • The orchestration of body iron intake: how and where do enterocytes receive their cues?
    • Frazer DM, Anderson GJ. The orchestration of body iron intake: how and where do enterocytes receive their cues? Blood Cells Mol Dis. 2003;30:288-97.
    • (2003) Blood Cells Mol Dis. , vol.30 , pp. 288-297
    • Frazer, D.M.1    Anderson, G.J.2
  • 95
    • 34548825938 scopus 로고    scopus 로고
    • Iron transferrin regulates hepcidin synthesis in primary hepatocyte culture through hemojuvelin and BMP2/4
    • Lin L, Valore EV, Nemeth E, Goodnough JB, Gabayan V, Ganz T. Iron transferrin regulates hepcidin synthesis in primary hepatocyte culture through hemojuvelin and BMP2/4. Blood. 2007;110:2182-9.
    • (2007) Blood. , vol.110 , pp. 2182-2189
    • Lin, L.1    Valore, E.V.2    Nemeth, E.3    Goodnough, J.B.4    Gabayan, V.5    Ganz, T.6
  • 96
    • 10244255021 scopus 로고    scopus 로고
    • Regulation of transferrin receptor 2 protein levels by transferrin
    • Robb A, Wessling-Resnick M. Regulation of transferrin receptor 2 protein levels by transferrin. Blood. 2004;104:4294-9.
    • (2004) Blood. , vol.104 , pp. 4294-4299
    • Robb, A.1    Wessling-Resnick, M.2
  • 99
    • 0036196205 scopus 로고    scopus 로고
    • Mechanisms of iron accumulation in hereditary hemochromatosis
    • Fleming RE, Sly WS. Mechanisms of iron accumulation in hereditary hemochromatosis. Annu Rev Physiol. 2002;64:663-80.
    • (2002) Annu Rev Physiol. , vol.64 , pp. 663-680
    • Fleming, R.E.1    Sly, W.S.2
  • 100
    • 0033585129 scopus 로고    scopus 로고
    • The hemochromatosis protein HFE competes with transferrin for binding to the transferrin receptor
    • Lebron JA, West Jr AP, Bjorkman PJ. The hemochromatosis protein HFE competes with transferrin for binding to the transferrin receptor. J Mol Biol. 1999;294:239-45.
    • (1999) J Mol Biol. , vol.294 , pp. 239-245
    • Lebron, J.A.1    West, A.P.2    Bjorkman, P.J.3
  • 101
    • 37549055467 scopus 로고    scopus 로고
    • HFE modulates transferrin receptor 2 levels in hepatoma cells via interactions that differ from transferrin receptor 1-HFE interactions
    • Chen J, Chloupkova M, Gao J, Chapman-Arvedson TL, Enns CA. HFE modulates transferrin receptor 2 levels in hepatoma cells via interactions that differ from transferrin receptor 1-HFE interactions. J Biol Chem. 2007;282:36862-70.
    • (2007) J Biol Chem. , vol.282 , pp. 36862-36870
    • Chen, J.1    Chloupkova, M.2    Gao, J.3    Chapman-Arvedson, T.L.4    Enns, C.A.5
  • 102
    • 60649103774 scopus 로고    scopus 로고
    • Interaction of the hereditary hemochromatosis protein HFE with transferrin receptor 2 is required for transferrin-induced hepcidin expression
    • Gao J, Chen J, Kramer M, Tsukamoto H, Zhang AS, Enns CA. Interaction of the hereditary hemochromatosis protein HFE with transferrin receptor 2 is required for transferrin-induced hepcidin expression. Cell Metab. 2009;9:217-27.
    • (2009) Cell Metab. , vol.9 , pp. 217-227
    • Gao, J.1    Chen, J.2    Kramer, M.3    Tsukamoto, H.4    Zhang, A.S.5    Enns, C.A.6
  • 103
    • 27144459908 scopus 로고    scopus 로고
    • Competitive regulation of hepcidin mRNA by soluble and cell-associated hemojuvelin
    • Lin L, Goldberg YP, Ganz T. Competitive regulation of hepcidin mRNA by soluble and cell-associated hemojuvelin. Blood. 2005;106:2884-9.
    • (2005) Blood. , vol.106 , pp. 2884-2889
    • Lin, L.1    Goldberg, Y.P.2    Ganz, T.3
  • 104
    • 44449177930 scopus 로고    scopus 로고
    • The serine protease TMPRSS6 is required to sense iron deficiency
    • Du X, She E, Gelbart T, Truksa J, Lee P, Xia Y, et al. The serine protease TMPRSS6 is required to sense iron deficiency. Science. 2008;320:1088-92.
    • (2008) Science. , vol.320 , pp. 1088-1092
    • Du, X.1    She, E.2    Gelbart, T.3    Truksa, J.4    Lee, P.5    Xia, Y.6
  • 106
    • 56449096622 scopus 로고    scopus 로고
    • The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin
    • Silvestri L, Pagani A, Nai A, De Domenico I, Kaplan J, Camaschella C. The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin. Cell Metab. 2008;8:502-11.
    • (2008) Cell Metab. , vol.8 , pp. 502-511
    • Silvestri, L.1    Pagani, A.2    Nai, A.3    De Domenico, I.4    Kaplan, J.5    Camaschella, C.6


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