메뉴 건너뛰기




Volumn 7, Issue 5, 2005, Pages 365-372

Recent advances in intestinal iron transport

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME B; FERROPORTIN 1; HEMOJUVELIN; HEPCIDIN; HEPHAESTIN; HFE PROTEIN; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 2; OXIDOREDUCTASE; TRANSFERRIN; TRANSFERRIN RECEPTOR; UNCLASSIFIED DRUG;

EID: 28244458880     PISSN: 15228037     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11894-005-0005-1     Document Type: Review
Times cited : (27)

References (50)
  • 1
    • 0026470429 scopus 로고
    • Contributions of heme and nonheme iron to human nutrition
    • Carpenter CE, Mahoney AW: Contributions of heme and nonheme iron to human nutrition. Crit Rev Food Sci Nutr 1992, 31:333-367.
    • (1992) Crit. Rev. Food Sci. Nutr. , vol.31 , pp. 333-367
    • Carpenter, C.E.1    Mahoney, A.W.2
  • 2
    • 4544259474 scopus 로고    scopus 로고
    • Proton pump inhibitors and iron deficiency: Is the connection real?
    • Nand S, Tanvetyanon T: Proton pump inhibitors and iron deficiency: Is the connection real? South Med J 2004, 97:799.
    • (2004) South Med. J. , vol.97 , pp. 799
    • Nand, S.1    Tanvetyanon, T.2
  • 3
    • 13944278864 scopus 로고    scopus 로고
    • Iron-deficiency anemia and Helicobacter pylori infection: A review of the evidence
    • DuBois S, Kearney DJ: Iron-deficiency anemia and Helicobacter pylori infection: a review of the evidence. Am J Gastroenterol 2005, 100:453-459.
    • (2005) Am. J. Gastroenterol. , vol.100 , pp. 453-459
    • DuBois, S.1    Kearney, D.J.2
  • 4
    • 20144388176 scopus 로고    scopus 로고
    • The prevalence of celiac disease in average-risk and at-risk Western European populations: A systematic review
    • Dubé C, Rostom A, Sy R, et al.: The prevalence of celiac disease in average-risk and at-risk Western European populations: a systematic review. Gastroenterology 2005, 128:S57-S67.
    • (2005) Gastroenterology , vol.128
    • Dubé, C.1    Rostom, A.2    Sy, R.3
  • 5
    • 0035793856 scopus 로고    scopus 로고
    • An iron-regulated ferric reductase associated with the absorption of dietary iron
    • McKie AT, Barrow D, Latunde-Dada GO, et al.: An iron-regulated ferric reductase associated with the absorption of dietary iron. Science 2001, 291:1755-1759.
    • (2001) Science , vol.291 , pp. 1755-1759
    • McKie, A.T.1    Barrow, D.2    Latunde-Dada, G.O.3
  • 6
    • 0030763856 scopus 로고    scopus 로고
    • Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene
    • Fleming MD, Trenor III CC, Su MA, et al.: Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene. Nat Genet 1997, 16:383-386.
    • (1997) Nat. Genet. , vol.16 , pp. 383-386
    • Fleming, M.D.1    Trenor III, C.C.2    Su, M.A.3
  • 7
    • 0030755366 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian proton-coupled metal-ion transporter
    • Gunshin H, Mackenzie B, Berger UV, et al.: Cloning and characterization of a mammalian proton-coupled metal-ion transporter. Nature 1997, 388:482-488.
    • (1997) Nature , vol.388 , pp. 482-488
    • Gunshin, H.1    Mackenzie, B.2    Berger, U.V.3
  • 8
    • 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, 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
  • 9
    • 0034677467 scopus 로고    scopus 로고
    • Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter
    • Donovan A, Brownlie A, Zhou Y, et al.: Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter. Nature 2000, 403:776-781.
    • (2000) Nature , vol.403 , pp. 776-781
    • Donovan, A.1    Brownlie, A.2    Zhou, Y.3
  • 10
    • 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, 275:19906-19912.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19906-19912
    • Abboud, S.1    Haile, D.J.2
  • 11
    • 0032909207 scopus 로고    scopus 로고
    • Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse
    • Vulpe CD, Kuo Y, Murphy TL, et al.: Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse. Nat Genet 1999, 21:195-199.
    • (1999) Nat. Genet. , vol.21 , pp. 195-199
    • Vulpe, C.D.1    Kuo, Y.2    Murphy, T.L.3
  • 12
    • 0035902605 scopus 로고    scopus 로고
    • Lack of hepcidin gene expression and severe tissue iron overload in upstream stimulatory factor 2 (USF2) knockout mice
    • Nicolas G, Bennoun M, Devaux I, et al.: Lack of hepcidin gene expression and severe tissue iron overload in upstream stimulatory factor 2 (USF2) knockout mice. Proc Natl Acad Sci U S A 2001, 98:8780-8785.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 8780-8785
    • Nicolas, G.1    Bennoun, M.2    Devaux, I.3
  • 13
    • 0037460697 scopus 로고    scopus 로고
    • Disrupted hepcidin regulation in HFE-associated haemochromatosis and the liver as a regulator of body iron homeostasis
    • Bridle KR, Frazer DM, Wilkins SJ, et al.: Disrupted hepcidin regulation in HFE-associated haemochromatosis and the liver as a regulator of body iron homeostasis. Lancet 2003, 361:669-673.
    • (2003) Lancet , vol.361 , pp. 669-673
    • Bridle, K.R.1    Frazer, D.M.2    Wilkins, S.J.3
  • 14
    • 13544250486 scopus 로고    scopus 로고
    • Hepcidin is decreased in TFR2 hemochromatosis
    • Nemeth E, Roetto A, Garozzo G, et al.: Hepcidin is decreased in TFR2 hemochromatosis. Blood 2005, 105:1803-1806.
    • (2005) Blood , vol.105 , pp. 1803-1806
    • Nemeth, E.1    Roetto, A.2    Garozzo, G.3
  • 15
    • 9144252017 scopus 로고    scopus 로고
    • Mutations in HFE2 cause iron overload in chromosome 1q-linked juvenile hemochromatosis
    • Papanikolaou G, Samuels ME, Ludwig EH, et al.: Mutations in HFE2 cause iron overload in chromosome 1q-linked juvenile hemochromatosis. Nat Genet 2004, 36:77-82.
    • (2004) Nat. Genet. , vol.36 , pp. 77-82
    • Papanikolaou, G.1    Samuels, M.E.2    Ludwig, E.H.3
  • 16
    • 24144459870 scopus 로고    scopus 로고
    • Identification of an intestinal heme transporter
    • in press
    • Shayeghi M, Latunde-dada GO, Oakhill JS, et al.: Identification of an intestinal heme transporter. Cell 2005, in press.
    • (2005) Cell
    • Shayeghi, M.1    Latunde-Dada, G.O.2    Oakhill, J.S.3
  • 17
    • 0016326163 scopus 로고
    • Intestinal absorption of hemoglobin iron: Heme cleavage by mucosal heme oxygenase
    • Raffin SB, Woo CH, Roost KT, et al.: Intestinal absorption of hemoglobin iron: heme cleavage by mucosal heme oxygenase. J Clin Invest 1974, 54:1344-1352.
    • (1974) J. Clin. Invest. , vol.54 , pp. 1344-1352
    • Raffin, S.B.1    Woo, C.H.2    Roost, K.T.3
  • 18
    • 3142781945 scopus 로고    scopus 로고
    • Iron, ferritin, and nutrition
    • Theil EC: Iron, ferritin, and nutrition. Annu Rev Nutr 2004, 24:327-343.
    • (2004) Annu. Rev. Nutr. , vol.24 , pp. 327-343
    • Theil, E.C.1
  • 19
    • 0032477866 scopus 로고    scopus 로고
    • NRAMP2 is mutated in the anemic Belgrade (b) rat: Evidence of a role for Nramp2 in endosomal iron transport
    • Fleming MD, Romano MA, Su MA, et al.: NRAMP2 is mutated in the anemic Belgrade (b) rat: evidence of a role for Nramp2 in endosomal iron transport. Proc Natl Acad Sci U S A 1998, 95:1148-1153.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 1148-1153
    • Fleming, M.D.1    Romano, M.A.2    Su, M.A.3
  • 20
    • 1342281234 scopus 로고    scopus 로고
    • SLC11 family of H+-coupled metal-ion transporters NRAMP1 and DMT1
    • Mackenzie B, Hediger MA: SLC11 family of H+-coupled metal-ion transporters NRAMP1 and DMT1. Pflugers Arch 2004, 447:571-579.
    • (2004) Pflugers Arch. , vol.447 , pp. 571-579
    • Mackenzie, B.1    Hediger, M.A.2
  • 21
    • 4644301624 scopus 로고    scopus 로고
    • Delayed hepcidin response explains the lag period in iron absorption following a stimulus to increase erythropoiesis
    • Frazer DM, Inglis HR, Wilkins SJ, et al.: Delayed hepcidin response explains the lag period in iron absorption following a stimulus to increase erythropoiesis. Gut 2004, 53:1509-1515.
    • (2004) Gut , vol.53 , pp. 1509-1515
    • Frazer, D.M.1    Inglis, H.R.2    Wilkins, S.J.3
  • 22
    • 0032104739 scopus 로고    scopus 로고
    • The human Nramp2 gene: Characterization of the gene structure, alternative splicing, promotor region and polymorphisms
    • Lee PL, Gelbart T, West C, et al.: The human Nramp2 gene: characterization of the gene structure, alternative splicing, promotor region and polymorphisms. Blood Cells Mol Dis 1998, 24:199-215.
    • (1998) Blood Cells Mol. Dis. , vol.24 , pp. 199-215
    • Lee, P.L.1    Gelbart, T.2    West, C.3
  • 23
    • 0034070941 scopus 로고    scopus 로고
    • Localisation of divalent metal transporter 1 (DMT1) to the microvillus membrane of rat duodenal enterocytes in iron deficiency, but to hepatocytes in iron overload
    • Trinder D, Oates PS, Thomas C, et al.: Localisation of divalent metal transporter 1 (DMT1) to the microvillus membrane of rat duodenal enterocytes in iron deficiency, but to hepatocytes in iron overload. Gut 2000, 46:270-276.
    • (2000) Gut , vol.46 , pp. 270-276
    • Trinder, D.1    Oates, P.S.2    Thomas, C.3
  • 24
    • 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, et al.: Identification of a human mutation of DMT1 in a patient with microcytic anemia and iron overload. Blood 2005, 105:1337-1342.
    • (2005) Blood , vol.105 , pp. 1337-1342
    • Mims, M.P.1    Guan, Y.2    Pospisilova, D.3
  • 25
    • 0025824547 scopus 로고
    • Regulation of intestinal iron absorption and mucosal iron kinetics in hereditary hemochromatosis
    • McLaren GD, Nathanson MH, Jacobs A, et al.: Regulation of intestinal iron absorption and mucosal iron kinetics in hereditary hemochromatosis. J Lab Clin Med 1991, 117:390-401.
    • (1991) J. Lab. Clin. Med. , vol.117 , pp. 390-401
    • McLaren, G.D.1    Nathanson, M.H.2    Jacobs, A.3
  • 26
    • 20444416123 scopus 로고    scopus 로고
    • The iron exporter ferroportin/Slc40a1 is essential for iron homeostasis
    • Donovan A, Lima CA, Pinkus JL, et al.: The iron exporter ferroportin/Slc40a1 is essential for iron homeostasis. Cell Metabolism 2005, 1:191-200.
    • (2005) Cell Metabolism , vol.1 , pp. 191-200
    • Donovan, A.1    Lima, C.A.2    Pinkus, J.L.3
  • 27
    • 0034786537 scopus 로고    scopus 로고
    • Cloning and gastrointestinal expression of hephaestin: Relationship to other iron transport proteins
    • Frazer DM, Vulpe CD, McKie AT, et al.: Cloning and gastrointestinal expression of hephaestin: relationship to other iron transport proteins. Am J Physiol 2001, 281:G931-G939.
    • (2001) Am. J. Physiol. , vol.281
    • Frazer, D.M.1    Vulpe, C.D.2    McKie, A.T.3
  • 28
    • 2342508341 scopus 로고    scopus 로고
    • Hephaestin is a ferroxidase that maintains partial activity in sex-linked anemia mice
    • Chen H, Attieh ZK, Su T, et al.: Hephaestin is a ferroxidase that maintains partial activity in sex-linked anemia mice. Blood 2004, 103:3933-3939.
    • (2004) Blood , vol.103 , pp. 3933-3939
    • Chen, H.1    Attieh, Z.K.2    Su, T.3
  • 29
    • 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, et al.: Mislocalisation of hephaestin, a multicopper ferroxidase involved in basolateral intestinal iron transport, in the sex linked anaemia mouse. Gut 2004, 53:201-206.
    • (2004) Gut , vol.53 , pp. 201-206
    • Kuo, Y.M.1    Su, T.2    Chen, H.3
  • 30
  • 31
    • 23044508432 scopus 로고    scopus 로고
    • Resistance to hepcidin is conferred by hemochromatosis-associated mutations of ferroportin
    • Drakesmith H, Schimanski LM, Ormerod E, et al.: Resistance to hepcidin is conferred by hemochromatosis-associated mutations of ferroportin. Blood 2005, 106:1092-1097.
    • (2005) Blood , vol.106 , pp. 1092-1097
    • Drakesmith, H.1    Schimanski, L.M.2    Ormerod, E.3
  • 32
    • 0028049495 scopus 로고
    • Regulators of iron balance in humans
    • Finch C: Regulators of iron balance in humans. Blood 1994, 84:1697-1702.
    • (1994) Blood , vol.84 , pp. 1697-1702
    • Finch, C.1
  • 33
    • 0013361913 scopus 로고    scopus 로고
    • Regulation of intestinal iron transport
    • Edited by Templeton DM. New York: Marcel Dekker, Inc
    • Anderson GJ, Vulpe CD: Regulation of intestinal iron transport. In Molecular and Cellular Iron Transport. Edited by Templeton DM. New York: Marcel Dekker, Inc; 2002:559-598.
    • (2002) Molecular and Cellular Iron Transport , pp. 559-598
    • Anderson, G.J.1    Vulpe, C.D.2
  • 34
    • 0030841393 scopus 로고    scopus 로고
    • Iron, infections, and anemia of inflammation
    • Jurado RL: Iron, infections, and anemia of inflammation. Clin Infect Dis 1997, 25:888-895.
    • (1997) Clin. Infect. Dis. , vol.25 , pp. 888-895
    • Jurado, R.L.1
  • 35
    • 9344224529 scopus 로고    scopus 로고
    • A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis
    • Feder JN, Gnirke A, Thomas W, et al.: A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis. Nat Genet 1996, 13:399-408.
    • (1996) Nat. Genet. , vol.13 , pp. 399-408
    • Feder, J.N.1    Gnirke, A.2    Thomas, W.3
  • 37
    • 0034022636 scopus 로고    scopus 로고
    • The gene TFR2 is mutated in a new type of haemochromatosis mapping to 7q22
    • Camaschella C, Roetto A, Calì A, et al.: The gene TFR2 is mutated in a new type of haemochromatosis mapping to 7q22. Nat Genet 2000, 25:14-15.
    • (2000) Nat. Genet. , vol.25 , pp. 14-15
    • Camaschella, C.1    Roetto, A.2    Calì, A.3
  • 38
    • 20244388240 scopus 로고    scopus 로고
    • Mutant antimicrobial peptide hepcidin is associated with severe juvenile hemochromatosis
    • Roetto A, Papanikolaou G, Politou M, et al.: Mutant antimicrobial peptide hepcidin is associated with severe juvenile hemochromatosis. Nat Genet 2003, 33:21-22.
    • (2003) Nat. Genet. , vol.33 , pp. 21-22
    • Roetto, A.1    Papanikolaou, G.2    Politou, M.3
  • 39
    • 0033597780 scopus 로고    scopus 로고
    • Molecular cloning of transferrin receptor 2: A new member of the transferrin receptor-like family
    • Kawabata H, Yang R, Hirama T, et al.: Molecular cloning of transferrin receptor 2: a new member of the transferrin receptor-like family. J Biol Chem 1999, 274:20826-20832.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20826-20832
    • Kawabata, H.1    Yang, R.2    Hirama, T.3
  • 40
    • 0035896642 scopus 로고    scopus 로고
    • Hepcidin, a urinary antimicrobial peptide synthesized in the liver
    • Park CH, Valore EV, Waring AJ, Ganz T: Hepcidin, a urinary antimicrobial peptide synthesized in the liver. J Biol Chem 2001, 276:7806-7810.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7806-7810
    • Park, C.H.1    Valore, E.V.2    Waring, A.J.3    Ganz, T.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
    • Pigeon C, Ilyin G, Courselaud B, et al.: A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin, is overexpressed during iron overload. J Biol Chem 2001, 276:7811-7819.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7811-7819
    • Pigeon, C.1    Ilyin, G.2    Courselaud, B.3
  • 42
    • 0037007064 scopus 로고    scopus 로고
    • Severe iron deficiency anemia in transgenic mice expressing liver hepcidin
    • Nicolas G, Bennon M, Porteu A, et al.: Severe iron deficiency anemia in transgenic mice expressing liver hepcidin. Proc Natl Acad Sci U S A 2002, 99:4596-4601.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 4596-4601
    • Nicolas, G.1    Bennon, M.2    Porteu, A.3
  • 43
    • 0036791486 scopus 로고    scopus 로고
    • The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation
    • Nicolas G, Chauvet C, Viatte L, et al.: The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation. J Clin Invest 2002, 110:1037-1044.
    • (2002) J. Clin. Invest. , vol.110 , pp. 1037-1044
    • Nicolas, G.1    Chauvet, C.2    Viatte, L.3
  • 44
    • 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
    • Millard KN, Frazer DM, Wilkins SJ, Anderson GJ: Changes in the expression of intestinal iron transport and hepatic regulatory molecules explain the enhanced iron absorption associated with pregnancy in the rat. Gut 2004, 53:655-660.
    • (2004) Gut , vol.53 , pp. 655-660
    • Millard, K.N.1    Frazer, D.M.2    Wilkins, S.J.3    Anderson, G.J.4
  • 45
    • 0036727925 scopus 로고    scopus 로고
    • Hepcidin expression inversely correlates with the expression of duodenal iron transporters and iron absorption in rats
    • Frazer DM, Wilkins SJ, Becker EM, et al.: Hepcidin expression inversely correlates with the expression of duodenal iron transporters and iron absorption in rats. Gastroenterology 2002, 123:835-844.
    • (2002) Gastroenterology , vol.123 , pp. 835-844
    • Frazer, D.M.1    Wilkins, S.J.2    Becker, E.M.3
  • 46
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization
    • Nemeth E, Tuttle MS, Powelson J, et al.: Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science 2004, 306:2090-2093.
    • (2004) Science , vol.306 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3
  • 47
    • 0030712463 scopus 로고    scopus 로고
    • Association of the transferrin receptor in human placenta with HFE, the protein defective in hereditary hemochromatosis
    • Parkkila S, Waheed A, Britton RS, et al.: Association of the transferrin receptor in human placenta with HFE, the protein defective in hereditary hemochromatosis. Proc Natl Acad Sci U S A 1997, 94:13198-13202.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 13198-13202
    • Parkkila, S.1    Waheed, A.2    Britton, R.S.3
  • 48
    • 0038312385 scopus 로고    scopus 로고
    • Decreased liver hepcidin expression in the Hfe knockout mouse
    • Ahmad KA, Ahmann JR, Migas MC, et al.: Decreased liver hepcidin expression in the Hfe knockout mouse. Blood Cells Mol Dis 2002, 29:361-366.
    • (2002) Blood Cells Mol. Dis. , vol.29 , pp. 361-366
    • Ahmad, K.A.1    Ahmann, J.R.2    Migas, M.C.3
  • 49
    • 0037847496 scopus 로고    scopus 로고
    • Constitutive hepcidin expression prevents iron overload in a mouse model of hemochromatosis
    • Nicolas G, Viatte L, Lou DQ, et al.: Constitutive hepcidin expression prevents iron overload in a mouse model of hemochromatosis. Nat Genet 2003, 34:97-101.
    • (2003) Nat. Genet. , vol.34 , pp. 97-101
    • Nicolas, G.1    Viatte, L.2    Lou, D.Q.3
  • 50
    • 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, 30:288-297.
    • (2003) Blood Cells Mol. Dis. , vol.30 , pp. 288-297
    • Frazer, D.M.1    Anderson, G.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.