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Volumn 53, Issue 10, 2004, Pages 1509-1515

Delayed hepcidin response explains the lag period in iron absorption following a stimulus to increase erythropoiesis

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME B; HEPCIDIN; IRON; METAL; PHENYLHYDRAZINE; TRANSFERRIN;

EID: 4644301624     PISSN: 00175749     EISSN: None     Source Type: Journal    
DOI: 10.1136/gut.2003.037416     Document Type: Article
Times cited : (86)

References (44)
  • 1
    • 50349143880 scopus 로고
    • Absorption and excretion of iron
    • McCance RA, Widdowson EM. Absorption and excretion of iron. Lancet 1937;ii:680-4.
    • (1937) Lancet , vol.2 , pp. 680-684
    • McCance, R.A.1    Widdowson, E.M.2
  • 2
    • 0030959086 scopus 로고    scopus 로고
    • Regulation of intestinal non-haem iron absorption
    • Lombard M, Chua E, O'Toole P. Regulation of intestinal non-haem iron absorption. Gut 1997;40:435-9.
    • (1997) Gut , vol.40 , pp. 435-439
    • Lombard, M.1    Chua, E.2    O'Toole, P.3
  • 3
    • 0033599057 scopus 로고    scopus 로고
    • Disorders of iron metabolism
    • Andrews NC. Disorders of iron metabolism. N Engl J Med 1999;341:1986-95.
    • (1999) N Engl J Med , vol.341 , pp. 1986-1995
    • Andrews, N.C.1
  • 4
    • 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
  • 6
    • 84965094627 scopus 로고
    • The role of the intestinal mucosa in iron absorption
    • Charlton RW, Jacobs P, Bothwell TH. The role of the intestinal mucosa in iron absorption. J Clin Invest 1965;44:543-54.
    • (1965) J Clin Invest , vol.44 , pp. 543-554
    • Charlton, R.W.1    Jacobs, P.2    Bothwell, T.H.3
  • 7
    • 0034284595 scopus 로고    scopus 로고
    • LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity
    • Krause A, Neitz S, Mägert H, et al. LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity. FEBS Lett 2000;480:147-50.
    • (2000) FEBS Lett , vol.480 , pp. 147-150
    • Krause, A.1    Neitz, S.2    Mägert, H.3
  • 8
    • 0035896642 scopus 로고    scopus 로고
    • Hepcidin, a urinary antimicrobial peptide synthesized in the liver
    • Park CH, Valore EV, Waring AJ, et al. Hepcidin, a urinary antimicrobial peptide synthesized in the liver. J Biol Chem 2001;276:7806-10.
    • (2001) J Biol Chem , vol.276 , pp. 7806-7810
    • Park, C.H.1    Valore, E.V.2    Waring, A.J.3
  • 9
    • 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;276:7811-19.
    • (2001) J Biol Chem , vol.276 , pp. 7811-7819
    • Pigeon, C.1    Ilyin, G.2    Courselaud, B.3
  • 10
    • 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;29:361-6.
    • (2002) Blood Cells Mol Dis , vol.29 , pp. 361-366
    • Ahmad, K.A.1    Ahmann, J.R.2    Migas, M.C.3
  • 11
    • 0242300677 scopus 로고    scopus 로고
    • Dietary iron regulates hepatic hepcidin 1 and 2 mRNAs in mice
    • Mazur A, Feillet-Coudray C, Romier B, et al. Dietary iron regulates hepatic hepcidin 1 and 2 mRNAs in mice. Metabolism 2003;52:1229-31.
    • (2003) Metabolism , vol.52 , pp. 1229-1231
    • Mazur, A.1    Feillet-Coudray, C.2    Romier, B.3
  • 12
    • 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;110:1037-44.
    • (2002) J Clin Invest , vol.110 , pp. 1037-1044
    • Nicolas, G.1    Chauvet, C.2    Viatte, L.3
  • 13
    • 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;98:8780-5.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 8780-8785
    • Nicolas, G.1    Bennoun, M.2    Devaux, I.3
  • 14
    • 0037007064 scopus 로고    scopus 로고
    • Severe iron deficiency anemia in transgenic mice expressing liver hepcidin
    • Nicolas G, Bennoun M, Porteu A, et al. Severe iron deficiency anemia in transgenic mice expressing liver hepcidin. Proc Natl Acad Sci U S A 2002;99:4596-601.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 4596-4601
    • Nicolas, G.1    Bennoun, M.2    Porteu, A.3
  • 15
    • 0037460697 scopus 로고    scopus 로고
    • Failure of hepcidin upregulation in HFE-associated haemochromatosis implicates the liver in the regulation of body iron homeostasis
    • Bridle KR, Frazer DM, Wilkins SJ, et al. Failure of hepcidin upregulation in HFE-associated haemochromatosis implicates the liver in the regulation of body iron homeostasis. Lancet 2003;361:669-73.
    • (2003) Lancet , vol.361 , pp. 669-673
    • Bridle, K.R.1    Frazer, D.M.2    Wilkins, S.J.3
  • 16
    • 20244388240 scopus 로고    scopus 로고
    • Mutant antimicrobial peptide hepcidin is associated with severe juvenile hemochromatosis
    • Roelto A, Paponikolaou G, Politou M, et al. Mutant antimicrobial peptide hepcidin is associated with severe juvenile hemochromatosis. Nat Genet 2003;33:21-2.
    • (2003) Nat Genet , vol.33 , pp. 21-22
    • Roelto, A.1    Paponikolaou, G.2    Politou, M.3
  • 17
    • 0014104334 scopus 로고
    • Effect of endotoxin on iron absorption
    • Cortell S, Conrad ME. Effect of endotoxin on iron absorption. Am J Physiol 1967;213:43-7.
    • (1967) Am J Physiol , vol.213 , pp. 43-47
    • Cortell, S.1    Conrad, M.E.2
  • 18
    • 0036670737 scopus 로고    scopus 로고
    • Relationship between intestinal iron-transporter expression, hepatic hepcidin levels and the control of iron absorption
    • Anderson GJ, Frazer DM, Wilkins SJ, et al. Relationship between intestinal iron-transporter expression, hepatic hepcidin levels and the control of iron absorption. Biochem Soc Trans 2002;30:724-6.
    • (2002) Biochem Soc Trans , vol.30 , pp. 724-726
    • Anderson, G.J.1    Frazer, D.M.2    Wilkins, S.J.3
  • 19
    • 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;123:835-44.
    • (2002) Gastroenterology , vol.123 , pp. 835-844
    • Frazer, D.M.1    Wilkins, S.J.2    Becker, E.M.3
  • 20
    • 0002973627 scopus 로고
    • The significance of iron turnover in the control of iron absorption
    • Weintraub LR, Conrad ME, Crosby WH. The significance of iron turnover in the control of iron absorption. Blood 1964;24:19-24.
    • (1964) Blood , vol.24 , pp. 19-24
    • Weintraub, L.R.1    Conrad, M.E.2    Crosby, W.H.3
  • 21
    • 0027972484 scopus 로고
    • The endocytosis of transferrin by rat intestinal epithelial cells
    • Anderson GJ, Powell LW, Halliday JW. The endocytosis of transferrin by rat intestinal epithelial cells. Gastroenterology 1994;106:414-22.
    • (1994) Gastroenterology , vol.106 , pp. 414-422
    • Anderson, G.J.1    Powell, L.W.2    Halliday, J.W.3
  • 23
    • 0014267781 scopus 로고
    • A simple technique for measuring storage iron concentrations in formalinised liver samples
    • Torrance JD, Bothwell TH. A simple technique for measuring storage iron concentrations in formalinised liver samples. S Afr J Med Sci 1968;33:9-11.
    • (1968) S Afr J Med Sci , vol.33 , pp. 9-11
    • Torrance, J.D.1    Bothwell, T.H.2
  • 24
    • 0036197931 scopus 로고    scopus 로고
    • Increase in ferric and ferrous iron in the rat hippocampus with time after kainate-induced excitotoxic injury
    • Wang XS, Ong WY, Connor JR. Increase in ferric and ferrous iron in the rat hippocampus with time after kainate-induced excitotoxic injury. Exp Brain Res 2002;143:137-48.
    • (2002) Exp Brain Res , vol.143 , pp. 137-148
    • Wang, X.S.1    Ong, W.Y.2    Connor, J.R.3
  • 25
    • 0017100245 scopus 로고
    • The detection of four molecular forms of human transferrin during the iron binding process
    • Makey DG, Seal US. The detection of four molecular forms of human transferrin during the iron binding process. Biochim Biophys Acta 1976;453:250-6.
    • (1976) Biochim Biophys Acta , vol.453 , pp. 250-256
    • Makey, D.G.1    Seal, U.S.2
  • 26
    • 0019198386 scopus 로고
    • The electrophoresis of transferrins in urea/polyacrylamide gels
    • Evans RW, Williams J. The electrophoresis of transferrins in urea/polyacrylamide gels. Biochem J 1980;189:541-6.
    • (1980) Biochem J , vol.189 , pp. 541-546
    • Evans, R.W.1    Williams, J.2
  • 27
    • 0020047241 scopus 로고
    • Estimation of the saturation of serum transferrin by an electrophoretic technique
    • Davy P, Bingham D, Walters G, et al. Estimation of the saturation of serum transferrin by an electrophoretic technique. Ann Clin Biochem 1982;19:57-9.
    • (1982) Ann Clin Biochem , vol.19 , pp. 57-59
    • Davy, P.1    Bingham, D.2    Walters, G.3
  • 28
    • 0034786537 scopus 로고    scopus 로고
    • Cloning and gastrointestinal expression of rat hephaestin: Relationship to other iron transport proteins
    • Frazer DM, Vulpe CD, McKie AT, et al. Cloning and gastrointestinal expression of rat hephaestin: relationship to other iron transport proteins. Am J Physiol 2001;281:G931-9.
    • (2001) Am J Physiol , vol.281
    • Frazer, D.M.1    Vulpe, C.D.2    McKie, A.T.3
  • 29
    • 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;388:482-8.
    • (1997) Nature , vol.388 , pp. 482-488
    • Gunshin, H.1    Mackenzie, B.2    Berger, U.V.3
  • 30
    • 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;16:383-6.
    • (1997) Nat Genet , vol.16 , pp. 383-386
    • Fleming, M.D.1    Trenor III, C.C.2    Su, M.A.3
  • 31
    • 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;291:1755-9.
    • (2001) Science , vol.291 , pp. 1755-1759
    • McKie, A.T.1    Barrow, D.2    Latunde-Dada, G.O.3
  • 32
    • 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
  • 33
    • 0034677467 scopus 로고    scopus 로고
    • Postional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter
    • Donovan A, Brownlie A, Zhou Y, et al. Postional 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
  • 34
    • 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
  • 36
    • 0028049495 scopus 로고
    • Regulators of iron balance in humans
    • Finch C. Regulators of iron balance in humans. Blood 1994;84:1697-702.
    • (1994) Blood , vol.84 , pp. 1697-1702
    • Finch, C.1
  • 37
    • 0019590731 scopus 로고
    • Radioimmunochemical measurement of the transferrin receptor in human trophoblast and reticulocyte membranes with a specific anti-receptor antibody
    • Enns CA, Shindelman JE, Tonik SE, et al. Radioimmunochemical measurement of the transferrin receptor in human trophoblast and reticulocyte membranes with a specific anti-receptor antibody. Proc Natl Acad Sci U S A 1981;78:4222-5.
    • (1981) Proc Natl Acad Sci U S A , vol.78 , pp. 4222-4225
    • Enns, C.A.1    Shindelman, J.E.2    Tonik, S.E.3
  • 38
    • 0021265943 scopus 로고
    • The effect of the iron saturation of transferrin on its binding and uptake by rabbit reticulocytes
    • Young SP, Bomford A, Williams R. The effect of the iron saturation of transferrin on its binding and uptake by rabbit reticulocytes. Biochem J 1984;219:505-10.
    • (1984) Biochem J , vol.219 , pp. 505-510
    • Young, S.P.1    Bomford, A.2    Williams, R.3
  • 39
    • 0022263305 scopus 로고
    • Molecular advantage of diferric transferrin in delivering iron to reticulocytes: A comparative study
    • Huebers H, Csiba E, Huebers E, et al. Molecular advantage of diferric transferrin in delivering iron to reticulocytes: a comparative study. Proc Soc Exp Biol Med 1985;179:222-6.
    • (1985) Proc Soc Exp Biol Med , vol.179 , pp. 222-226
    • Huebers, H.1    Csiba, E.2    Huebers, E.3
  • 41
    • 0001369958 scopus 로고
    • Studies on congenital hemolytic syndromes. IV. Gastrointestinal absorption of iron
    • Erlandson ME, Waldon B, Stern G, et al. Studies on congenital hemolytic syndromes. IV. Gastrointestinal absorption of iron. Blood 1962;19:359-78.
    • (1962) Blood , vol.19 , pp. 359-378
    • Erlandson, M.E.1    Waldon, B.2    Stern, G.3
  • 42
    • 0021171846 scopus 로고
    • Increased red blood cell protoporphyrin in thalassemia: A result of relative iron deficiency
    • Pootrakul P, Wattanasaree J, Anuwatanakulchai MS, et al. Increased red blood cell protoporphyrin in thalassemia: a result of relative iron deficiency. Am J Clin Pathol 1984;82:289-93.
    • (1984) Am J Clin Pathol , vol.82 , pp. 289-293
    • Pootrakul, P.1    Wattanasaree, J.2    Anuwatanakulchai, M.S.3
  • 43
    • 0023547952 scopus 로고
    • Adequacy of iron supply for erythropoiesis: In vivo observations in humans
    • Cazzola M, Pootrakul P, Bergamaschi G, et al. Adequacy of iron supply for erythropoiesis: in vivo observations in humans. J Lab Clin Med 1987;110:734-9.
    • (1987) J Lab Clin Med , vol.110 , pp. 734-739
    • Cazzola, M.1    Pootrakul, P.2    Bergamaschi, G.3
  • 44
    • 0346433908 scopus 로고    scopus 로고
    • Decreased hepcidin mRNA expression in thalassemic mice
    • Adamsky K, Weizer O, Amariglio N, et al. Decreased hepcidin mRNA expression in thalassemic mice. B J Haematol 2004;124:123-5.
    • (2004) B J Haematol , vol.124 , pp. 123-125
    • Adamsky, K.1    Weizer, O.2    Amariglio, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.