메뉴 건너뛰기




Volumn 28, Issue 6, 2005, Pages 372-380

Recent advance in the understanding of iron metabolism and its role on host defense

Author keywords

hepcidin; IRE; iron; iron refractory anemia; IRP

Indexed keywords

ANTIMICROBIAL CATIONIC PEPTIDE; HEPCIDIN; IRON; IRON REGULATORY FACTOR;

EID: 33644836576     PISSN: 09114300     EISSN: 13497413     Source Type: Journal    
DOI: 10.2177/jsci.28.372     Document Type: Article
Times cited : (1)

References (29)
  • 1
    • 0038662619 scopus 로고    scopus 로고
    • Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein.
    • Nemeth, E., Valore, E. V., Territo, M. et al.: Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein. Blood 101: 2461–2463, 2003.
    • (2003) Blood , vol.101 , pp. 2461-2463
    • Nemeth, E.1    Valore, E.V.2    Territo, M.3
  • 2
    • 0027452550 scopus 로고
    • Regulating the fate of mRNA: the control of cellular iron metabolism.
    • Klausner, R. D., Rouault, T. A. and Harford, J. B.: Regulating the fate of mRNA: the control of cellular iron metabolism. Cell 72: 19–28, 1993.
    • (1993) Cell , vol.72 , pp. 19-28
    • Klausner, R.D.1    Rouault, T.A.2    Harford, J.B.3
  • 3
    • 7044263003 scopus 로고    scopus 로고
    • Prevention of hepatitis C virus-related hepatocellular carcinoma
    • Heathcote, E. J.: Prevention of hepatitis C virus-related hepatocellular carcinoma. Gastroenterology 127: S294-S302, 2004.
    • (2004) Gastroenterology , vol.127 , pp. S294-S302
    • Heathcote, E.J.1
  • 4
    • 0034572933 scopus 로고    scopus 로고
    • Iron homeostasis: insights from genetics and animal models.
    • Andrews, N. C.: Iron homeostasis: insights from genetics and animal models. Nat Rev Genet 1: 208–217, 2000.
    • (2000) Nat Rev Genet , vol.1 , pp. 208-217
    • Andrews, N.C.1
  • 5
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: molecular control of mammalian iron metabolism.
    • Hentze, M. W., Muckenthaler, M. U. and Andrews, N. C.: Balancing acts: molecular control of mammalian iron metabolism. Cell 117: 285–297, 2004.
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 6
    • 0030755366 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian proton-coupled metal-ion transporter.
    • Gunshin, H., Mackenzie, B., Berger, U. V. et al.: Cloning and characterization of a mammalian proton-coupled metal-ion transporter. Nature 388: 482–488, 1997.
    • (1997) Nature , vol.388 , pp. 482-488
    • Gunshin, H.1    Mackenzie, B.2    Berger, U.V.3
  • 7
    • 24144459870 scopus 로고    scopus 로고
    • Identification of an intestinal heme transporter.
    • Shayeghi, M., Latunde-Dada, G. O., Oakhill, J. S. et al.: Identification of an intestinal heme transporter. Cell 122: 789–801, 2005.
    • (2005) Cell , vol.122 , pp. 789-801
    • Shayeghi, M.1    Latunde-Dada, G.O.2    Oakhill, J.S.3
  • 8
    • 0036362991 scopus 로고    scopus 로고
    • The expression and regulation of the iron transport molecules hephaestin and IREG1: implications for the control of iron export from the small intestine.
    • Anderson, G. J., Frazer, D. M., McKie, A. T. et al.: The expression and regulation of the iron transport molecules hephaestin and IREG1: implications for the control of iron export from the small intestine. Cell Biochem Biophys 36: 137–146, 2002.
    • (2002) Cell Biochem Biophys , vol.36 , pp. 137-146
    • Anderson, G.J.1    Frazer, D.M.2    McKie, A.T.3
  • 9
    • 0028895749 scopus 로고
    • A mutation in the ceruloplasmin gene is associated with systemic hemosiderosis in humans.
    • Yoshida, K., Furihata, K., Takeda, S. et al.: A mutation in the ceruloplasmin gene is associated with systemic hemosiderosis in humans. Nat Genet 9: 267–272, 1995.
    • (1995) Nat Genet , vol.9 , pp. 267-272
    • Yoshida, K.1    Furihata, K.2    Takeda, S.3
  • 10
    • 0028903259 scopus 로고
    • Aceruloplasminemia: molecular characterization of this disorder of iron metabolism.
    • Harris, Z. L., Takahashi, Y., Miyajima, H. et al.: Aceruloplasminemia: molecular characterization of this disorder of iron metabolism. Proc Natl Acad Sci U S A 92: 2539–2543, 1995.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 2539-2543
    • Harris, Z.L.1    Takahashi, Y.2    Miyajima, H.3
  • 11
    • 0035896642 scopus 로고    scopus 로고
    • Hepcidin, a urinary antimicrobial peptide synthesized in the liver.
    • Park, C. H., Valore, E. V., Waring, A. J. et al.: Hepcidin, a urinary antimicrobial peptide synthesized in the liver. J Biol Chem 276: 7806–7810, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 7806-7810
    • Park, C.H.1    Valore, E.V.2    Waring, A.J.3
  • 12
    • 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 276: 7811–7819, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 7811-7819
    • Pigeon, C.1    Ilyin, G.2    Courselaud, B.3
  • 13
    • 0041672570 scopus 로고    scopus 로고
    • Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation.
    • Ganz, T.: Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation. Blood 102: 783–788, 2003.
    • (2003) Blood , vol.102 , pp. 783-788
    • Ganz, T.1
  • 14
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization.
    • Nemeth, E., Tuttle, M. S., Powelson, J. et al.: Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science 306: 2090–2093, 2004.
    • (2004) Science , vol.306 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3
  • 15
    • 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 USA 98: 8780–8785, 2001.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8780-8785
    • Nicolas, G.1    Bennoun, M.2    Devaux, I.3
  • 16
    • 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 USA 99: 4596–4601, 2002.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4596-4601
    • Nicolas, G.1    Bennoun, M.2    Porteu, A.3
  • 17
    • 11144314814 scopus 로고    scopus 로고
    • Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron.
    • Flo, T. H., Smith, K. D., Sato, S. et al.: Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron. Nature 432: 917–921, 2004.
    • (2004) Nature , vol.432 , pp. 917-921
    • Flo, T.H.1    Smith, K.D.2    Sato, S.3
  • 18
    • 9344224529 scopus 로고    scopus 로고
    • A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis.
    • Feder, J. N., Gnirke, A., Thomas, W. et al.: A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis. Nat Genet 13: 399–408, 1996.
    • (1996) Nat Genet , vol.13 , pp. 399-408
    • Feder, J.N.1    Gnirke, A.2    Thomas, W.3
  • 19
    • 0029670047 scopus 로고    scopus 로고
    • beta2 knockout mice develop parenchymal iron overload: A putative role for class I genes of the major histocompatibility complex in iron metabolism.
    • Rothenberg, B. E. and Voland, J. R.: beta2 knockout mice develop parenchymal iron overload: A putative role for class I genes of the major histocompatibility complex in iron metabolism. Proc Natl Acad Sci USA 93: 1529–1534, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1529-1534
    • Rothenberg, B.E.1    Voland, J.R.2
  • 20
    • 0141814727 scopus 로고    scopus 로고
    • An ubiquitin ligase recognizing a protein oxidized by iron: implications for the turnover of oxidatively damaged proteins.
    • Iwai, K.: An ubiquitin ligase recognizing a protein oxidized by iron: implications for the turnover of oxidatively damaged proteins. J Biochem (Tokyo) 134: 175–182, 2003.
    • (2003) J Biochem (Tokyo) , vol.134 , pp. 175-182
    • Iwai, K.1
  • 21
    • 10744223491 scopus 로고    scopus 로고
    • Genetic ablations of iron regulatory proteins 1 and 2 reveal why iron regulatory protein 2 dominates iron homeostasis.
    • Meyron-Holtz, E. G., Ghosh, M. C., Iwai, K. et al.: Genetic ablations of iron regulatory proteins 1 and 2 reveal why iron regulatory protein 2 dominates iron homeostasis. Embo J 23: 386–395, 2004.
    • (2004) Embo J , vol.23 , pp. 386-395
    • Meyron-Holtz, E.G.1    Ghosh, M.C.2    Iwai, K.3
  • 22
    • 0028788316 scopus 로고
    • Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2.
    • Iwai, K., Klausner, R. D. and Rouault, T. A.: Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2. Embo J 14: 5350–5357, 1995.
    • (1995) Embo J , vol.14 , pp. 5350-5357
    • Iwai, K.1    Klausner, R.D.2    Rouault, T.A.3
  • 23
    • 0032574765 scopus 로고    scopus 로고
    • Iron-dependent oxidation, ubiquitination, and degradation of iron regulatory protein 2: implications for degradation of oxidized proteins.
    • Iwai, K., Drake, S. K., Wehr, N. B. et al.: Iron-dependent oxidation, ubiquitination, and degradation of iron regulatory protein 2: implications for degradation of oxidized proteins. Proc Natl Acad Sci USA 95: 4924–4928, 1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4924-4928
    • Iwai, K.1    Drake, S.K.2    Wehr, N.B.3
  • 24
    • 0141989227 scopus 로고    scopus 로고
    • Identification of the ubiquitin protein ligase that recognizes oxidized IRP2.
    • Yamanaka, K., Ishikawa, H., Megumi, Y. et al.: Identification of the ubiquitin protein ligase that recognizes oxidized IRP2. Nat Cell Biol 5: 336–340, 2003.
    • (2003) Nat Cell Biol , vol.5 , pp. 336-340
    • Yamanaka, K.1    Ishikawa, H.2    Megumi, Y.3
  • 25
    • 22544452148 scopus 로고    scopus 로고
    • Involvement of heme regulatory motif in heme-mediated ubiquitination and degradation of IRP2.
    • Ishikawa, H., Kato, M., Hori, H. et al.: Involvement of heme regulatory motif in heme-mediated ubiquitination and degradation of IRP2. Mol Cell 19: 171–181, 2005.
    • (2005) Mol Cell , vol.19 , pp. 171-181
    • Ishikawa, H.1    Kato, M.2    Hori, H.3
  • 26
    • 0028049495 scopus 로고
    • Regulators of iron balance in humans.
    • Finch, C.: Regulators of iron balance in humans. Blood 84: 1697–1702, 1994.
    • (1994) Blood , vol.84 , pp. 1697-1702
    • Finch, C.1
  • 27
    • 33144456592 scopus 로고    scopus 로고
    • Hemochromatosis: Genetics and Pathophysiology
    • Beutler, E.: Hemochromatosis: Genetics and Pathophysiology. Annu Rev Med 2006.
    • (2006) Annu Rev Med
    • Beutler, E.1
  • 28
    • 85047693999 scopus 로고    scopus 로고
    • Anemia of inflammation: the cytokinehepcidin link.
    • Andrews, N. C.: Anemia of inflammation: the cytokinehepcidin link. J Clin Invest 113: 1251–1253, 2004.
    • (2004) J Clin Invest , vol.113 , pp. 1251-1253
    • Andrews, N.C.1
  • 29
    • 0028318340 scopus 로고
    • Improvement of serum aminotransferase levels after phlebotomy in patients with chronic active hepatitis C and excess hepatic iron.
    • Hayashi, H., Takikawa, T., Nishimura, N. et al.: Improvement of serum aminotransferase levels after phlebotomy in patients with chronic active hepatitis C and excess hepatic iron. Am J Gastroenterol 89: 986–988, 1994.
    • (1994) Am J Gastroenterol , vol.89 , pp. 986-988
    • Hayashi, H.1    Takikawa, T.2    Nishimura, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.