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Volumn 7, Issue 3, 2008, Pages 205-214

The Transferrin Receptor Modulates Hfe-Dependent Regulation of Hepcidin Expression

Author keywords

HUMDISEASE

Indexed keywords

CD71 ANTIGEN; HEPCIDIN; HFE PROTEIN; TRANSFERRIN RECEPTOR;

EID: 39649115776     PISSN: 15504131     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cmet.2007.11.016     Document Type: Article
Times cited : (292)

References (45)
  • 1
    • 0018850440 scopus 로고
    • Iron transport and storage proteins
    • Aisen P., and Listowsky I. Iron transport and storage proteins. Annu. Rev. Biochem. 49 (1980) 357-393
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 357-393
    • Aisen, P.1    Listowsky, I.2
  • 2
    • 0037103357 scopus 로고    scopus 로고
    • Regulation of iron absorption in Hfe mutant mice
    • Ajioka R.S., Levy J.E., Andrews N.C., and Kushner J.P. Regulation of iron absorption in Hfe mutant mice. Blood 100 (2002) 1465-1469
    • (2002) Blood , vol.100 , pp. 1465-1469
    • Ajioka, R.S.1    Levy, J.E.2    Andrews, N.C.3    Kushner, J.P.4
  • 3
    • 0034610781 scopus 로고    scopus 로고
    • Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor
    • Bennett M.J., Lebron J.A., and Bjorkman P.J. Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor. Nature 403 (2000) 46-53
    • (2000) Nature , vol.403 , pp. 46-53
    • Bennett, M.J.1    Lebron, J.A.2    Bjorkman, P.J.3
  • 5
    • 4644336057 scopus 로고    scopus 로고
    • No hepatic iron overload 12 years after liver transplantation for hereditary hemochromatosis
    • Bralet M.P., Duclos-Vallee J.C., Castaing D., Samuel D., and Guettier C. No hepatic iron overload 12 years after liver transplantation for hereditary hemochromatosis. Hepatology 40 (2004) 762
    • (2004) Hepatology , vol.40 , pp. 762
    • Bralet, M.P.1    Duclos-Vallee, J.C.2    Castaing, D.3    Samuel, D.4    Guettier, C.5
  • 8
    • 0016860906 scopus 로고
    • Internal regulation of iron absorption
    • Cavill I., Worwood M., and Jacobs A. Internal regulation of iron absorption. Nature 256 (1975) 328-329
    • (1975) Nature , vol.256 , pp. 328-329
    • Cavill, I.1    Worwood, M.2    Jacobs, A.3
  • 9
    • 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 T.L., and Enns C.A. HFE modulates transferrin receptor 2 levels in hepatoma cells via interactions that differ from transferrin receptor 1-HFE interactions. J. Biol. Chem. 282 (2007) 36862-36870
    • (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
  • 11
    • 0033826764 scopus 로고    scopus 로고
    • Iron regulatory proteins and the molecular control of mammalian iron metabolism
    • Eisenstein R.S. Iron regulatory proteins and the molecular control of mammalian iron metabolism. Annu. Rev. Nutr. 20 (2000) 627-662
    • (2000) Annu. Rev. Nutr. , vol.20 , pp. 627-662
    • Eisenstein, R.S.1
  • 13
    • 2942554825 scopus 로고    scopus 로고
    • HFE and transferrin directly compete for transferrin receptor in solution and at the cell surface
    • Giannetti A.M., and Bjorkman P.J. HFE and transferrin directly compete for transferrin receptor in solution and at the cell surface. J. Biol. Chem. 279 (2004) 25866-25875
    • (2004) J. Biol. Chem. , vol.279 , pp. 25866-25875
    • Giannetti, A.M.1    Bjorkman, P.J.2
  • 14
    • 2442657217 scopus 로고    scopus 로고
    • Mechanism for multiple ligand recognition by the human transferrin receptor
    • Giannetti A.M., Snow P.M., Zak O., and Bjorkman P.J. Mechanism for multiple ligand recognition by the human transferrin receptor. PLoS Biol. 1 (2003) E51
    • (2003) PLoS Biol. , vol.1
    • Giannetti, A.M.1    Snow, P.M.2    Zak, O.3    Bjorkman, P.J.4
  • 15
    • 33749393565 scopus 로고    scopus 로고
    • Hereditary hemochromatosis protein, HFE, interaction with transferrin receptor 2 suggests a molecular mechanism for mammalian iron sensing
    • Goswami T., and Andrews N.C. Hereditary hemochromatosis protein, HFE, interaction with transferrin receptor 2 suggests a molecular mechanism for mammalian iron sensing. J. Biol. Chem. 281 (2006) 28494-28498
    • (2006) J. Biol. Chem. , vol.281 , pp. 28494-28498
    • Goswami, T.1    Andrews, N.C.2
  • 16
    • 10244265904 scopus 로고    scopus 로고
    • Regulation of transferrin receptor 2 by transferrin: diferric transferrin regulates transferrin receptor 2 protein stability
    • Johnson M.B., and Enns C.A. Regulation of transferrin receptor 2 by transferrin: diferric transferrin regulates transferrin receptor 2 protein stability. Blood 104 (2004) 4287-4293
    • (2004) Blood , vol.104 , pp. 4287-4293
    • Johnson, M.B.1    Enns, C.A.2
  • 17
    • 33947111426 scopus 로고    scopus 로고
    • Transferrin receptor 2: evidence for ligand-induced stabilization and redirection to a recycling pathway
    • Johnson M.B., Chen J., Murchison N., Green F.A., and Enns C.A. Transferrin receptor 2: evidence for ligand-induced stabilization and redirection to a recycling pathway. Mol. Biol. Cell 18 (2007) 743-754
    • (2007) Mol. Biol. Cell , vol.18 , pp. 743-754
    • Johnson, M.B.1    Chen, J.2    Murchison, N.3    Green, F.A.4    Enns, C.A.5
  • 18
    • 0033020518 scopus 로고    scopus 로고
    • The transferrin receptor binding site on HFE, the class I MHC-related protein mutated in hereditary hemochromatosis
    • Lebron J.A., and Bjorkman P.J. The transferrin receptor binding site on HFE, the class I MHC-related protein mutated in hereditary hemochromatosis. J. Mol. Biol. 289 (1999) 1109-1118
    • (1999) J. Mol. Biol. , vol.289 , pp. 1109-1118
    • Lebron, J.A.1    Bjorkman, P.J.2
  • 19
    • 0032478524 scopus 로고    scopus 로고
    • Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor
    • Lebron J.A., Bennett M.J., Vaughn D.E., Chirino A.J., Snow P.M., Mintier G.A., Feder J.N., and Bjorkman P.J. Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor. Cell 93 (1998) 111-123
    • (1998) Cell , vol.93 , pp. 111-123
    • Lebron, J.A.1    Bennett, M.J.2    Vaughn, D.E.3    Chirino, A.J.4    Snow, P.M.5    Mintier, G.A.6    Feder, J.N.7    Bjorkman, P.J.8
  • 20
    • 0033585129 scopus 로고    scopus 로고
    • The hemochromatosis protein HFE competes with transferrin for binding to the transferrin receptor
    • Lebron J.A., West Jr. A.P., and Bjorkman P.J. The hemochromatosis protein HFE competes with transferrin for binding to the transferrin receptor. J. Mol. Biol. 294 (1999) 239-245
    • (1999) J. Mol. Biol. , vol.294 , pp. 239-245
    • Lebron, J.A.1    West Jr., A.P.2    Bjorkman, P.J.3
  • 21
    • 0032959574 scopus 로고    scopus 로고
    • Transferrin receptor is necessary for development of erythrocytes and the nervous system
    • Levy J.E., Jin O., Fujiwara Y., Kuo F., and Andrews N.C. Transferrin receptor is necessary for development of erythrocytes and the nervous system. Nat. Genet. 21 (1999) 396-399
    • (1999) Nat. Genet. , vol.21 , pp. 396-399
    • Levy, J.E.1    Jin, O.2    Fujiwara, Y.3    Kuo, F.4    Andrews, N.C.5
  • 22
    • 0033168767 scopus 로고    scopus 로고
    • The C282Y mutation causing hereditary hemochromatosis does not produce a null allele
    • Levy J.E., Montross L.K., Cohen D.E., Fleming M.D., and Andrews N.C. 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
  • 23
    • 0034062537 scopus 로고    scopus 로고
    • Genes that modify the hemochromatosis phenotype in mice
    • Levy J.E., Montross L.K., and Andrews N.C. Genes that modify the hemochromatosis phenotype in mice. J. Clin. Invest. 105 (2000) 1209-1216
    • (2000) J. Clin. Invest. , vol.105 , pp. 1209-1216
    • Levy, J.E.1    Montross, L.K.2    Andrews, N.C.3
  • 24
    • 0023243675 scopus 로고
    • Functional expression of the human transferrin receptor cDNA in Chinese hamster ovary cells deficient in endogenous transferrin receptor
    • McGraw T.E., Greenfield L., and Maxfield F.R. Functional expression of the human transferrin receptor cDNA in Chinese hamster ovary cells deficient in endogenous transferrin receptor. J. Cell Biol. 105 (1987) 207-214
    • (1987) J. Cell Biol. , vol.105 , pp. 207-214
    • McGraw, T.E.1    Greenfield, L.2    Maxfield, F.R.3
  • 25
    • 0141816698 scopus 로고    scopus 로고
    • Hfe deficiency increases susceptibility to cardiotoxicity and exacerbates changes in iron metabolism induced by doxorubicin
    • Miranda C.J., Makui H., Soares R.J., Bilodeau M., Mui J., Vali H., Bertrand R., Andrews N.C., and Santos M.M. Hfe deficiency increases susceptibility to cardiotoxicity and exacerbates changes in iron metabolism induced by doxorubicin. Blood 102 (2003) 2574-2580
    • (2003) Blood , vol.102 , pp. 2574-2580
    • Miranda, C.J.1    Makui, H.2    Soares, R.J.3    Bilodeau, M.4    Mui, J.5    Vali, H.6    Bertrand, R.7    Andrews, N.C.8    Santos, M.M.9
  • 27
    • 2342510407 scopus 로고    scopus 로고
    • IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin
    • Nemeth E., Rivera S., Gabayan V., Keller C., Taudorf S., Pedersen B.K., and Ganz T. 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
  • 28
    • 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., Vaughn M.B., Donovan A., Ward D.M., Ganz T., and Kaplan J. Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science 306 (2004) 2090-2093
    • (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    Ganz, T.7    Kaplan, J.8
  • 32
    • 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., and Loreal O. 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
  • 33
    • 10244255021 scopus 로고    scopus 로고
    • Regulation of transferrin receptor 2 protein levels by transferrin
    • Robb A., and Wessling-Resnick M. Regulation of transferrin receptor 2 protein levels by transferrin. Blood 104 (2004) 4294-4299
    • (2004) Blood , vol.104 , pp. 4294-4299
    • Robb, A.1    Wessling-Resnick, M.2
  • 34
    • 0033605595 scopus 로고    scopus 로고
    • The hereditary hemochromatosis protein, HFE, specifically regulates transferrin-mediated iron uptake in HeLa cells
    • Roy C.N., Penny D.M., Feder J.N., and Enns C.A. The hereditary hemochromatosis protein, HFE, specifically regulates transferrin-mediated iron uptake in HeLa cells. J. Biol. Chem. 274 (1999) 9022-9028
    • (1999) J. Biol. Chem. , vol.274 , pp. 9022-9028
    • Roy, C.N.1    Penny, D.M.2    Feder, J.N.3    Enns, C.A.4
  • 35
    • 34247366783 scopus 로고    scopus 로고
    • Hepcidin antimicrobial peptide transgenic mice exhibit features of the anemia of inflammation
    • Roy C.N., Mak H.H., Akpan I., Losyev G., Zurakowski D., and Andrews N.C. Hepcidin antimicrobial peptide transgenic mice exhibit features of the anemia of inflammation. Blood 109 (2007) 4038-4044
    • (2007) Blood , vol.109 , pp. 4038-4044
    • Roy, C.N.1    Mak, H.H.2    Akpan, I.3    Losyev, G.4    Zurakowski, D.5    Andrews, N.C.6
  • 37
    • 0013973902 scopus 로고
    • Iron absorption in relation to transferrin saturation and other factors
    • Taylor M.R., and Gatenby P.B. Iron absorption in relation to transferrin saturation and other factors. Br. J. Haematol. 12 (1966) 747-753
    • (1966) Br. J. Haematol. , vol.12 , pp. 747-753
    • Taylor, M.R.1    Gatenby, P.B.2
  • 40
    • 0037370747 scopus 로고    scopus 로고
    • Heterotypic interactions between transferrin receptor and transferrin receptor 2
    • Vogt T.M., Blackwell A.D., Giannetti A.M., Bjorkman P.J., and Enns C.A. Heterotypic interactions between transferrin receptor and transferrin receptor 2. Blood 101 (2003) 2008-2014
    • (2003) Blood , vol.101 , pp. 2008-2014
    • Vogt, T.M.1    Blackwell, A.D.2    Giannetti, A.M.3    Bjorkman, P.J.4    Enns, C.A.5
  • 42
    • 0037111732 scopus 로고    scopus 로고
    • Inappropriate expression of hepcidin is associated with iron refractory anemia: implications for the anemia of chronic disease
    • Weinstein D.A., Roy C.N., Fleming M.D., Loda M.F., Wolfsdorf J.I., and Andrews N.C. 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
  • 44
    • 0025008962 scopus 로고
    • Distinct positive and negative elements control the limited hepatocyte and choroid plexus expression of transthyretin in transgenic mice
    • Yan C., Costa R.H., Darnell Jr. J.E., Chen J.D., and Van Dyke T.A. Distinct positive and negative elements control the limited hepatocyte and choroid plexus expression of transthyretin in transgenic mice. EMBO J. 9 (1990) 869-878
    • (1990) EMBO J. , vol.9 , pp. 869-878
    • Yan, C.1    Costa, R.H.2    Darnell Jr., J.E.3    Chen, J.D.4    Van Dyke, T.A.5
  • 45
    • 0842263988 scopus 로고    scopus 로고
    • Localization of iron metabolism-related mRNAs in rat liver indicate that HFE is expressed predominantly in hepatocytes
    • Zhang A.S., Xiong S., Tsukamoto H., and Enns C.A. Localization of iron metabolism-related mRNAs in rat liver indicate that HFE is expressed predominantly in hepatocytes. Blood 103 (2004) 1509-1514
    • (2004) Blood , vol.103 , pp. 1509-1514
    • Zhang, A.S.1    Xiong, S.2    Tsukamoto, H.3    Enns, C.A.4


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