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Volumn 31, Issue , 2011, Pages 117-137

Knockout mouse models of iron homeostasis

Author keywords

Anemia; Floxed genes; Hemochromatosis; Hepcidin; Iron transport

Indexed keywords

5 AMINOLEVULINATE SYNTHASE; ABC TRANSPORTER; BETA 2 MICROGLOBULIN; BONE MORPHOGENETIC PROTEIN 6; CERULOPLASMIN; CYTOCHROME B; FERRITIN; FERROCHELATASE; FERROPORTIN; FRATAXIN; HAPTOGLOBIN; HEME OXYGENASE 1; HEMOGLOBIN; HEMOJUVELIN; HEMOPEXIN; HEPCIDIN; HEPHAESTIN; IRON; IRON BINDING PROTEIN; IRON REGULATORY PROTEIN 1; IRON REGULATORY PROTEIN 2; SMAD4 PROTEIN; TRANSFERRIN; TRANSFERRIN RECEPTOR; TRANSFERRIN RECEPTOR 2;

EID: 79960504861     PISSN: 01999885     EISSN: 15454312     Source Type: Book Series    
DOI: 10.1146/annurev-nutr-072610-145117     Document Type: Article
Times cited : (35)

References (144)
  • 2
    • 0037103357 scopus 로고    scopus 로고
    • Regulation of iron absorption in Hfe mutant mice
    • DOI 10.1182/blood-2001-11-0037
    • Ajioka RS, Levy JE, Andrews NC, Kushner JP. 2002. Regulation of iron absorption in Hfe mutant mice. Blood 100:1465-69 (Pubitemid 34864306)
    • (2002) Blood , vol.100 , Issue.4 , pp. 1465-1469
    • Ajioka, R.S.1    Levy, J.E.2    Andrews, N.C.3    Kushner, J.P.4
  • 4
    • 0032920837 scopus 로고    scopus 로고
    • Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-linked sideroblastic anemia and ataxia (XLSA/A)
    • Allikmets R, RaskindWH,Hutchinson A, SchueckND, Dean M, KoellerDM. 1999. Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-linked sideroblastic anemia and ataxia (XLSA/A). Hum. Mol. Genet. 8:743-49 (Pubitemid 29189041)
    • (1999) Human Molecular Genetics , vol.8 , Issue.5 , pp. 743-749
    • Allikmets, R.1    Raskind, W.H.2    Hutchinson, A.3    Schueck, N.D.4    Dean, M.5    Koeller, D.M.6
  • 6
    • 0034572933 scopus 로고    scopus 로고
    • Iron homeostasis: Insights from genetics and animal models
    • AndrewsNC. 2000. Iron homeostasis: insights from genetics and animal models. Nat. Rev. Genet. 1:208-17
    • (2000) Nat. Rev. Genet. , vol.1 , pp. 208-217
    • Andrews, N.C.1
  • 7
    • 0042810742 scopus 로고    scopus 로고
    • Animal models of hereditary iron transport disorders
    • Andrews NC. 2002. Animal models of hereditary iron transport disorders. Adv. Exp.Med. Biol. 509:1-17
    • (2002) Adv. Exp.Med. Biol. , vol.509 , pp. 1-17
    • Andrews, N.C.1
  • 8
    • 63449103712 scopus 로고    scopus 로고
    • BMP6 is a key endogenous regulator of hepcidin expression and iron metabolism
    • Andriopoulos B Jr, Corradini E, Xia Y, Faasse SA, Chen S, et al. 2009. BMP6 is a key endogenous regulator of hepcidin expression and iron metabolism. Nat. Genet. 41:482-87
    • (2009) Nat. Genet. , vol.41 , pp. 482-487
    • Andriopoulos Jr., B.1    Corradini, E.2    Xia, Y.3    Faasse, S.A.4    Chen, S.5
  • 9
    • 33646370235 scopus 로고    scopus 로고
    • Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression
    • Babitt JL,Huang FW,Wrighting DM, Xia Y, Sidis Y, et al. 2006. Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression. Nat. Genet. 38:531-39
    • (2006) Nat. Genet. , vol.38 , pp. 531-539
    • Babitt, J.L.1    Huang, F.W.2    Wrighting, D.M.3    Xia, Y.4    Sidis, Y.5
  • 10
    • 0033539556 scopus 로고    scopus 로고
    • Experimental hemochromatosis due to MHC class i HFE deficiency: Immune status and iron metabolism
    • Bahram S, Gilfillan S, Kuhn LC, Moret R, Schulze JB, et al. 1999. Experimental hemochromatosis due to MHC class I HFE deficiency: immune status and iron metabolism. Proc. Natl. Acad. Sci. USA 96:13312-17
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13312-13317
    • Bahram, S.1    Gilfillan, S.2    Kuhn, L.C.3    Moret, R.4    Schulze, J.B.5
  • 12
    • 2142768213 scopus 로고    scopus 로고
    • Multigenic Control of Hepatic Iron Loading in a Murine Model of Hemochromatosis
    • DOI 10.1053/j.gastro.2004.01.021
    • Bensaid M, Fruchon S,Mazeres C, Bahram S, RothMP, Coppin H. 2004. Multigenic control of hepatic iron loading in a murine model of hemochromatosis. Gastroenterology 126:1400-8 (Pubitemid 38552803)
    • (2004) Gastroenterology , vol.126 , Issue.5 , pp. 1400-1408
    • Bensaid, M.1    Fruchon, S.2    Mazeres, C.3    Bahram, S.4    Roth, M.-P.5    Coppin, H.6
  • 13
    • 0023522698 scopus 로고
    • Hereditary hypotranferrinemia with hemosiderosis, a murine disorder resembling human atransferrinemia
    • Bernstein SE. 1987. Hereditary hypotransferrinemia with hemosiderosis, a murine disorder resembling human atransferrinemia. J. Lab. Clin. Med. 110:690-705 (Pubitemid 18033263)
    • (1987) Journal of Laboratory and Clinical Medicine , vol.110 , Issue.6 , pp. 690-705
    • Bernstein, S.E.1
  • 14
    • 0023219279 scopus 로고
    • Anemia of the Belgrade rat: Evidence for defective membrane transport of iron
    • Bowen BJ, Morgan EH. 1987. Anemia of the Belgrade rat: evidence for defective membrane transport of iron. Blood 70:38-44 (Pubitemid 17111238)
    • (1987) Blood , vol.70 , Issue.1 , pp. 38-44
    • Bowen, B.J.1    Morgan, E.H.2
  • 16
    • 51249119361 scopus 로고    scopus 로고
    • Recent advances in the understanding of inherited sideroblastic anaemia
    • Camaschella C. 2008. Recent advances in the understanding of inherited sideroblastic anaemia. Br. J. Haematol. 143:27-38
    • (2008) Br. J. Haematol. , vol.143 , pp. 27-38
    • Camaschella, C.1
  • 18
    • 54349098472 scopus 로고    scopus 로고
    • Newand old players in the hepcidin pathway
    • Camaschella C, SilvestriL. 2008.Newand old players in the hepcidin pathway. Haematologica 93:1441-44
    • (2008) Haematologica , vol.93 , pp. 1441-1444
    • Camaschella, C.1    Silvestri, L.2
  • 19
    • 0034548853 scopus 로고    scopus 로고
    • The Nramp2/DMT1 iron transporter is induced in the duodenum of microcytic anemia mk mice but is not properly targeted to the intestinal brush border
    • Canonne-Hergaux F, Fleming MD, Levy JE, Gauthier S, Ralph T, et al. 2000. The Nramp2/DMT1 iron transporter is induced in the duodenum of microcytic anemia mk mice but is not properly targeted to the intestinal brush border. Blood 96:3964-70
    • (2000) Blood , vol.96 , pp. 3964-3970
    • Canonne-Hergaux, F.1    Fleming, M.D.2    Levy, J.E.3    Gauthier, S.4    Ralph, T.5
  • 20
    • 64049112236 scopus 로고    scopus 로고
    • Iron is essential for neuron development and memory function in mouse hippocampus
    • Carlson ES, Tkac I, Magid R, O'Connor MB, Andrews NC, et al. 2009. Iron is essential for neuron development and memory function in mouse hippocampus. J. Nutr. 139:672-79
    • (2009) J. Nutr. , vol.139 , pp. 672-679
    • Carlson, E.S.1    Tkac, I.2    Magid, R.3    O'Connor, M.B.4    Andrews, N.C.5
  • 21
    • 70349479539 scopus 로고    scopus 로고
    • Abcb10 physically interacts with mitoferrin-1 (Slc25a37) to enhance its stability and function in the erythroid mitochondria
    • Chen W, Paradkar PN, Li L, Pierce EL, Langer NB, et al. 2009. Abcb10 physically interacts with mitoferrin-1 (Slc25a37) to enhance its stability and function in the erythroid mitochondria. Proc. Natl. Acad. Sci. USA 106:16263-68
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 16263-16268
    • Chen, W.1    Paradkar, P.N.2    Li, L.3    Pierce, E.L.4    Langer, N.B.5
  • 22
    • 23044503950 scopus 로고    scopus 로고
    • Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2
    • Cooperman SS, Meyron-Holtz EG, Olivierre-Wilson H, Ghosh MC, McConnell JP, Rouault TA. 2005. Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2. Blood 106:1084-91
    • Blood , vol.106 , pp. 1084-1091
    • Cooperman, S.S.1    Meyron-Holtz, E.G.2    Olivierre-Wilson, H.3    Ghosh, M.C.4    McConnell, J.P.5    Rouault, T.A.6
  • 23
    • 70349494083 scopus 로고    scopus 로고
    • Bone morphogenetic protein signaling is impaired in an HFE knockout mouse model of hemochromatosis
    • Corradini E, Garuti C, Montosi G, Ventura P, Andriopoulos B Jr, et al. 2009. Bone morphogenetic protein signaling is impaired in an HFE knockout mouse model of hemochromatosis. Gastroenterology 137:1489-97
    • (2009) Gastroenterology , vol.137 , pp. 1489-1497
    • Corradini, E.1    Garuti, C.2    Montosi, G.3    Ventura, P.4    Andriopoulos Jr., B.5
  • 25
    • 34250800318 scopus 로고    scopus 로고
    • Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin
    • DOI 10.1038/sj.emboj.7601735, PII 7601735
    • De Domenico I, Ward DM, di Patti MC, Jeong SY, David S, et al. 2007. Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin. EMBO J. 26:2823-31 (Pubitemid 46975784)
    • (2007) EMBO Journal , vol.26 , Issue.12 , pp. 2823-2831
    • De Domenico, I.1    Ward, D.M.2    Di Patti, M.C.B.3    Jeong, S.Y.4    David, S.5    Musci, G.6    Kaplan, J.7
  • 31
    • 0014866334 scopus 로고
    • Hereditary defect of intestinal iron transport inmice with sex-linked anemia
    • Edwards JA, Bannerman RM. 1970. Hereditary defect of intestinal iron transport inmice with sex-linked anemia. J. Clin. Invest. 49:1869-71
    • (1970) J. Clin. Invest. , vol.49 , pp. 1869-1871
    • Edwards, J.A.1    Bannerman, R.M.2
  • 32
    • 0016750343 scopus 로고
    • Red cell iron uptake in hereditary microcytic anemia
    • Edwards JA, Hoke JE. 1975. Red cell iron uptake in hereditary microcytic anemia. Blood 46:381-88
    • (1975) Blood , vol.46 , pp. 381-388
    • Edwards, J.A.1    Hoke, J.E.2
  • 33
    • 0018831028 scopus 로고
    • Defective delivery of iron to the developing red cell of the Belgrade laboratory rat
    • Edwards JA, Sullivan AL, Hoke JE. 1980. Defective delivery of iron to the developing red cell of the Belgrade laboratory rat. Blood 55:645-48 (Pubitemid 10138849)
    • (1980) Blood , vol.55 , Issue.4 , pp. 645-648
    • Edwards, J.A.1    Sullivan, A.L.2    Hoke, J.E.3
  • 34
    • 84974183672 scopus 로고
    • The genetics of sex-linked anaemia in the mouse
    • Falconer DS, Isaacson JH. 1962. The genetics of sex-linked anaemia in the mouse. Genet. Res. 3:248-50
    • (1962) Genet. Res. , vol.3 , pp. 248-250
    • Falconer, D.S.1    Isaacson, J.H.2
  • 36
    • 67651087324 scopus 로고    scopus 로고
    • The molecular basis of hepcidin-resistant hereditary hemochromatosis
    • Fernandes A, Preza GC, Phung Y, De Domenico I, Kaplan J, et al. 2009. The molecular basis of hepcidin-resistant hereditary hemochromatosis. Blood 114:437-43
    • (2009) Blood , vol.114 , pp. 437-443
    • Fernandes, A.1    Preza, G.C.2    Phung, Y.3    De Domenico, I.4    Kaplan, J.5
  • 38
    • 60249084746 scopus 로고    scopus 로고
    • Cell-autonomous and systemic context-dependent functions of iron regulatory protein 2 in mammalian iron metabolism
    • Ferring-Appel D, Hentze MW, Galy B. 2009. Cell-autonomous and systemic context-dependent functions of iron regulatory protein 2 in mammalian iron metabolism. Blood 113:679-87
    • (2009) Blood , vol.113 , pp. 679-687
    • Ferring-Appel, D.1    Hentze, M.W.2    Galy, B.3
  • 43
    • 54349096688 scopus 로고    scopus 로고
    • Membrane-bound serine protease matriptase-2 (Tmprss6) is an essential regulator of iron homeostasis
    • Folgueras AR, de Lara FM, Pendas AM, Garabaya C, Rodriguez F, et al. 2008. Membrane-bound serine protease matriptase-2 (Tmprss6) is an essential regulator of iron homeostasis. Blood 112:2539-45
    • (2008) Blood , vol.112 , pp. 2539-2545
    • Folgueras, A.R.1    De Lara, F.M.2    Pendas, A.M.3    Garabaya, C.4    Rodriguez, F.5
  • 44
    • 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, GroneHJ, Hentze MW. 2008. Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum. Cell Metab. 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
  • 45
    • 30944449709 scopus 로고    scopus 로고
    • Generation of conditional alleles of the murine iron regulatory protein (IRP)-1 and -2 genes
    • DOI 10.1002/gene.20169
    • Galy B, Ferring D, Hentze MW. 2005. Generation of conditional alleles of the murine iron regulatory protein (IRP)-1 and-2 genes. Genesis 43:181-88 (Pubitemid 43117834)
    • (2005) Genesis , vol.43 , Issue.4 , pp. 181-188
    • Galy, B.1    Feering, D.2    Hentze, M.W.3
  • 46
    • 27144467097 scopus 로고    scopus 로고
    • Altered body iron distribution and microcytosis in mice deficient in iron regulatory protein 2 (IRP2)
    • DOI 10.1182/blood-2005-04-1365
    • Galy B, Ferring D, Minana B, Bell O, Janser HG, et al. 2005. Altered body iron distribution and microcytosis in mice deficient in iron regulatory protein 2 (IRP2). Blood 106:2580-89 (Pubitemid 41510837)
    • (2005) Blood , vol.106 , Issue.7 , pp. 2580-2589
    • Galy, B.1    Ferring, D.2    Minana, B.3    Bell, O.4    Janser, H.G.5    Muckenthaler, M.6    Schumann, K.7    Hentze, M.W.8
  • 47
    • 33748297526 scopus 로고    scopus 로고
    • Iron homeostasis in the brain: Complete iron regulatory protein 2 deficiency without symptomatic neurodegeneration in the mouse [4]
    • DOI 10.1038/ng0906-967, PII NG0906967
    • Galy B, Holter SM, Klopstock T, Ferring D, Becker L, et al. 2006. Iron homeostasis in the brain: complete iron regulatory protein 2 deficiency without symptomatic neurodegeneration in the mouse. Nat. Genet. 38:967-69 (Pubitemid 44325914)
    • (2006) Nature Genetics , vol.38 , Issue.9 , pp. 967-969
    • Galy, B.1    Holter, S.M.2    Klopstock, T.3    Ferring, D.4    Becker, L.5    Kaden, S.6    Wurst, W.7    Grone, H.-J.8    Hentze, M.W.9
  • 48
    • 0041672570 scopus 로고    scopus 로고
    • Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation
    • DOI 10.1182/blood-2003-03-0672
    • Ganz T. 2003. Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation. Blood 102:783-88 (Pubitemid 36917762)
    • (2003) Blood , vol.102 , Issue.3 , pp. 783-788
    • Ganz, T.1
  • 49
    • 84974069733 scopus 로고
    • A sex-linked anaemia in the mouse
    • Grewal MD. 1962. A sex-linked anaemia in the mouse. Genet. Res. 3:238-47
    • (1962) Genet. Res. , vol.3 , pp. 238-247
    • Grewal, M.D.1
  • 50
    • 0033103978 scopus 로고    scopus 로고
    • The iron transport protein NRAMP2 is an integral membrane glycoprotein that colocalizes with transferrin in recycling endosomes
    • DOI 10.1084/jem.189.5.831
    • Gruenheid S, Canonne-Hergaux F, Gauthier S, Hackam DJ, Grinstein S, Gros P. 1999. The iron transport protein NRAMP2 is an integral membrane glycoprotein that colocalizes with transferrin in recycling endosomes. J. Exp. Med. 189:831-41 (Pubitemid 29189688)
    • (1999) Journal of Experimental Medicine , vol.189 , Issue.5 , pp. 831-841
    • Gruenheid, S.1    Canonne-Hergaux, F.2    Gauthier, S.3    Hackam, D.J.4    Grinstein, S.5    Gros, P.6
  • 51
    • 18244399587 scopus 로고    scopus 로고
    • Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver
    • DOI 10.1172/JCI200524356
    • Gunshin H, Fujiwara Y, Custodio AO, Direnzo C, Robine S, Andrews NC. 2005. Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver. J. Clin. Invest. 115:1258-66 (Pubitemid 40629044)
    • (2005) Journal of Clinical Investigation , vol.115 , Issue.5 , pp. 1258-1266
    • Gunshin, H.1    Fujiwara, Y.2    Custodio, A.O.3    DiRenzo, C.4    Robine, S.5    Andrews, N.C.6
  • 58
    • 37049019507 scopus 로고    scopus 로고
    • Brief report: Erythropoiesis and iron metabolism in dominant erythropoietic protoporphyria
    • DOI 10.1182/blood-2007-04-088120
    • Holme SA, Worwood M, Anstey AV, Elder GH, Badminton MN. 2007. Erythropoiesis and iron metabolism in dominant erythropoietic protoporphyria. Blood 110:4108-10 (Pubitemid 350248469)
    • (2007) Blood , vol.110 , Issue.12 , pp. 4108-4110
    • Holme, S.A.1    Worwood, M.2    Anstey, A.V.3    Elder, G.H.4    Badminton, M.N.5
  • 60
    • 63149128149 scopus 로고    scopus 로고
    • Molecular basis of inheritedmicrocytic anemia due to defects in iron acquisition or heme synthesis
    • Iolascon A,De Falco L, Beaumont C. 2009. Molecular basis of inheritedmicrocytic anemia due to defects in iron acquisition or heme synthesis. Haematologica 94:395-408
    • (2009) Haematologica , vol.94 , pp. 395-408
    • Iolascon, A.1    De Falco, L.2    Beaumont, C.3
  • 61
    • 33748889489 scopus 로고    scopus 로고
    • Age-related changes in iron homeostasis and cell death in the cerebellum of ceruloplasmin-deficient mice
    • DOI 10.1523/JNEUROSCI.2922-06.2006
    • Jeong SY, David S. 2006. Age-related changes in iron homeostasis and cell death in the cerebellum of ceruloplasmin-deficient mice. J. Neurosci. 26:9810-19 (Pubitemid 44427720)
    • (2006) Journal of Neuroscience , vol.26 , Issue.38 , pp. 9810-9819
    • Suh, Y.J.1    David, S.2
  • 62
    • 70350494274 scopus 로고    scopus 로고
    • BMP/Smad signaling is not enhanced in Hfe-deficient mice despite increased Bmp6 expression
    • Kautz L, Meynard D, Besson-Fournier C, Darnaud V, Al Saati T, et al. 2009. BMP/Smad signaling is not enhanced in Hfe-deficient mice despite increased Bmp6 expression. Blood 114:2515-20
    • (2009) Blood , vol.114 , pp. 2515-2520
    • Kautz, L.1    Meynard, D.2    Besson-Fournier, C.3    Darnaud, V.4    Al Saati, T.5
  • 64
    • 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, Vuong PT, Kawano S, et al. 1999. Molecular cloning of transferrin receptor 2. A new member of the transferrin receptor-like family. J. Biol. Chem. 274:20826-32
    • (1999) J. Biol. Chem. , vol.274 , pp. 20826-20832
    • Kawabata, H.1    Yang, R.2    Hirama, T.3    Vuong, P.T.4    Kawano, S.5
  • 67
    • 0033644144 scopus 로고    scopus 로고
    • Conditional gene knockout using Cre recombinase
    • Le Y, Sauer B. 2000. Conditional gene knockout using Cre recombinase. Methods Mol. Biol. 136:477-85
    • (2000) Methods Mol. Biol. , vol.136 , pp. 477-485
    • Le, Y.1    Sauer, B.2
  • 69
    • 0032959574 scopus 로고    scopus 로고
    • Transferrin receptor is necessary for development of erythrocytes and the nervous system
    • DOI 10.1038/7727
    • Levy JE, Jin O, Fujiwara Y, Kuo F, Andrews NC. 1999. Transferrin receptor is necessary for development of erythrocytes and the nervous system. Nat. Genet. 21:396-99 (Pubitemid 29159576)
    • (1999) Nature Genetics , vol.21 , Issue.4 , pp. 396-399
    • Levy, J.E.1    Jin, O.2    Fujiwara, Y.3    Kuo, F.4    Andrews, N.C.5
  • 71
    • 0033168767 scopus 로고    scopus 로고
    • The C282Y mutation causing hereditary hemochromatosis does not produce a null allele
    • Levy JE, Montross LK, Cohen DE, Fleming MD, Andrews NC. 1999. The C282Y mutation causing hereditary hemochromatosis does not produce a null allele. Blood 94:9-11 (Pubitemid 29300128)
    • (1999) Blood , vol.94 , Issue.1 , pp. 9-11
    • Levy, J.E.1    Montross, L.K.2    Cohen, D.E.3    Fleming, M.D.4    Andrews, N.C.5
  • 74
    • 0037103294 scopus 로고    scopus 로고
    • An exon 10 deletion in the mouse ferrochelatase gene has a dominant-negative effect and causes mild protoporphyria
    • DOI 10.1182/blood-2001-12-0283
    • Magness ST, Maeda N, Brenner DA. 2002. An exon 10 deletion in the mouse ferrochelatase gene has a dominant-negative effect and causes mild protoporphyria. Blood 100:1470-77 (Pubitemid 34864307)
    • (2002) Blood , vol.100 , Issue.4 , pp. 1470-1477
    • Magness, S.T.1    Maeda, N.2    Brenner, D.A.3
  • 75
    • 0014984114 scopus 로고
    • Intestinal iron-transport defect in the mouse with sex-linked anemia
    • Manis J. 1971. Intestinal iron-transport defect in the mouse with sex-linked anemia. Am. J. Physiol. 220:135-39
    • (1971) Am. J. Physiol. , vol.220 , pp. 135-139
    • Manis, J.1
  • 76
    • 34848925133 scopus 로고    scopus 로고
    • Lack of haptoglobin affects iron transport across duodenum bymodulating ferroportin expression
    • Marro S, Barisani D, Chiabrando D, Fagoonee S, Muckenthaler MU, et al. 2007. Lack of haptoglobin affects iron transport across duodenum bymodulating ferroportin expression. Gastroenterology 133:1261-71
    • (2007) Gastroenterology , vol.133 , pp. 1261-1271
    • Marro, S.1    Barisani, D.2    Chiabrando, D.3    Fagoonee, S.4    Muckenthaler, M.U.5
  • 77
    • 59149096376 scopus 로고    scopus 로고
    • The role of Dcytb in iron metabolism: An update
    • McKie AT. 2008. The role of Dcytb in iron metabolism: an update. Biochem. Soc. Trans. 36:1239-41
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1239-1241
    • McKie, A.T.1
  • 81
    • 77449150120 scopus 로고    scopus 로고
    • Hemopexin affects iron distribution and ferritin expression in mouse brain
    • Morello N, Tonoli E, Logrand F, Fiorito V, Fagoonee S, et al. 2009. Hemopexin affects iron distribution and ferritin expression in mouse brain. J. Cell Mol. Med. 13:4192-204
    • (2009) J. Cell Mol. Med. , vol.13 , pp. 4192-204
    • Morello, N.1    Tonoli, E.2    Logrand, F.3    Fiorito, V.4    Fagoonee, S.5
  • 82
    • 50949102412 scopus 로고    scopus 로고
    • Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network
    • Muckenthaler MU, Galy B, Hentze MW. 2008. Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network. Annu. Rev. Nutr. 28:197-213
    • (2008) Annu. Rev. Nutr. , vol.28 , pp. 197-213
    • Muckenthaler, M.U.1    Galy, B.2    Hentze, M.W.3
  • 84
    • 0034059140 scopus 로고    scopus 로고
    • Cre recombinase: The universal reagent for genome tailoring
    • DOI 10.1002/(SICI)1526-968X(200002)26:2<99::AID-GENE1>3.0.CO;2-B
    • Nagy A. 2000. Cre recombinase: the universal reagent for genome tailoring. Genesis 26:99-109 (Pubitemid 30158089)
    • (2000) Genesis , vol.26 , Issue.2 , pp. 99-109
    • Nagy, A.1
  • 85
    • 33646754660 scopus 로고    scopus 로고
    • Transgenic rescue of erythroid 5-aminolevulinate synthase-deficient mice results in the formation of ring sideroblasts and siderocytes
    • DOI 10.1111/j.1365-2443.2006.00973.x
    • Nakajima O, Okano S, Harada H, Kusaka T, Gao X, et al. 2006. Transgenic rescue of erythroid 5-aminolevulinate synthase-deficient mice results in the formation of ring sideroblasts and siderocytes. Genes Cells 11:685-700 (Pubitemid 43744818)
    • (2006) Genes to Cells , vol.11 , Issue.6 , pp. 685-700
    • Nakajima, O.1    Okano, S.2    Harada, H.3    Kusaka, T.4    Gao, X.5    Hosoya, T.6    Suzuki, N.7    Takahashi, S.8    Yamamoto, M.9
  • 86
    • 0006908742 scopus 로고
    • The inheritance of "mick,"a new anemia in the house mouse
    • Nash DJ, Kent E, Dickie MM, Russell ES. 1964. The inheritance of "mick,"a new anemia in the house mouse. Am. Zool. 4:404-5
    • (1964) Am. Zool. , vol.4 , pp. 404-405
    • Nash, D.J.1    Kent, E.2    Dickie, M.M.3    Russell, E.S.4
  • 87
    • 70450214396 scopus 로고    scopus 로고
    • The role of hepcidin in iron metabolism
    • Nemeth E, Ganz T. 2009. The role of hepcidin in iron metabolism. Acta Haematol. 122:78-86
    • (2009) Acta Haematol. , vol.122 , pp. 78-86
    • Nemeth, E.1    Ganz, T.2
  • 88
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization
    • DOI 10.1126/science.1104742
    • Nemeth E, Tuttle MS, Powelson J, Vaughn MB, Donovan A, et al. 2004. Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science 306:2090-93 (Pubitemid 40007660)
    • (2004) Science , vol.306 , Issue.5704 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3    Vaughn, M.D.4    Donovan, A.5    Ward, D.M.6    Ganz, T.7    Kaplan, J.8
  • 91
    • 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, et al. 2002. The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation. J. Clin. Invest. 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
  • 92
    • 23644444316 scopus 로고    scopus 로고
    • Hemojuvelin is essential for dietary iron sensing, and its mutation leads to severe iron overload
    • DOI 10.1172/JCI25683
    • Niederkofler V, Salie R, Arber S. 2005. Hemojuvelin is essential for dietary iron sensing, and its mutation leads to severe iron overload. J. Clin. Invest. 115:2180-86 (Pubitemid 41134159)
    • (2005) Journal of Clinical Investigation , vol.115 , Issue.8 , pp. 2180-2186
    • Niederkofler, V.1    Salie, R.2    Arber, S.3
  • 93
    • 27644570377 scopus 로고    scopus 로고
    • Nm1054: A spontaneous, recessive, hypochromic, microcytic anemia mutation in the mouse
    • DOI 10.1182/blood-2005-01-0379
    • Ohgami RS, Campagna DR, Antiochos B, Wood EB, Sharp JJ, et al. 2005. nm1054: a spontaneous, recessive, hypochromic, microcytic anemia mutation in the mouse. Blood 106:3625-31 (Pubitemid 41609203)
    • (2005) Blood , vol.106 , Issue.10 , pp. 3625-3631
    • Ohgami, R.S.1    Campagna, D.R.2    Antiochos, B.3    Wood, E.B.4    Sharp, J.J.5    Barker, J.E.6    Fleming, M.D.7
  • 97
    • 59449083869 scopus 로고    scopus 로고
    • Regulation of mitochondrial iron import through differential turnover of mitoferrin 1 and mitoferrin 2
    • Paradkar PN, Zumbrennen KB, Paw BH, Ward DM, Kaplan J. 2009. Regulation of mitochondrial iron import through differential turnover of mitoferrin 1 and mitoferrin 2. Mol. Cell Biol. 29:1007-16
    • (2009) Mol. Cell Biol. , vol.29 , pp. 1007-1016
    • Paradkar, P.N.1    Zumbrennen, K.B.2    Paw, B.H.3    Ward, D.M.4    Kaplan, J.5
  • 100
    • 28444436913 scopus 로고    scopus 로고
    • Non-HFE hemochromatosis
    • DOI 10.1055/s-2005-923316
    • Pietrangelo A. 2005. Non-HFE hemochromatosis. Semin. Liver Dis. 25:450-60 (Pubitemid 41741261)
    • (2005) Seminars in Liver Disease , vol.25 , Issue.4 , pp. 450-460
    • Pietrangelo, A.1
  • 101
    • 36349028180 scopus 로고    scopus 로고
    • Hemochromatosis: An endocrine liver disease
    • DOI 10.1002/hep.21886
    • Pietrangelo A. 2007. Hemochromatosis: an endocrine liver disease. Hepatology 46:1291-301 (Pubitemid 350144793)
    • (2007) Hepatology , vol.46 , Issue.4 , pp. 1291-1301
    • Pietrangelo, A.1
  • 102
    • 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, et al. 2001. A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin, is overexpressed during iron overload. J. Biol. Chem. 276:7811-19
    • (2001) J. Biol. Chem. , vol.276 , pp. 7811-7819
    • Pigeon, C.1    Ilyin, G.2    Courselaud, B.3    Leroyer, P.4    Turlin, B.5
  • 104
    • 34147158934 scopus 로고    scopus 로고
    • Abcb7, the gene responsible for X-linked sideroblastic anemia with ataxia, is essential for hematopoiesis
    • DOI 10.1182/blood-2006-04-015768
    • Pondarre C, Campagna DR, Antiochos B, Sikorski L, Mulhern H, Fleming MD. 2007. Abcb7, the gene responsible for X-linked sideroblastic anemia with ataxia, is essential for hematopoiesis. Blood 109:3567-69 (Pubitemid 46572551)
    • (2007) Blood , vol.109 , Issue.8 , pp. 3567-3569
    • Pondarre, C.1    Campagna, D.R.2    Antiochos, B.3    Sikorski, L.4    Mulhern, H.5    Fleming, M.D.6
  • 106
    • 62549107492 scopus 로고    scopus 로고
    • Multicellular models of Friedreich ataxia
    • Puccio H. 2009. Multicellular models of Friedreich ataxia. J. Neurol. 256(Suppl. 1):18-24
    • (2009) J. Neurol. , vol.256 , Issue.SUPPL. 1 , pp. 18-24
    • Puccio, H.1
  • 110
    • 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 BE, Voland JR. 1996. 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 93:1529-34
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1529-1534
    • Rothenberg, B.E.1    Voland, J.R.2
  • 111
    • 33746361251 scopus 로고    scopus 로고
    • The role of iron regulatory proteins in mammalian iron homeostasis and disease
    • DOI 10.1038/nchembio807, PII NCHEMBIO807
    • Rouault TA. 2006. The role of iron regulatory proteins in mammalian iron homeostasis and disease. Nat. Chem. Biol. 2:406-14 (Pubitemid 44114917)
    • (2006) Nature Chemical Biology , vol.2 , Issue.8 , pp. 406-414
    • Rouault, T.A.1
  • 112
    • 34247366783 scopus 로고    scopus 로고
    • Hepcidin antimicrobial peptide transgenic mice exhibit features of the anemia of inflammation
    • DOI 10.1182/blood-2006-10-051755
    • Roy CN, Mak HH, Akpan I, Losyev G, Zurakowski D, Andrews NC. 2007. Hepcidin antimicrobial peptide transgenic mice exhibit features of the anemia of inflammation. Blood 109:4038-44 (Pubitemid 46641759)
    • (2007) Blood , vol.109 , Issue.9 , pp. 4038-4044
    • Roy, C.N.1    Mak, H.H.2    Akpan, I.3    Losyev, G.4    Zurakowski, D.5    Andrews, N.C.6
  • 113
    • 0037369165 scopus 로고    scopus 로고
    • 2002 E. Mead Johnson Award for research in pediatrics lecture: The molecular biology of the anemia of chronic disease: A hypothesis
    • DOI 10.1203/01.PDR.0000049513.67410.2D
    • Roy CN, Weinstein DA, Andrews NC. 2003. 2002 E. Mead Johnson Award for Research in Pediatrics Lecture: the molecular biology of the anemia of chronic disease: a hypothesis. Pediatr. Res. 53:507-12 (Pubitemid 36237409)
    • (2003) Pediatric Research , vol.53 , Issue.3 , pp. 507-512
    • Roy, C.N.1    Weinstein, D.A.2    Andrews, N.C.3
  • 114
    • 0014647432 scopus 로고
    • An additional house mouse mutant with anemia (hemoglobin deficiency)
    • Scheufler H. 1969. An additional house mouse mutant with anemia (hemoglobin deficiency). Z. Versuchstierkd. 11:348-53
    • (1969) Z. Versuchstierkd. , vol.11 , pp. 348-353
    • Scheufler, H.1
  • 117
    • 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. 2008. The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin. Cell Metab. 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
  • 119
    • 33645307993 scopus 로고    scopus 로고
    • Complete loss of iron regulatory proteins 1 and 2 prevents viability ofmurine zygotes beyond the blastocyst stage of embryonic development
    • Smith SR, Ghosh MC, Ollivierre-Wilson H, Hang Tong W, Rouault TA. 2006. Complete loss of iron regulatory proteins 1 and 2 prevents viability ofmurine zygotes beyond the blastocyst stage of embryonic development. Blood Cells Mol. Dis. 36:283-87
    • (2006) Blood Cells Mol. Dis. , vol.36 , pp. 283-287
    • Smith, S.R.1    Ghosh, M.C.2    Ollivierre-Wilson, H.3    Hang Tong, W.4    Rouault, T.A.5
  • 120
    • 0032530922 scopus 로고    scopus 로고
    • The G185R mutation disrupts function of the iron transporter Nramp2
    • Su MA, Trenor CC, Fleming JC, Fleming MD, Andrews NC. 1998. The G185R mutation disrupts function of the iron transporter Nramp2. Blood 92:2157-63 (Pubitemid 28446707)
    • (1998) Blood , vol.92 , Issue.6 , pp. 2157-2163
    • Su, M.A.1    Trenor III, C.C.2    Fleming, J.C.3    Fleming, M.D.4    Andrews, N.C.5
  • 121
    • 59149084006 scopus 로고    scopus 로고
    • Ceruloplasmin in neurodegenerative diseases
    • Texel SJ, Xu X, Harris ZL. 2008. Ceruloplasmin in neurodegenerative diseases. Biochem. Soc. Trans. 36:1277-81
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1277-1281
    • Texel, S.J.1    Xu, X.2    Harris, Z.L.3
  • 124
    • 0036259938 scopus 로고    scopus 로고
    • Hemopexin: Structure, function, and regulation
    • DOI 10.1089/104454902753759717
    • Tolosano E, Altruda F. 2002. Hemopexin: structure, function, and regulation.DNACell Biol. 21:297-306 (Pubitemid 34594543)
    • (2002) DNA and Cell Biology , vol.21 , Issue.4 , pp. 297-306
    • Tolosano, E.1    Altruda, F.2
  • 125
    • 17044421761 scopus 로고    scopus 로고
    • Haptoglobin modifies the hemochromatosis phenotype in mice
    • Tolosano E, Fagoonee S, Garuti C, Valli L, Andrews NC, et al. 2005. Haptoglobin modifies the hemochromatosis phenotype in mice. Blood 105:3353-55
    • (2005) Blood , vol.105 , pp. 3353-3355
    • Tolosano, E.1    Fagoonee, S.2    Garuti, C.3    Valli, L.4    Andrews, N.C.5
  • 126
    • 0033485566 scopus 로고    scopus 로고
    • Defective recovery and severe renal damage after acute hemolysis in hemopexin-deficient mice
    • Tolosano E, Hirsch E, Patrucco E, Camaschella C, Navone R, et al. 1999. Defective recovery and severe renal damage after acute hemolysis in hemopexin-deficient mice. Blood 94:3906-14
    • (1999) Blood , vol.94 , pp. 3906-3914
    • Tolosano, E.1    Hirsch, E.2    Patrucco, E.3    Camaschella, C.4    Navone, R.5
  • 129
    • 77956327702 scopus 로고    scopus 로고
    • Intestinal ferritin H is required for an accurate control of iron absorption
    • Vanoaica L, Darshan D, Richman L, Schumann K, Kuhn LC. 2010. Intestinal ferritin H is required for an accurate control of iron absorption. Cell Metab. 12:273-82
    • (2010) Cell Metab. , vol.12 , pp. 273-282
    • Vanoaica, L.1    Darshan, D.2    Richman, L.3    Schumann, K.4    Kuhn, L.C.5
  • 130
    • 46749135674 scopus 로고    scopus 로고
    • Hemopexin prevents endothelial damage and liver congestion in a mouse model of heme overload
    • DOI 10.2353/ajpath.2008.071130
    • Vinchi F, Gastaldi S, Silengo L, Altruda F, Tolosano E. 2008. Hemopexin prevents endothelial damage and liver congestion in a mouse model of heme overload. Am. J. Pathol. 173:289-99 (Pubitemid 351947975)
    • (2008) American Journal of Pathology , vol.173 , Issue.1 , pp. 289-299
    • Vinchi, F.1    Gastaldi, S.2    Silengo, L.3    Altruda, F.4    Tolosano, E.5
  • 134
    • 0030732164 scopus 로고    scopus 로고
    • Hereditary hemochromatosis: Effects of C282Y andH63D mutations on association with beta2-microglobulin, intracellular processing, and cell surface expression of the HFE protein in COS-7 cells
    • Waheed A, Parkkila S, Zhou XY, Tomatsu S, Tsuchihashi Z, et al. 1997. Hereditary hemochromatosis: effects of C282Y andH63D mutations on association with beta2-microglobulin, intracellular processing, and cell surface expression of the HFE protein in COS-7 cells. Proc. Natl. Acad. Sci. USA 94:12384-89
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12384-12389
    • Waheed, A.1    Parkkila, S.2    Zhou, X.Y.3    Tomatsu, S.4    Tsuchihashi, Z.5
  • 135
    • 73149083742 scopus 로고    scopus 로고
    • Combined deletion of Hfe and transferrin receptor 2 in mice leads to marked dysregulation of hepcidin and iron overload
    • Wallace DF, Summerville L, Crampton EM, Frazer DM, Anderson GJ, Subramaniam VN. 2009. Combined deletion of Hfe and transferrin receptor 2 in mice leads to marked dysregulation of hepcidin and iron overload. Hepatology 50:1992-2000
    • (2009) Hepatology , vol.50 , pp. 1992-2000
    • Wallace, D.F.1    Summerville, L.2    Crampton, E.M.3    Frazer, D.M.4    Anderson, G.J.5    Subramaniam, V.N.6
  • 136
    • 21044434748 scopus 로고    scopus 로고
    • First phenotypic description of transferrin receptor 2 knockout mouse, and the role of hepcidin
    • DOI 10.1136/gut.2004.062018
    • Wallace DF, Summerville L, Lusby PE, Subramaniam VN. 2005. First phenotypic description of transferrin receptor 2 knockout mouse, and the role of hepcidin. Gut 54:980-86 (Pubitemid 40873913)
    • (2005) Gut , vol.54 , Issue.7 , pp. 980-986
    • Wallace, D.F.1    Summerville, L.2    Lusby, P.E.3    Subramaniam, V.N.4
  • 137
    • 33846225653 scopus 로고    scopus 로고
    • Targeted disruption of the hepatic transferrin receptor 2 gene in mice leads to iron overload
    • DOI 10.1053/j.gastro.2006.11.028, PII S0016508506024838
    • Wallace DF, Summerville L, Subramaniam VN. 2007. Targeted disruption of the hepatic transferrin receptor 2 gene in mice leads to iron overload. Gastroenterology 132:301-10 (Pubitemid 46108757)
    • (2007) Gastroenterology , vol.132 , Issue.1 , pp. 301-310
    • Wallace, D.F.1    Summerville, L.2    Subramaniam, V.N.3
  • 138
    • 33644876815 scopus 로고    scopus 로고
    • A role of SMAD4 in iron metabolism through the positive regulation of hepcidin expression
    • Wang RH, Li C, Xu X, Zheng Y, Xiao C, et al. 2005. A role of SMAD4 in iron metabolism through the positive regulation of hepcidin expression. Cell Metab. 2:399-409
    • (2005) Cell Metab. , vol.2 , pp. 399-409
    • Wang, R.H.1    Li, C.2    Xu, X.3    Zheng, Y.4    Xiao, C.5
  • 139
    • 28644444443 scopus 로고    scopus 로고
    • Iron metabolism mutant hbd mice have a deletion in Sec15l1, which has homology to a yeast gene for vesicle docking
    • DOI 10.1016/j.ygeno.2005.09.015, PII S088875430500279X
    • White RA, Boydston LA, Brookshier TR, McNulty SG, Nsumu NN, et al. 2005. Iron metabolism mutant hbd mice have a deletion in Sec15l1, which has homology to a yeast gene for vesicle docking. Genomics 86:668-73 (Pubitemid 41752947)
    • (2005) Genomics , vol.86 , Issue.6 , pp. 668-673
    • White, R.A.1    Boydston, L.A.2    Brookshier, T.R.3    McNulty, S.G.4    Nsumu, N.N.5    Brewer, B.P.6    Blackmore, K.7
  • 141
    • 0034243386 scopus 로고    scopus 로고
    • Animal models for X-linked sideroblastic anemia
    • Yamamoto M, Nakajima O. 2000. Animal models for X-linked sideroblastic anemia. Int. J. Hematol. 72:157-64
    • (2000) Int. J. Hematol. , vol.72 , pp. 157-164
    • Yamamoto, M.1    Nakajima, O.2
  • 142
    • 33646104690 scopus 로고    scopus 로고
    • The anemia of "haemoglobin-deficit" (hbd/hbd ) mice is caused by a defect in transferrin cycling
    • Zhang AS, Sheftel AD, Ponka P. 2006. The anemia of "haemoglobin- deficit" (hbd/hbd ) mice is caused by a defect in transferrin cycling. Exp. Hematol. 34:593-98
    • (2006) Exp. Hematol. , vol.34 , pp. 593-598
    • Zhang, A.S.1    Sheftel, A.D.2    Ponka, P.3


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