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Volumn 7, Issue 1, 2008, Pages 79-85

Iron Regulatory Proteins Are Essential for Intestinal Function and Control Key Iron Absorption Molecules in the Duodenum

Author keywords

DNA; HUMDISEASE; SIGNALING

Indexed keywords

CRE RECOMBINASE; IRON; IRON REGULATORY PROTEIN 1; IRON REGULATORY PROTEIN 2; MESSENGER RNA; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 2;

EID: 37449009448     PISSN: 15504131     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cmet.2007.10.006     Document Type: Article
Times cited : (165)

References (32)
  • 1
    • 0034733635 scopus 로고    scopus 로고
    • A novel mammalian iron-regulated protein involved in intracellular iron metabolism
    • Abboud S., and Haile D.J. A novel mammalian iron-regulated protein involved in intracellular iron metabolism. J. Biol. Chem. 275 (2000) 19906-19912
    • (2000) J. Biol. Chem. , vol.275 , pp. 19906-19912
    • Abboud, S.1    Haile, D.J.2
  • 4
    • 23044503950 scopus 로고    scopus 로고
    • Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2
    • Cooperman S.S., Meyron-Holtz E.G., Olivierre-Wilson H., Ghosh M.C., McConnell J.P., and Rouault T.A. Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2. Blood 106 (2005) 1084-1091
    • (2005) 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
  • 6
    • 14644407428 scopus 로고    scopus 로고
    • Advances in understanding the molecular basis for the regulation of dietary iron absorption
    • Fleming R.E. Advances in understanding the molecular basis for the regulation of dietary iron absorption. Curr. Opin. Gastroenterol. 21 (2005) 201-206
    • (2005) Curr. Opin. Gastroenterol. , vol.21 , pp. 201-206
    • Fleming, R.E.1
  • 8
    • 3042577347 scopus 로고    scopus 로고
    • Targeted mutagenesis of the murine IRP1 and IRP2 genes reveals context-dependent RNA processing differences in vivo
    • Galy B., Ferring D., Benesova M., Benes V., and Hentze M.W. Targeted mutagenesis of the murine IRP1 and IRP2 genes reveals context-dependent RNA processing differences in vivo. RNA 10 (2004) 1019-1025
    • (2004) RNA , vol.10 , pp. 1019-1025
    • Galy, B.1    Ferring, D.2    Benesova, M.3    Benes, V.4    Hentze, M.W.5
  • 9
    • 27144467097 scopus 로고    scopus 로고
    • Altered body iron distribution and microcytosis in mice deficient in iron regulatory protein 2 (IRP2)
    • Galy B., Ferring D., Minana B., Bell O., Janser H.G., Muckenthaler M., Schümann K., and Hentze M.W. Altered body iron distribution and microcytosis in mice deficient in iron regulatory protein 2 (IRP2). Blood 106 (2005) 2580-2589
    • (2005) Blood , vol.106 , pp. 2580-2589
    • Galy, B.1    Ferring, D.2    Minana, B.3    Bell, O.4    Janser, H.G.5    Muckenthaler, M.6    Schümann, K.7    Hentze, M.W.8
  • 10
    • 30944449709 scopus 로고    scopus 로고
    • Generation of conditional alleles of the murine Iron Regulatory Protein (IRP)-1 and -2 genes
    • Galy B., Ferring D., and Hentze M.W. Generation of conditional alleles of the murine Iron Regulatory Protein (IRP)-1 and -2 genes. Genesis 43 (2005) 181-188
    • (2005) Genesis , vol.43 , pp. 181-188
    • Galy, B.1    Ferring, D.2    Hentze, M.W.3
  • 11
    • 0028006911 scopus 로고
    • Differentiation and self-renewal in the mouse gastrointestinal epithelium
    • Gordon J.I., and Hermiston M.L. Differentiation and self-renewal in the mouse gastrointestinal epithelium. Curr. Opin. Cell Biol. 6 (1994) 795-803
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 795-803
    • Gordon, J.I.1    Hermiston, M.L.2
  • 13
    • 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 (2004) 285-297
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 14
    • 0037126002 scopus 로고    scopus 로고
    • Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: implications for regulation and cellular function
    • Hubert N., and Hentze M.W. Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: implications for regulation and cellular function. Proc. Natl. Acad. Sci. USA 99 (2002) 12345-12350
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12345-12350
    • Hubert, N.1    Hentze, M.W.2
  • 15
    • 0035138456 scopus 로고    scopus 로고
    • Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice
    • LaVaute T., Smith S., Cooperman S., Iwai K., Land W., Meyron-Holtz E., Drake S.K., Miller G., Abu-Asab M., Tsokos M., et al. Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice. Nat. Genet. 27 (2001) 209-214
    • (2001) Nat. Genet. , vol.27 , pp. 209-214
    • LaVaute, T.1    Smith, S.2    Cooperman, S.3    Iwai, K.4    Land, W.5    Meyron-Holtz, E.6    Drake, S.K.7    Miller, G.8    Abu-Asab, M.9    Tsokos, M.10
  • 17
    • 0037031856 scopus 로고    scopus 로고
    • Cis elements of the villin gene control expression in restricted domains of the vertical (crypt) and horizontal (duodenum, cecum) axes of the intestine
    • Madison B.B., Dunbar L., Qiao X.T., Braunstein K., Braunstein E., and Gumucio D.L. Cis elements of the villin gene control expression in restricted domains of the vertical (crypt) and horizontal (duodenum, cecum) axes of the intestine. J. Biol. Chem. 277 (2002) 33275-33283
    • (2002) J. Biol. Chem. , vol.277 , pp. 33275-33283
    • Madison, B.B.1    Dunbar, L.2    Qiao, X.T.3    Braunstein, K.4    Braunstein, E.5    Gumucio, D.L.6
  • 20
    • 10844282789 scopus 로고    scopus 로고
    • Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo
    • Meyron-Holtz E.G., Ghosh M.C., and Rouault T.A. Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo. Science 306 (2004) 2087-2090
    • (2004) Science , vol.306 , pp. 2087-2090
    • Meyron-Holtz, E.G.1    Ghosh, M.C.2    Rouault, T.A.3
  • 21
    • 0034059140 scopus 로고    scopus 로고
    • Cre recombinase: the universal reagent for genome tailoring
    • Nagy A. Cre recombinase: the universal reagent for genome tailoring. Genesis 26 (2000) 99-109
    • (2000) Genesis , vol.26 , pp. 99-109
    • Nagy, A.1
  • 22
    • 33750133047 scopus 로고    scopus 로고
    • Regulation of iron metabolism by hepcidin
    • Nemeth E., and Ganz T. Regulation of iron metabolism by hepcidin. Annu. Rev. Nutr. 26 (2006) 323-342
    • (2006) Annu. Rev. Nutr. , vol.26 , pp. 323-342
    • Nemeth, E.1    Ganz, T.2
  • 23
    • 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
  • 24
    • 33746868342 scopus 로고    scopus 로고
    • Hereditary hemochromatosis
    • Pietrangelo A. Hereditary hemochromatosis. Biochim. Biophys. Acta 1763 (2006) 700-710
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 700-710
    • Pietrangelo, A.1
  • 25
    • 2442693043 scopus 로고    scopus 로고
    • Influence of native and hypochlorite-modified low-density lipoprotein on gene expression in human proximal tubular epithelium
    • Porubsky S., Schmid H., Bonrouhi M., Kretzler M., Malle E., Nelson P.J., and Gröne H.J. Influence of native and hypochlorite-modified low-density lipoprotein on gene expression in human proximal tubular epithelium. Am. J. Pathol. 164 (2004) 2175-2187
    • (2004) Am. J. Pathol. , vol.164 , pp. 2175-2187
    • Porubsky, S.1    Schmid, H.2    Bonrouhi, M.3    Kretzler, M.4    Malle, E.5    Nelson, P.J.6    Gröne, H.J.7
  • 26
    • 0034672236 scopus 로고    scopus 로고
    • Iron homeostasis: new tales from the crypt
    • Roy C.N., and Enns C.A. Iron homeostasis: new tales from the crypt. Blood 96 (2000) 4020-4027
    • (2000) Blood , vol.96 , pp. 4020-4027
    • Roy, C.N.1    Enns, C.A.2
  • 27
    • 34247628002 scopus 로고    scopus 로고
    • Iron-regulatory proteins limit hypoxia-inducible factor-2alpha expression in iron deficiency
    • Sanchez M., Galy B., Muckenthaler M.U., and Hentze M.W. Iron-regulatory proteins limit hypoxia-inducible factor-2alpha expression in iron deficiency. Nat. Struct. Mol. Biol. 14 (2007) 420-426
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 420-426
    • Sanchez, M.1    Galy, B.2    Muckenthaler, M.U.3    Hentze, M.W.4
  • 28
    • 0032488980 scopus 로고    scopus 로고
    • Iron differentially stimulates translation of mitochondrial aconitase and ferritin mRNAs in mammalian cells. Implications for iron regulatory proteins as regulators of mitochondrial citrate utilization
    • Schalinske K.L., Chen O.S., and Eisenstein R.S. Iron differentially stimulates translation of mitochondrial aconitase and ferritin mRNAs in mammalian cells. Implications for iron regulatory proteins as regulators of mitochondrial citrate utilization. J. Biol. Chem. 273 (1998) 3740-3746
    • (1998) J. Biol. Chem. , vol.273 , pp. 3740-3746
    • Schalinske, K.L.1    Chen, O.S.2    Eisenstein, R.S.3
  • 29
    • 0033106390 scopus 로고    scopus 로고
    • Iron regulatory protein as an endogenous sensor of iron in rat intestinal mucosa. Possible implications for the regulation of iron absorption
    • Schümann K., Moret R., Kunzle H., and Kühn L.C. Iron regulatory protein as an endogenous sensor of iron in rat intestinal mucosa. Possible implications for the regulation of iron absorption. Eur. J. Biochem. 260 (1999) 362-372
    • (1999) Eur. J. Biochem. , vol.260 , pp. 362-372
    • Schümann, K.1    Moret, R.2    Kunzle, H.3    Kühn, L.C.4
  • 30
    • 33645307993 scopus 로고    scopus 로고
    • Complete loss of iron regulatory proteins 1 and 2 prevents viability of murine zygotes beyond the blastocyst stage of embryonic development
    • Smith S.R., Ghosh M.C., Ollivierre-Wilson H., Tong W.H., and Rouault T.A. Complete loss of iron regulatory proteins 1 and 2 prevents viability of murine zygotes beyond the blastocyst stage of embryonic development. Blood Cells Mol. Dis. 36 (2006) 283-287
    • (2006) Blood Cells Mol. Dis. , vol.36 , pp. 283-287
    • Smith, S.R.1    Ghosh, M.C.2    Ollivierre-Wilson, H.3    Tong, W.H.4    Rouault, T.A.5
  • 31
    • 28344453346 scopus 로고    scopus 로고
    • Mammalian lactoferrin receptors: structure and function
    • Suzuki Y.A., Lopez V., and Lönnerdal B. Mammalian lactoferrin receptors: structure and function. Cell. Mol. Life Sci. 62 (2005) 2560-2575
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2560-2575
    • Suzuki, Y.A.1    Lopez, V.2    Lönnerdal, B.3
  • 32
    • 33746864096 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron homeostasis by iron regulatory proteins
    • Wallander M.L., Leibold E.A., and Eisenstein R.S. Molecular control of vertebrate iron homeostasis by iron regulatory proteins. Biochim. Biophys. Acta 1763 (2006) 668-689
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 668-689
    • Wallander, M.L.1    Leibold, E.A.2    Eisenstein, R.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.