메뉴 건너뛰기




Volumn 119, Issue 5, 2009, Pages 1159-1166

HIF-2α, but not HIF-1α, promotes iron absorption in mice

Author keywords

[No Author keywords available]

Indexed keywords

HEPCIDIN; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 2ALPHA; IRON; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 2; ANTIMICROBIAL CATIONIC PEPTIDE; BASIC HELIX LOOP HELIX TRANSCRIPTION FACTOR; CATION TRANSPORT PROTEIN; CYTOCHROME B; ENDOTHELIAL PAS DOMAIN CONTAINING PROTEIN 1; ENDOTHELIAL PAS DOMAIN-CONTAINING PROTEIN 1; HEMOGLOBIN; HIF1A PROTEIN, MOUSE; METAL TRANSPORTING PROTEIN 1; SOLUTE CARRIER FAMILY 11 (PROTON COUPLED DIVALENT METAL ION TRANSPORTERS), MEMBER 2; SOLUTE CARRIER FAMILY 11- (PROTON-COUPLED DIVALENT METAL ION TRANSPORTERS), MEMBER 2;

EID: 66449124596     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI38499     Document Type: Article
Times cited : (411)

References (37)
  • 1
    • 47649126246 scopus 로고    scopus 로고
    • Forging a field: The golden age of iron biology
    • Andrews, N.C. 2008. Forging a field: the golden age of iron biology. Blood. 112:219-230.
    • (2008) Blood , vol.112 , pp. 219-230
    • Andrews, N.C.1
  • 2
    • 50949102412 scopus 로고    scopus 로고
    • Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network
    • Muckenthaler, M.U., Galy, B., and Hentze, M.W. 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
  • 3
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization
    • Nemeth, E., et al. 2004. Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science. 306:2090-2093.
    • (2004) Science , vol.306 , pp. 2090-2093
    • Nemeth, E.1
  • 4
    • 0036791486 scopus 로고    scopus 로고
    • The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation
    • Nicolas, G., et al. 2002. The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation. J. Clin. Invest. 110:1037-1044.
    • (2002) J. Clin. Invest , vol.110 , pp. 1037-1044
    • Nicolas, G.1
  • 5
    • 20444413054 scopus 로고    scopus 로고
    • Deregulation of proteins involved in iron metabolism in hepcidin-deficient mice
    • Viatte, L., et al. 2005. Deregulation of proteins involved in iron metabolism in hepcidin-deficient mice. Blood. 105:4861-4864.
    • (2005) Blood , vol.105 , pp. 4861-4864
    • Viatte, L.1
  • 6
    • 25444435160 scopus 로고    scopus 로고
    • Increased duodenal iron uptake and transfer in a rat model of chronic hypoxia is accompanied by reduced hepcidin expression
    • Leung, P.S., Srai, S.K., Mascarenhas, M., Churchill, L.J., and Debnam, E.S. 2005. Increased duodenal iron uptake and transfer in a rat model of chronic hypoxia is accompanied by reduced hepcidin expression. Gut. 54:1391-1395.
    • (2005) Gut , vol.54 , pp. 1391-1395
    • Leung, P.S.1    Srai, S.K.2    Mascarenhas, M.3    Churchill, L.J.4    Debnam, E.S.5
  • 7
    • 36849055112 scopus 로고    scopus 로고
    • Hypoxia and gastrointestinal disease
    • Taylor, C.T., and Colgan, S.P. 2007. Hypoxia and gastrointestinal disease. J. Mol. Med. 85:1295-1300.
    • (2007) J. Mol. Med , vol.85 , pp. 1295-1300
    • Taylor, C.T.1    Colgan, S.P.2
  • 8
    • 0037315337 scopus 로고    scopus 로고
    • Widespread hypoxia-inducible expression of HIF-2alpha in distinct cell populations of different organs
    • Wiesener, M.S., et al. 2003. Widespread hypoxia-inducible expression of HIF-2alpha in distinct cell populations of different organs. FASEB J. 17:271-273.
    • (2003) FASEB J , vol.17 , pp. 271-273
    • Wiesener, M.S.1
  • 9
    • 15444342958 scopus 로고    scopus 로고
    • Cellular and developmental control of O2 homeostasis by hypoxia-inducible factor 1 alpha
    • Iyer, N.V., et al. 1998. Cellular and developmental control of O2 homeostasis by hypoxia-inducible factor 1 alpha. Genes Dev. 12:149-162.
    • (1998) Genes Dev , vol.12 , pp. 149-162
    • Iyer, N.V.1
  • 10
    • 0032100732 scopus 로고    scopus 로고
    • HIF-1 alpha is required for solid tumor formation and embryonic vascularization
    • Ryan, H.E., Lo, J., and Johnson, R.S. 1998. HIF-1 alpha is required for solid tumor formation and embryonic vascularization. EMBO J. 17:3005-3015.
    • (1998) EMBO J , vol.17 , pp. 3005-3015
    • Ryan, H.E.1    Lo, J.2    Johnson, R.S.3
  • 11
    • 0035983324 scopus 로고    scopus 로고
    • Loss of HIF-2alpha and inhibition of VEGF impair fetal lung maturation, whereas treatment with VEGF prevents fatal respiratory distress in premature mice
    • Compernolle, V., et al. 2002. Loss of HIF-2alpha and inhibition of VEGF impair fetal lung maturation, whereas treatment with VEGF prevents fatal respiratory distress in premature mice. Nat. Med. 8:702-710.
    • (2002) Nat. Med , vol.8 , pp. 702-710
    • Compernolle, V.1
  • 12
    • 0034682513 scopus 로고    scopus 로고
    • The transcription factor EPAS-1/hypoxia-inducible factor 2alpha plays an important role in vascular remodeling
    • Peng, J., Zhang, L., Drysdale, L., and Fong, G.H. 2000. The transcription factor EPAS-1/hypoxia-inducible factor 2alpha plays an important role in vascular remodeling. Proc. Natl. Acad. Sci. U. S. A. 97:8386-8391.
    • (2000) Proc. Natl. Acad. Sci. U. S. A , vol.97 , pp. 8386-8391
    • Peng, J.1    Zhang, L.2    Drysdale, L.3    Fong, G.H.4
  • 13
    • 0032213236 scopus 로고    scopus 로고
    • The hypoxia-responsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development
    • Tian, H., et al. 1998. The hypoxia-responsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development. Genes Dev. 12:3320-3324.
    • (1998) Genes Dev , vol.12 , pp. 3320-3324
    • Tian, H.1
  • 14
    • 33847796951 scopus 로고    scopus 로고
    • Acute postnatal ablation of Hif-2alpha results in anemia
    • Gruber, M., et al. 2007. Acute postnatal ablation of Hif-2alpha results in anemia. Proc. Natl. Acad. Sci. U. S. A. 104:2301-2306.
    • (2007) Proc. Natl. Acad. Sci. U. S. A , vol.104 , pp. 2301-2306
    • Gruber, M.1
  • 15
    • 34147124264 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-2 (HIF-2) regulates hepatic erythropoietin in vivo
    • Rankin, E.B., et al. 2007. Hypoxia-inducible factor-2 (HIF-2) regulates hepatic erythropoietin in vivo. J. Clin. Invest. 117:1068-1077.
    • (2007) J. Clin. Invest , vol.117 , pp. 1068-1077
    • Rankin, E.B.1
  • 16
    • 34447120059 scopus 로고    scopus 로고
    • Regulation of iron homeostasis by the hypoxia-inducible transcription factors (HIFs)
    • Peyssonnaux, C., et al. 2007. Regulation of iron homeostasis by the hypoxia-inducible transcription factors (HIFs). J. Clin. Invest. 117:1926-1932.
    • (2007) J. Clin. Invest , vol.117 , pp. 1926-1932
    • Peyssonnaux, C.1
  • 17
    • 58749094789 scopus 로고    scopus 로고
    • Intestinal hypoxia-inducible transcription factors are essential for iron absorption following iron deficiency
    • Shah, Y.M., Matsubara, T., Ito, S., Yim, S.H., and Gonzalez, F.J. 2009. Intestinal hypoxia-inducible transcription factors are essential for iron absorption following iron deficiency. Cell Metab. 9:152-164.
    • (2009) Cell Metab , vol.9 , pp. 152-164
    • Shah, Y.M.1    Matsubara, T.2    Ito, S.3    Yim, S.H.4    Gonzalez, F.J.5
  • 18
    • 0033564656 scopus 로고    scopus 로고
    • Cellular and subcellular localization of the Nramp2 iron transporter in the intestinal brush border and regulation by dietary iron
    • Canonne-Hergaux, F., Gruenheid, S., Ponka, P., and Gros, P. 1999. Cellular and subcellular localization of the Nramp2 iron transporter in the intestinal brush border and regulation by dietary iron. Blood. 93:4406-4417.
    • (1999) Blood , vol.93 , pp. 4406-4417
    • Canonne-Hergaux, F.1    Gruenheid, S.2    Ponka, P.3    Gros, P.4
  • 19
    • 0035793856 scopus 로고    scopus 로고
    • An iron-regulated ferric reductase associated with the absorption of dietary iron
    • McKie, A.T., et al. 2001. An iron-regulated ferric reductase associated with the absorption of dietary iron. Science. 291:1755-1759.
    • (2001) Science , vol.291 , pp. 1755-1759
    • McKie, A.T.1
  • 20
    • 27144507493 scopus 로고    scopus 로고
    • Cybrd1 (duodenal cytochrome b) is not necessary for dietary iron absorption in mice
    • Gunshin, H., et al. 2005. Cybrd1 (duodenal cytochrome b) is not necessary for dietary iron absorption in mice. Blood. 106:2879-2883.
    • (2005) Blood , vol.106 , pp. 2879-2883
    • Gunshin, H.1
  • 21
    • 18244399587 scopus 로고    scopus 로고
    • Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver
    • Gunshin, H., et al. 2005. Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver. J. Clin. Invest. 115:1258-1266.
    • (2005) J. Clin. Invest , vol.115 , pp. 1258-1266
    • Gunshin, H.1
  • 22
    • 0030755366 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian proton-coupled metal-ion transporter
    • Gunshin, H., et al. 1997. Cloning and characterization of a mammalian proton-coupled metal-ion transporter. Nature. 388:482-488.
    • (1997) Nature , vol.388 , pp. 482-488
    • Gunshin, H.1
  • 23
    • 0032477866 scopus 로고    scopus 로고
    • Nramp2 is mutated in the anemic Belgrade (b) rat: Evidence of a role for Nramp2 in endosomal iron transport
    • Fleming, M.D., et al. 1998. Nramp2 is mutated in the anemic Belgrade (b) rat: evidence of a role for Nramp2 in endosomal iron transport. Proc. Natl. Acad. Sci. U. S. A. 95:1148-1153.
    • (1998) Proc. Natl. Acad. Sci. U. S. A , vol.95 , pp. 1148-1153
    • Fleming, M.D.1
  • 24
    • 0030763856 scopus 로고    scopus 로고
    • Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene
    • Fleming, M.D., et al. 1997. Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene. Nat. Genet. 16:383-386.
    • (1997) Nat. Genet , vol.16 , pp. 383-386
    • Fleming, M.D.1
  • 25
    • 33646537173 scopus 로고    scopus 로고
    • Two new human DMT1 gene mutations in a patient with microcytic anemia, low ferritinemia, and liver iron overload
    • Beaumont, C., et al. 2006. Two new human DMT1 gene mutations in a patient with microcytic anemia, low ferritinemia, and liver iron overload. Blood. 107:4168-4170.
    • (2006) Blood , vol.107 , pp. 4168-4170
    • Beaumont, C.1
  • 26
    • 12844260664 scopus 로고    scopus 로고
    • Identification of a human mutation of DMT1 in a patient with microcytic anemia and iron overload
    • Mims, M.P., et al. 2005. Identification of a human mutation of DMT1 in a patient with microcytic anemia and iron overload. Blood. 105:1337-1342.
    • (2005) Blood , vol.105 , pp. 1337-1342
    • Mims, M.P.1
  • 27
    • 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. 2002. Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: implications for regulation and cellular function. Proc. Natl. Acad. Sci. U. S. A. 99:12345-12350.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 12345-12350
    • Hubert, N.1    Hentze, M.W.2
  • 28
    • 19344376879 scopus 로고    scopus 로고
    • Hypoxia induces changes in expression of isoforms of the divalent metal transporter (DMT1) in rat pheochromocytoma (PC12) cells
    • Lis, A., et al. 2005. Hypoxia induces changes in expression of isoforms of the divalent metal transporter (DMT1) in rat pheochromocytoma (PC12) cells. Biochem. Pharmacol. 69:1647-1655.
    • (2005) Biochem. Pharmacol , vol.69 , pp. 1647-1655
    • Lis, A.1
  • 29
    • 33646257081 scopus 로고    scopus 로고
    • Methods and options for estimating iron and zinc bioavailability using Caco-2 cell models: Benefits and limitations
    • Sharp, P. 2005. Methods and options for estimating iron and zinc bioavailability using Caco-2 cell models: benefits and limitations. Int. J. Vitam. Nutr. Res. 75:413-421.
    • (2005) Int. J. Vitam. Nutr. Res , vol.75 , pp. 413-421
    • Sharp, P.1
  • 30
    • 38349111676 scopus 로고    scopus 로고
    • Role of the hypoxia inducible factors HIF in iron metabolism
    • Peyssonnaux, C., Nizet, V., and Johnson, R.S. 2008. Role of the hypoxia inducible factors HIF in iron metabolism. Cell Cycle. 7:28-32.
    • (2008) Cell Cycle , vol.7 , pp. 28-32
    • Peyssonnaux, C.1    Nizet, V.2    Johnson, R.S.3
  • 31
    • 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., Grone, H.J., and Hentze, M.W. 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
  • 32
    • 33646248422 scopus 로고    scopus 로고
    • Differential regulation of the transcriptional activities of hypoxia-inducible factor 1 alpha (HIF-1alpha) and HIF-2alpha in stem cells
    • Hu, C.J., et al. 2006. Differential regulation of the transcriptional activities of hypoxia-inducible factor 1 alpha (HIF-1alpha) and HIF-2alpha in stem cells. Mol. Cell. Biol. 26:3514-3526.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 3514-3526
    • Hu, C.J.1
  • 33
    • 35848938945 scopus 로고    scopus 로고
    • The N-terminal transactivation domain confers target gene specificity of hypoxia-inducible factors HIF-1alpha and HIF-2alpha
    • Hu, C.J., Sataur, A., Wang, L., Chen, H., and Simon, M.C. 2007. The N-terminal transactivation domain confers target gene specificity of hypoxia-inducible factors HIF-1alpha and HIF-2alpha. Mol. Biol. Cell. 18:4528-4542.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4528-4542
    • Hu, C.J.1    Sataur, A.2    Wang, L.3    Chen, H.4    Simon, M.C.5
  • 34
    • 0023897841 scopus 로고
    • In vivo studies on the relationship between intestinal iron (Fe3+) absorption, hypoxia and erythropoiesis in the mouse
    • Raja, K.B., Simpson, R.J., Pippard, M.J., and Peters, T.J. 1988. In vivo studies on the relationship between intestinal iron (Fe3+) absorption, hypoxia and erythropoiesis in the mouse. Br. J. Haematol. 68:373-378.
    • (1988) Br. J. Haematol , vol.68 , pp. 373-378
    • Raja, K.B.1    Simpson, R.J.2    Pippard, M.J.3    Peters, T.J.4
  • 35
    • 0035917808 scopus 로고    scopus 로고
    • Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation
    • Jaakkola, P., et al. 2001. Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation. Science. 292:468-472.
    • (2001) Science , vol.292 , pp. 468-472
    • Jaakkola, P.1
  • 36
    • 0037007064 scopus 로고    scopus 로고
    • Severe iron deficiency anemia in transgenic mice expressing liver hepcidin
    • Nicolas, G., et al. 2002. Severe iron deficiency anemia in transgenic mice expressing liver hepcidin. Proc. Natl. Acad. Sci. U. S. A. 99:4596-4601.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 4596-4601
    • Nicolas, G.1
  • 37
    • 33847661809 scopus 로고    scopus 로고
    • Protocol for the fast chromatin immunoprecipitation (ChIP) method
    • Nelson, J.D., Denisenko, O., and Bomsztyk, K. 2006. Protocol for the fast chromatin immunoprecipitation (ChIP) method. Nat. Protoc. 1:179-185.
    • (2006) Nat. Protoc , vol.1 , pp. 179-185
    • Nelson, J.D.1    Denisenko, O.2    Bomsztyk, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.