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Volumn 45, Issue 3, 2010, Pages 233-237

Iron metabolism gene expression in human skeletal muscle

Author keywords

Genes; Iron metabolism; Liver; Skeletal muscle

Indexed keywords

BETA ACTIN; CD71 ANTIGEN; CERULOPLASMIN; FERRITIN; FERROPORTIN 1; HEMOJUVELIN; HEPCIDIN; HEPHAESTIN; HFE PROTEIN; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 2; NEUTROPHIL GELATINASE ASSOCIATED LIPOCALIN; PROTEIN FTH1; TRANSFERRIN RECEPTOR 2; UNCLASSIFIED DRUG;

EID: 77956880215     PISSN: 10799796     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcmd.2010.07.002     Document Type: Article
Times cited : (16)

References (46)
  • 1
    • 0015651975 scopus 로고
    • The myoglobin content of human skeletal muscle
    • Bulton F.E. The myoglobin content of human skeletal muscle. Br. J. Haematol. 1973, 25:281.
    • (1973) Br. J. Haematol. , vol.25 , pp. 281
    • Bulton, F.E.1
  • 2
    • 33644772206 scopus 로고    scopus 로고
    • Animal models with enhanced erythropoiesis and iron absorption
    • Latunde-Dada G.O., McKie A.T., Simpson R.J., et al. Animal models with enhanced erythropoiesis and iron absorption. Biochim. Biophys. Acta 2006, 1762:414-423.
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 414-423
    • Latunde-Dada, G.O.1    McKie, A.T.2    Simpson, R.J.3
  • 3
    • 0036077111 scopus 로고    scopus 로고
    • Molecular pathogenesis of iron overload
    • Trinder D., Fox C., Vautier G., et al. Molecular pathogenesis of iron overload. Gut 2002, 51:290-295.
    • (2002) Gut , vol.51 , pp. 290-295
    • Trinder, D.1    Fox, C.2    Vautier, G.3
  • 4
    • 0022464750 scopus 로고
    • Biochemical basis for the manifestation of iron deficiency
    • Dallman P.R. Biochemical basis for the manifestation of iron deficiency. Annu. Rev. Nutr. 1986, 6:13-40.
    • (1986) Annu. Rev. Nutr. , vol.6 , pp. 13-40
    • Dallman, P.R.1
  • 5
    • 34249675806 scopus 로고    scopus 로고
    • Strong iron demand during hypoxia-induces erythropoiesis is associated with down-regulation of iron-related proteins and myoglobin in human skeletal muscle
    • Robach P., Cairo G., Gelfi C., et al. Strong iron demand during hypoxia-induces erythropoiesis is associated with down-regulation of iron-related proteins and myoglobin in human skeletal muscle. Blood 2007, 109:4724-4731.
    • (2007) Blood , vol.109 , pp. 4724-4731
    • Robach, P.1    Cairo, G.2    Gelfi, C.3
  • 6
    • 69249217850 scopus 로고    scopus 로고
    • Alterations of systemic and muscle iron metabolism in human subjects treated with low-dose recombinant erythropoietin
    • Robach P., Recalcati S., Girelli D., et al. Alterations of systemic and muscle iron metabolism in human subjects treated with low-dose recombinant erythropoietin. Blood 2009, 113:6707-6715.
    • (2009) Blood , vol.113 , pp. 6707-6715
    • Robach, P.1    Recalcati, S.2    Girelli, D.3
  • 7
    • 37549047172 scopus 로고    scopus 로고
    • Effects of iron loading on muscle: genome-wide mRNA expression profiling in the mouse
    • Rodriguez A., Hilvo M., Kytömäki L., et al. Effects of iron loading on muscle: genome-wide mRNA expression profiling in the mouse. BMC Genomics 2007, 19:379.
    • (2007) BMC Genomics , vol.19 , pp. 379
    • Rodriguez, A.1    Hilvo, M.2    Kytömäki, L.3
  • 9
    • 44949231424 scopus 로고    scopus 로고
    • Analyzing real-time PCR data by the comparative C(T) method
    • Schmittgen T.D., Livak K.J. Analyzing real-time PCR data by the comparative C(T) method. Nat. Protoc. 2008, 3:1101-1108.
    • (2008) Nat. Protoc. , vol.3 , pp. 1101-1108
    • Schmittgen, T.D.1    Livak, K.J.2
  • 10
    • 0031963449 scopus 로고    scopus 로고
    • Function and regulation of transferrin and ferritin
    • Ponka P., Beaumont C., Richardson D.R. Function and regulation of transferrin and ferritin. Semin. Hematol. 1998, 35:35-54.
    • (1998) Semin. Hematol. , vol.35 , pp. 35-54
    • Ponka, P.1    Beaumont, C.2    Richardson, D.R.3
  • 11
    • 14544273227 scopus 로고    scopus 로고
    • Examination of the distribution of the transferrin homologue, melanotransferrin (tumor antigen p97), in mouse and human
    • Sekyere E.O., Dunn L.L., Richardson D.R. Examination of the distribution of the transferrin homologue, melanotransferrin (tumor antigen p97), in mouse and human. Biochim. Biophys. Acta 2005, 1722:131-142.
    • (2005) Biochim. Biophys. Acta , vol.1722 , pp. 131-142
    • Sekyere, E.O.1    Dunn, L.L.2    Richardson, D.R.3
  • 12
    • 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. 1996, 13:399-408.
    • (1996) Nat. Genet. , vol.13 , pp. 399-408
    • Feder, J.N.1    Gnirke, A.2    Thomas, W.3
  • 13
    • 0034610781 scopus 로고    scopus 로고
    • Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor
    • Benett M.J., Lebr n J., Bjorkman P.J. Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor. Nature 2000, 403:46-53.
    • (2000) Nature , vol.403 , pp. 46-53
    • Benett, M.J.1    Lebr, N.J.2    Bjorkman, P.J.3
  • 14
    • 24344468431 scopus 로고    scopus 로고
    • Contribution of Hfe expression in macrophages to the regulation of hepatic hepcidin levels and iron loading
    • Makui H., Soares R.J., Jiang W., et al. Contribution of Hfe expression in macrophages to the regulation of hepatic hepcidin levels and iron loading. Blood 2005, 106:2189-2195.
    • (2005) Blood , vol.106 , pp. 2189-2195
    • Makui, H.1    Soares, R.J.2    Jiang, W.3
  • 15
    • 0033597780 scopus 로고    scopus 로고
    • Molecular cloning of transferrin receptor 2
    • Kawabata H., Yang R., Hirama T., et al. Molecular cloning of transferrin receptor 2. J. Biol. Chem. 1999, 274:20826-20832.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20826-20832
    • Kawabata, H.1    Yang, R.2    Hirama, T.3
  • 16
    • 0034022636 scopus 로고    scopus 로고
    • The gene TFR2 is mutated in a new type of haemochromatosis mapping to 7q22
    • Camaschella C., Roetto A., Calì A., et al. The gene TFR2 is mutated in a new type of haemochromatosis mapping to 7q22. Nat. Genet. 2002, 25:14-15.
    • (2002) Nat. Genet. , vol.25 , pp. 14-15
    • Camaschella, C.1    Roetto, A.2    Calì, A.3
  • 17
    • 33749393565 scopus 로고    scopus 로고
    • Hereditary hemochromatosis protein, HFE, interaction with transferrin receptor 2 suggests a molecular mechanism for mammalian iron sensing
    • Goswami T., Andrews N.C. Hereditary hemochromatosis protein, HFE, interaction with transferrin receptor 2 suggests a molecular mechanism for mammalian iron sensing. J. Biol. Chem. 2006, 281:28494-28498.
    • (2006) J. Biol. Chem. , vol.281 , pp. 28494-28498
    • Goswami, T.1    Andrews, N.C.2
  • 18
    • 34250850987 scopus 로고    scopus 로고
    • The iron regulatory peptide hepcidin is expressed in the heart and regulated by hypoxia and inflammation
    • Merle U., Fein E., Gehrke S.G., et al. The iron regulatory peptide hepcidin is expressed in the heart and regulated by hypoxia and inflammation. Endocrinology 2007, 148:2663-2668.
    • (2007) Endocrinology , vol.148 , pp. 2663-2668
    • Merle, U.1    Fein, E.2    Gehrke, S.G.3
  • 19
    • 0037126002 scopus 로고    scopus 로고
    • Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: implications for regulation and cellular function
    • Hubert N., Hentze M.W. Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: implications for regulation and cellular function. Proc. Natl. Acad. Sci. 2002, 99:12345-12350.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 12345-12350
    • Hubert, N.1    Hentze, M.W.2
  • 20
    • 0036865552 scopus 로고    scopus 로고
    • The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition
    • Goetz D.H., Holmes M.A., Borregaard N., et al. The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition. Mol. Cell 2002, 10:1033-1043.
    • (2002) Mol. Cell , vol.10 , pp. 1033-1043
    • Goetz, D.H.1    Holmes, M.A.2    Borregaard, N.3
  • 21
    • 0031260224 scopus 로고    scopus 로고
    • Molecular characterization and pattern of tissue expression of the gene for neutrophil gelatinase-associated lipocalin from humans
    • Cowland J.B., Borregaard N. Molecular characterization and pattern of tissue expression of the gene for neutrophil gelatinase-associated lipocalin from humans. Genomics 1997, 45:17-23.
    • (1997) Genomics , vol.45 , pp. 17-23
    • Cowland, J.B.1    Borregaard, N.2
  • 22
    • 0034029610 scopus 로고    scopus 로고
    • Expression of NRL/NGAL (neu-related lipocalin/neutrophil gelatinase-associated lipocalin) during mammalian embryonic development and in inflammation
    • Zegera B., Cermelli S., Michelis B., et al. Expression of NRL/NGAL (neu-related lipocalin/neutrophil gelatinase-associated lipocalin) during mammalian embryonic development and in inflammation. Eur. J. Cell Biol. 2000, 79:165-172.
    • (2000) Eur. J. Cell Biol. , vol.79 , pp. 165-172
    • Zegera, B.1    Cermelli, S.2    Michelis, B.3
  • 23
    • 32444442757 scopus 로고    scopus 로고
    • Lipocalin 2-deficient mice exhibit increased sensitivity to Escherichia coli infection but not to ischemia-reperfusion injury
    • Berger T., Togawa A., Duncan G.S., et al. Lipocalin 2-deficient mice exhibit increased sensitivity to Escherichia coli infection but not to ischemia-reperfusion injury. Proc. Natl. Acad. Sci. 2006, 103:1834-1839.
    • (2006) Proc. Natl. Acad. Sci. , vol.103 , pp. 1834-1839
    • Berger, T.1    Togawa, A.2    Duncan, G.S.3
  • 24
    • 33646947821 scopus 로고    scopus 로고
    • Neutrophil gelatinase-associated lipocalin, a siderophore-binding eukaryotic protein
    • Borregaard N., Cowland J.B. Neutrophil gelatinase-associated lipocalin, a siderophore-binding eukaryotic protein. Biometals 2006, 19:211-215.
    • (2006) Biometals , vol.19 , pp. 211-215
    • Borregaard, N.1    Cowland, J.B.2
  • 25
    • 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 2004, 306:2051-2053.
    • (2004) Science , vol.306 , pp. 2051-2053
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3
  • 27
    • 0142222530 scopus 로고    scopus 로고
    • The ceruloplasmin homolog hephaestin and the control of intestinal iron absorption
    • Anderson G.J., Frazer D.M., McKie A.T., et al. The ceruloplasmin homolog hephaestin and the control of intestinal iron absorption. Blood Cells Mol. Dis. 2002, 29:367-375.
    • (2002) Blood Cells Mol. Dis. , vol.29 , pp. 367-375
    • Anderson, G.J.1    Frazer, D.M.2    McKie, A.T.3
  • 28
    • 33645070287 scopus 로고    scopus 로고
    • Unexpected role of ceruloplassmin in intestinal iron absorption
    • Cherukuri S., Potla R., Sarkar J., et al. Unexpected role of ceruloplassmin in intestinal iron absorption. Cell Metab. 2005, 2:309-319.
    • (2005) Cell Metab. , vol.2 , pp. 309-319
    • Cherukuri, S.1    Potla, R.2    Sarkar, J.3
  • 29
    • 0041438849 scopus 로고    scopus 로고
    • Systemic regulation of hephaestin and Ireg 1 revealed in studies of genetic and nutritional iron deficiency
    • Chen H., Su T., Attieh Z.K., et al. Systemic regulation of hephaestin and Ireg 1 revealed in studies of genetic and nutritional iron deficiency. Blood 2003, 102:1893-1899.
    • (2003) Blood , vol.102 , pp. 1893-1899
    • Chen, H.1    Su, T.2    Attieh, Z.K.3
  • 30
    • 0032909207 scopus 로고    scopus 로고
    • Haephestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in sla mouse
    • Vulpe C.D., Kuo Y., Murphy T.L., et al. Haephestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in sla mouse. Nat. Genet. 1999, 21:195-199.
    • (1999) Nat. Genet. , vol.21 , pp. 195-199
    • Vulpe, C.D.1    Kuo, Y.2    Murphy, T.L.3
  • 31
    • 0025331837 scopus 로고
    • Human ceruloplasmin: tissue specific expression of transcripts produced by alternative splicing
    • Yang F., Friedrichs W.E., Cupples R.L., et al. Human ceruloplasmin: tissue specific expression of transcripts produced by alternative splicing. J. Biol. Chem. 1990, 265:10780-10785.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10780-10785
    • Yang, F.1    Friedrichs, W.E.2    Cupples, R.L.3
  • 32
    • 0026335256 scopus 로고
    • Tissue-specific ceruloplasmin gene expression in the mammary gland
    • Jaeger J.L., Shimizu N., Gitlin J.D. Tissue-specific ceruloplasmin gene expression in the mammary gland. Biochem. J. 1991, 280:671-617.
    • (1991) Biochem. J. , vol.280 , pp. 671-617
    • Jaeger, J.L.1    Shimizu, N.2    Gitlin, J.D.3
  • 33
    • 0030036172 scopus 로고    scopus 로고
    • Ceruloplasmin gene expression in the murine central nervous system
    • Klomp L.W., Farhangrazi Z.S., Dugan L.L., et al. Ceruloplasmin gene expression in the murine central nervous system. J. Clin. Invest. 1996, 98:207-215.
    • (1996) J. Clin. Invest. , vol.98 , pp. 207-215
    • Klomp, L.W.1    Farhangrazi, Z.S.2    Dugan, L.L.3
  • 34
    • 0032875387 scopus 로고    scopus 로고
    • Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux
    • Harris Z.L., Durley A.P., Kwong Man T., et al. Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux. Proc. Natl. Acad. Sci. 1999, 96:10812-10817.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 10812-10817
    • Harris, Z.L.1    Durley, A.P.2    Kwong Man, T.3
  • 35
    • 1842504248 scopus 로고    scopus 로고
    • Aceruloplasminemia: an inherited neurodegenerative disease with impairment of iron homeostasis
    • Xu X., Pin S., Gathinji M., et al. Aceruloplasminemia: an inherited neurodegenerative disease with impairment of iron homeostasis. Ann. N. Y. Acad. Sci. 2004, 1012:299-305.
    • (2004) Ann. N. Y. Acad. Sci. , vol.1012 , pp. 299-305
    • Xu, X.1    Pin, S.2    Gathinji, M.3
  • 36
    • 34250865977 scopus 로고    scopus 로고
    • The molecular mechanism of hepcidin-mediated ferroportin down-regulation
    • De Domenico I., Ward D.M., Langelier C., et al. The molecular mechanism of hepcidin-mediated ferroportin down-regulation. Mol. Biol. Cell 2007, 18:2569-2578.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2569-2578
    • De Domenico, I.1    Ward, D.M.2    Langelier, C.3
  • 37
    • 0037962795 scopus 로고    scopus 로고
    • The orchestration of body iron intake: how and where do enterocytes receive their cues?
    • Frazer D.M., Anderson G.J. The orchestration of body iron intake: how and where do enterocytes receive their cues?. Blood Cells Mol. Dis. 2003, 30:288-297.
    • (2003) Blood Cells Mol. Dis. , vol.30 , pp. 288-297
    • Frazer, D.M.1    Anderson, G.J.2
  • 38
    • 9144252017 scopus 로고    scopus 로고
    • Mutations in HFE2 cause iron overload inchromosome 1q-linked juvenile hemochromatosis
    • Papanikolaou G., Samuels M.E., Ludwig E.H., et al. Mutations in HFE2 cause iron overload inchromosome 1q-linked juvenile hemochromatosis. Nat. Genet. 2004, 36:77-82.
    • (2004) Nat. Genet. , vol.36 , pp. 77-82
    • Papanikolaou, G.1    Samuels, M.E.2    Ludwig, E.H.3
  • 39
    • 20244388240 scopus 로고    scopus 로고
    • Mutant antimicrobial peptide hepcidin is associated with severe juvenile hemochromatosis
    • Roetto A., Papanikolaou G., Politou M., et al. Mutant antimicrobial peptide hepcidin is associated with severe juvenile hemochromatosis. Nat. Genet. 2002, 33:21-22.
    • (2002) Nat. Genet. , vol.33 , pp. 21-22
    • Roetto, A.1    Papanikolaou, G.2    Politou, M.3
  • 40
    • 27144459908 scopus 로고    scopus 로고
    • Competitive regulation of hepcidin mRNA by soluble and cell-associated hemojuvelin
    • Lin L., Goldberg P., Ganz T. Competitive regulation of hepcidin mRNA by soluble and cell-associated hemojuvelin. Blood 2005, 106:2884-2889.
    • (2005) Blood , vol.106 , pp. 2884-2889
    • Lin, L.1    Goldberg, P.2    Ganz, T.3
  • 41
    • 33748797945 scopus 로고    scopus 로고
    • Complex biosynthesis of the muscle-enriched iron regulator RGMc
    • Kuninger D., Kuns-Hashimoto R., Kuzmickas R., et al. Complex biosynthesis of the muscle-enriched iron regulator RGMc. J. Cell Sci. 2006, 119:3273-3283.
    • (2006) J. Cell Sci. , vol.119 , pp. 3273-3283
    • Kuninger, D.1    Kuns-Hashimoto, R.2    Kuzmickas, R.3
  • 42
    • 34250308049 scopus 로고    scopus 로고
    • Evidence that inhibition of hemojuvelin shedding in response to iron is mediated through neogenin
    • Zhang A.S., Anderson S.A., Meyers K.R., et al. Evidence that inhibition of hemojuvelin shedding in response to iron is mediated through neogenin. Biol. Chem. 2007, 282:12547-12556.
    • (2007) Biol. Chem. , vol.282 , pp. 12547-12556
    • Zhang, A.S.1    Anderson, S.A.2    Meyers, K.R.3
  • 43
    • 33646228833 scopus 로고    scopus 로고
    • Tissue-specific expression of ferritin H regulates cellular iron homeostasis in vivo
    • Wilkinson J., Di X., Schönig K., et al. Tissue-specific expression of ferritin H regulates cellular iron homeostasis in vivo. Biochem. J. 2006, 395:501-507.
    • (2006) Biochem. J. , vol.395 , pp. 501-507
    • Wilkinson, J.1    Di, X.2    Schönig, K.3
  • 44
    • 0034964604 scopus 로고    scopus 로고
    • A mutation, in iron-responsive element of H ferritin mRNA, causing autosomal dominant iron overload
    • Kato J., Fujikawa K., Kanda M., et al. A mutation, in iron-responsive element of H ferritin mRNA, causing autosomal dominant iron overload. Am. J. Hum. Genet. 2001, 69:191-197.
    • (2001) Am. J. Hum. Genet. , vol.69 , pp. 191-197
    • Kato, J.1    Fujikawa, K.2    Kanda, M.3
  • 45
    • 38349194098 scopus 로고    scopus 로고
    • Furin mediated release of soluble hemojuvelin: a new link between hypoxia and iron homeostasis
    • Silvestri L., Pagani A., Camaschella C. Furin mediated release of soluble hemojuvelin: a new link between hypoxia and iron homeostasis. Blood 2008, 111:924-931.
    • (2008) Blood , vol.111 , pp. 924-931
    • Silvestri, L.1    Pagani, A.2    Camaschella, C.3
  • 46
    • 34447137331 scopus 로고    scopus 로고
    • Modulation of bone morphogenetic protein signaling in vivo regulates systemic iron balance
    • Babitt J.L., Huang F.W., Xia Y., et al. Modulation of bone morphogenetic protein signaling in vivo regulates systemic iron balance. J. Clin. Invest. 2007, 117:1933-1939.
    • (2007) J. Clin. Invest. , vol.117 , pp. 1933-1939
    • Babitt, J.L.1    Huang, F.W.2    Xia, Y.3


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