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Volumn 29, Issue 4, 2008, Pages 569-576

Manganese transport in eukaryotes: The role of DMT1

Author keywords

DMT1; Manganese; NRAMP 2; Transport

Indexed keywords

MANGANESE; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 2;

EID: 46149116517     PISSN: 0161813X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuro.2008.04.022     Document Type: Review
Times cited : (204)

References (81)
  • 1
    • 0030660482 scopus 로고    scopus 로고
    • Structure and dynamics of the iron responsive element RNA: implications for binding of the RNA by iron regulatory binding proteins
    • Addess K.J., Basilion J.P., Klausner R.D., Rouault T.A., and Pardi A. Structure and dynamics of the iron responsive element RNA: implications for binding of the RNA by iron regulatory binding proteins. J Mol Biol 274 1 (1997) 72-83
    • (1997) J Mol Biol , vol.274 , Issue.1 , pp. 72-83
    • Addess, K.J.1    Basilion, J.P.2    Klausner, R.D.3    Rouault, T.A.4    Pardi, A.5
  • 2
    • 0032829676 scopus 로고    scopus 로고
    • The iron transporter DMT1
    • Andrews N.C. The iron transporter DMT1. Int J Biochem Cell Biol 31 10 (1999) 991-994
    • (1999) Int J Biochem Cell Biol , vol.31 , Issue.10 , pp. 991-994
    • Andrews, N.C.1
  • 3
    • 0033911123 scopus 로고    scopus 로고
    • Manganese: brain transport and emerging research needs
    • Aschner M. Manganese: brain transport and emerging research needs. Environ Health Perspect 108 Suppl. 3 (2000) 429-432
    • (2000) Environ Health Perspect , vol.108 , Issue.SUPPL. 3 , pp. 429-432
    • Aschner, M.1
  • 4
    • 0025895433 scopus 로고
    • Manganese neurotoxicity: cellular effects and blood-brain barrier transport
    • Aschner M., and Aschner J.L. Manganese neurotoxicity: cellular effects and blood-brain barrier transport. Neurosci Biobehav Rev 15 3 (1991) 333-340
    • (1991) Neurosci Biobehav Rev , vol.15 , Issue.3 , pp. 333-340
    • Aschner, M.1    Aschner, J.L.2
  • 5
    • 0028366603 scopus 로고
    • Manganese (Mn) transport across the rat blood-brain barrier: saturable and transferrin-dependent transport mechanisms
    • Aschner M., and Gannon M. Manganese (Mn) transport across the rat blood-brain barrier: saturable and transferrin-dependent transport mechanisms. Brain Res Bull 33 3 (1994) 345-349
    • (1994) Brain Res Bull , vol.33 , Issue.3 , pp. 345-349
    • Aschner, M.1    Gannon, M.2
  • 6
    • 0026536560 scopus 로고
    • Manganese uptake and efflux in cultured rat astrocytes
    • Aschner M., Gannon M., and Kimelberg H.K. Manganese uptake and efflux in cultured rat astrocytes. J Neurochem 58 2 (1992) 730-735
    • (1992) J Neurochem , vol.58 , Issue.2 , pp. 730-735
    • Aschner, M.1    Gannon, M.2    Kimelberg, H.K.3
  • 8
    • 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., Delaunay J., Hetet G., Grandchamp B., de Montalembert M., and Tchernia G. Two new human DMT1 gene mutations in a patient with microcytic anemia, low ferritinemia, and liver iron overload. Blood 107 10 (2006) 4168-4170
    • (2006) Blood , vol.107 , Issue.10 , pp. 4168-4170
    • Beaumont, C.1    Delaunay, J.2    Hetet, G.3    Grandchamp, B.4    de Montalembert, M.5    Tchernia, G.6
  • 9
    • 5344275957 scopus 로고    scopus 로고
    • Phenotypic deconstruction reveals involvement of manganese transporter malvolio in honey bee division of labor
    • Ben-Shahar Y., Dudek N.L., and Robinson G.E. Phenotypic deconstruction reveals involvement of manganese transporter malvolio in honey bee division of labor. J Exp Biol 207 Pt 19 (2004) 3281-3288
    • (2004) J Exp Biol , vol.207 , Issue.PART 19 , pp. 3281-3288
    • Ben-Shahar, Y.1    Dudek, N.L.2    Robinson, G.E.3
  • 10
    • 0035892632 scopus 로고    scopus 로고
    • Distribution of divalent metal transporter 1 and metal transport protein 1 in the normal and Belgrade rat
    • Burdo J.R., Menzies S.L., Simpson I.A., Garrick L.M., Garrick M.D., Dolan K.G., et al. Distribution of divalent metal transporter 1 and metal transport protein 1 in the normal and Belgrade rat. J Neurosci Res 66 6 (2001) 1198-1207
    • (2001) J Neurosci Res , vol.66 , Issue.6 , pp. 1198-1207
    • Burdo, J.R.1    Menzies, S.L.2    Simpson, I.A.3    Garrick, L.M.4    Garrick, M.D.5    Dolan, K.G.6
  • 11
    • 0028023508 scopus 로고
    • Manganism and idiopathic parkinsonism: similarities and differences
    • Calne D.B., Chu N.S., Huang C.C., Lu C.S., and Olanow W. Manganism and idiopathic parkinsonism: similarities and differences. Neurology 44 9 (1994) 1583-1586
    • (1994) Neurology , vol.44 , Issue.9 , pp. 1583-1586
    • Calne, D.B.1    Chu, N.S.2    Huang, C.C.3    Lu, C.S.4    Olanow, W.5
  • 12
    • 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. Cellular and subcellular localization of the Nramp2 iron transporter in the intestinal brush border and regulation by dietary iron. Blood 93 12 (1999) 4406-4417
    • (1999) Blood , vol.93 , Issue.12 , pp. 4406-4417
    • Canonne-Hergaux, F.1    Gruenheid, S.2    Ponka, P.3    Gros, P.4
  • 14
    • 0031194722 scopus 로고    scopus 로고
    • Manganese metabolism is impaired in the Belgrade laboratory rat
    • Chua A.C., and Morgan E.H. Manganese metabolism is impaired in the Belgrade laboratory rat. J Comp Physiol B 167 5 (1997) 361-369
    • (1997) J Comp Physiol B , vol.167 , Issue.5 , pp. 361-369
    • Chua, A.C.1    Morgan, E.H.2
  • 15
    • 0034721927 scopus 로고    scopus 로고
    • The family of SMF metal ion transporters in yeast cells
    • Cohen A., Nelson H., and Nelson N. The family of SMF metal ion transporters in yeast cells. J Biol Chem 275 43 (2000) 33388-33394
    • (2000) J Biol Chem , vol.275 , Issue.43 , pp. 33388-33394
    • Cohen, A.1    Nelson, H.2    Nelson, N.3
  • 16
    • 33947400266 scopus 로고    scopus 로고
    • Recent progress in structure-function analyses of Nramp proton-dependent metal-ion transporters
    • Courville P., Chaloupka R., and Cellier M.F. Recent progress in structure-function analyses of Nramp proton-dependent metal-ion transporters. Biochem Cell Biol 84 6 (2006) 960-978
    • (2006) Biochem Cell Biol , vol.84 , Issue.6 , pp. 960-978
    • Courville, P.1    Chaloupka, R.2    Cellier, M.F.3
  • 17
    • 1342347993 scopus 로고    scopus 로고
    • Manganese distribution across the blood-brain barrier III. The divalent metal transporter-1 is not the major mechanism mediating brain manganese uptake
    • Crossgrove J.S., and Yokel R.A. Manganese distribution across the blood-brain barrier III. The divalent metal transporter-1 is not the major mechanism mediating brain manganese uptake. Neurotoxicology 25 3 (2004) 451-460
    • (2004) Neurotoxicology , vol.25 , Issue.3 , pp. 451-460
    • Crossgrove, J.S.1    Yokel, R.A.2
  • 18
    • 0033166065 scopus 로고    scopus 로고
    • Functional complementation of the malvolio mutation in the taste pathway of Drosophila melanogaster by the human natural resistance-associated macrophage protein 1 (Nramp-1)
    • D'Souza J., Cheah P.Y., Gros P., Chia W., and Rodrigues V. Functional complementation of the malvolio mutation in the taste pathway of Drosophila melanogaster by the human natural resistance-associated macrophage protein 1 (Nramp-1). J Exp Biol 202 Pt 14 (1999) 1909-1915
    • (1999) J Exp Biol , vol.202 , Issue.PART 14 , pp. 1909-1915
    • D'Souza, J.1    Cheah, P.Y.2    Gros, P.3    Chia, W.4    Rodrigues, V.5
  • 19
    • 0024305980 scopus 로고
    • Identification of transferrin as the major plasma carrier protein for manganese introduced orally or intravenously or after in vitro addition in the rat
    • Davidsson L., Lonnerdal B., Sandstrom B., Kunz C., and Keen C.L. Identification of transferrin as the major plasma carrier protein for manganese introduced orally or intravenously or after in vitro addition in the rat. J Nutr 119 10 (1989) 1461-1464
    • (1989) J Nutr , vol.119 , Issue.10 , pp. 1461-1464
    • Davidsson, L.1    Lonnerdal, B.2    Sandstrom, B.3    Kunz, C.4    Keen, C.L.5
  • 21
    • 2442566013 scopus 로고    scopus 로고
    • Nasal toxicity of manganese sulfate and manganese phosphate in young male rats following subchronic (13-week) inhalation exposure
    • Dorman D.C., McManus B.E., Parkinson C.U., Manuel C.A., McElveen A.M., and Everitt J.I. Nasal toxicity of manganese sulfate and manganese phosphate in young male rats following subchronic (13-week) inhalation exposure. Inhal Toxicol 16 6/7 (2004) 481-488
    • (2004) Inhal Toxicol , vol.16 , Issue.6-7 , pp. 481-488
    • Dorman, D.C.1    McManus, B.E.2    Parkinson, C.U.3    Manuel, C.A.4    McElveen, A.M.5    Everitt, J.I.6
  • 22
    • 0031845660 scopus 로고    scopus 로고
    • The molecular biology of metal ion transport in Saccharomyces cerevisiae
    • Eide D.J. The molecular biology of metal ion transport in Saccharomyces cerevisiae. Annu Rev Nutr 18 (1998) 441-469
    • (1998) Annu Rev Nutr , vol.18 , pp. 441-469
    • Eide, D.J.1
  • 23
    • 17444402049 scopus 로고    scopus 로고
    • The importance of glutamate, glycine, and gamma-aminobutyric acid transport and regulation in manganese, mercury and lead neurotoxicity
    • Fitsanakis V.A., and Aschner M. The importance of glutamate, glycine, and gamma-aminobutyric acid transport and regulation in manganese, mercury and lead neurotoxicity. Toxicol Appl Pharmacol 204 3 (2005) 343-354
    • (2005) Toxicol Appl Pharmacol , vol.204 , Issue.3 , pp. 343-354
    • Fitsanakis, V.A.1    Aschner, M.2
  • 24
    • 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., Romano M.A., Su M.A., Garrick L.M., Garrick M.D., and Andrews N.C. Nramp2 is mutated in the anemic Belgrade (b) rat: evidence of a role for Nramp2 in endosomal iron transport. Proc Natl Acad Sci USA 95 3 (1998) 1148-1153
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.3 , pp. 1148-1153
    • Fleming, M.D.1    Romano, M.A.2    Su, M.A.3    Garrick, L.M.4    Garrick, M.D.5    Andrews, N.C.6
  • 25
    • 0041940266 scopus 로고    scopus 로고
    • Iron, manganese, and cobalt transport by Nramp1 (Slc11a1) and Nramp2 (Slc11a2) expressed at the plasma membrane
    • Forbes J.R., and Gros P. Iron, manganese, and cobalt transport by Nramp1 (Slc11a1) and Nramp2 (Slc11a2) expressed at the plasma membrane. Blood 102 5 (2003) 1884-1892
    • (2003) Blood , vol.102 , Issue.5 , pp. 1884-1892
    • Forbes, J.R.1    Gros, P.2
  • 26
    • 33745801577 scopus 로고    scopus 로고
    • A manganese-enhanced diet alters brain metals and transporters in the developing brain
    • Garcia S.J., Gellein K., Syversen T., and Aschner M. A manganese-enhanced diet alters brain metals and transporters in the developing brain. Toxicol Sci 92 2 (2006) 516-525
    • (2006) Toxicol Sci , vol.92 , Issue.2 , pp. 516-525
    • Garcia, S.J.1    Gellein, K.2    Syversen, T.3    Aschner, M.4
  • 28
    • 0033103978 scopus 로고    scopus 로고
    • The iron transport protein NRAMP2 is an integral membrane glycoprotein that colocalizes with transferrin in recycling endosomes
    • Gruenheid S., Canonne-Hergaux F., Gauthier S., Hackam D.J., Grinstein S., and Gros P. The iron transport protein NRAMP2 is an integral membrane glycoprotein that colocalizes with transferrin in recycling endosomes. J Exp Med 189 5 (1999) 831-841
    • (1999) J Exp Med , 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
  • 29
    • 0028962892 scopus 로고
    • Identification and characterization of a second mouse Nramp gene
    • Gruenheid S., Cellier M., Vidal S., and Gros P. Identification and characterization of a second mouse Nramp gene. Genomics 25 2 (1995) 514-525
    • (1995) Genomics , vol.25 , Issue.2 , pp. 514-525
    • Gruenheid, S.1    Cellier, M.2    Vidal, S.3    Gros, P.4
  • 30
    • 0030755366 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian proton-coupled metal-ion transporter
    • Gunshin H., Mackenzie B., Berger U.V., Gunshin Y., Romero M.F., Boron W.F., et al. Cloning and characterization of a mammalian proton-coupled metal-ion transporter. Nature 388 6641 (1997) 482-488
    • (1997) Nature , vol.388 , Issue.6641 , pp. 482-488
    • Gunshin, H.1    Mackenzie, B.2    Berger, U.V.3    Gunshin, Y.4    Romero, M.F.5    Boron, W.F.6
  • 31
    • 33745249951 scopus 로고    scopus 로고
    • ZIP8, member of the solute-carrier-39 (SLC39) metal-transporter family: characterization of transporter properties
    • He L., Girijashanker K., Dalton T.P., Reed J., Li H., Soleimani M., et al. ZIP8, member of the solute-carrier-39 (SLC39) metal-transporter family: characterization of transporter properties. Mol Pharmacol 70 1 (2006) 171-180
    • (2006) Mol Pharmacol , vol.70 , Issue.1 , pp. 171-180
    • He, L.1    Girijashanker, K.2    Dalton, T.P.3    Reed, J.4    Li, H.5    Soleimani, M.6
  • 32
    • 4644365735 scopus 로고    scopus 로고
    • Distribution of divalent metal transporter-1 in the monkey basal ganglia
    • Huang E., Ong W.Y., and Connor J.R. Distribution of divalent metal transporter-1 in the monkey basal ganglia. Neuroscience 128 3 (2004) 487-496
    • (2004) Neuroscience , vol.128 , Issue.3 , pp. 487-496
    • Huang, E.1    Ong, W.Y.2    Connor, J.R.3
  • 33
    • 34548690553 scopus 로고    scopus 로고
    • High-throughput in vivo analysis of gene expression in Caenorhabditis elegans
    • Hunt-Newbury R., Viveiros R., Johnsen R., Mah A., Anastas D., Fang L., et al. High-throughput in vivo analysis of gene expression in Caenorhabditis elegans. PLoS Biol 5 9 (2007) e237
    • (2007) PLoS Biol , vol.5 , Issue.9
    • Hunt-Newbury, R.1    Viveiros, R.2    Johnsen, R.3    Mah, A.4    Anastas, D.5    Fang, L.6
  • 34
    • 30144443274 scopus 로고    scopus 로고
    • Microcytic anemia and hepatic iron overload in a child with compound heterozygous mutations in DMT1 (SCL11A2)
    • Iolascon A., d'Apolito M., Servedio V., Cimmino F., Piga A., and Camaschella C. Microcytic anemia and hepatic iron overload in a child with compound heterozygous mutations in DMT1 (SCL11A2). Blood 107 1 (2006) 349-354
    • (2006) Blood , vol.107 , Issue.1 , pp. 349-354
    • Iolascon, A.1    d'Apolito, M.2    Servedio, V.3    Cimmino, F.4    Piga, A.5    Camaschella, C.6
  • 35
    • 0142180122 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae high affinity phosphate transporter encoded by PHO84 also functions in manganese homeostasis
    • Jensen L.T., Ajua-Alemanji M., and Culotta V.C. The Saccharomyces cerevisiae high affinity phosphate transporter encoded by PHO84 also functions in manganese homeostasis. J Biol Chem 278 43 (2003) 42036-42040
    • (2003) J Biol Chem , vol.278 , Issue.43 , pp. 42036-42040
    • Jensen, L.T.1    Ajua-Alemanji, M.2    Culotta, V.C.3
  • 36
    • 0034527137 scopus 로고    scopus 로고
    • Calcium sequestering ability of mitochondria modulates influx of calcium through glutamate receptor channel
    • Kannurpatti S.S., Joshi P.G., and Joshi N.B. Calcium sequestering ability of mitochondria modulates influx of calcium through glutamate receptor channel. Neurochem Res 25 12 (2000) 1527-1536
    • (2000) Neurochem Res , vol.25 , Issue.12 , pp. 1527-1536
    • Kannurpatti, S.S.1    Joshi, P.G.2    Joshi, N.B.3
  • 37
    • 14644408729 scopus 로고    scopus 로고
    • Transport of divalent transition-metal ions is lost in small-intestinal tissue of b/b Belgrade rats
    • Knopfel M., Zhao L., and Garrick M.D. Transport of divalent transition-metal ions is lost in small-intestinal tissue of b/b Belgrade rats. Biochemistry 44 9 (2005) 3454-3465
    • (2005) Biochemistry , vol.44 , Issue.9 , pp. 3454-3465
    • Knopfel, M.1    Zhao, L.2    Garrick, M.D.3
  • 38
    • 33646849617 scopus 로고    scopus 로고
    • A novel R416C mutation in human DMT1 (SLC11A2) displays pleiotropic effects on function and causes microcytic anemia and hepatic iron overload
    • Lam-Yuk-Tseung S., Camaschella C., Iolascon A., and Gros P. A novel R416C mutation in human DMT1 (SLC11A2) displays pleiotropic effects on function and causes microcytic anemia and hepatic iron overload. Blood Cells Mol Dis 36 3 (2006) 347-354
    • (2006) Blood Cells Mol Dis , vol.36 , Issue.3 , pp. 347-354
    • Lam-Yuk-Tseung, S.1    Camaschella, C.2    Iolascon, A.3    Gros, P.4
  • 39
    • 24644482572 scopus 로고    scopus 로고
    • Functional characterization of the E399D DMT1/NRAMP2/SLC11A2 protein produced by an exon 12 mutation in a patient with microcytic anemia and iron overload
    • Lam-Yuk-Tseung S., Mathieu M., and Gros P. Functional characterization of the E399D DMT1/NRAMP2/SLC11A2 protein produced by an exon 12 mutation in a patient with microcytic anemia and iron overload. Blood Cells Mol Dis 35 2 (2005) 212-216
    • (2005) Blood Cells Mol Dis , vol.35 , Issue.2 , pp. 212-216
    • Lam-Yuk-Tseung, S.1    Mathieu, M.2    Gros, P.3
  • 40
    • 24644489085 scopus 로고    scopus 로고
    • Carboxyl-terminus determinants of the iron transporter DMT1/SLC11A2 isoform II (-IRE/1B) mediate internalization from the plasma membrane into recycling endosomes
    • Lam-Yuk-Tseung S., Touret N., Grinstein S., and Gros P. Carboxyl-terminus determinants of the iron transporter DMT1/SLC11A2 isoform II (-IRE/1B) mediate internalization from the plasma membrane into recycling endosomes. Biochemistry 44 36 (2005) 12149-12159
    • (2005) Biochemistry , vol.44 , Issue.36 , pp. 12149-12159
    • Lam-Yuk-Tseung, S.1    Touret, N.2    Grinstein, S.3    Gros, P.4
  • 41
    • 0032104739 scopus 로고    scopus 로고
    • The human Nramp2 gene: characterization of the gene structure, alternative splicing, promoter region and polymorphisms
    • Lee P.L., Gelbart T., West C., Halloran C., and Beutler E. The human Nramp2 gene: characterization of the gene structure, alternative splicing, promoter region and polymorphisms. Blood Cells Mol Dis 24 2 (1998) 199-215
    • (1998) Blood Cells Mol Dis , vol.24 , Issue.2 , pp. 199-215
    • Lee, P.L.1    Gelbart, T.2    West, C.3    Halloran, C.4    Beutler, E.5
  • 42
    • 0035930436 scopus 로고    scopus 로고
    • Manganese stimulates stellation of cultured rat cortical astrocytes
    • Liao S.L., and Chen C.J. Manganese stimulates stellation of cultured rat cortical astrocytes. Neuroreport 12 18 (2001) 3877-3881
    • (2001) Neuroreport , vol.12 , Issue.18 , pp. 3877-3881
    • Liao, S.L.1    Chen, C.J.2
  • 43
    • 0033021618 scopus 로고    scopus 로고
    • Mutational analysis of Saccharomyces cerevisiae Smf1p, a member of the Nramp family of metal transporters
    • Liu X.F., and Culotta V.C. Mutational analysis of Saccharomyces cerevisiae Smf1p, a member of the Nramp family of metal transporters. J Mol Biol 289 4 (1999) 885-891
    • (1999) J Mol Biol , vol.289 , Issue.4 , pp. 885-891
    • Liu, X.F.1    Culotta, V.C.2
  • 44
    • 0001352978 scopus 로고    scopus 로고
    • Post-translation control of Nramp metal transport in yeast. Role of metal ions and the BSD2 gene
    • Liu X.F., and Culotta V.C. Post-translation control of Nramp metal transport in yeast. Role of metal ions and the BSD2 gene. J Biol Chem 274 8 (1999) 4863-4868
    • (1999) J Biol Chem , vol.274 , Issue.8 , pp. 4863-4868
    • Liu, X.F.1    Culotta, V.C.2
  • 45
    • 0030883645 scopus 로고    scopus 로고
    • Manganese transport through human erythrocyte membranes. An EPR study
    • Lucaciu C.M., Dragu C., Copaescu L., and Morariu V.V. Manganese transport through human erythrocyte membranes. An EPR study. Biochim Biophys Acta 1328 2 (1997) 90-98
    • (1997) Biochim Biophys Acta , vol.1328 , Issue.2 , pp. 90-98
    • Lucaciu, C.M.1    Dragu, C.2    Copaescu, L.3    Morariu, V.V.4
  • 46
    • 0035861588 scopus 로고    scopus 로고
    • Manganese superoxide dismutase in Saccharomyces cerevisiae acquires its metal co-factor through a pathway involving the Nramp metal transporter, Smf2p
    • Luk E.E., and Culotta V.C. Manganese superoxide dismutase in Saccharomyces cerevisiae acquires its metal co-factor through a pathway involving the Nramp metal transporter, Smf2p. J Biol Chem 276 50 (2001) 47556-47562
    • (2001) J Biol Chem , vol.276 , Issue.50 , pp. 47556-47562
    • Luk, E.E.1    Culotta, V.C.2
  • 47
    • 0033134765 scopus 로고    scopus 로고
    • Existing and emerging mechanisms for transport of iron and manganese to the brain
    • Malecki E.A., Devenyi A.G., Beard J.L., and Connor J.R. Existing and emerging mechanisms for transport of iron and manganese to the brain. J Neurosci Res 56 2 (1999) 113-122
    • (1999) J Neurosci Res , vol.56 , Issue.2 , pp. 113-122
    • Malecki, E.A.1    Devenyi, A.G.2    Beard, J.L.3    Connor, J.R.4
  • 48
    • 12844260664 scopus 로고    scopus 로고
    • Identification of a human mutation of DMT1 in a patient with microcytic anemia and iron overload
    • Mims M.P., Guan Y., Pospisilova D., Priwitzerova M., Indrak K., Ponka P., et al. Identification of a human mutation of DMT1 in a patient with microcytic anemia and iron overload. Blood 105 3 (2005) 1337-1342
    • (2005) Blood , vol.105 , Issue.3 , pp. 1337-1342
    • Mims, M.P.1    Guan, Y.2    Pospisilova, D.3    Priwitzerova, M.4    Indrak, K.5    Ponka, P.6
  • 49
    • 0026331709 scopus 로고
    • Saturable transport of manganese(II) across the rat blood-brain barrier
    • Murphy V.A., Wadhwani K.C., Smith Q.R., and Rapoport S.I. Saturable transport of manganese(II) across the rat blood-brain barrier. J Neurochem 57 3 (1991) 948-954
    • (1991) J Neurochem , vol.57 , Issue.3 , pp. 948-954
    • Murphy, V.A.1    Wadhwani, K.C.2    Smith, Q.R.3    Rapoport, S.I.4
  • 50
    • 0033575729 scopus 로고    scopus 로고
    • Metal ion transporters and homeostasis
    • Nelson N. Metal ion transporters and homeostasis. EMBO J 18 16 (1999) 4361-4371
    • (1999) EMBO J , vol.18 , Issue.16 , pp. 4361-4371
    • Nelson, N.1
  • 51
    • 38349052169 scopus 로고    scopus 로고
    • Site-directed mutagenesis investigation of coupling properties of metal ion transport by DCT1
    • Nevo Y. Site-directed mutagenesis investigation of coupling properties of metal ion transport by DCT1. Biochim Biophys Acta 1778 1 (2007) 334-341
    • (2007) Biochim Biophys Acta , vol.1778 , Issue.1 , pp. 334-341
    • Nevo, Y.1
  • 52
    • 1842504319 scopus 로고    scopus 로고
    • Manganese-induced parkinsonism and Parkinson's disease
    • Olanow C.W. Manganese-induced parkinsonism and Parkinson's disease. Ann NY Acad Sci 1012 (2004) 209-223
    • (2004) Ann NY Acad Sci , vol.1012 , pp. 209-223
    • Olanow, C.W.1
  • 53
    • 0031933728 scopus 로고    scopus 로고
    • Metal ions suppress the abnormal taste behavior of the Drosophila mutant malvolio
    • Orgad S., Nelson H., Segal D., and Nelson N. Metal ions suppress the abnormal taste behavior of the Drosophila mutant malvolio. J Exp Biol 201 Pt 1 (1998) 115-120
    • (1998) J Exp Biol , vol.201 , Issue.PART 1 , pp. 115-120
    • Orgad, S.1    Nelson, H.2    Segal, D.3    Nelson, N.4
  • 54
    • 7044245930 scopus 로고    scopus 로고
    • Health and environmental testing of manganese exhaust products from use of methylcyclopentadienyl manganese tricarbonyl in gasoline
    • Pfeifer G.D., Roper J.M., Dorman D., and Lynam D.R. Health and environmental testing of manganese exhaust products from use of methylcyclopentadienyl manganese tricarbonyl in gasoline. Sci Total Environ 334-335 (2004) 397-408
    • (2004) Sci Total Environ , vol.334-335 , pp. 397-408
    • Pfeifer, G.D.1    Roper, J.M.2    Dorman, D.3    Lynam, D.R.4
  • 55
    • 0030684012 scopus 로고    scopus 로고
    • Functional complementation of the yeast divalent cation transporter family SMF by NRAMP2, a member of the mammalian natural resistance-associated macrophage protein family
    • Pinner E., Gruenheid S., Raymond M., and Gros P. Functional complementation of the yeast divalent cation transporter family SMF by NRAMP2, a member of the mammalian natural resistance-associated macrophage protein family. J Biol Chem 272 46 (1997) 28933-28938
    • (1997) J Biol Chem , vol.272 , Issue.46 , pp. 28933-28938
    • Pinner, E.1    Gruenheid, S.2    Raymond, M.3    Gros, P.4
  • 56
    • 0037084179 scopus 로고    scopus 로고
    • The distinct methods by which manganese and iron regulate the Nramp transporters in yeast
    • Portnoy M.E., Jensen L.T., and Culotta V.C. The distinct methods by which manganese and iron regulate the Nramp transporters in yeast. Biochem J 362 Pt 1 (2002) 119-124
    • (2002) Biochem J , vol.362 , Issue.PART 1 , pp. 119-124
    • Portnoy, M.E.1    Jensen, L.T.2    Culotta, V.C.3
  • 57
    • 0033773040 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae expresses three functionally distinct homologues of the nramp family of metal transporters
    • Portnoy M.E., Liu X.F., and Culotta V.C. Saccharomyces cerevisiae expresses three functionally distinct homologues of the nramp family of metal transporters. Mol Cell Biol 20 21 (2000) 7893-7902
    • (2000) Mol Cell Biol , vol.20 , Issue.21 , pp. 7893-7902
    • Portnoy, M.E.1    Liu, X.F.2    Culotta, V.C.3
  • 58
    • 0033616579 scopus 로고    scopus 로고
    • Manganese oxide minerals: crystal structures and economic and environmental significance
    • Post J.E. Manganese oxide minerals: crystal structures and economic and environmental significance. Proc Natl Acad Sci USA 96 7 (1999) 3447-3454
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.7 , pp. 3447-3454
    • Post, J.E.1
  • 59
    • 28444482404 scopus 로고    scopus 로고
    • Functional consequences of the human DMT1 (SLC11A2) mutation on protein expression and iron uptake
    • Priwitzerova M., Nie G., Sheftel A.D., Pospisilova D., Divoky V., and Ponka P. Functional consequences of the human DMT1 (SLC11A2) mutation on protein expression and iron uptake. Blood 106 12 (2005) 3985-3987
    • (2005) Blood , vol.106 , Issue.12 , pp. 3985-3987
    • Priwitzerova, M.1    Nie, G.2    Sheftel, A.D.3    Pospisilova, D.4    Divoky, V.5    Ponka, P.6
  • 60
    • 0023253286 scopus 로고
    • Functions of trace elements in brain metabolism
    • Prohaska J.R. Functions of trace elements in brain metabolism. Physiol Rev 67 3 (1987) 858-901
    • (1987) Physiol Rev , vol.67 , Issue.3 , pp. 858-901
    • Prohaska, J.R.1
  • 61
    • 0027293473 scopus 로고
    • Rapid brain uptake of manganese(II) across the blood-brain barrier
    • Rabin O., Hegedus L., Bourre J.M., and Smith Q.R. Rapid brain uptake of manganese(II) across the blood-brain barrier. J Neurochem 61 2 (1993) 509-517
    • (1993) J Neurochem , vol.61 , Issue.2 , pp. 509-517
    • Rabin, O.1    Hegedus, L.2    Bourre, J.M.3    Smith, Q.R.4
  • 62
    • 0033457543 scopus 로고    scopus 로고
    • Manganese speciation in exhaust particulates of automobiles using MMT-containing gasoline
    • Ressler T., Wong J., and Roos J. Manganese speciation in exhaust particulates of automobiles using MMT-containing gasoline. J Synchrotron Radiat 6 Pt 3 (1999) 656-658
    • (1999) J Synchrotron Radiat , vol.6 , Issue.PART 3 , pp. 656-658
    • Ressler, T.1    Wong, J.2    Roos, J.3
  • 64
    • 0028797538 scopus 로고
    • Malvolio, the Drosophila homologue of mouse NRAMP-1 (Bcg), is expressed in macrophages and in the nervous system and is required for normal taste behaviour
    • Rodrigues V., Cheah P.Y., Ray K., and Chia W. Malvolio, the Drosophila homologue of mouse NRAMP-1 (Bcg), is expressed in macrophages and in the nervous system and is required for normal taste behaviour. EMBO J 14 13 (1995) 3007-3020
    • (1995) EMBO J , vol.14 , Issue.13 , pp. 3007-3020
    • Rodrigues, V.1    Cheah, P.Y.2    Ray, K.3    Chia, W.4
  • 65
    • 5044226831 scopus 로고    scopus 로고
    • Blood manganese concentrations among first-grade schoolchildren in two South African cities
    • Rollin H., Mathee A., Levin J., Theodorou P., and Wewers F. Blood manganese concentrations among first-grade schoolchildren in two South African cities. Environ Res 97 1 (2005) 93-99
    • (2005) Environ Res , vol.97 , Issue.1 , pp. 93-99
    • Rollin, H.1    Mathee, A.2    Levin, J.3    Theodorou, P.4    Wewers, F.5
  • 67
    • 0035744950 scopus 로고    scopus 로고
    • Properties of the mammalian and yeast metal-ion transporters DCT1 and Smf1p expressed in Xenopus laevis oocytes
    • Sacher A., Cohen A., and Nelson N. Properties of the mammalian and yeast metal-ion transporters DCT1 and Smf1p expressed in Xenopus laevis oocytes. J Exp Biol 204 Pt 6 (2001) 1053-1061
    • (2001) J Exp Biol , vol.204 , Issue.PART 6 , pp. 1053-1061
    • Sacher, A.1    Cohen, A.2    Nelson, N.3
  • 68
    • 0032530922 scopus 로고    scopus 로고
    • The G185R mutation disrupts function of the iron transporter Nramp2
    • Su M.A., Trenor C.C., Fleming J.C., Fleming M.D., and Andrews N.C. The G185R mutation disrupts function of the iron transporter Nramp2. Blood 92 6 (1998) 2157-2163
    • (1998) Blood , vol.92 , Issue.6 , pp. 2157-2163
    • Su, M.A.1    Trenor, C.C.2    Fleming, J.C.3    Fleming, M.D.4    Andrews, N.C.5
  • 69
    • 0029978512 scopus 로고    scopus 로고
    • A yeast manganese transporter related to the macrophage protein involved in conferring resistance to mycobacteria
    • Supek F., Supekova L., Nelson H., and Nelson N. A yeast manganese transporter related to the macrophage protein involved in conferring resistance to mycobacteria. Proc Natl Acad Sci USA 93 10 (1996) 5105-5110
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.10 , pp. 5105-5110
    • Supek, F.1    Supekova, L.2    Nelson, H.3    Nelson, N.4
  • 70
    • 0034698023 scopus 로고    scopus 로고
    • Human NRAMP2/DMT1, which mediates iron transport across endosomal membranes, is localized to late endosomes and lysosomes in HEp-2 cells
    • Tabuchi M., Yoshimori T., Yamaguchi K., Yoshida T., and Kishi F. Human NRAMP2/DMT1, which mediates iron transport across endosomal membranes, is localized to late endosomes and lysosomes in HEp-2 cells. J Biol Chem 275 29 (2000) 22220-22228
    • (2000) J Biol Chem , vol.275 , Issue.29 , pp. 22220-22228
    • Tabuchi, M.1    Yoshimori, T.2    Yamaguchi, K.3    Yoshida, T.4    Kishi, F.5
  • 71
    • 0037222388 scopus 로고    scopus 로고
    • Manganese action in brain function
    • Takeda A. Manganese action in brain function. Brain Res Brain Res Rev 41 1 (2003) 79-87
    • (2003) Brain Res Brain Res Rev , vol.41 , Issue.1 , pp. 79-87
    • Takeda, A.1
  • 72
    • 0033984237 scopus 로고    scopus 로고
    • Nramp2 expression is associated with pH-dependent iron uptake across the apical membrane of human intestinal Caco-2 cells
    • Tandy S., Williams M., Leggett A., Lopez-Jimenez M., Dedes M., Ramesh B., et al. Nramp2 expression is associated with pH-dependent iron uptake across the apical membrane of human intestinal Caco-2 cells. J Biol Chem 275 2 (2000) 1023-1029
    • (2000) J Biol Chem , vol.275 , Issue.2 , pp. 1023-1029
    • Tandy, S.1    Williams, M.2    Leggett, A.3    Lopez-Jimenez, M.4    Dedes, M.5    Ramesh, B.6
  • 74
    • 0015131535 scopus 로고
    • Interrelation of intestinal transport system for manganese and iron
    • Thomson A.B., Olatunbosun D., and Valverg L.S. Interrelation of intestinal transport system for manganese and iron. J Lab Clin Med 78 4 (1971) 642-655
    • (1971) J Lab Clin Med , vol.78 , Issue.4 , pp. 642-655
    • Thomson, A.B.1    Olatunbosun, D.2    Valverg, L.S.3
  • 75
    • 0038491413 scopus 로고    scopus 로고
    • Dynamic traffic through the recycling compartment couples the metal transporter Nramp2 (DMT1) with the transferrin receptor
    • Touret N., Furuya W., Forbes J., Gros P., and Grinstein S. Dynamic traffic through the recycling compartment couples the metal transporter Nramp2 (DMT1) with the transferrin receptor. J Biol Chem 278 28 (2003) 25548-25557
    • (2003) J Biol Chem , vol.278 , Issue.28 , pp. 25548-25557
    • Touret, N.1    Furuya, W.2    Forbes, J.3    Gros, P.4    Grinstein, S.5
  • 76
    • 0029278789 scopus 로고
    • Cloning and characterization of a second human NRAMP gene on chromosome 12q13
    • Vidal S., Belouchi A.M., Cellier M., Beatty B., and Gros P. Cloning and characterization of a second human NRAMP gene on chromosome 12q13. Mamm Genome 6 4 (1995) 224-230
    • (1995) Mamm Genome , vol.6 , Issue.4 , pp. 224-230
    • Vidal, S.1    Belouchi, A.M.2    Cellier, M.3    Beatty, B.4    Gros, P.5
  • 77
    • 33745907562 scopus 로고    scopus 로고
    • Upregulation of DMT1 expression in choroidal epithelia of the blood-CSF barrier following manganese exposure in vitro
    • Wang X., Li G.J., and Zheng W. Upregulation of DMT1 expression in choroidal epithelia of the blood-CSF barrier following manganese exposure in vitro. Brain Res 1097 1 (2006) 1-10
    • (2006) Brain Res , vol.1097 , Issue.1 , pp. 1-10
    • Wang, X.1    Li, G.J.2    Zheng, W.3
  • 78
    • 0035732296 scopus 로고    scopus 로고
    • A light and electron microscopic study of the iron transporter protein DMT-1 in the monkey cerebral neocortex and hippocampus
    • Wang X.S., Ong W.Y., and Connor J.R. A light and electron microscopic study of the iron transporter protein DMT-1 in the monkey cerebral neocortex and hippocampus. J Neurocytol 30 4 (2001) 353-360
    • (2001) J Neurocytol , vol.30 , Issue.4 , pp. 353-360
    • Wang, X.S.1    Ong, W.Y.2    Connor, J.R.3
  • 79
    • 0021728238 scopus 로고
    • Glutamine synthetase: the major Mn(II) enzyme in mammalian brain
    • Wedler F.C., and Denman R.B. Glutamine synthetase: the major Mn(II) enzyme in mammalian brain. Curr Top Cell Regul 24 (1984) 153-169
    • (1984) Curr Top Cell Regul , vol.24 , pp. 153-169
    • Wedler, F.C.1    Denman, R.B.2
  • 80
    • 0020477024 scopus 로고
    • Glutamine synthetase from ovine brain is a manganese(II) enzyme
    • Wedler F.C., Denman R.B., and Roby W.G. Glutamine synthetase from ovine brain is a manganese(II) enzyme. Biochemistry 21 25 (1982) 6389-6396
    • (1982) Biochemistry , vol.21 , Issue.25 , pp. 6389-6396
    • Wedler, F.C.1    Denman, R.B.2    Roby, W.G.3
  • 81
    • 0026491078 scopus 로고
    • Two related genes encoding extremely hydrophobic proteins suppress a lethal mutation in the yeast mitochondrial processing enhancing protein
    • West A.H., Clark D.J., Martin J., Neupert W., Hartl F.U., and Horwich A.L. Two related genes encoding extremely hydrophobic proteins suppress a lethal mutation in the yeast mitochondrial processing enhancing protein. J Biol Chem 267 34 (1992) 24625-24633
    • (1992) J Biol Chem , vol.267 , Issue.34 , pp. 24625-24633
    • West, A.H.1    Clark, D.J.2    Martin, J.3    Neupert, W.4    Hartl, F.U.5    Horwich, A.L.6


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