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Volumn 287, Issue 41, 2012, Pages 34032-34043

ZIP8 is an iron and zinc transporter whose cell-surface expression is up-regulated by cellular iron loading

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE RESIDUE; CELL LINES; CELL SURFACE EXPRESSION; CELL SURFACES; ENDOSOMES; EXPRESSION PROFILE; GLYCOSYLATED; HEPATOMA CELLS; HUMAN TISSUES; IMMUNOFLUORESCENCE ANALYSIS; IRON LOADING; IRON METABOLISM; IRON TRANSPORT; IRON TRANSPORT PROTEINS; N-GLYCOSYLATION; PH DEPENDENCE; REDUCED IRON; SITE DIRECTED MUTAGENESIS; SUBCELLULAR LOCALIZATIONS; XENOPUS OOCYTE; ZINC TRANSPORT; ZINC TRANSPORTERS;

EID: 84867249792     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.367284     Document Type: Article
Times cited : (308)

References (63)
  • 1
    • 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, A. O., Direnzo, C., Robine, S., and Andrews, N. C. (2005) Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver. J. Clin. Invest. 115, 1258-1266 (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
  • 4
    • 11844279752 scopus 로고    scopus 로고
    • Structure-function analysis of a novel member of the LIV-1 subfamily of zinc transporters, ZIP14
    • DOI 10.1016/j.febslet.2004.12.006, PII S0014579304015303
    • Taylor, K. M., Morgan, H. E., Johnson, A., and Nicholson, R. I. (2005) Structure-function analysis of a novel member of the LIV-1 subfamily of zinc transporters, ZIP14. FEBS Lett. 579, 427-432 (Pubitemid 40092422)
    • (2005) FEBS Letters , vol.579 , Issue.2 , pp. 427-432
    • Taylor, K.M.1    Morgan, H.E.2    Johnson, A.3    Nicholson, R.I.4
  • 6
    • 34147189116 scopus 로고    scopus 로고
    • Functional properties of multiple isoforms of human divalent metal-ion transporter 1 (DMT1)
    • DOI 10.1042/BJ20061290
    • Mackenzie, B., Takanaga, H., Hubert, N., Rolfs, A., and Hediger, M. A. (2007) Functional properties of multiple isoforms of human divalent metal-ion transporter 1 (DMT1). Biochem. J. 403, 59-69 (Pubitemid 46569867)
    • (2007) Biochemical Journal , vol.403 , Issue.1 , pp. 59-69
    • Mackenzie, B.1    Takanaga, H.2    Hubert, N.3    Rolfs, A.4    Hediger, M.A.5
  • 8
    • 0033984237 scopus 로고    scopus 로고
    • Nramp2 expression is associated with pH-dependent iron uptake across the apical membrane of human intestinal Caco-2 cells
    • DOI 10.1074/jbc.275.2.1023
    • Tandy, S., Williams, M., Leggett, A., Lopez-Jimenez, M., Dedes, M., Ramesh, B., Srai, S. K., and Sharp, P. (2000) Nramp2 expression is associated with pH-dependent iron uptake across the apical membrane of human intestinal Caco-2 cells. J. Biol. Chem. 275, 1023-1029 (Pubitemid 30051149)
    • (2000) Journal of Biological Chemistry , 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    Srai, S.K.7    Sharp, P.8
  • 10
    • 77957783944 scopus 로고    scopus 로고
    • ZRT/IRT-like protein 14 (ZIP14) promotes the cellular assimilation of iron from transferrin
    • Zhao, N., Gao, J., Enns, C. A., and Knutson, M. D. (2010) ZRT/IRT-like protein 14 (ZIP14) promotes the cellular assimilation of iron from transferrin. J. Biol. Chem. 285, 32141-32150
    • (2010) J. Biol. Chem. , vol.285 , pp. 32141-32150
    • Zhao, N.1    Gao, J.2    Enns, C.A.3    Knutson, M.D.4
  • 12
    • 0035983839 scopus 로고    scopus 로고
    • IRT1, an Arabidopsis transporter essential for iron uptake from the soil and for plant growth
    • DOI 10.1105/tpc.001388
    • Vert, G., Grotz, N., Dédaldéchamp, F., Gaymard, F., Guerinot, M. L., Briat, J. F., and Curie, C. (2002) IRT1, an Arabidopsis transporter essential for iron uptake from the soil and for plant growth. Plant Cell 14, 1223-1233 (Pubitemid 34780429)
    • (2002) Plant Cell , vol.14 , Issue.6 , pp. 1223-1233
    • Vert, G.1    Grotz, N.2    Dedaldechamp, F.3    Gaymard, F.4    Guerinot, M.L.5    Briat, J.-F.6    Curie, C.7
  • 13
    • 0034965318 scopus 로고    scopus 로고
    • Arabidopsis IRT2 gene encodes a root-periphery iron transporter
    • DOI 10.1046/j.1365-313X.2001.01018.x
    • Vert, G., Briat, J. F., and Curie, C. (2001) Arabidopsis IRT2 gene encodes a root-periphery iron transporter. Plant J. 26, 181-189 (Pubitemid 32532725)
    • (2001) Plant Journal , vol.26 , Issue.2 , pp. 181-189
    • Vert, G.1    Briat, J.-F.2    Curie, C.3
  • 14
    • 14244251491 scopus 로고    scopus 로고
    • The metal permease ZupT from Escherichia coli is a transporter with a broad substrate spectrum
    • DOI 10.1128/JB.187.5.1604-1611.2005
    • Grass, G., Franke, S., Taudte, N., Nies, D. H., Kucharski, L. M., Maguire, M. E., and Rensing, C. (2005) The metal permease ZupT from Escherichia coli is a transporter with a broad substrate spectrum. J. Bacteriol. 187, 1604-1611 (Pubitemid 40289360)
    • (2005) Journal of Bacteriology , vol.187 , Issue.5 , pp. 1604-1611
    • Grass, G.1    Franke, S.2    Taudte, N.3    Nies, D.H.4    Kucharski, L.M.5    Maguire, M.E.6    Rensing, C.7
  • 15
    • 33749325014 scopus 로고    scopus 로고
    • A Leishmania amazonensis ZIP family iron transporter is essential for parasite replication within macrophage phagolysosomes
    • DOI 10.1084/jem.20060559
    • Huynh, C., Sacks, D. L., and Andrews, N. W. (2006) A Leishmania amazonensis ZIP family iron transporter is essential for parasite replication within macrophage phagolysosomes. J. Exp. Med. 203, 2363-2375 (Pubitemid 44498370)
    • (2006) Journal of Experimental Medicine , vol.203 , Issue.10 , pp. 2363-2375
    • Huynh, C.1    Sacks, D.L.2    Andrews, N.W.3
  • 16
    • 84864923612 scopus 로고    scopus 로고
    • Physiologic implications of metal-ion transport by ZIP14 and ZIP8
    • Jenkitkasemwong, S., Wang, C. Y., Mackenzie, B., and Knutson, M. D. (2012) Physiologic implications of metal-ion transport by ZIP14 and ZIP8. Biometals 25, 643-655
    • (2012) Biometals , vol.25 , pp. 643-655
    • Jenkitkasemwong, S.1    Wang, C.Y.2    Mackenzie, B.3    Knutson, M.D.4
  • 17
    • 0031794474 scopus 로고    scopus 로고
    • Sequence analyses and phylogenetic characterization of the ZIP family of metal ion transport proteins
    • DOI 10.1007/s002329900442
    • Eng, B. H., Guerinot, M. L., Eide, D., and Saier, M. H., Jr. (1998) Sequence analyses and phylogenetic characterization of the ZIP family of metal ion transport proteins. J. Membr. Biol. 166, 1-7 (Pubitemid 28516079)
    • (1998) Journal of Membrane Biology , vol.166 , Issue.1 , pp. 1-7
    • Eng, B.H.1    Guerinot, M.L.2    Eide, D.3    Saier Jr., M.H.4
  • 18
    • 0036939017 scopus 로고    scopus 로고
    • Mycobacterium bovis BCG cell wall and lipopolysaccharide induce a novel gene, BIGM103, encoding a 7-TM protein: Identification of a new protein family having Zn-transporter and Zn-metalloprotease signatures
    • DOI 10.1006/geno.2002.7000
    • Begum, N. A., Kobayashi, M., Moriwaki, Y., Matsumoto, M., Toyoshima, K., and Seya, T. (2002) Mycobacterium bovis BCG cell wall and lipopolysaccharide induce a novel gene, BIGM103, encoding a 7-TM protein. Identification of a new protein family having Zn-transporter and Zn-metalloprotease signatures. Genomics 80, 630-645 (Pubitemid 36062651)
    • (2002) Genomics , vol.80 , Issue.6 , pp. 630-645
    • Begum, N.A.1    Kobayashi, M.2    Moriwaki, Y.3    Matsumoto, M.4    Toyoshima, K.5    Seya, T.6
  • 19
    • 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., and Nebert, D. W. (2006) ZIP8, member of the solute-carrier-39 (SLC39) metal-transporter family. Characterization of transporter properties. Mol. Pharmacol. 70, 171-180
    • (2006) Mol. Pharmacol. , vol.70 , pp. 171-180
    • He, L.1    Girijashanker, K.2    Dalton, T.P.3    Reed, J.4    Li, H.5    Soleimani, M.6    Nebert, D.W.7
  • 20
    • 0037608596 scopus 로고    scopus 로고
    • Selected techniques in membrane transport
    • (Van Winkle, L. J., ed) Academic Press, San Diego, CA
    • Mackenzie, B. (1999) Selected techniques in membrane transport, in Biomembrane Transport (Van Winkle, L. J., ed) pp. 327-342, Academic Press, San Diego, CA
    • (1999) Biomembrane Transport , pp. 327-342
    • Mackenzie, B.1
  • 21
    • 0036133984 scopus 로고    scopus 로고
    • Generation of epitope-tagged proteins by inverse polymerase chain reaction mutagenesis
    • Gama, L., and Breitwieser, G. E. (2002) Generation of epitope-tagged proteins by inverse polymerase chain reaction mutagenesis. Methods Mol. Biol. 182, 77-83
    • (2002) Methods Mol. Biol. , vol.182 , pp. 77-83
    • Gama, L.1    Breitwieser, G.E.2
  • 22
    • 84861214679 scopus 로고    scopus 로고
    • Effect of dietary iron deficiency and overload on the expression of ZIP metal-ion transporters in rat liver
    • Nam, H., and Knutson, M. D. (2012) Effect of dietary iron deficiency and overload on the expression of ZIP metal-ion transporters in rat liver. Biometals 25, 115-124
    • (2012) Biometals , vol.25 , pp. 115-124
    • Nam, H.1    Knutson, M.D.2
  • 23
    • 4444226451 scopus 로고    scopus 로고
    • Nontransferrin-bound iron uptake by hepatocytes is increased in the Hfe knockout mouse model of hereditary hemochromatosis
    • DOI 10.1182/blood-2003-11-3872
    • Chua, A. C., Olynyk, J. K., Leedman, P. J., and Trinder, D. (2004) Nontransferrin-bound iron uptake by hepatocytes is increased in the Hfe knockout mouse model of hereditary hemochromatosis. Blood 104, 1519-1525 (Pubitemid 39166533)
    • (2004) Blood , vol.104 , Issue.5 , pp. 1519-1525
    • Chua, A.C.G.1    Olynyk, J.K.2    Leedman, P.J.3    Trinder, D.4
  • 26
    • 0024953316 scopus 로고
    • Transferrin receptor expression in normal, iron-deficient and iron-overloaded rats
    • Lu, J. P., Hayashi, K., and Awai, M. (1989) Transferrin receptor expression in normal, iron-deficient and iron-overloaded rats. Acta Pathol. Jpn. 39, 759-764 (Pubitemid 20090090)
    • (1989) Acta Pathologica Japonica , vol.39 , Issue.12 , pp. 759-764
    • Lu, J.-P.1    Hayashi, K.2    Awai, M.3
  • 27
    • 0026085602 scopus 로고
    • Transferrin receptor expression and the regulation of placental iron uptake
    • Bierings, M. B., Baert, M. R., van Eijk, H. G., and van Dijk, J. P. (1991) Transferrin receptor expression and the regulation of placental iron uptake. Mol. Cell. Biochem. 100, 31-38
    • (1991) Mol. Cell. Biochem. , vol.100 , pp. 31-38
    • Bierings, M.B.1    Baert, M.R.2    Van Eijk, H.G.3    Van Dijk, J.P.4
  • 29
    • 0142009677 scopus 로고    scopus 로고
    • Structure-function analysis of LIV-1, the breast cancer-associated protein that belongs to a new subfamily of zinc transporters
    • DOI 10.1042/BJ20030478
    • Taylor, K. M., Morgan, H. E., Johnson, A., Hadley, L. J., and Nicholson, R. I. (2003) Structure-function analysis of LIV-1, the breast cancer-associated protein that belongs to a new subfamily of zinc transporters. Biochem. J. 375, 51-59 (Pubitemid 37255381)
    • (2003) Biochemical Journal , vol.375 , Issue.1 , pp. 51-59
    • Taylor, K.M.1    Morgan, H.E.2    Johnson, A.3    Hadley, L.J.4    Nicholson, R.I.5
  • 30
    • 0024564712 scopus 로고
    • Non-transferrin-bound iron in plasma or serum from patients with idiopathic hemochromatosis. Characterization by high performance liquid chromatography and nuclear magnetic resonance spectroscopy
    • Grootveld, M., Bell, J. D., Halliwell, B., Aruoma, O. I., Bomford, A., and Sadler, P. J. (1989) Non-transferrin-bound iron in plasma or serum from patients with idiopathic hemochromatosis. Characterization by high performance liquid chromatography and nuclear magnetic resonance spectroscopy. J. Biol. Chem. 264, 4417-4422 (Pubitemid 19081342)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.8 , pp. 4417-4422
    • Grootveld, M.1    Bell, J.D.2    Halliwell, B.3    Aruoma, O.I.4    Bomford, A.5    Sadler, P.J.6
  • 31
    • 0011938460 scopus 로고
    • Tissue distribution and clearance kinetics of non-transferrin-bound iron in the hypotransferrinemic mouse: A rodent model for hemochromatosis
    • DOI 10.1073/pnas.84.10.3457
    • Craven, C. M., Alexander, J., Eldridge, M., Kushner, J. P., Bernstein, S., and Kaplan, J. (1987) Tissue distribution and clearance kinetics of non-transferrin-bound iron in the hypotransferrinemic mouse. A rodent model for hemochromatosis. Proc. Natl. Acad. Sci. U.S.A. 84, 3457-3461 (Pubitemid 17085423)
    • (1987) Proceedings of the National Academy of Sciences of the United States of America , vol.84 , Issue.10 , pp. 3457-3461
    • Craven, C.M.1    Alexander, J.2    Eldridge, M.3
  • 32
    • 0041308113 scopus 로고    scopus 로고
    • Role of non-transferrin-bound iron in the pathogenesis of iron overload and toxicity
    • Brissot, P., and Loréal, O. (2002) Role of non-transferrin-bound iron in the pathogenesis of iron overload and toxicity. Adv. Exp. Med. Biol. 509, 45-53
    • (2002) Adv. Exp. Med. Biol. , vol.509 , pp. 45-53
    • Brissot, P.1    Loréal, O.2
  • 34
    • 0028244452 scopus 로고
    • Uptake of non-transferrin-bound iron by both reductive and nonreductive processes is modulated by intracellular iron
    • Randell, E. W., Parkes, J. G., Olivieri, N. F., and Templeton, D. M. (1994) Uptake of non-transferrin-bound iron by both reductive and nonreductive processes is modulated by intracellular iron. J. Biol. Chem. 269, 16046-16053 (Pubitemid 24209290)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.23 , pp. 16046-16053
    • Randell, E.W.1    Parkes, J.G.2    Olivieri, N.F.3    Templeton, D.M.4
  • 35
    • 0033083678 scopus 로고    scopus 로고
    • Activation of an iron uptake mechanism from transferrin in hepatocytes by small-molecular-weight iron complexes: Implications for the pathogenesis of iron-overload disease
    • DOI 10.1016/S0022-2143(99)90007-0
    • Richardson, D. R., Chua, A. C., and Baker, E. (1999) Activation of an iron uptake mechanism from transferrin in hepatocytes by small-molecular-weight iron complexes. Implications for the pathogenesis of iron-overload disease. J. Lab. Clin. Med. 133, 144-151 (Pubitemid 29073238)
    • (1999) Journal of Laboratory and Clinical Medicine , vol.133 , Issue.2 , pp. 144-151
    • Richardson, D.R.1    Chua, A.C.G.2    Baker, E.3
  • 36
    • 0038392370 scopus 로고    scopus 로고
    • Influence of parenteral iron preparations on non-transferrin bound iron uptake, the iron regulatory protein and the expression of ferritin and the divalent metal transporter DMT-1 in HepG2 human hepatoma cells
    • DOI 10.1016/S0006-2952(03)00181-3
    • Scheiber-Mojdehkar, B., Sturm, B., Plank, L., Kryzer, I., and Goldenberg, H. (2003) Influence of parenteral iron preparations on non-transferrin bound iron uptake, the iron regulatory protein and the expression of ferritin and the divalent metal transporter DMT-1 in HepG2 human hepatoma cells. Biochem. Pharmacol. 65, 1973-1978 (Pubitemid 36629581)
    • (2003) Biochemical Pharmacology , vol.65 , Issue.12 , pp. 1973-1978
    • Scheiber-Mojdehkar, B.1    Sturm, B.2    Plank, L.3    Kryzer, I.4    Goldenberg, H.5
  • 39
    • 67650050211 scopus 로고    scopus 로고
    • Mammalian zinc transporters. Nutritional and physiologic regulation
    • Lichten, L. A., and Cousins, R. J. (2009) Mammalian zinc transporters. Nutritional and physiologic regulation. Annu. Rev. Nutr. 29, 153-176
    • (2009) Annu. Rev. Nutr. , vol.29 , pp. 153-176
    • Lichten, L.A.1    Cousins, R.J.2
  • 40
    • 67650050212 scopus 로고    scopus 로고
    • Zinc transporter ZIP8 (SLC39A8) and zinc influence IFN-γ expression in activated human T cells
    • Aydemir, T. B., Liuzzi, J. P., McClellan, S., and Cousins, R. J. (2009) Zinc transporter ZIP8 (SLC39A8) and zinc influence IFN-γ expression in activated human T cells. J. Leukocyte Biol. 86, 337-348
    • (2009) J. Leukocyte Biol. , vol.86 , pp. 337-348
    • Aydemir, T.B.1    Liuzzi, J.P.2    McClellan, S.3    Cousins, R.J.4
  • 41
    • 0031683398 scopus 로고    scopus 로고
    • Influence of iron overload on manganese, zinc, and copper concentration in rat tissues in vivo. Study of liver, spleen, and brain
    • Vayenas, D. V., Repanti, M., Vassilopoulos, A., and Papanastasiou, D. A. (1998) Influence of iron overload on manganese, zinc, and copper concentration in rat tissues in vivo. Study of liver, spleen, and brain. Int. J. Clin. Lab. Res. 28, 183-186
    • (1998) Int. J. Clin. Lab. Res. , vol.28 , pp. 183-186
    • Vayenas, D.V.1    Repanti, M.2    Vassilopoulos, A.3    Papanastasiou, D.A.4
  • 42
    • 63149173764 scopus 로고    scopus 로고
    • Hepatic distribution of iron, copper, zinc and cadmium-containing proteins in normal and iron overload mice
    • Zhang, Y., Li, B., Chen, C., and Gao, Z. (2009) Hepatic distribution of iron, copper, zinc and cadmium-containing proteins in normal and iron overload mice. Biometals 22, 251-259
    • (2009) Biometals , vol.22 , pp. 251-259
    • Zhang, Y.1    Li, B.2    Chen, C.3    Gao, Z.4
  • 44
    • 0025211404 scopus 로고
    • Mobilization of iron from endocytic vesicles. The effects of acidification and reduction
    • Núñez, M. T., Gaete, V., Watkins, J. A., and Glass, J. (1990) Mobilization of iron from endocytic vesicles. The effects of acidification and reduction. J. Biol. Chem. 265, 6688-6692
    • (1990) J. Biol. Chem. , vol.265 , pp. 6688-6692
    • Núñez, M.T.1    Gaete, V.2    Watkins, J.A.3    Glass, J.4
  • 45
    • 84861601366 scopus 로고    scopus 로고
    • The zinc transporter Zip14 influences c-Met phosphorylation and hepatocyte proliferation during liver regeneration in mice
    • Aydemir, T. B., Sitren, H. S., and Cousins, R. J. (2012) The zinc transporter Zip14 influences c-Met phosphorylation and hepatocyte proliferation during liver regeneration in mice. Gastroenterology 142, 1536-1546.e5
    • (2012) Gastroenterology , vol.142
    • Aydemir, T.B.1    Sitren, H.S.2    Cousins, R.J.3
  • 49
    • 0036225268 scopus 로고    scopus 로고
    • Cadmium overload and toxicity
    • Jarup, L. (2002) Cadmium overload and toxicity. Nephrol. Dial. Transplant. 17, (Suppl. 2) 35-39
    • (2002) Nephrol. Dial. Transplant. , vol.17 , Issue.SUPPL. 2 , pp. 35-39
    • Jarup, L.1
  • 50
    • 80155168985 scopus 로고    scopus 로고
    • Role of the placenta in regulation of fetal iron status
    • McArdle, H. J., Lang, C., Hayes, H., and Gambling, L. (2011) Role of the placenta in regulation of fetal iron status. Nutr. Rev. 69, (Suppl. 1) S17-S22
    • (2011) Nutr. Rev. , vol.69 , Issue.SUPPL. 1
    • McArdle, H.J.1    Lang, C.2    Hayes, H.3    Gambling, L.4
  • 51
    • 79952977920 scopus 로고    scopus 로고
    • The zinc transporter SLC39A14/ZIP14 controls G-protein coupled receptor-mediated signaling required for systemic growth
    • Hojyo, S., Fukada, T., Shimoda, S., Ohashi, W., Bin, B. H., Koseki, H., and Hirano, T. (2011) The zinc transporter SLC39A14/ZIP14 controls G-protein coupled receptor-mediated signaling required for systemic growth. PloS one 6, e18059
    • (2011) PloS One , vol.6
    • Hojyo, S.1    Fukada, T.2    Shimoda, S.3    Ohashi, W.4    Bin, B.H.5    Koseki, H.6    Hirano, T.7
  • 53
    • 34347328067 scopus 로고    scopus 로고
    • Targeting of the mouse Slc39a2 (Zip2) gene reveals highly cell-specific patterns of expression, and unique functions in zinc, iron, and calcium homeostasis
    • DOI 10.1002/dvg.20297
    • Peters, J. L., Dufner-Beattie, J., Xu, W., Geiser, J., Lahner, B., Salt, D. E., and Andrews, G. K. (2007) Targeting of the mouse Slc39a2 (Zip2) gene reveals highly cell-specific patterns of expression, and unique functions in zinc, iron, and calcium homeostasis. Genesis 45, 339-352 (Pubitemid 47015320)
    • (2007) Genesis , vol.45 , Issue.6 , pp. 339-352
    • Peters, J.L.1    Dufner-Beattie, J.2    Xu, W.3    Geiser, J.4    Lahner, B.5    Salt, D.E.6    Andrews, G.K.7
  • 54
    • 79960156125 scopus 로고    scopus 로고
    • Molecular and genetic features of zinc transporters in physiology and pathogenesis
    • Fukada, T., and Kambe, T. (2011) Molecular and genetic features of zinc transporters in physiology and pathogenesis. Metallomics 3, 662-674
    • (2011) Metallomics , vol.3 , pp. 662-674
    • Fukada, T.1    Kambe, T.2
  • 55
    • 1542376716 scopus 로고    scopus 로고
    • Acrodermatitis enteropathica mutations affect transport activity, localization and zinc-responsive trafficking of the mouse ZIP4 zinc transporter
    • DOI 10.1093/hmg/ddh049
    • Wang, F., Kim, B. E., Dufner-Beattie, J., Petris, M. J., Andrews, G., and Eide, D. J. (2004) Acrodermatitis enteropathica mutations affect transport activity, localization and zinc-responsive trafficking of the mouse ZIP4 zinc transporter. Hum. Mol. Genet. 13, 563-571 (Pubitemid 38324501)
    • (2004) Human Molecular Genetics , vol.13 , Issue.5 , pp. 563-571
    • Wang, F.1    Kim, B.-E.2    Dufner-Beattie, J.3    Petris, M.J.4    Andrews, G.5    Eide, D.J.6
  • 56
    • 10944273358 scopus 로고    scopus 로고
    • The mammalian Zip5 protein is a zinc transporter that localizes to the basolateral surface of polarized cells
    • DOI 10.1074/jbc.M408361200
    • Wang, F., Kim, B. E., Petris, M. J., and Eide, D. J. (2004) The mammalian Zip5 protein is a zinc transporter that localizes to the basolateral surface of polarized cells. J. Biol. Chem. 279, 51433-51441 (Pubitemid 40017891)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.49 , pp. 51433-51441
    • Wang, F.1    Kim, B.-E.2    Petris, M.J.3    Eide, D.J.4
  • 57
    • 42449154695 scopus 로고    scopus 로고
    • Slc39a14 gene encodes ZIP14, a metal/bicarbonate symporter: Similarities to the ZIP8 transporter
    • DOI 10.1124/mol.107.043588
    • Girijashanker, K., He, L., Soleimani, M., Reed, J. M., Li, H., Liu, Z., Wang, B., Dalton, T. P., and Nebert, D. W. (2008) Slc39a14 gene encodes ZIP14, a metal/bicarbonate symporter. Similarities to the ZIP8 transporter. Mol. Pharmacol. 73, 1413-1423 (Pubitemid 351574831)
    • (2008) Molecular Pharmacology , vol.73 , Issue.5 , pp. 1413-1423
    • Girijashanker, K.1    He, L.2    Soleimani, M.3    Reed, J.M.4    Li, H.5    Liu, Z.6    Wang, B.7    Dalton, T.P.8    Nebert, D.W.9
  • 58
    • 0041940266 scopus 로고    scopus 로고
    • Iron, manganese, and cobalt transport by Nramp1 (Slc11a1) and Nramp2 (Slc11a2) expressed at the plasma membrane
    • DOI 10.1182/blood-2003-02-0425
    • Forbes, J. R., and Gros, P. (2003) Iron, manganese, and cobalt transport by Nramp1 (Slc11a1) and Nramp2 (Slc11a2) expressed at the plasma membrane. Blood 102, 1884-1892 (Pubitemid 37022588)
    • (2003) Blood , vol.102 , Issue.5 , pp. 1884-1892
    • Forbes, J.R.1    Gros, P.2
  • 59
    • 84865714279 scopus 로고    scopus 로고
    • Substrate profile and metal-ion selectivity of human divalent metal-ion transporter-1
    • Illing, A. C., Shawki, A., Cunningham, C. L., and Mackenzie, B. (2012) Substrate profile and metal-ion selectivity of human divalent metal-ion transporter-1. J. Biol. Chem. 287, 30485-30496
    • (2012) J. Biol. Chem. , vol.287 , pp. 30485-30496
    • Illing, A.C.1    Shawki, A.2    Cunningham, C.L.3    Mackenzie, B.4
  • 60
    • 0014465766 scopus 로고
    • Alteration in cobalt absorption in patients with disorders of iron metabolism
    • Valberg, L. S., Ludwig, J., and Olatunbosun, D. (1969) Alteration in cobalt absorption in patients with disorders of iron metabolism. Gastroenterology 56, 241-251
    • (1969) Gastroenterology , vol.56 , pp. 241-251
    • Valberg, L.S.1    Ludwig, J.2    Olatunbosun, D.3
  • 62
    • 0028303126 scopus 로고
    • Health risks associated with cobalt exposure - An overview
    • DOI 10.1016/0048-9697(94)90125-2
    • Lauwerys, R., and Lison, D. (1994) Health risks associated with cobalt exposure. An overview. Sci. Total Environ. 150, 1-6 (Pubitemid 24210681)
    • (1994) Science of the Total Environment , vol.150 , Issue.1-3 , pp. 1-6
    • Lauwerys, R.1    Lison, D.2
  • 63
    • 0021994330 scopus 로고
    • Trace elements in human body fluids and tissues
    • Versieck, J. (1985) Trace elements in human body fluids and tissues. Crit. Rev. Clin. Lab. Sci. 22, 97-184
    • (1985) Crit. Rev. Clin. Lab. Sci. , vol.22 , pp. 97-184
    • Versieck, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.