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Volumn 13, Issue 7-8, 2007, Pages 337-343

Mechanism and regulation of cellular zinc transport

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; ZINC; ZINC TRANSPORTER;

EID: 34548484857     PISSN: 10761551     EISSN: None     Source Type: Journal    
DOI: 10.2119/2007-00037.Sekler     Document Type: Conference Paper
Times cited : (187)

References (82)
  • 1
    • 0029866646 scopus 로고    scopus 로고
    • The galvanization of biology: A growing appreciation for the roles of zinc
    • Berg JM, Shi Y. (1996) The galvanization of biology: a growing appreciation for the roles of zinc. Science 271:1081-5.
    • (1996) Science , vol.271 , pp. 1081-1085
    • Berg, J.M.1    Shi, Y.2
  • 2
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • Vallee BL, Falchuk KH. (1993) The biochemical basis of zinc physiology. Physiol-Rev 73:79-118.
    • (1993) Physiol-Rev , vol.73 , pp. 79-118
    • Vallee, B.L.1    Falchuk, K.H.2
  • 3
    • 33646036991 scopus 로고    scopus 로고
    • Zinc requirements and the risks and benefits of zinc supplementation
    • Maret W, Sandstead HH. (2006) Zinc requirements and the risks and benefits of zinc supplementation. J. Trace Elem. Med. Biol. 20:3-18.
    • (2006) J. Trace Elem. Med. Biol , vol.20 , pp. 3-18
    • Maret, W.1    Sandstead, H.H.2
  • 4
    • 0034063878 scopus 로고    scopus 로고
    • The role of zinc in growth and cell proliferation
    • MacDonald RS. (2000) The role of zinc in growth and cell proliferation. J. Nutr. 130:1500S-8S.
    • (2000) J. Nutr , vol.130
    • MacDonald, R.S.1
  • 7
    • 1842536773 scopus 로고    scopus 로고
    • Rethinking the excitotoxic ionic milieu: The emerging role of Zn(2+) in ischemic neuronal injury
    • Sensi SL, Jeng JM. (2004) Rethinking the excitotoxic ionic milieu: the emerging role of Zn(2+) in ischemic neuronal injury. Curr. Mol. Med. 4:87-111.
    • (2004) Curr. Mol. Med , vol.4 , pp. 87-111
    • Sensi, S.L.1    Jeng, J.M.2
  • 8
    • 9344254033 scopus 로고    scopus 로고
    • Nitrosative stress and potassium channel-mediated neuronal apoptosis: Is zinc the link?
    • Pal S, He K, Aizenman E. (2004) Nitrosative stress and potassium channel-mediated neuronal apoptosis: is zinc the link? Pflugers Arch. 448:296-303.
    • (2004) Pflugers Arch , vol.448 , pp. 296-303
    • Pal, S.1    He, K.2    Aizenman, E.3
  • 9
    • 9344268817 scopus 로고    scopus 로고
    • Peroxynitrite-induced neuronal apoptosis is mediated by intracellular zinc release and 12-lipoxygenase activation
    • Zhang Y, Wang H, Li J, et al. (2004) Peroxynitrite-induced neuronal apoptosis is mediated by intracellular zinc release and 12-lipoxygenase activation. J. Neurosci. 24:10616-27.
    • (2004) J. Neurosci , vol.24 , pp. 10616-10627
    • Zhang, Y.1    Wang, H.2    Li, J.3
  • 10
    • 0037049243 scopus 로고    scopus 로고
    • Zinc translocation accelerates infarction after mild transient focal ischemia
    • Lee JM, Zipfel GJ, Park KH, He YY, Hsu CY, Choi DW. (2002) Zinc translocation accelerates infarction after mild transient focal ischemia. Neuroscience. 115:871-8.
    • (2002) Neuroscience , vol.115 , pp. 871-878
    • Lee, J.M.1    Zipfel, G.J.2    Park, K.H.3    He, Y.Y.4    Hsu, C.Y.5    Choi, D.W.6
  • 12
    • 0034964390 scopus 로고    scopus 로고
    • Cherny RAet al. (2001) Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron. 30:665-76.
    • Cherny RAet al. (2001) Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron. 30:665-76.
  • 13
    • 0034006766 scopus 로고    scopus 로고
    • Zinc as a paracrine effector in pancreatic islet cell death
    • Kim BJ et al. (2000) Zinc as a paracrine effector in pancreatic islet cell death. Diabetes. 49:367-72.
    • (2000) Diabetes , vol.49 , pp. 367-372
    • Kim, B.J.1
  • 14
    • 2442645184 scopus 로고    scopus 로고
    • Role of calcium in pancreatic islet cell death by IFN-gamma/TNF-alpha
    • Chang I et al. (2004) Role of calcium in pancreatic islet cell death by IFN-gamma/TNF-alpha. J. Immunol. 172:7008-14.
    • (2004) J. Immunol , vol.172 , pp. 7008-7014
    • Chang, I.1
  • 15
    • 33744979762 scopus 로고    scopus 로고
    • Zinc influx and physiological consequences in the beta-insulinoma cell line, Min6
    • Priel T, Hershfinkel M. (2006) Zinc influx and physiological consequences in the beta-insulinoma cell line, Min6. Biochem. Biophys. Res. Commun. 346:205-12.
    • (2006) Biochem. Biophys. Res. Commun , vol.346 , pp. 205-212
    • Priel, T.1    Hershfinkel, M.2
  • 16
    • 0033712121 scopus 로고    scopus 로고
    • The actions of synaptically released zinc at hippocampal mossy fiber synapses
    • Vogt K, Mellor J, Tong G, Nicoll R. (2000) The actions of synaptically released zinc at hippocampal mossy fiber synapses. Neuron. 26:187-96.
    • (2000) Neuron , vol.26 , pp. 187-196
    • Vogt, K.1    Mellor, J.2    Tong, G.3    Nicoll, R.4
  • 17
    • 33745029895 scopus 로고    scopus 로고
    • Measuring picomolar intracellular exchangeable zinc in PC-12 cells using a ratiometric fluorescence biosensor
    • Bozym RA, Thompson RB, Stoddard AK, Fierke CA. (2006) Measuring picomolar intracellular exchangeable zinc in PC-12 cells using a ratiometric fluorescence biosensor. ACS Chem Biol. 1:103-11.
    • (2006) ACS Chem Biol , vol.1 , pp. 103-111
    • Bozym, R.A.1    Thompson, R.B.2    Stoddard, A.K.3    Fierke, C.A.4
  • 18
    • 0037028562 scopus 로고    scopus 로고
    • Detection and imaging of zinc secretion from pancreatic beta-cells using a new fluorescent zinc indicator
    • Gee KR, Zhou ZL, Qian WJ, Kennedy R. (2002) Detection and imaging of zinc secretion from pancreatic beta-cells using a new fluorescent zinc indicator. J. Am. Chem. Soc. 124:776-8.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 776-778
    • Gee, K.R.1    Zhou, Z.L.2    Qian, W.J.3    Kennedy, R.4
  • 19
    • 24744439439 scopus 로고    scopus 로고
    • Zinc-ligand interactions modulate assembly and stability of the insulin hexamer - a review
    • Dunn MF. (2005) Zinc-ligand interactions modulate assembly and stability of the insulin hexamer - a review. Biometals. 18:295-303.
    • (2005) Biometals , vol.18 , pp. 295-303
    • Dunn, M.F.1
  • 22
    • 1342344814 scopus 로고    scopus 로고
    • The SLC39 family of metal ion transporters
    • Eide DJ. (2004) The SLC39 family of metal ion transporters. Pflugers Arch. 447:796-800.
    • (2004) Pflugers Arch , vol.447 , pp. 796-800
    • Eide, D.J.1
  • 23
    • 0038670762 scopus 로고    scopus 로고
    • Cellular zinc and redox states converge in the metallothionein/thionein pair
    • Maret W. (2003) Cellular zinc and redox states converge in the metallothionein/thionein pair. J. Nutr. 133:1460S-2S.
    • (2003) J. Nutr , vol.133
    • Maret, W.1
  • 24
    • 0036431502 scopus 로고    scopus 로고
    • A new zinc-protein coordination site in intracellular metal trafficking: Solution structure of the Apo and Zn(II) forms of ZntA(46-118)
    • Band L, Bertini I, Ciofi-Baffoni S, Finney LA, Outten CE, O'Halloran TV. (2002) A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118). J. Mol. Biol. 323:883-97.
    • (2002) J. Mol. Biol , vol.323 , pp. 883-897
    • Band, L.1    Bertini, I.2    Ciofi-Baffoni, S.3    Finney, L.A.4    Outten, C.E.5    O'Halloran, T.V.6
  • 25
    • 33845917294 scopus 로고    scopus 로고
    • A novel regulatory metal binding domain is present in the C terminus of Arabidopsis Zn2+-ATPase HMA2
    • Eren E, Kennedy DC, Maroney MJ, Arguello JM, Eren E, Arguello JM. (2006) A novel regulatory metal binding domain is present in the C terminus of Arabidopsis Zn2+-ATPase HMA2. J. Biol. Chem. 281:33881-91.
    • (2006) J. Biol. Chem , vol.281 , pp. 33881-33891
    • Eren, E.1    Kennedy, D.C.2    Maroney, M.J.3    Arguello, J.M.4    Eren, E.5    Arguello, J.M.6
  • 26
    • 11144223456 scopus 로고    scopus 로고
    • Arabidopsis HMA2, a divalent heavy metal-transporting P(IB)-type ATPase, is involved in cytoplasmic Zn2+ homeostasis
    • Eren E, Arguello JM. (2004) Arabidopsis HMA2, a divalent heavy metal-transporting P(IB)-type ATPase, is involved in cytoplasmic Zn2+ homeostasis. Plant Physiol. 136:3712-23.
    • (2004) Plant Physiol , vol.136 , pp. 3712-3723
    • Eren, E.1    Arguello, J.M.2
  • 27
    • 0028040512 scopus 로고
    • Characterization of the Wilson disease gene encoding a P-type copper transporting ATPase: Genomic organization, alternative splicing, and structure/function predictions
    • Petrukhin K, Lutsenko S, Chernov I, Ross BM, Kaplan JH, Gilliam TC. (1994) Characterization of the Wilson disease gene encoding a P-type copper transporting ATPase: genomic organization, alternative splicing, and structure/function predictions. Hum. Mol. Genet. 3:1647-56.
    • (1994) Hum. Mol. Genet , vol.3 , pp. 1647-1656
    • Petrukhin, K.1    Lutsenko, S.2    Chernov, I.3    Ross, B.M.4    Kaplan, J.H.5    Gilliam, T.C.6
  • 28
    • 0031466709 scopus 로고    scopus 로고
    • Measurement of intracellular free zinc in living cortical neurons: Routes of entry
    • Sensi SL et al. (1997) Measurement of intracellular free zinc in living cortical neurons: routes of entry. J. Neurosci. 17:9554-64.
    • (1997) J. Neurosci , vol.17 , pp. 9554-9564
    • Sensi, S.L.1
  • 29
    • 1042266640 scopus 로고    scopus 로고
    • A sodium zinc exchange mechanism is mediating extrusion of zinc in Mammalian cells
    • Ohana E et al. (2004) A sodium zinc exchange mechanism is mediating extrusion of zinc in Mammalian cells. J. Biol. Chem. 279:4278-84.
    • (2004) J. Biol. Chem , vol.279 , pp. 4278-4284
    • Ohana, E.1
  • 30
    • 33747723380 scopus 로고    scopus 로고
    • Mammalian zinc transport, trafficking, and signals
    • Cousins RJ, Liuzzi JP, Lichten LA. (2006) Mammalian zinc transport, trafficking, and signals. J. Biol. Chem. 281:24085-9.
    • (2006) J. Biol. Chem , vol.281 , pp. 24085-24089
    • Cousins, R.J.1    Liuzzi, J.P.2    Lichten, L.A.3
  • 31
    • 0346749515 scopus 로고    scopus 로고
    • Structure, function, and regulation of a subfamily of mouse zinc transporter genes
    • Dufner-Beattie J, Langmade SJ, Wang F, Eide D, Andrews GK. (2003) Structure, function, and regulation of a subfamily of mouse zinc transporter genes. J. Biol. Chem. 278:50142-50.
    • (2003) J. Biol. Chem , vol.278 , pp. 50142-50150
    • Dufner-Beattie, J.1    Langmade, S.J.2    Wang, F.3    Eide, D.4    Andrews, G.K.5
  • 32
    • 0034602175 scopus 로고    scopus 로고
    • The transcription factor MTF-1 mediates metal regulation of the mouse ZnT1 gene
    • Langmade SJ, Ravindra R, Daniels PJ, Andrews GK. (2000) The transcription factor MTF-1 mediates metal regulation of the mouse ZnT1 gene. J. Biol. Chem. 275:34803-9.
    • (2000) J. Biol. Chem , vol.275 , pp. 34803-34809
    • Langmade, S.J.1    Ravindra, R.2    Daniels, P.J.3    Andrews, G.K.4
  • 33
    • 3242676985 scopus 로고    scopus 로고
    • Differential regulation of zinc efflux transporters ZnT-1, ZnT-5 and ZnT-7 gene expression by zinc levels: A real-time RT-PCR study
    • Devergnas S et al. (2004) Differential regulation of zinc efflux transporters ZnT-1, ZnT-5 and ZnT-7 gene expression by zinc levels: a real-time RT-PCR study. Biochem. Pharmacol. 68:699-709.
    • (2004) Biochem. Pharmacol , vol.68 , pp. 699-709
    • Devergnas, S.1
  • 34
    • 0037131363 scopus 로고    scopus 로고
    • Biochemical properties of vacuolar zinc transport systems of Saccharomyces cerevisiae
    • MacDiarmid CW, Milanick MA, Eide DJ. (2002) Biochemical properties of vacuolar zinc transport systems of Saccharomyces cerevisiae. J. Biol. Chem. 277:39187-194.
    • (2002) J. Biol. Chem , vol.277 , pp. 39187-39194
    • MacDiarmid, C.W.1    Milanick, M.A.2    Eide, D.J.3
  • 35
    • 1842530384 scopus 로고    scopus 로고
    • Kinetic study of the antiport mechanism of an Escherichia coli zinc transporter, ZitB
    • Chao Y, Fu D. (2004) Kinetic study of the antiport mechanism of an Escherichia coli zinc transporter, ZitB. J. Biol. Chem. 279:12043-50.
    • (2004) J. Biol. Chem , vol.279 , pp. 12043-12050
    • Chao, Y.1    Fu, D.2
  • 36
    • 34548492425 scopus 로고    scopus 로고
    • Acidosis enhances toxicity induced by kainate and zinc exposure in aged cultured astrocytes
    • Sensi SL, Rockabrand E, Canzoniero LM. (2006) Acidosis enhances toxicity induced by kainate and zinc exposure in aged cultured astrocytes. Biogerontology. 7:367-74.
    • (2006) Biogerontology , vol.7 , pp. 367-374
    • Sensi, S.L.1    Rockabrand, E.2    Canzoniero, L.M.3
  • 37
    • 1842636876 scopus 로고    scopus 로고
    • Protection against zinc toxicity by metallothionein and zinc transporter 1
    • Palmiter RD. (2004) Protection against zinc toxicity by metallothionein and zinc transporter 1. Proc. Natl. Acad. Sci. U. S. A. 101:4918-23.
    • (2004) Proc. Natl. Acad. Sci. U. S. A , vol.101 , pp. 4918-4923
    • Palmiter, R.D.1
  • 38
    • 9144252732 scopus 로고    scopus 로고
    • ZnT-1 expression in astroglial cells protects against zinc toxicity and slows the accumulation of intracellular zinc
    • Nolte C et al. (2004) ZnT-1 expression in astroglial cells protects against zinc toxicity and slows the accumulation of intracellular zinc. Glia. 48:145-55.
    • (2004) Glia , vol.48 , pp. 145-155
    • Nolte, C.1
  • 39
    • 0037013710 scopus 로고    scopus 로고
    • Distribution of the zinc transporter ZnT-1 in comparison with chelatable zinc in the mouse brain
    • Sekler I et al. (2002) Distribution of the zinc transporter ZnT-1 in comparison with chelatable zinc in the mouse brain. J. Comp. Neurol. 447:201-9.
    • (2002) J. Comp. Neurol , vol.447 , pp. 201-209
    • Sekler, I.1
  • 41
    • 0028948696 scopus 로고
    • Cloning and functional characterization of a mammalian zinc transporter that confers resistance to zinc
    • Palmiter RD, Findley SD. (1995) Cloning and functional characterization of a mammalian zinc transporter that confers resistance to zinc. EMBO-J. 14:639-49.
    • (1995) EMBO-J , vol.14 , pp. 639-649
    • Palmiter, R.D.1    Findley, S.D.2
  • 42
    • 33748291477 scopus 로고    scopus 로고
    • Silencing of ZnT-1 expression enhances heavy metal influx and toxicity
    • Ohana E et al. (2006) Silencing of ZnT-1 expression enhances heavy metal influx and toxicity. J. Mol. Med. 84:753-63.
    • (2006) J. Mol. Med , vol.84 , pp. 753-763
    • Ohana, E.1
  • 46
    • 0035830711 scopus 로고    scopus 로고
    • Removing zinc from synaptic vesicles does not impair spatial learning, memory, or sensorimotor functions in the mouse
    • Cole TB, Martyanova A, Palmiter RD. (2001) Removing zinc from synaptic vesicles does not impair spatial learning, memory, or sensorimotor functions in the mouse. Brain Res. 891:253-65.
    • (2001) Brain Res , vol.891 , pp. 253-265
    • Cole, T.B.1    Martyanova, A.2    Palmiter, R.D.3
  • 47
    • 0037439069 scopus 로고    scopus 로고
    • Lack of vesicular zinc in mossy fibers does not affect synaptic excitability of CA3 pyramidal cells in zinc transporter 3 knockout mice
    • Lopantsev V, Wenzel HJ, Cole TB, Palmiter RD, Schwartzkroin PA. (2003) Lack of vesicular zinc in mossy fibers does not affect synaptic excitability of CA3 pyramidal cells in zinc transporter 3 knockout mice. Neuroscience. 116:237-48.
    • (2003) Neuroscience , vol.116 , pp. 237-248
    • Lopantsev, V.1    Wenzel, H.J.2    Cole, T.B.3    Palmiter, R.D.4    Schwartzkroin, P.A.5
  • 48
    • 0344394903 scopus 로고    scopus 로고
    • Zinc released from metallothionein-iii may contribute to hippocampal CA1 and thalamic neuronal death following acute brain injury
    • Lee JY, Kim JH, Palmiter RD, Koh JY. (2003) Zinc released from metallothionein-iii may contribute to hippocampal CA1 and thalamic neuronal death following acute brain injury. Exp. Neurol. 184:337-47.
    • (2003) Exp. Neurol , vol.184 , pp. 337-347
    • Lee, J.Y.1    Kim, J.H.2    Palmiter, R.D.3    Koh, J.Y.4
  • 49
    • 1842506368 scopus 로고    scopus 로고
    • Neuronal zinc exchange with the blood vessel wall promotes cerebral amyloid angiopathy in an animal model of Alzheimer's disease
    • Friedlich AL et al. (2004) Neuronal zinc exchange with the blood vessel wall promotes cerebral amyloid angiopathy in an animal model of Alzheimer's disease. J. Neurosci. 24:3453-9.
    • (2004) J. Neurosci , vol.24 , pp. 3453-3459
    • Friedlich, A.L.1
  • 51
    • 33746223009 scopus 로고    scopus 로고
    • Zinc modulates bidirectional hippocampal plasticity by effects on NMDA receptors
    • Tzumi Y, Auberson YP, Zorumski CF. (2006) Zinc modulates bidirectional hippocampal plasticity by effects on NMDA receptors. J. Neurosci. 26:7181-8.
    • (2006) J. Neurosci , vol.26 , pp. 7181-7188
    • Tzumi, Y.1    Auberson, Y.P.2    Zorumski, C.F.3
  • 52
    • 0035140476 scopus 로고    scopus 로고
    • Hippocampal mossy fiber LTP is independent of postsynaptic calcium
    • Mellor J, Nicoll RA. (2001) Hippocampal mossy fiber LTP is independent of postsynaptic calcium. Nature Neuroscience. 4:125-6.
    • (2001) Nature Neuroscience , vol.4 , pp. 125-126
    • Mellor, J.1    Nicoll, R.A.2
  • 53
    • 33745842537 scopus 로고    scopus 로고
    • Zinc transport complexes contribute to the homeostatic maintenance of secretory pathway function in vertebrate cells
    • Ishihara K et al. (2006) Zinc transport complexes contribute to the homeostatic maintenance of secretory pathway function in vertebrate cells. J. Biol. Chem. 281:17743-50.
    • (2006) J. Biol. Chem , vol.281 , pp. 17743-17750
    • Ishihara, K.1
  • 54
    • 12844265345 scopus 로고    scopus 로고
    • Zinc transporters, ZnT5 and ZnT7, are required for the activation of alkaline phosphatases, zinc-requiring enzymes that are glycosylphosphatidylinositol-anchored to the cytoplasmic membrane
    • Suzuki T et al. (2005) Zinc transporters, ZnT5 and ZnT7, are required for the activation of alkaline phosphatases, zinc-requiring enzymes that are glycosylphosphatidylinositol-anchored to the cytoplasmic membrane. J. Biol. Chem. 280:637-43.
    • (2005) J. Biol. Chem , vol.280 , pp. 637-643
    • Suzuki, T.1
  • 55
    • 0037098959 scopus 로고    scopus 로고
    • Osteopenia and male-specific sudden cardiac death in mice lacking a zinc transporter gene, Znt5
    • Inoue K et al. (2002) Osteopenia and male-specific sudden cardiac death in mice lacking a zinc transporter gene, Znt5. Hum. Mol. Genet. 11:1775-84.
    • (2002) Hum. Mol. Genet , vol.11 , pp. 1775-1784
    • Inoue, K.1
  • 56
    • 33751192688 scopus 로고    scopus 로고
    • Essential trace and toxic element distribution in the scalp hair of Pakistani myocardial infarction patients and controls
    • Afridi HI, Kazi TG, Kazi GH, Jamali MK, Shar GQ. (2006) Essential trace and toxic element distribution in the scalp hair of Pakistani myocardial infarction patients and controls. Biol. Trace Elem. Res. 113:19-34.
    • (2006) Biol. Trace Elem. Res , vol.113 , pp. 19-34
    • Afridi, H.I.1    Kazi, T.G.2    Kazi, G.H.3    Jamali, M.K.4    Shar, G.Q.5
  • 57
    • 0037135606 scopus 로고    scopus 로고
    • Functional characterization of a novel mammalian zinc transporter, ZnT6
    • Huang L, Kirschke CP, Gitschier J. (2002) Functional characterization of a novel mammalian zinc transporter, ZnT6. J. Biol. Chem. 277:26389-95.
    • (2002) J. Biol. Chem , vol.277 , pp. 26389-26395
    • Huang, L.1    Kirschke, C.P.2    Gitschier, J.3
  • 58
    • 23344440858 scopus 로고    scopus 로고
    • Heteromeric protein complexes mediate zinc transport into the secretory pathway of eukaryotic cells
    • Ellis CD, Macdiarmid CW, Eide DJ. (2005) Heteromeric protein complexes mediate zinc transport into the secretory pathway of eukaryotic cells. J. Biol. Chem. 280:28811-8.
    • (2005) J. Biol. Chem , vol.280 , pp. 28811-28818
    • Ellis, C.D.1    Macdiarmid, C.W.2    Eide, D.J.3
  • 59
    • 34249850816 scopus 로고    scopus 로고
    • Splice variants of the human zinc transporter ZnT5 (SLC30A5) are differentially localized and regulated by zinc through transcription and mRNA stability
    • Jackson KA, Helston RM, McKay JA, O'Neill E D, Mathers JC, Ford D. (2007) Splice variants of the human zinc transporter ZnT5 (SLC30A5) are differentially localized and regulated by zinc through transcription and mRNA stability. J. Biol. Chem. 282:10423-31.
    • (2007) J. Biol. Chem , vol.282 , pp. 10423-10431
    • Jackson, K.A.1    Helston, R.M.2    McKay, J.A.3    O'Neill, E.D.4    Mathers, J.C.5    Ford, D.6
  • 60
    • 4344665860 scopus 로고    scopus 로고
    • Identification and cloning of a beta-cell-specific zinc transporter, ZnT-8, localized into insulin secretory granules
    • Chimienti F, Devergnas S, Favier A, Seve M. (2004) Identification and cloning of a beta-cell-specific zinc transporter, ZnT-8, localized into insulin secretory granules. Diabetes. 53:2330-7.
    • (2004) Diabetes , vol.53 , pp. 2330-2337
    • Chimienti, F.1    Devergnas, S.2    Favier, A.3    Seve, M.4
  • 61
    • 33751183948 scopus 로고    scopus 로고
    • In vivo expression and functional characterization of the zinc transporter ZnT8 in glucose-induced insulin secretion
    • Chimienti F et al. (2006) In vivo expression and functional characterization of the zinc transporter ZnT8 in glucose-induced insulin secretion. J. Cell Sci. 119:4199-206.
    • (2006) J. Cell Sci , vol.119 , pp. 4199-4206
    • Chimienti, F.1
  • 62
    • 33847176604 scopus 로고    scopus 로고
    • A genome-wide association study identifies novel risk loci for type 2 diabetes
    • Sladek R et al. (2007) A genome-wide association study identifies novel risk loci for type 2 diabetes. Nature. 445:881-5.
    • (2007) Nature , vol.445 , pp. 881-885
    • Sladek, R.1
  • 63
    • 2442471606 scopus 로고    scopus 로고
    • Intracellular copper transport in mammals
    • Prohaska JR, Gybina AA. (2004) Intracellular copper transport in mammals. J Nutr. 134:1003-6.
    • (2004) J Nutr , vol.134 , pp. 1003-1006
    • Prohaska, J.R.1    Gybina, A.A.2
  • 64
    • 19444371698 scopus 로고    scopus 로고
    • Vglut1 and ZnT3 co-targeting mechanisms regulate vesicular zinc stores in PC12 cells
    • Salazar G, Craige B, Love R, Kalman D, Faundez V. (2005) Vglut1 and ZnT3 co-targeting mechanisms regulate vesicular zinc stores in PC12 cells. J. Cell Sci. 118:1911-21.
    • (2005) J. Cell Sci , vol.118 , pp. 1911-1921
    • Salazar, G.1    Craige, B.2    Love, R.3    Kalman, D.4    Faundez, V.5
  • 65
    • 3242725995 scopus 로고    scopus 로고
    • A molecular technique for detecting the liberation of intracellular zinc in cultured neurons
    • Hara H, Aizenman E. (2004) A molecular technique for detecting the liberation of intracellular zinc in cultured neurons. J. Neurosci. Methods. 137:175-80.
    • (2004) J. Neurosci. Methods , vol.137 , pp. 175-180
    • Hara, H.1    Aizenman, E.2
  • 66
  • 68
    • 33747620096 scopus 로고    scopus 로고
    • Fluorescence-based zinc ion sensor for zinc ion release from pancreatic cells
    • Crivat G et al. (2006) Fluorescence-based zinc ion sensor for zinc ion release from pancreatic cells. Anal. Chem. 78:5799-804.
    • (2006) Anal. Chem , vol.78 , pp. 5799-5804
    • Crivat, G.1
  • 69
    • 22944437471 scopus 로고    scopus 로고
    • Selective zinc sensor molecules with various affinities for Zn2+, revealing dynamics and regional distribution of synaptically released Zn2+ in hippocampal slices
    • Komatsu K, Kikuchi K, Kojima H, Urano Y, Nagano T. (2005) Selective zinc sensor molecules with various affinities for Zn2+, revealing dynamics and regional distribution of synaptically released Zn2+ in hippocampal slices. J. Am. Chem. Soc. 127:10197-204.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 10197-10204
    • Komatsu, K.1    Kikuchi, K.2    Kojima, H.3    Urano, Y.4    Nagano, T.5
  • 71
    • 8444252173 scopus 로고    scopus 로고
    • Mouse zinc transporter 1 gene provides an essential function during early embryonic development
    • Andrews GK, Wang H, Dey SK, Palmiter RD. (2004) Mouse zinc transporter 1 gene provides an essential function during early embryonic development. Genesis. 40:74-81.
    • (2004) Genesis , vol.40 , pp. 74-81
    • Andrews, G.K.1    Wang, H.2    Dey, S.K.3    Palmiter, R.D.4
  • 72
    • 33947727880 scopus 로고    scopus 로고
    • Zinc transporter 2 (SLC30A2) can suppress the vesicular zinc defect of adaptor protein 3-depleted fibroblasts by promoting zinc accumulation in lysosomes
    • Falcon-Perez JM, Dell'angelica EC. (2007) Zinc transporter 2 (SLC30A2) can suppress the vesicular zinc defect of adaptor protein 3-depleted fibroblasts by promoting zinc accumulation in lysosomes. Exp. Cell Res. 313:1473-83.
    • (2007) Exp. Cell Res , vol.313 , pp. 1473-1483
    • Falcon-Perez, J.M.1    Dell'angelica, E.C.2
  • 73
    • 0029873677 scopus 로고    scopus 로고
    • ZnT-2, a mammalian protein that confers resistance to zinc by facilitating vesicular sequestration
    • Palmiter RD, Cole TB, Findley SD. (1996) ZnT-2, a mammalian protein that confers resistance to zinc by facilitating vesicular sequestration. EMBO-J. 15:1784-91.
    • (1996) EMBO-J , vol.15 , pp. 1784-1791
    • Palmiter, R.D.1    Cole, T.B.2    Findley, S.D.3
  • 74
    • 0037188530 scopus 로고    scopus 로고
    • Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice
    • Lee JY, Cole TB, Palmiter RD, Suh SW, Koh JY. (2002) Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice. Proc. Natl. Acad. Sci. U. S. A. 99:7705-10.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 7705-7710
    • Lee, J.Y.1    Cole, T.B.2    Palmiter, R.D.3    Suh, S.W.4    Koh, J.Y.5
  • 75
    • 0030724951 scopus 로고    scopus 로고
    • A novel gene involved in zinc transport is deficient in the lethal milk mouse
    • Huang L, Gitschier J. (1997) A novel gene involved in zinc transport is deficient in the lethal milk mouse. Nat. Genet. 17:292-7.
    • (1997) Nat. Genet , vol.17 , pp. 292-297
    • Huang, L.1    Gitschier, J.2
  • 76
    • 0042065348 scopus 로고    scopus 로고
    • Analysis of zinc transporter, hZnT4 (Slc30A4), gene expression in a mammary gland disorder leading to reduced zinc secretion into milk
    • Michalczyk A, Varigos G, Catto-Smith A, Blomeley RC, Ackland ML. (2003) Analysis of zinc transporter, hZnT4 (Slc30A4), gene expression in a mammary gland disorder leading to reduced zinc secretion into milk. Hum. Genet. 113:202-10.
    • (2003) Hum. Genet , vol.113 , pp. 202-210
    • Michalczyk, A.1    Varigos, G.2    Catto-Smith, A.3    Blomeley, R.C.4    Ackland, M.L.5
  • 77
    • 0033369167 scopus 로고    scopus 로고
    • Cloning, expression, and vesicular localization of zinc transporter Dri 27/ZnT4 in intestinal tissue and cells
    • Murgia C, Vespignani I, Cerase J, Nobili F, Perozzi G. (1999) Cloning, expression, and vesicular localization of zinc transporter Dri 27/ZnT4 in intestinal tissue and cells. Am. J. Physiol 277:G1231-9.
    • (1999) Am. J. Physiol , vol.277
    • Murgia, C.1    Vespignani, I.2    Cerase, J.3    Nobili, F.4    Perozzi, G.5
  • 78
    • 33847034407 scopus 로고    scopus 로고
    • Anti-inflammatory effects of zinc and alterations in zinc transporter mRNA in mouse models of allergic inflammation
    • Lang C et al. (2007) Anti-inflammatory effects of zinc and alterations in zinc transporter mRNA in mouse models of allergic inflammation. Am. J. Physiol. Lung Cell Mol Physiol. 292:L577-84.
    • (2007) Am. J. Physiol. Lung Cell Mol Physiol , vol.292
    • Lang, C.1
  • 79
    • 33747206832 scopus 로고    scopus 로고
    • Altered expression of zinc transporters-4 and -6 in mild cognitive impairment, early and late Alzheimer's disease brain
    • Smith JL, Xiong S, Markesbery WR, Lovell MA. (2006) Altered expression of zinc transporters-4 and -6 in mild cognitive impairment, early and late Alzheimer's disease brain. Neuroscience. 140:879-88.
    • (2006) Neuroscience , vol.140 , pp. 879-888
    • Smith, J.L.1    Xiong, S.2    Markesbery, W.R.3    Lovell, M.A.4
  • 80
    • 0037166325 scopus 로고    scopus 로고
    • Cloning and characterization of a novel mammalian zinc transporter, zinc transporter 5, abundantly expressed in pancreatic beta cells
    • Kambe T et al. (2002) Cloning and characterization of a novel mammalian zinc transporter, zinc transporter 5, abundantly expressed in pancreatic beta cells. J. Biol. Chem. 277:19049-55.
    • (2002) J. Biol. Chem , vol.277 , pp. 19049-19055
    • Kambe, T.1
  • 81
    • 0037423203 scopus 로고    scopus 로고
    • ZnT7, a novel mammalian zinc transporter, accumulates zinc in the Golgi apparatus
    • Kirschke CP, Huang L. (2003) ZnT7, a novel mammalian zinc transporter, accumulates zinc in the Golgi apparatus J. Biol. Chem. 278:4096-102.
    • (2003) J. Biol. Chem , vol.278 , pp. 4096-4102
    • Kirschke, C.P.1    Huang, L.2
  • 82
    • 33750967658 scopus 로고    scopus 로고
    • Localization of ZnT7 and zinc ions in mouse retina - immunohistochemistry and selenium autometallography
    • Wang X et al. (2006) Localization of ZnT7 and zinc ions in mouse retina - immunohistochemistry and selenium autometallography. Brain Res. Bull. 71:91-6.
    • (2006) Brain Res. Bull , vol.71 , pp. 91-96
    • Wang, X.1


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