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Deletion of hepatic Ctr1 reveals its function in copper acquisition and compensatory mechanisms for copper homeostasis
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Kim H., Son H.Y., Bailey S.M., and Lee J. Deletion of hepatic Ctr1 reveals its function in copper acquisition and compensatory mechanisms for copper homeostasis. Am J Physiol Gastrointest Liver Physiol 296 2 (2009) G356-G364
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Kim, H.1
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34548813087
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Human copper transporter hCTR1 mediates basolateral uptake of copper into enterocytes: implications for copper homeostasis
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By measuring transport of radioactive copper and performing surface biotinylation in polarized cells the authors demonstrate the presence of CTR1 in basolateral membrane of intestinal cells. This observation suggests a general role for CTR1 in copper acquisition from the blood.
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Zimnicka A.M., Maryon E.B., and Kaplan J.H. Human copper transporter hCTR1 mediates basolateral uptake of copper into enterocytes: implications for copper homeostasis. J Biol Chem 282 36 (2007) 26471-26480. By measuring transport of radioactive copper and performing surface biotinylation in polarized cells the authors demonstrate the presence of CTR1 in basolateral membrane of intestinal cells. This observation suggests a general role for CTR1 in copper acquisition from the blood.
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Zimnicka, A.M.1
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Copper transport during lactation in transgenic mice expressing the human ATP7A protein
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Llanos R.M., Michalczyk A.A., Freestone D.J., Currie S., Linder M.C., Ackland M.L., and Mercer J.F. Copper transport during lactation in transgenic mice expressing the human ATP7A protein. Biochem Biophys Res Commun 372 4 (2008) 613-617
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Expression, localisation and hormone regulation of the human copper transporter hCTR1 in placenta and choriocarcinoma Jeg-3 cells
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Hardman B., Manuelpillai U., Wallace E., Monty J., Kramer D., Kuo Y., Mercer J., and Ackland M. Expression, localisation and hormone regulation of the human copper transporter hCTR1 in placenta and choriocarcinoma Jeg-3 cells. Placenta 27 9-10 (2006) 968-977
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Ackland, M.8
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Copper is taken up efficiently from albumin and alpha2-macroglobulin by cultured human cells by more than one mechanism
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Moriya M., Ho Y.H., Grana A., Nguyen L., Alvarez A., Jamil R., Ackland M.L., Michalczyk A., Hamer P., Ramos D., et al. Copper is taken up efficiently from albumin and alpha2-macroglobulin by cultured human cells by more than one mechanism. Am J Physiol Cell Physiol 295 3 (2008) C708-C721
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Ramos, D.10
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6
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33747849534
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Ctr1 drives intestinal copper absorption and is essential for growth, iron metabolism, and neonatal cardiac function
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Using tissue-specific knockout mice, the authors provide the first demonstration of the role of CTR1 in dietary copper absorption. The potential second role of CTR1 in the release of from intracellular vesicles was suggested by animals' phenotype.
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Nose Y., Kim B.E., and Thiele D.J. Ctr1 drives intestinal copper absorption and is essential for growth, iron metabolism, and neonatal cardiac function. Cell Metab 4 3 (2006) 235-244. Using tissue-specific knockout mice, the authors provide the first demonstration of the role of CTR1 in dietary copper absorption. The potential second role of CTR1 in the release of from intracellular vesicles was suggested by animals' phenotype.
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Molloy S.A., and Kaplan J.H. Copper-dependent recycling of hCTR1, the human high affinity copper transporter. J Biol Chem 284 43 (2009) 29704-29713
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Transcription factor Sp1 plays an important role in the regulation of copper homeostasis in mammalian cells
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The authors show that the levels of CTR1 mRNA are under tight homeostatic control and suggest the mechanisms for CTR1 regulation.
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Song I.S., Chen H.H.W., Aiba I., Hossain A., Liang Z.D., Klomp L.W.J., and Kuo M.T. Transcription factor Sp1 plays an important role in the regulation of copper homeostasis in mammalian cells. Mol Pharmacol 74 3 (2008) 705-713. The authors show that the levels of CTR1 mRNA are under tight homeostatic control and suggest the mechanisms for CTR1 regulation.
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Copper transport into the secretory pathway is regulated by oxygen in macrophages
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By measuring levels of proteins involved in copper trafficking and the activity of copper-dependent enzymes in the cytosol and the secretory pathway, the authors provide evidence for redirection of intracellular copper flow in response to hypoxia.
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White C., Kambe T., Fulcher Y.G., Sachdev S.W., Bush A.I., Fritsche K., Lee J., Quinn T.P., and Petris M.J. Copper transport into the secretory pathway is regulated by oxygen in macrophages. J Cell Sci 122 Pt 9 (2009) 1315-1321. By measuring levels of proteins involved in copper trafficking and the activity of copper-dependent enzymes in the cytosol and the secretory pathway, the authors provide evidence for redirection of intracellular copper flow in response to hypoxia.
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White, C.1
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Petris, M.J.9
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A role for the ATP7A copper-transporting ATPase in macrophage bactericidal activity
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The observed increased of copper uptake and trafficking of ATP7A in response to inflammatory stimuli suggests the role for mammalian Cu-ATPases in response to infection. In bacterial cells the Cu-ATPase appear to play a reciprocal role increasing cell pathogenicity.
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White C., Lee J., Kambe T., Fritsche K., and Petris M.J. A role for the ATP7A copper-transporting ATPase in macrophage bactericidal activity. J Biol Chem 284 49 (2009) 33949-33956. The observed increased of copper uptake and trafficking of ATP7A in response to inflammatory stimuli suggests the role for mammalian Cu-ATPases in response to infection. In bacterial cells the Cu-ATPase appear to play a reciprocal role increasing cell pathogenicity.
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Copper transporter 1, metallothionein and glutathione reductase genes are differentially expressed in tissues of sea bream (Sparus aurata) after exposure to dietary or waterborne copper
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Minghetti M., Leaver M.J., Carpenè E., and George S.G. Copper transporter 1, metallothionein and glutathione reductase genes are differentially expressed in tissues of sea bream (Sparus aurata) after exposure to dietary or waterborne copper. Comp Biochem Physiol C Toxicol Pharmacol 147 4 (2008) 450-459
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Human copper transporter 2 is localized in late endosomes and lysosomes and facilitates cellular copper uptake
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van den Berghe P.V., Folmer D.E., Malingré H.E.M., vanBeurden E., Klomp A.E.M., vandeSluis B., Merkx M., Berger R., and Klomp L.W.J. Human copper transporter 2 is localized in late endosomes and lysosomes and facilitates cellular copper uptake. Biochem J 407 1 (2007) 49-59
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Ctr2 is partially localized to the plasma membrane and stimulates copper uptake in COS-7 cells
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Bertinato J., Swist E., Plouffe L.J., Brooks S.P.J., and L'abbe M.R. Ctr2 is partially localized to the plasma membrane and stimulates copper uptake in COS-7 cells. Biochem J 409 3 (2008) 731-740
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Rees E.M., and Thiele D.J. Identification of a vacuole-associated metalloreductase and its role in Ctr2-mediated intracellular copper mobilization. J Biol Chem 282 30 (2007) 21629-21638
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Pulling the plug" on cellular copper: the role of mitochondria in copper export
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A comprehensive and detailed review on the copper handing machinery in mitochondria and a cross-talk between copper distribution pathways in a cell.
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Leary S.C., Winge D.R., and Cobine P.A. Pulling the plug" on cellular copper: the role of mitochondria in copper export. Biochim Biophys Acta 1793 1 (2009) 146-153. A comprehensive and detailed review on the copper handing machinery in mitochondria and a cross-talk between copper distribution pathways in a cell.
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Different regulation of wild-type and mutant Cu, Zn superoxide dismutase localization in mammalian mitochondria
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A systematic analysis of factors that influence mitochondria localization of SOD1 mitochondrial localization. The authors formulate the idea that CCS couples the function of copper chaperon with oxygen sensing.
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Kawamata H., and Manfredi G. Different regulation of wild-type and mutant Cu, Zn superoxide dismutase localization in mammalian mitochondria. Hum Mol Genet 17 21 (2008) 3303-3317. A systematic analysis of factors that influence mitochondria localization of SOD1 mitochondrial localization. The authors formulate the idea that CCS couples the function of copper chaperon with oxygen sensing.
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Kawamata, H.1
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Wood L.K., and Thiele D.J. Transcriptional activation in yeast in response to copper deficiency involves copper-zinc superoxide dismutase. J Biol Chem 284 1 (2009) 404-413
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Novel role of antioxidant-1 (Atox1) as a copper-dependent transcription factor involved in cell proliferation
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Itoh S., Won Kim H., Nakagawa O., Ozumi K., Lessner S.M., Aoki H., Akram K., McKinney R.D., Ushio-Fukai M., and Fukai T. Novel role of antioxidant-1 (Atox1) as a copper-dependent transcription factor involved in cell proliferation. J Biol Chem 283 14 (2008) 9157-9167
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McRae R., Lai B., and Fahrni C.J. Copper redistribution in Atox1-deficient mouse fibroblast cells. J Biol Inorg Chem (2009). http://www.springerlink.com/content/k84m26m527232246/ http://www.springerlink.com/content/k84m26m527232246/
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McRae, R.1
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Fahrni, C.J.3
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23
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44349167847
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Mitochondrial copper(I) transfer from Cox17 to Sco1 is coupled to electron transfer
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Using solution NMR, the authors discover simultaneous transfer of copper and electrons; this process may represent a new mechanism of selective copper delivery.
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Banci L., Bertini I., Ciofi-Baffoni S., Hadjiloi T., Martinelli M., and Palumaa P. Mitochondrial copper(I) transfer from Cox17 to Sco1 is coupled to electron transfer. Proc Natl Acad Sci USA 105 19 (2008) 6803-6808. Using solution NMR, the authors discover simultaneous transfer of copper and electrons; this process may represent a new mechanism of selective copper delivery.
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Banci, L.1
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24
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Human SCO2 is required for the synthesis of CO II and as a thiol-disulphide oxidoreductase for SCO1
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A comprehensive studies demonstrating that each of two SCO protein has distinct, stage-specific functions during CCO biosynthesis and CuA site maturation.
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Leary S.C., Sasarman F., Nishimura T., and Shoubridge E.A. Human SCO2 is required for the synthesis of CO II and as a thiol-disulphide oxidoreductase for SCO1. Hum Mol Genet 18 12 (2009) 2230-2240. A comprehensive studies demonstrating that each of two SCO protein has distinct, stage-specific functions during CCO biosynthesis and CuA site maturation.
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Crystal structure of human copper homeostasis protein CutC reveals a potential copper-binding site
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Li Y., Du J., Zhang P., and Ding J. Crystal structure of human copper homeostasis protein CutC reveals a potential copper-binding site. J Struct Biol (2009) doi:10.1016/j.jsb.2009.10.012
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Calafato S., Swain S., Hughes S., Kille P., and Stürzenbaum S.R. Knock down of Caenorhabditis elegans cutc-1 exacerbates the sensitivity toward high levels of copper. Toxicol Sci 106 2 (2008) 384-391
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Human copper transporter Ctr1 is functional in Drosophila, revealing a high degree of conservation between mammals and insects
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Hua H., Georgiev O., Schaffner W., and Steiger D. Human copper transporter Ctr1 is functional in Drosophila, revealing a high degree of conservation between mammals and insects. J Biol Inorg Chem 15 1 (2010) 107-113
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Three-dimensional structure of the human copper transporter hCTR1
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The structure allows for visualization of copper translocation pathways and suggest the mechanism for copper entry and exit from the transporter. Copper binding to CTR1 is directly demonstrated.
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De Feo C.J., Aller S.G., Siluvai G.S., Blackburn N.J., and Unger V.M. Three-dimensional structure of the human copper transporter hCTR1. Proc Natl Acad Sci USA 106 11 (2009) 4237-4242. The structure allows for visualization of copper translocation pathways and suggest the mechanism for copper entry and exit from the transporter. Copper binding to CTR1 is directly demonstrated.
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Proc Natl Acad Sci USA
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A comprehensive review summarizing a rapidly growing set of data on the structure of proteins involved in cellular copper delivery and transport in various organisms.
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Boal A.K., and Rosenzweig A.C. Structural biology of copper trafficking. Chem Rev 109 10 (2009) 4760-4779. A comprehensive review summarizing a rapidly growing set of data on the structure of proteins involved in cellular copper delivery and transport in various organisms.
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Miyayama T., Suzuki K.T., and Ogra Y. Copper accumulation and compartmentalization in mouse fibroblast lacking metallothionein and copper chaperone, Atox1. Toxicol Appl Pharmacol 237 2 (2009) 205-213
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Hernandez S., Tsuchiya Y., García-Ruiz J.P., Lalioti V., Nielsen S., Cassio D., and Sandoval I.V. ATP7B copper-regulated traffic and association with the tight junctions: copper excretion into the bile. Gastroenterology 134 4 (2008) 1215-1223
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The first in vivo demonstration that the downregulation of ATP7B in animals via a targeted siRNA delivery facilitates the potency of cisplatin treatment and decreases tumor growth.
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Mangala L.S., et al. Therapeutic Targeting of ATP7B in Ovarian Carcinoma. Clin Cancer Res 15 11 (2009) 3770-3780. The first in vivo demonstration that the downregulation of ATP7B in animals via a targeted siRNA delivery facilitates the potency of cisplatin treatment and decreases tumor growth.
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