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Volumn 34, Issue 1, 2012, Pages 67-80

Gene expression profiling of nephrotoxicity from copper nanoparticles in rats after repeated oral administration

Author keywords

Copper nanoparticals; Microarray; Nanotoxicology; Nephrotoxicity; Toxicogenomics

Indexed keywords

COMPLEMENT; COPPER DERIVATIVE; COPPER NANOPARTICLE; CREATININE; GLUTATHIONE; ISOLEUCINE; LEUCINE; METAL NANOPARTICLE; MICROCOPPER; MITOGEN ACTIVATED PROTEIN KINASE; NANOCOPPER; NITROGEN; TRANSCRIPTOME; UNCLASSIFIED DRUG; UREA; VALINE;

EID: 84859097539     PISSN: 13826689     EISSN: 18727077     Source Type: Journal    
DOI: 10.1016/j.etap.2011.05.014     Document Type: Article
Times cited : (73)

References (52)
  • 2
    • 23144451917 scopus 로고    scopus 로고
    • Cdc2-cyclin E complexes regulate the G1/S phase transition
    • Aleem E., Kiyokawa H., Kaldis P. Cdc2-cyclin E complexes regulate the G1/S phase transition. Nat Cell Biol. 2005, 7:831-836.
    • (2005) Nat Cell Biol. , vol.7 , pp. 831-836
    • Aleem, E.1    Kiyokawa, H.2    Kaldis, P.3
  • 4
    • 0037131165 scopus 로고    scopus 로고
    • Shedding of kidney injury molecule-1, a putative adhesion protein involved in renal regeneration
    • Bailly V., Zhang Z., Meier W., Cate R., Sanicola M., Bonventre J.V. Shedding of kidney injury molecule-1, a putative adhesion protein involved in renal regeneration. J. Biol. Chem. 2002, 277:39739-39748.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39739-39748
    • Bailly, V.1    Zhang, Z.2    Meier, W.3    Cate, R.4    Sanicola, M.5    Bonventre, J.V.6
  • 5
    • 0037836057 scopus 로고    scopus 로고
    • Dedifferentiation and proliferation of surviving epithelial cells in acute renal failure
    • Bonventre J.V. Dedifferentiation and proliferation of surviving epithelial cells in acute renal failure. J. Am. Soc. Nephrol. 2003, 14(Suppl. 1):S55-S61.
    • (2003) J. Am. Soc. Nephrol. , vol.14 , Issue.SUPPL. 1
    • Bonventre, J.V.1
  • 6
    • 33746329868 scopus 로고    scopus 로고
    • Energy converting NADH: quinone oxidoreductase (Complex I)
    • Brandt U. Energy converting NADH: quinone oxidoreductase (Complex I). Annu. Rev. Biochem. 2006, 75:69-92.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 69-92
    • Brandt, U.1
  • 7
    • 23444432514 scopus 로고    scopus 로고
    • Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit
    • Carbajo R.J., Kellas F.A., Runswick M.J., Montgomery M.G., Walker J.E., Neuhaus D. Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit. J. Mol. Biol. 2005, 351:824-838.
    • (2005) J. Mol. Biol. , vol.351 , pp. 824-838
    • Carbajo, R.J.1    Kellas, F.A.2    Runswick, M.J.3    Montgomery, M.G.4    Walker, J.E.5    Neuhaus, D.6
  • 12
    • 28944450314 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase (MAPK)
    • Cuschieri J., Maier R.V. Mitogen-activated protein kinase (MAPK). Crit. Care Med. 2005, 33:S417-S419.
    • (2005) Crit. Care Med. , vol.33
    • Cuschieri, J.1    Maier, R.V.2
  • 13
    • 28844501956 scopus 로고    scopus 로고
    • Thioredoxin and its role in premature newborn biology
    • Das K.C. Thioredoxin and its role in premature newborn biology. Antioxid. Redox Signal. 2005, 7:1740-1743.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 1740-1743
    • Das, K.C.1
  • 14
    • 33745597580 scopus 로고    scopus 로고
    • Carbon nanotubes: a review of their properties in relation to pulmonary toxicology and workplace safety
    • Donaldson K., Aitken R., Tran L., Stone V., Duffin R., Forrest G., Alexander A. Carbon nanotubes: a review of their properties in relation to pulmonary toxicology and workplace safety. Toxicol. Sci. 2006, 92:5-22.
    • (2006) Toxicol. Sci. , vol.92 , pp. 5-22
    • Donaldson, K.1    Aitken, R.2    Tran, L.3    Stone, V.4    Duffin, R.5    Forrest, G.6    Alexander, A.7
  • 15
    • 0024565997 scopus 로고
    • Cdc2 protein kinase is complexed with both cyclin A and B: evidence for proteolytic inactivation of MPF
    • Draetta G., Luca F., Westendorf J., Brizuela L., Ruderman J., Beach D. Cdc2 protein kinase is complexed with both cyclin A and B: evidence for proteolytic inactivation of MPF. Cell 1989, 56:829-838.
    • (1989) Cell , vol.56 , pp. 829-838
    • Draetta, G.1    Luca, F.2    Westendorf, J.3    Brizuela, L.4    Ruderman, J.5    Beach, D.6
  • 16
    • 0035809921 scopus 로고    scopus 로고
    • The localization of human cyclins B1 and B2 determines CDK1 substrate specificity and neither enzyme requires MEK to disassemble the Golgi apparatus
    • Draviam V.M., Orrechia S., Lowe M., Pardi R., Pines J. The localization of human cyclins B1 and B2 determines CDK1 substrate specificity and neither enzyme requires MEK to disassemble the Golgi apparatus. J. Cell Biol. 2001, 152:945-958.
    • (2001) J. Cell Biol. , vol.152 , pp. 945-958
    • Draviam, V.M.1    Orrechia, S.2    Lowe, M.3    Pardi, R.4    Pines, J.5
  • 19
    • 0027994002 scopus 로고
    • An osmosensing signal transduction pathway in mammalian cells
    • Galcheva-Garzova Z., Derijard B., Wu J.H., Davis R.J. An osmosensing signal transduction pathway in mammalian cells. Science 1994, 265:806-808.
    • (1994) Science , vol.265 , pp. 806-808
    • Galcheva-Garzova, Z.1    Derijard, B.2    Wu, J.H.3    Davis, R.J.4
  • 21
    • 0029119740 scopus 로고
    • Cell cycle control in mammalian cells: role of cyclins, cyclin dependent kinases (CDKs), growth suppressor genes and cyclin-dependent kinase inhibitors (CKIs)
    • Grana X., Reddy E.P. Cell cycle control in mammalian cells: role of cyclins, cyclin dependent kinases (CDKs), growth suppressor genes and cyclin-dependent kinase inhibitors (CKIs). Oncogene 1995, 11:211-219.
    • (1995) Oncogene , vol.11 , pp. 211-219
    • Grana, X.1    Reddy, E.P.2
  • 22
    • 0141920354 scopus 로고    scopus 로고
    • Comparing protein abundance and mRNA expression levels on a genomic scale
    • Greenbaum D., Colangelo C., Williams K., Gerstein M. Comparing protein abundance and mRNA expression levels on a genomic scale. Genome Biol. 2003, 4(9):117.
    • (2003) Genome Biol. , vol.4 , Issue.9 , pp. 117
    • Greenbaum, D.1    Colangelo, C.2    Williams, K.3    Gerstein, M.4
  • 24
    • 59149102096 scopus 로고    scopus 로고
    • Comparison of molecular and histological changes in zebrafish gills exposed to metallic nanoparticles
    • Griffit R.J., Hyndman K., Denslow N.D., Barber D.S. Comparison of molecular and histological changes in zebrafish gills exposed to metallic nanoparticles. Toxicol. Sci. 2009, 107(2):404-415.
    • (2009) Toxicol. Sci. , vol.107 , Issue.2 , pp. 404-415
    • Griffit, R.J.1    Hyndman, K.2    Denslow, N.D.3    Barber, D.S.4
  • 25
  • 26
    • 0036314217 scopus 로고    scopus 로고
    • Kidney Injury Molecule-1 (KIM-1): a novel biomarker for human renal proximal tubule injury
    • Han W.K., Bailly V., Abichandani R., Thadhani R., Bonventre J.V. Kidney Injury Molecule-1 (KIM-1): a novel biomarker for human renal proximal tubule injury. Kidney Int. 2002, 62:237-244.
    • (2002) Kidney Int. , vol.62 , pp. 237-244
    • Han, W.K.1    Bailly, V.2    Abichandani, R.3    Thadhani, R.4    Bonventre, J.V.5
  • 27
    • 28744434298 scopus 로고    scopus 로고
    • Differential oxidation of thioredoxin-1, thioredoxin-2, and glutathione by metal ions
    • Hansen J.M., Zhang H., Hones D.P. Differential oxidation of thioredoxin-1, thioredoxin-2, and glutathione by metal ions. Free Radic. Biol. Med. 2006, 40:138-145.
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 138-145
    • Hansen, J.M.1    Zhang, H.2    Hones, D.P.3
  • 28
    • 0032874845 scopus 로고    scopus 로고
    • Glutathione and glutathione-dependent enzymes represent a coordinately regulated defence against oxidative stress
    • Hayes J.D., McLellan L.I. Glutathione and glutathione-dependent enzymes represent a coordinately regulated defence against oxidative stress. Free Radic. Res. 1999, 31:273-300.
    • (1999) Free Radic. Res. , vol.31 , pp. 273-300
    • Hayes, J.D.1    McLellan, L.I.2
  • 30
    • 0029032249 scopus 로고
    • The regulation of AP-1 activity by mitogen-activated protein kinases
    • Karin M. The regulation of AP-1 activity by mitogen-activated protein kinases. J. Biol. Chem. 1995, 270:16483-16486.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16483-16486
    • Karin, M.1
  • 32
    • 0030198344 scopus 로고    scopus 로고
    • Protein kinase cascades activated by stress and inflammatory cytokines
    • Kyriakis J.M., Avruch J. Protein kinase cascades activated by stress and inflammatory cytokines. Bioessays 1996, 18:567-577.
    • (1996) Bioessays , vol.18 , pp. 567-577
    • Kyriakis, J.M.1    Avruch, J.2
  • 33
    • 0034595448 scopus 로고    scopus 로고
    • Uninterrupted Mcm2-7 function required for DNA replication fork progression
    • Labib K., Tercero J.A., Diffley J.F. Uninterrupted Mcm2-7 function required for DNA replication fork progression. Science 2000, 288:1643-1647.
    • (2000) Science , vol.288 , pp. 1643-1647
    • Labib, K.1    Tercero, J.A.2    Diffley, J.F.3
  • 34
    • 38849111818 scopus 로고    scopus 로고
    • Cytotoxicity of nanoparticles
    • Lewinski N., Colvin V., Drezek R. Cytotoxicity of nanoparticles. Small 2008, 4:26-49.
    • (2008) Small , vol.4 , pp. 26-49
    • Lewinski, N.1    Colvin, V.2    Drezek, R.3
  • 36
    • 10044268629 scopus 로고    scopus 로고
    • Investigation of the mending effect and mechanism of copper nanoparticles on a tribologically stressed surface
    • Liu G., Li X., Qin B., Xing D., Guo Y., Fan R. Investigation of the mending effect and mechanism of copper nanoparticles on a tribologically stressed surface. Tribology Lett. 2004, 17:961-966.
    • (2004) Tribology Lett. , vol.17 , pp. 961-966
    • Liu, G.1    Li, X.2    Qin, B.3    Xing, D.4    Guo, Y.5    Fan, R.6
  • 37
    • 23644432822 scopus 로고    scopus 로고
    • The effects of stress and aging on glutathione metabolism
    • Maher P. The effects of stress and aging on glutathione metabolism. Ageing Res. Rev. 2005, 4:288-314.
    • (2005) Ageing Res. Rev. , vol.4 , pp. 288-314
    • Maher, P.1
  • 43
    • 36148936711 scopus 로고    scopus 로고
    • Ultrahigh reactivity provokes nanotoxicity: explanation of oral toxicity of nano-copper particles
    • Meng H., Chen Z., Xing G.M., Yuan H., Chen C.Y., Zhao F., Zhang C.C., Zhao Y.L. Ultrahigh reactivity provokes nanotoxicity: explanation of oral toxicity of nano-copper particles. Toxicol. Lett. 2007, 175:102-110.
    • (2007) Toxicol. Lett. , vol.175 , pp. 102-110
    • Meng, H.1    Chen, Z.2    Xing, G.M.3    Yuan, H.4    Chen, C.Y.5    Zhao, F.6    Zhang, C.C.7    Zhao, Y.L.8
  • 44
    • 0035963372 scopus 로고    scopus 로고
    • Cyclin-dependent kinases prevent DNA re-replication through multiple mechanisms
    • Nguyen V.Q., Co C., Li J.J. Cyclin-dependent kinases prevent DNA re-replication through multiple mechanisms. Nature 2001, 411:1068-1073.
    • (2001) Nature , vol.411 , pp. 1068-1073
    • Nguyen, V.Q.1    Co, C.2    Li, J.J.3
  • 46
    • 0026583746 scopus 로고
    • Cyclin A is required at two points in the human cell cycle
    • Pagano M., Pepperkok R., Verde F., Ansorge W., Draetta G. Cyclin A is required at two points in the human cell cycle. EMBO J. 1992, 11:961-971.
    • (1992) EMBO J. , vol.11 , pp. 961-971
    • Pagano, M.1    Pepperkok, R.2    Verde, F.3    Ansorge, W.4    Draetta, G.5
  • 47
    • 34247156315 scopus 로고    scopus 로고
    • Induction of reactive oxygen species and apoptosis in BEAS-2B cells by mercuric chloride
    • Park E.J., Park K. Induction of reactive oxygen species and apoptosis in BEAS-2B cells by mercuric chloride. Toxicol. In Vitro 2007, 21:789-794.
    • (2007) Toxicol. In Vitro , vol.21 , pp. 789-794
    • Park, E.J.1    Park, K.2
  • 48
    • 0024427288 scopus 로고
    • Isolation of a human cyclin cDNA: evidence for cyclin mRNA and protein regulation in the cell cycle and for interaction with p34cdc2
    • Pines J., Hunter T. Isolation of a human cyclin cDNA: evidence for cyclin mRNA and protein regulation in the cell cycle and for interaction with p34cdc2. Cell 1989, 58:833-846.
    • (1989) Cell , vol.58 , pp. 833-846
    • Pines, J.1    Hunter, T.2
  • 49
    • 33748202049 scopus 로고    scopus 로고
    • Glutathione levels and enzyme activity in the tissues of bank vole Clethrionomys glareolus chronically exposed to a mixture of metal contaminants
    • Swiergosz-Kowalewska R., Bednarska A., Kafel A. Glutathione levels and enzyme activity in the tissues of bank vole Clethrionomys glareolus chronically exposed to a mixture of metal contaminants. Chemosphere 2006, 65:963-974.
    • (2006) Chemosphere , vol.65 , pp. 963-974
    • Swiergosz-Kowalewska, R.1    Bednarska, A.2    Kafel, A.3
  • 50
    • 33745713048 scopus 로고    scopus 로고
    • The peripheral stalk of the mitochondrial ATP synthase
    • Walker J.E., Dickson V.K. The peripheral stalk of the mitochondrial ATP synthase. Biochim. Biophys. Acta 2006, 1757:286-296.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 286-296
    • Walker, J.E.1    Dickson, V.K.2
  • 51
    • 0001359504 scopus 로고
    • Glutathione peroxidase
    • Academic Press, New York, NY
    • Wendel A. Glutathione peroxidase. Enzymatic Basis of Detoxification 1980, vol. 1:333-353. Academic Press, New York, NY.
    • (1980) Enzymatic Basis of Detoxification , vol.1 , pp. 333-353
    • Wendel, A.1
  • 52
    • 38949151103 scopus 로고    scopus 로고
    • Nanotechnology in Germany: from forecasting to technological assessment to sustainability studies
    • Zweck A., Bachmann G., Luther W., Ploetz C. Nanotechnology in Germany: from forecasting to technological assessment to sustainability studies. J. Cleaner Prod. 2008, 16:977-987.
    • (2008) J. Cleaner Prod. , vol.16 , pp. 977-987
    • Zweck, A.1    Bachmann, G.2    Luther, W.3    Ploetz, C.4


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