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Volumn 8, Issue 4, 2012, Pages

Genetic inhibition of solute-linked carrier 39 family transporter 1 ameliorates Aβ pathology in a Drosophila model of Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; UNCLASSIFIED DRUG; ZINC; ZINC TRANSPORTER; ZRT IRT LIKE PROTEIN; AMYLOID BETA PROTEIN; CATION TRANSPORT PROTEIN; DROSOPHILA PROTEIN; SLC39A1 PROTEIN, HUMAN; ZIP1 PROTEIN, DROSOPHILA;

EID: 84860549387     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1002683     Document Type: Article
Times cited : (48)

References (42)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • Medicine - The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ, (2002) Medicine- The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 297: 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 2
    • 33749177143 scopus 로고    scopus 로고
    • A hundred years of Alzheimer's disease research
    • Hardy J, (2006) A hundred years of Alzheimer's disease research. Neuron 52: 3-13.
    • (2006) Neuron , vol.52 , pp. 3-13
    • Hardy, J.1
  • 3
    • 34248190279 scopus 로고    scopus 로고
    • Abeta Oligomers - a decade of discovery
    • Walsh DM, Selkoe DJ, (2007) Abeta Oligomers- a decade of discovery. Journal of Neurochemistry 101: 1172-1184.
    • (2007) Journal of Neurochemistry , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 4
    • 0030804608 scopus 로고    scopus 로고
    • Increased amount of zinc in the hippocampus and amygdala of Alzheimer's diseased brains: A proton-induced X-ray emission spectroscopic analysis of cryostat sections from autopsy material
    • Danscher G, Jensen KB, Frederickson CJ, Kemp K, Andreasen A, et al. (1997) Increased amount of zinc in the hippocampus and amygdala of Alzheimer's diseased brains: A proton-induced X-ray emission spectroscopic analysis of cryostat sections from autopsy material. Journal of Neuroscience Methods 76: 53-59.
    • (1997) Journal of Neuroscience Methods , vol.76 , pp. 53-59
    • Danscher, G.1    Jensen, K.B.2    Frederickson, C.J.3    Kemp, K.4    Andreasen, A.5
  • 6
    • 0035696287 scopus 로고    scopus 로고
    • Synaptically released zinc: Physiological functions and pathological effects
    • Frederickson CJ, Bush AI, (2001) Synaptically released zinc: Physiological functions and pathological effects. Biometals 14: 353-366.
    • (2001) Biometals , vol.14 , pp. 353-366
    • Frederickson, C.J.1    Bush, A.I.2
  • 7
    • 0032557425 scopus 로고    scopus 로고
    • Dramatic aggregation of Alzheimer Abeta by Cu(II) is induced by conditions representing physiological acidosis
    • Atwood CS, Moir RD, Huang XD, Scarpa RC, Bacarra NME, et al. (1998) Dramatic aggregation of Alzheimer Abeta by Cu(II) is induced by conditions representing physiological acidosis. Journal of Biological Chemistry 273: 12817-12826.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 12817-12826
    • Atwood, C.S.1    Moir, R.D.2    Huang, X.D.3    Scarpa, R.C.4    Bacarra, N.M.E.5
  • 10
    • 36649017112 scopus 로고    scopus 로고
    • Amyloid plaques arise from zinc-enriched cortical layers in APP/PS1 transgenic mice and are paradoxically enlarged with dietary zinc deficiency
    • Stoltenberg M, Bush AI, Bach G, Smidt K, Larsen A, et al. (2007) Amyloid plaques arise from zinc-enriched cortical layers in APP/PS1 transgenic mice and are paradoxically enlarged with dietary zinc deficiency. Neuroscience 150: 357-369.
    • (2007) Neuroscience , vol.150 , pp. 357-369
    • Stoltenberg, M.1    Bush, A.I.2    Bach, G.3    Smidt, K.4    Larsen, A.5
  • 11
    • 0037174856 scopus 로고    scopus 로고
    • Metalloenzyme-like activity of Alzheimer's disease beta-amyloid. Cu-dependent catalytic conversion of dopamine, cholesterol, and biological reducing agents to neurotoxic H2O2
    • Opazo C, Huang XD, Cherny RA, Moir RD, Roher AE, et al. (2002) Metalloenzyme-like activity of Alzheimer's disease beta-amyloid. Cu-dependent catalytic conversion of dopamine, cholesterol, and biological reducing agents to neurotoxic H2O2. Journal of Biological Chemistry 277: 40302-40308.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 40302-40308
    • Opazo, C.1    Huang, X.D.2    Cherny, R.A.3    Moir, R.D.4    Roher, A.E.5
  • 13
    • 0030297178 scopus 로고    scopus 로고
    • Copper, iron, and zinc imbalances in severely degenerated brain regions in Alzheimer's disease: Possible relation to oxidative stress
    • Deibel MA, Ehmann WD, Markesbery WR, (1996) Copper, iron, and zinc imbalances in severely degenerated brain regions in Alzheimer's disease: Possible relation to oxidative stress. Journal of the Neurological Sciences 143: 137-142.
    • (1996) Journal of the Neurological Sciences , vol.143 , pp. 137-142
    • Deibel, M.A.1    Ehmann, W.D.2    Markesbery, W.R.3
  • 14
    • 0031800225 scopus 로고    scopus 로고
    • Imbalances of trace elements related to oxidative damage in Alzheimer's disease brain
    • Cornett CR, Markesbery WR, Ehmann WD, (1998) Imbalances of trace elements related to oxidative damage in Alzheimer's disease brain. Neurotoxicology 19: 339-345.
    • (1998) Neurotoxicology , vol.19 , pp. 339-345
    • Cornett, C.R.1    Markesbery, W.R.2    Ehmann, W.D.3
  • 15
    • 0027327488 scopus 로고
    • Aluminum, Iron, and Zinc Ions Promote Aggregation of Physiological Concentrations of Beta-Amyloid Peptide
    • Mantyh PW, Ghilardi JR, Rogers S, Demaster E, Allen CJ, et al. (1993) Aluminum, Iron, and Zinc Ions Promote Aggregation of Physiological Concentrations of Beta-Amyloid Peptide. Journal of Neurochemistry 61: 1171-1174.
    • (1993) Journal of Neurochemistry , vol.61 , pp. 1171-1174
    • Mantyh, P.W.1    Ghilardi, J.R.2    Rogers, S.3    Demaster, E.4    Allen, C.J.5
  • 17
    • 0030024168 scopus 로고    scopus 로고
    • Aggregation and metal-binding properties of mutant forms of the amyloid Abeta peptide of Alzheimer's disease
    • Clements A, Allsop D, Walsh DM, Williams CH, (1996) Aggregation and metal-binding properties of mutant forms of the amyloid Abeta peptide of Alzheimer's disease. Journal of Neurochemistry 66: 740-747.
    • (1996) Journal of Neurochemistry , vol.66 , pp. 740-747
    • Clements, A.1    Allsop, D.2    Walsh, D.M.3    Williams, C.H.4
  • 19
    • 0034964390 scopus 로고    scopus 로고
    • Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice
    • Cherny RA, Atwood CS, Xilinas ME, Gray DN, Jones WD, et al. (2001) Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron 30: 665-676.
    • (2001) Neuron , vol.30 , pp. 665-676
    • Cherny, R.A.1    Atwood, C.S.2    Xilinas, M.E.3    Gray, D.N.4    Jones, W.D.5
  • 20
    • 33745860362 scopus 로고    scopus 로고
    • Degradation of the Alzheimer disease amyloid beta-peptide by metal-dependent up-regulation of metalloprotease activity
    • White AR, Du T, Laughton KM, Volitakis I, Sharples RA, et al. (2006) Degradation of the Alzheimer disease amyloid beta-peptide by metal-dependent up-regulation of metalloprotease activity. Journal of Biological Chemistry 281: 17670-17680.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 17670-17680
    • White, A.R.1    Du, T.2    Laughton, K.M.3    Volitakis, I.4    Sharples, R.A.5
  • 21
    • 41949115990 scopus 로고    scopus 로고
    • Selective intracellular release of copper and zinc ions from bis(thiosemicarbazonato) complexes reduces levels of Alzheimer disease amyloid-beta peptide
    • Donnelly PS, Caragounis A, Du T, Laughton KM, Volitakis I, et al. (2008) Selective intracellular release of copper and zinc ions from bis(thiosemicarbazonato) complexes reduces levels of Alzheimer disease amyloid-beta peptide. Journal of Biological Chemistry 283: 4568-4577.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 4568-4577
    • Donnelly, P.S.1    Caragounis, A.2    Du, T.3    Laughton, K.M.4    Volitakis, I.5
  • 22
    • 78650480388 scopus 로고    scopus 로고
    • The metal chelating and chaperoning effects of clioquinol: insights from yeast studies
    • Li C, Wang J, Zhou B, (2010) The metal chelating and chaperoning effects of clioquinol: insights from yeast studies. Journal of Alzheimer's Disease 21: 1249-1262.
    • (2010) Journal of Alzheimer's Disease , vol.21 , pp. 1249-1262
    • Li, C.1    Wang, J.2    Zhou, B.3
  • 24
    • 67650050211 scopus 로고    scopus 로고
    • Mammalian Zinc Transporters: Nutritional and Physiologic Regulation
    • Lichten LA, Cousins RJ, (2009) Mammalian Zinc Transporters: Nutritional and Physiologic Regulation. Annual Review of Nutrition 29: 153-176.
    • (2009) Annual Review of Nutrition , vol.29 , pp. 153-176
    • Lichten, L.A.1    Cousins, R.J.2
  • 25
    • 77951118744 scopus 로고    scopus 로고
    • Dietary Zinc Absorption: A Play of Zips and ZnTs in the Gut
    • Wang XX, Zhou B, (2010) Dietary Zinc Absorption: A Play of Zips and ZnTs in the Gut. Iubmb Life 62: 176-182.
    • (2010) Iubmb Life , vol.62 , pp. 176-182
    • Wang, X.X.1    Zhou, B.2
  • 26
    • 17644400171 scopus 로고    scopus 로고
    • The ZIP7 gene (Slc39a7) encodes a zinc transporter involved in zinc homeostasis of the Golgi apparatus
    • Huang LP, Kirschke CP, Zhang YF, Yu YY, (2005) The ZIP7 gene (Slc39a7) encodes a zinc transporter involved in zinc homeostasis of the Golgi apparatus. Journal of Biological Chemistry 280: 15456-15463.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 15456-15463
    • Huang, L.P.1    Kirschke, C.P.2    Zhang, Y.F.3    Yu, Y.Y.4
  • 30
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers-a decade of discovery
    • Walsh DM, Selkoe DJ, (2007) Aβ oligomers-a decade of discovery. J Neurochem 101: 1172-1184.
    • (2007) J Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 31
    • 0037390039 scopus 로고    scopus 로고
    • Insulin-degrading enzyme regulates the levels of insulin, amyloid b-protein, and the b-amyloid precursor protein intracellular domain in vivo
    • Farris W, Mansourian S, Chang Y, Lindsley L, Eckman EA, et al. (2003) Insulin-degrading enzyme regulates the levels of insulin, amyloid b-protein, and the b-amyloid precursor protein intracellular domain in vivo. Proc Natl Acad Sci USA 100: 4162-4167.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4162-4167
    • Farris, W.1    Mansourian, S.2    Chang, Y.3    Lindsley, L.4    Eckman, E.A.5
  • 32
    • 0033621739 scopus 로고    scopus 로고
    • Identification of the major Abeta1-42-degrading catabolic pathway in brain parenchyma: suppression leads to biochemical and pathological deposition
    • Iwata N, Tsubuki S, Takaki Y, Watanabe K, Sekiguchi M, et al. (2003) Identification of the major Abeta1-42-degrading catabolic pathway in brain parenchyma: suppression leads to biochemical and pathological deposition. Nat Med 6 (2): 143-150.
    • (2003) Nat Med , vol.6 , Issue.2 , pp. 143-150
    • Iwata, N.1    Tsubuki, S.2    Takaki, Y.3    Watanabe, K.4    Sekiguchi, M.5
  • 34
    • 0033986037 scopus 로고    scopus 로고
    • Histochemically-reactive zinc in amyloid plaques, angiopathy, and degenerating neurons of Alzheimer's diseased brains
    • Suh SW, Jensen KB, Jensen MS, Silva DS, Kesslak PJ, et al. (2000) Histochemically-reactive zinc in amyloid plaques, angiopathy, and degenerating neurons of Alzheimer's diseased brains. Brain Research 852: 274-278.
    • (2000) Brain Research , vol.852 , pp. 274-278
    • Suh, S.W.1    Jensen, K.B.2    Jensen, M.S.3    Silva, D.S.4    Kesslak, P.J.5
  • 36
    • 76149093866 scopus 로고    scopus 로고
    • Cognitive Loss in Zinc Transporter-3 Knock-Out Mice: A Phenocopy for the Synaptic and Memory Deficits of Alzheimer's Disease?
    • Adlard PA, Parncutt JM, Finkelstein DI, Bush AI, (2010) Cognitive Loss in Zinc Transporter-3 Knock-Out Mice: A Phenocopy for the Synaptic and Memory Deficits of Alzheimer's Disease? Journal of Neuroscience 30: 1631-1636.
    • (2010) Journal of Neuroscience , vol.30 , pp. 1631-1636
    • Adlard, P.A.1    Parncutt, J.M.2    Finkelstein, D.I.3    Bush, A.I.4
  • 37
    • 45949102576 scopus 로고    scopus 로고
    • Abeta 42 Mutants with Different Aggregation Profiles Induce Distinct Pathologies in Drosophila
    • doi:10.1371/journal.pone.0001703
    • Iijima K, Chiang HC, Hearn SA, Hakker I, Gatt A, et al. (2008) Abeta 42 Mutants with Different Aggregation Profiles Induce Distinct Pathologies in Drosophila. PLoS ONE 3: e1703 doi:10.1371/journal.pone.0001703.
    • (2008) PLoS ONE , vol.3
    • Iijima, K.1    Chiang, H.C.2    Hearn, S.A.3    Hakker, I.4    Gatt, A.5
  • 39
    • 0037711556 scopus 로고    scopus 로고
    • Making a better RNAi vector for Drosophila: use of intron spacers
    • Lee YS, Carthew RW, (2003) Making a better RNAi vector for Drosophila: use of intron spacers. Methods 30: 322-329.
    • (2003) Methods , vol.30 , pp. 322-329
    • Lee, Y.S.1    Carthew, R.W.2
  • 40
    • 0041880131 scopus 로고    scopus 로고
    • RNA-mediated neurodegeneration caused by the fragile X premutation rCGG repeats in Drosophila
    • Jin P, Zarnescu DC, Zhang FP, Pearson CE, Lucchesi JC, et al. (2003) RNA-mediated neurodegeneration caused by the fragile X premutation rCGG repeats in Drosophila. Neuron 39: 739-747.
    • (2003) Neuron , vol.39 , pp. 739-747
    • Jin, P.1    Zarnescu, D.C.2    Zhang, F.P.3    Pearson, C.E.4    Lucchesi, J.C.5
  • 41
    • 0027958969 scopus 로고
    • Genetic Dissection of Consolidated Memory in Drosophila
    • Tully T, Preat T, Boynton SC, Delvecchio M, (1994) Genetic Dissection of Consolidated Memory in Drosophila. Cell 79: 35-47.
    • (1994) Cell , vol.79 , pp. 35-47
    • Tully, T.1    Preat, T.2    Boynton, S.C.3    Delvecchio, M.4
  • 42
    • 0028073855 scopus 로고
    • Measurement of zinc in hepatocytes by using a fluorescent probe, Zinquin: relationship to metallothionein and intracellular zinc
    • Coyle P, Zalewski PD, Philcox JC, Forbes IJ, Ward AD, et al. (1994) Measurement of zinc in hepatocytes by using a fluorescent probe, Zinquin: relationship to metallothionein and intracellular zinc. Biochemical Journal 303: 781-786.
    • (1994) Biochemical Journal , vol.303 , pp. 781-786
    • Coyle, P.1    Zalewski, P.D.2    Philcox, J.C.3    Forbes, I.J.4    Ward, A.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.