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Volumn 28, Issue 8, 2003, Pages 406-410

The prion protein and neuronal zinc homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; METAL ION; PRION PROTEIN; ZINC ION;

EID: 0042658237     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(03)00166-X     Document Type: Article
Times cited : (75)

References (50)
  • 1
    • 0011119273 scopus 로고    scopus 로고
    • The biological roles of zinc and families of zinc metalloproteases
    • N.M. Hooper. Taylor & Francis
    • Hooper N.M. The biological roles of zinc and families of zinc metalloproteases. Hooper N.M. Zinc Metalloproteases in Health and Disease. 1996;1-21 Taylor & Francis.
    • (1996) Zinc Metalloproteases in Health and Disease , pp. 1-21
    • Hooper, N.M.1
  • 2
    • 0029866646 scopus 로고    scopus 로고
    • The galvanization of biology: A growing appreciation for the roles of zinc
    • Berg J.M., Shi Y. The galvanization of biology: a growing appreciation for the roles of zinc. Science. 271:1996;1081-1085.
    • (1996) Science , vol.271 , pp. 1081-1085
    • Berg, J.M.1    Shi, Y.2
  • 3
    • 0036468837 scopus 로고    scopus 로고
    • Carbonic anhydrase gating of attention: Memory therapy and enhancement
    • Sun M.K., Alkon D.L. Carbonic anhydrase gating of attention: memory therapy and enhancement. Trends Pharmacol. Sci. 23:2002;83-89.
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 83-89
    • Sun, M.K.1    Alkon, D.L.2
  • 4
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis
    • Outten C.E., O'Halloran T.V. Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science. 292:2001;2488-2492.
    • (2001) Science , vol.292 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 5
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • Pauly P.C., Harris D.A. Copper stimulates endocytosis of the prion protein. J. Biol. Chem. 273:1998;33107-33110.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 6
    • 0035799312 scopus 로고    scopus 로고
    • Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat region
    • Perera W.S.S., Hooper N.M. Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat region. Curr. Biol. 11:2001;519-523.
    • (2001) Curr. Biol. , vol.11 , pp. 519-523
    • Perera, W.S.S.1    Hooper, N.M.2
  • 7
    • 0034306057 scopus 로고    scopus 로고
    • 2+: A novel ionic mediator of neural injury in brain disease
    • 2+: a novel ionic mediator of neural injury in brain disease. Trends Pharmacol. Sci. 21:2000;395-401.
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 395-401
    • Weiss, J.H.1
  • 8
    • 0024779411 scopus 로고
    • Neurobiology of zinc and zinc-containing neurons
    • Frederickson C.J. Neurobiology of zinc and zinc-containing neurons. Int. Rev. Neurobiol. 31:1989;145-238.
    • (1989) Int. Rev. Neurobiol. , vol.31 , pp. 145-238
    • Frederickson, C.J.1
  • 9
    • 0033674209 scopus 로고    scopus 로고
    • Movement of zinc and its functional significance in the brain
    • Takeda A. Movement of zinc and its functional significance in the brain. Brain Res. Brain Res. Rev. 34:2000;137-148.
    • (2000) Brain Res. Brain Res. Rev. , vol.34 , pp. 137-148
    • Takeda, A.1
  • 10
    • 0021287299 scopus 로고
    • 2+ from brain tissue during activity
    • 2+ from brain tissue during activity. Nature. 308:1984;734-736.
    • (1984) Nature , vol.308 , pp. 734-736
    • Assaf, S.Y.1    Chung, S.H.2
  • 11
    • 0031953430 scopus 로고    scopus 로고
    • Mammalian zinc transporters
    • McMahon R.J., Cousins R.J. Mammalian zinc transporters. J. Nutr. 128:1998;667-670.
    • (1998) J. Nutr. , vol.128 , pp. 667-670
    • McMahon, R.J.1    Cousins, R.J.2
  • 12
    • 0034091981 scopus 로고    scopus 로고
    • Zinc transport in the brain: Routes of zinc influx and efflux in neurons
    • Colvin R.A., et al. Zinc transport in the brain: routes of zinc influx and efflux in neurons. J. Nutr. 130:2000;1484S-1487S.
    • (2000) J. Nutr. , vol.130
    • Colvin, R.A.1
  • 13
    • 0035693722 scopus 로고    scopus 로고
    • Eukaryotic zinc transporters and their regulation
    • Gaither L.A., Eide D.J. Eukaryotic zinc transporters and their regulation. Biometals. 14:2001;251-270.
    • (2001) Biometals , vol.14 , pp. 251-270
    • Gaither, L.A.1    Eide, D.J.2
  • 14
    • 0030755366 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian proton-coupled metal-ion transporter
    • Gunshin H., et al. Cloning and characterization of a mammalian proton-coupled metal-ion transporter. Nature. 388:1997;482-488.
    • (1997) Nature , vol.388 , pp. 482-488
    • Gunshin, H.1
  • 16
    • 0035254585 scopus 로고    scopus 로고
    • Prion and prejudice: Normal protein and the synapse
    • Brown D.R. Prion and prejudice: normal protein and the synapse. Trends Neurosci. 24:2001;85-90.
    • (2001) Trends Neurosci. , vol.24 , pp. 85-90
    • Brown, D.R.1
  • 17
    • 0033515029 scopus 로고    scopus 로고
    • Copper binding to the prion protein: Structural implications of four identical cooperative binding sites
    • Viles J.H., et al. Copper binding to the prion protein: structural implications of four identical cooperative binding sites. Proc. Natl. Acad. Sci. U. S. A. 96:1999;2042-2047.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 2042-2047
    • Viles, J.H.1
  • 18
    • 0033996803 scopus 로고    scopus 로고
    • Copper binding to octarepeat peptides of the prion protein monitored by mass spectrometry
    • Whittal R.M., et al. Copper binding to octarepeat peptides of the prion protein monitored by mass spectrometry. Protein Sci. 9:2000;332-343.
    • (2000) Protein Sci. , vol.9 , pp. 332-343
    • Whittal, R.M.1
  • 19
    • 0035902531 scopus 로고    scopus 로고
    • Location and properties of metal-binding sites on the human prion protein
    • Jackson G.S., et al. Location and properties of metal-binding sites on the human prion protein. Proc. Natl. Acad. Sci. U. S. A. 98:2001;8531-8535.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 8531-8535
    • Jackson, G.S.1
  • 20
    • 0037470178 scopus 로고    scopus 로고
    • Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: Insights from circular dichroism
    • Garnett A.P., Viles J.H. Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: insights from circular dichroism. J. Biol. Chem. 278:2003;6795-6802.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6795-6802
    • Garnett, A.P.1    Viles, J.H.2
  • 21
    • 0031444294 scopus 로고    scopus 로고
    • The cellular prion protein binds copper in vivo
    • Brown D.R., et al. The cellular prion protein binds copper in vivo. Nature. 390:1997;684-687.
    • (1997) Nature , vol.390 , pp. 684-687
    • Brown, D.R.1
  • 22
    • 0034654304 scopus 로고    scopus 로고
    • Consequences of manganese replacement of copper for prion protein function and proteinase resistance
    • Brown D.R., et al. Consequences of manganese replacement of copper for prion protein function and proteinase resistance. EMBO J. 19:2000;1180-1186.
    • (2000) EMBO J. , vol.19 , pp. 1180-1186
    • Brown, D.R.1
  • 23
    • 0037127206 scopus 로고    scopus 로고
    • Mapping Cu(II) binding sites in prion proteins by diethyl pyrocarbonate modification and matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometric footprinting
    • Qin K., et al. Mapping Cu(II) binding sites in prion proteins by diethyl pyrocarbonate modification and matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometric footprinting. J. Biol. Chem. 277:2002;1981-1990.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1981-1990
    • Qin, K.1
  • 24
    • 0036181492 scopus 로고    scopus 로고
    • Short peptides are not reliable models of thermodynamic and kinetic properties of the N-terminal metal binding site in serum albumin
    • Sokolowska M., et al. Short peptides are not reliable models of thermodynamic and kinetic properties of the N-terminal metal binding site in serum albumin. Eur. J. Biochem. 269:2002;1323-1331.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1323-1331
    • Sokolowska, M.1
  • 25
    • 0036301061 scopus 로고    scopus 로고
    • Prion protein interaction with glycosaminoglycan occurs with the formation of oligomeric complexes stabilized by Cu(II) bridges
    • Gonzalez-Iglesias R., et al. Prion protein interaction with glycosaminoglycan occurs with the formation of oligomeric complexes stabilized by Cu(II) bridges. J. Mol. Biol. 319:2002;527-540.
    • (2002) J. Mol. Biol. , vol.319 , pp. 527-540
    • Gonzalez-Iglesias, R.1
  • 26
    • 0034790685 scopus 로고    scopus 로고
    • Internalization of mammalian fluorescent cellular prion protein and N-terminal deletion mutants in living cells
    • Lee K.S., et al. Internalization of mammalian fluorescent cellular prion protein and N-terminal deletion mutants in living cells. J. Neurochem. 79:2001;79-87.
    • (2001) J. Neurochem. , vol.79 , pp. 79-87
    • Lee, K.S.1
  • 27
    • 0037715143 scopus 로고    scopus 로고
    • Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery
    • Rachidi W., et al. Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery. J. Biol. Chem. 278:2003;9064-9072.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9064-9072
    • Rachidi, W.1
  • 28
    • 0032999810 scopus 로고    scopus 로고
    • Mounting evidence for the involvement of zinc and copper in Alzheimer's disease
    • Moir R.D., et al. Mounting evidence for the involvement of zinc and copper in Alzheimer's disease. Eur. J. Clin. Invest. 29:1999;569-570.
    • (1999) Eur. J. Clin. Invest. , vol.29 , pp. 569-570
    • Moir, R.D.1
  • 29
    • 0033570367 scopus 로고    scopus 로고
    • Evidence of presynaptic location and function of the prion protein
    • Herms J., et al. Evidence of presynaptic location and function of the prion protein. J. Neurosci. 19:1999;8866-8875.
    • (1999) J. Neurosci. , vol.19 , pp. 8866-8875
    • Herms, J.1
  • 30
    • 0034678023 scopus 로고    scopus 로고
    • Brain copper content and cuproenzyme activity do not vary with prion protein expression level
    • Waggoner D.J., et al. Brain copper content and cuproenzyme activity do not vary with prion protein expression level. J. Biol. Chem. 275:2000;7455-7458.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7455-7458
    • Waggoner, D.J.1
  • 31
    • 0027204276 scopus 로고
    • A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells
    • Shyng S.-L., et al. A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells. J. Biol. Chem. 268:1993;15922-15928.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15922-15928
    • Shyng, S.-L.1
  • 32
    • 18344369706 scopus 로고    scopus 로고
    • Molecular features of the copper binding sites in the octarepeat domain of the prion protein
    • Burns C.S., et al. Molecular features of the copper binding sites in the octarepeat domain of the prion protein. Biochemistry. 41:2002;3991-4001.
    • (2002) Biochemistry , vol.41 , pp. 3991-4001
    • Burns, C.S.1
  • 33
    • 0008563243 scopus 로고
    • GPI anchors. More than just a membrane anchor
    • Hooper N.M. GPI anchors. More than just a membrane anchor. Curr. Biol. 2:1992;617-619.
    • (1992) Curr. Biol. , vol.2 , pp. 617-619
    • Hooper, N.M.1
  • 34
    • 0034665847 scopus 로고    scopus 로고
    • Signal transduction through prion protein
    • Mouillet-Richard S., et al. Signal transduction through prion protein. Science. 289:2000;1925-1928.
    • (2000) Science , vol.289 , pp. 1925-1928
    • Mouillet-Richard, S.1
  • 35
    • 0036645677 scopus 로고    scopus 로고
    • Cellular prion protein transduces neuroprotective signals
    • Chiarini L.B., et al. Cellular prion protein transduces neuroprotective signals. EMBO J. 21:2002;3317-3326.
    • (2002) EMBO J. , vol.21 , pp. 3317-3326
    • Chiarini, L.B.1
  • 36
    • 0035696301 scopus 로고    scopus 로고
    • Functions of zinc in signaling, proliferation and differentiation of mammalian cells
    • Beyersmann D., Haase H. Functions of zinc in signaling, proliferation and differentiation of mammalian cells. Biometals. 14:2001;331-341.
    • (2001) Biometals , vol.14 , pp. 331-341
    • Beyersmann, D.1    Haase, H.2
  • 37
    • 0034764599 scopus 로고    scopus 로고
    • Oxidative impairment in scrapie-infected mice is associated with brain metals perturbations and altered antioxidant activities
    • Wong B.S., et al. Oxidative impairment in scrapie-infected mice is associated with brain metals perturbations and altered antioxidant activities. J. Neurochem. 79:2001;689-698.
    • (2001) J. Neurochem. , vol.79 , pp. 689-698
    • Wong, B.S.1
  • 38
    • 0037083888 scopus 로고    scopus 로고
    • Metal imbalance and compromised antioxidant function are early changes in prion disease
    • Thackray A.M., et al. Metal imbalance and compromised antioxidant function are early changes in prion disease. Biochem. J. 362:2002;253-258.
    • (2002) Biochem. J. , vol.362 , pp. 253-258
    • Thackray, A.M.1
  • 39
    • 0035838471 scopus 로고    scopus 로고
    • Copper and zinc binding modulates the aggregation and neurotoxic properties of the prion peptide PrP106-126
    • Jobling M.F., et al. Copper and zinc binding modulates the aggregation and neurotoxic properties of the prion peptide PrP106-126. Biochemistry. 40:2001;8073-8084.
    • (2001) Biochemistry , vol.40 , pp. 8073-8084
    • Jobling, M.F.1
  • 40
    • 0036900691 scopus 로고    scopus 로고
    • TSE agent strains and PrP: Reconciling structure and function
    • Somerville R.A. TSE agent strains and PrP: reconciling structure and function. Trends Biochem. Sci. 27:2002;606-612.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 606-612
    • Somerville, R.A.1
  • 41
    • 0033130083 scopus 로고    scopus 로고
    • Strain-specific prion-protein conformation determined by metal ions
    • Wadsworth J.D.F., et al. Strain-specific prion-protein conformation determined by metal ions. Nat. Cell Biol. 1:1999;55-59.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 55-59
    • Wadsworth, J.D.F.1
  • 42
    • 0027220686 scopus 로고
    • A novel zinc(II) binding site modulates the function of the βA4 amyloid protein precursor of Alzheimer's disease
    • Bush A.I., et al. A novel zinc(II) binding site modulates the function of the βA4 amyloid protein precursor of Alzheimer's disease. J. Biol. Chem. 268:1993;16109-16112.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16109-16112
    • Bush, A.I.1
  • 43
    • 0033844944 scopus 로고    scopus 로고
    • Characterization of copper interactions with alzheimer amyloid β peptides: Identification of an attomolar-affinity copper binding site on amyloid β1-42
    • Atwood C.S., et al. Characterization of copper interactions with alzheimer amyloid β peptides: identification of an attomolar-affinity copper binding site on amyloid β1-42. J. Neurochem. 75:2000;1219-1233.
    • (2000) J. Neurochem. , vol.75 , pp. 1219-1233
    • Atwood, C.S.1
  • 44
    • 0034733705 scopus 로고    scopus 로고
    • Evidence that the β-amyloid plaques of Alzheimer's disease represent the redox-silencing and entombment of Aβ by zinc
    • Cuajungco M.P., et al. Evidence that the β-amyloid plaques of Alzheimer's disease represent the redox-silencing and entombment of Aβ by zinc. J. Biol. Chem. 275:2000;19439-19442.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19439-19442
    • Cuajungco, M.P.1
  • 45
    • 0028180196 scopus 로고
    • Modulation of Aβ adhesiveness and secretase site cleavage by zinc
    • Bush A.I., et al. Modulation of Aβ adhesiveness and secretase site cleavage by zinc. J. Biol. Chem. 269:1994;12152-12158.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12152-12158
    • Bush, A.I.1
  • 46
    • 0037188530 scopus 로고    scopus 로고
    • Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice
    • Lee J.Y., et al. Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice. Proc. Natl. Acad. Sci. U. S. A. 99:2002;7705-7710.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 7705-7710
    • Lee, J.Y.1
  • 47
    • 0034964390 scopus 로고    scopus 로고
    • Treatment with a copper-zinc chelator markedly and rapidly inhibits β-amyloid accumulation in Alzheimer's disease transgenic mice
    • Cherny R.A., et al. Treatment with a copper-zinc chelator markedly and rapidly inhibits β-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron. 30:2001;665-676.
    • (2001) Neuron , vol.30 , pp. 665-676
    • Cherny, R.A.1
  • 48
    • 18444399243 scopus 로고    scopus 로고
    • Treatment of Alzheimer's disease with clioquinol
    • Regland B., et al. Treatment of Alzheimer's disease with clioquinol. Dement. Geriatr. Cogn. Disord. 12:2001;408-414.
    • (2001) Dement. Geriatr. Cogn. Disord. , vol.12 , pp. 408-414
    • Regland, B.1
  • 49
    • 16044366720 scopus 로고    scopus 로고
    • Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein
    • Lyons T.J., et al. Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein. Proc. Natl. Acad. Sci. U. S. A. 93:1996;12240-12244.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 12240-12244
    • Lyons, T.J.1
  • 50
    • 0030833449 scopus 로고    scopus 로고
    • Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite
    • Crow J.P., et al. Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite. J. Neurochem. 69:1997;1936-1944.
    • (1997) J. Neurochem. , vol.69 , pp. 1936-1944
    • Crow, J.P.1


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