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Volumn 27, Issue 3, 2005, Pages 347-354

Mouse brain synaptosomes accumulate copper-67 efficiently by two distinct processes independent of cellular prion protein

Author keywords

[No Author keywords available]

Indexed keywords

COPPER 67; EDETIC ACID; HISTIDINE; NICKEL CHLORIDE; PRION PROTEIN; PROTEIN ANTIBODY; ZINC CHLORIDE;

EID: 27644529810     PISSN: 08958696     EISSN: None     Source Type: Journal    
DOI: 10.1385/JMN:27:3:347     Document Type: Article
Times cited : (28)

References (32)
  • 1
    • 0024990371 scopus 로고
    • Further characterization of the process of in vitro uptake of radiolabeled copper by the rat brain
    • Barnea A., Hartter D. E., Cho G., Bhasker K. R., Katz B. M., and Edwards M. D. (1990) Further characterization of the process of in vitro uptake of radiolabeled copper by the rat brain. J. Inorg. Biochem. 40, 103-110.
    • (1990) J. Inorg. Biochem. , vol.40 , pp. 103-110
    • Barnea, A.1    Hartter, D.E.2    Cho, G.3    Bhasker, K.R.4    Katz, B.M.5    Edwards, M.D.6
  • 2
    • 0037931743 scopus 로고    scopus 로고
    • Structure of the Alzheimer's disease amyloid precursor protein copper binding domain. A regulator of neuronal copper homeostasis
    • Barnham K. J., McKinstry W. J., Multhaup G., Galatis D., Morton C. J., Curtain C. C., et al. (2003) Structure of the Alzheimer's disease amyloid precursor protein copper binding domain. A regulator of neuronal copper homeostasis. J. Biol. Chem. 278, 17,401-17,407.
    • (2003) J. Biol. Chem. , vol.278
    • Barnham, K.J.1    McKinstry, W.J.2    Multhaup, G.3    Galatis, D.4    Morton, C.J.5    Curtain, C.C.6
  • 3
    • 2442454597 scopus 로고    scopus 로고
    • Maintaining copper homeostasis: Regulation of copper-trafficking proteins in response to copper deficiancy or overload
    • Bertinato J. and L'Abbe M. R. (2004) Maintaining copper homeostasis: regulation of copper-trafficking proteins in response to copper deficiancy or overload. J. Nutr. Biochem. 15, 316-322.
    • (2004) J. Nutr. Biochem. , vol.15 , pp. 316-322
    • Bertinato, J.1    L'Abbe, M.R.2
  • 4
    • 0141690230 scopus 로고    scopus 로고
    • Copper and zinc cause delivery of the prion protein from the plasma membrane to a subset of early endosomes and the Golgi
    • Brown L. R. and Harris D. A. (2003) Copper and zinc cause delivery of the prion protein from the plasma membrane to a subset of early endosomes and the Golgi. J. Neurochem. 87, 353-363.
    • (2003) J. Neurochem. , vol.87 , pp. 353-363
    • Brown, L.R.1    Harris, D.A.2
  • 6
    • 0026600865 scopus 로고
    • Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein
    • Büeler H., Fischer M., Lang Y., Bluethmann H., Lipp H. P., DeArmond S. J., et al. (1992) Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 356, 577-582.
    • (1992) Nature , vol.356 , pp. 577-582
    • Büeler, H.1    Fischer, M.2    Lang, Y.3    Bluethmann, H.4    Lipp, H.P.5    DeArmond, S.J.6
  • 7
    • 0034035616 scopus 로고    scopus 로고
    • Metals and neuroscience
    • Bush A. I. (2000) Metals and neuroscience. Curr. Opin. Chem. Biol. 4, 184-191.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 184-191
    • Bush, A.I.1
  • 9
    • 0019861796 scopus 로고
    • Synaptosomes from rat brain: Morphology, compartmentation, and transmembrane pH and electrical gradients
    • Deutsch C., Drown C., Rafalowska U., and Silver I. A. (1981) Synaptosomes from rat brain: morphology, compartmentation, and transmembrane pH and electrical gradients. J. Neurochem. 36, 2063-2072.
    • (1981) J. Neurochem. , vol.36 , pp. 2063-2072
    • Deutsch, C.1    Drown, C.2    Rafalowska, U.3    Silver, I.A.4
  • 10
    • 0016745250 scopus 로고
    • An improved method for the preparation of synaptosomal fractions in high purity
    • Hajos F. (1975) An improved method for the preparation of synaptosomal fractions in high purity. Brain Res. 93, 485-489.
    • (1975) Brain Res. , vol.93 , pp. 485-489
    • Hajos, F.1
  • 12
    • 0023830814 scopus 로고
    • Brain tissue accumulates 67copper by two ligand-dependent saturable processes. A high affinity, low capacity and a low affinity, high capacity process
    • Hartter D. E. and Barnea A. (1988) Brain tissue accumulates 67copper by two ligand-dependent saturable processes. A high affinity, low capacity and a low affinity, high capacity process. J. Biol. Chem. 263, 799-805.
    • (1988) J. Biol. Chem. , vol.263 , pp. 799-805
    • Hartter, D.E.1    Barnea, A.2
  • 13
    • 0033570367 scopus 로고    scopus 로고
    • Evidence of presynaptic location and function of the prion protein
    • Herms J., Tings T., Gall S., Madlung A., Giese A., Siebert H., et al. (1999) Evidence of presynaptic location and function of the prion protein. J. Neurosci. 19, 8866-8875.
    • (1999) J. Neurosci. , vol.19 , pp. 8866-8875
    • Herms, J.1    Tings, T.2    Gall, S.3    Madlung, A.4    Giese, A.5    Siebert, H.6
  • 14
    • 0034786489 scopus 로고    scopus 로고
    • Zinc and copper influence excitability of rat olfactory bulb neurons by multiple mechanisms
    • Horning M. S. and Trombley P. Q. (2001) Zinc and copper influence excitability of rat olfactory bulb neurons by multiple mechanisms. J. Neurophysiol. 86, 1652-1660.
    • (2001) J. Neurophysiol. , vol.86 , pp. 1652-1660
    • Horning, M.S.1    Trombley, P.Q.2
  • 15
    • 0028883341 scopus 로고
    • Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein
    • Hornshaw M. P., McDermott J. R., and Candy J. M. (1995a) Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein. Biochem. Biophys. Res. Commun. 207, 621-629.
    • (1995) Biochem. Biophys. Res. Commun. , vol.207 , pp. 621-629
    • Hornshaw, M.P.1    McDermott, J.R.2    Candy, J.M.3
  • 16
    • 0028844207 scopus 로고
    • Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: Structural studies using synthetic peptides
    • Hornshaw M. P., McDermott J. R., Candy J. M., and Lakey J. H. (1995b) Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: structural studies using synthetic peptides. Biochem. Biophys. Res. Commun. 214, 993-999.
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 993-999
    • Hornshaw, M.P.1    McDermott, J.R.2    Candy, J.M.3    Lakey, J.H.4
  • 18
    • 0030449597 scopus 로고    scopus 로고
    • Generation of monoclonal antibodies against human prion proteins in PrP0/0 mice
    • Krasemann S., Groschup M. H., Harmeyer S., Hunsmann G., and Bodemer W. (1996) Generation of monoclonal antibodies against human prion proteins in PrP0/0 mice. Mol. Med. 2, 725-734.
    • (1996) Mol. Med. , vol.2 , pp. 725-734
    • Krasemann, S.1    Groschup, M.H.2    Harmeyer, S.3    Hunsmann, G.4    Bodemer, W.5
  • 19
  • 21
    • 0036470471 scopus 로고    scopus 로고
    • Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration
    • Mallucci G. R., Ratte S., Asante E. A., Linehan J., Gowland I., Jefferys J. G., and Collinge J. (2002) Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration. EMBO J. 21, 202-210.
    • (2002) EMBO J. , vol.21 , pp. 202-210
    • Mallucci, G.R.1    Ratte, S.2    Asante, E.A.3    Linehan, J.4    Gowland, I.5    Jefferys, J.G.6    Collinge, J.7
  • 22
    • 0026795115 scopus 로고
    • Tetanus toxin and botulinum toxins type A and B inhibit glutamate, gamma-aminobutyric acid, aspartate, and met-enkephalin release from synaptosomes. Clues to the locus of action
    • McMahon H. T., Foran P., Dolly J. O., Verhage M., Wiegant V. M., and Nicholls D. G. (1992) Tetanus toxin and botulinum toxins type A and B inhibit glutamate, gamma-aminobutyric acid, aspartate, and met-enkephalin release from synaptosomes. Clues to the locus of action. J. Biol. Chem. 267, 21,338-21,343.
    • (1992) J. Biol. Chem. , vol.267
    • McMahon, H.T.1    Foran, P.2    Dolly, J.O.3    Verhage, M.4    Wiegant, V.M.5    Nicholls, D.G.6
  • 24
  • 25
    • 0027074458 scopus 로고
    • Purification and properties of the cellular prion protein from Syrian hamster brain
    • Pan K. M., Stahl N., and Prusiner S. B. (1992) Purification and properties of the cellular prion protein from Syrian hamster brain. Protein Sci. 1, 1343-1352.
    • (1992) Protein Sci. , vol.1 , pp. 1343-1352
    • Pan, K.M.1    Stahl, N.2    Prusiner, S.B.3
  • 26
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • Pauly P. C. and Harris D. A. (1998) Copper stimulates endocytosis of the prion protein. J. Biol. Chem. 273, 33,107-33,110.
    • (1998) J. Biol. Chem. , vol.273
    • Pauly, P.C.1    Harris, D.A.2
  • 28
    • 0017820108 scopus 로고
    • Evaluation of glutamate as a hippocampal neurotransmitter: Glutamate uptake and release from synaptosomes
    • Sandoval M. E., Horch P., and Cotman C. W. (1978) Evaluation of glutamate as a hippocampal neurotransmitter: glutamate uptake and release from synaptosomes. Brain Res. 142, 285-299.
    • (1978) Brain Res. , vol.142 , pp. 285-299
    • Sandoval, M.E.1    Horch, P.2    Cotman, C.W.3
  • 29
    • 0032932229 scopus 로고    scopus 로고
    • Genetic disorders of membrane transport. IV. Wilson's disease and Menkes disease
    • Schaefer M. and Gitlin J. D. (1999) Genetic disorders of membrane transport. IV. Wilson's disease and Menkes disease. Am. J. Physiol. 276, G311-G314.
    • (1999) Am. J. Physiol. , vol.276
    • Schaefer, M.1    Gitlin, J.D.2
  • 30
    • 0001552281 scopus 로고    scopus 로고
    • Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions
    • Shmerling D., Hegyi I., Fischer M., Blättler T., Brandner S., Götz J., et al. (1998) Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions. Cell 93, 203-214.
    • (1998) Cell , vol.93 , pp. 203-214
    • Shmerling, D.1    Hegyi, I.2    Fischer, M.3    Blättler, T.4    Brandner, S.5    Götz, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.