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Volumn 579, Issue 3, 2005, Pages 741-744

Extracellular copper ions regulate cellular prion protein (PrPC) expression and metabolism in neuronal cells

Author keywords

Cellular prion protein expression; Cellular prion protein physiology; Copper metabolism; GN11 cell

Indexed keywords

COPPER ION; MESSENGER RNA; PRION PROTEIN;

EID: 12744263653     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.12.053     Document Type: Article
Times cited : (21)

References (29)
  • 1
    • 0037301562 scopus 로고    scopus 로고
    • An evolutionary basis for scrapie disease: Identification of a fish prion mRNA
    • E. Rivera-Milla, C.A.O. Stuermer, and E. Malaga-Trillo An evolutionary basis for scrapie disease: identification of a fish prion mRNA Trends Genet. 19 2003 72 75
    • (2003) Trends Genet. , vol.19 , pp. 72-75
    • Rivera-Milla, E.1    Stuermer, C.A.O.2    Malaga-Trillo, E.3
  • 2
    • 0034899363 scopus 로고    scopus 로고
    • Nonneuronal cellular prion protein
    • J.G. Fournier Nonneuronal cellular prion protein Int. Rev. Cytol. 208 2001 121 160
    • (2001) Int. Rev. Cytol. , vol.208 , pp. 121-160
    • Fournier, J.G.1
  • 4
    • 0028883341 scopus 로고
    • Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein
    • M.P. Hornshaw, J.R. McDermott, and J.M. Candy Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein Biochem. Biophys. Res. Commun. 207 1995 621 629
    • (1995) Biochem. Biophys. Res. Commun. , vol.207 , pp. 621-629
    • Hornshaw, M.P.1    McDermott, J.R.2    Candy, J.M.3
  • 6
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: Their causes and molecular basis
    • J. Collinge Prion diseases of humans and animals: their causes and molecular basis Annu. Rev. Neurosci. 24 2001 519 550
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 519-550
    • Collinge, J.1
  • 10
    • 0029054937 scopus 로고
    • The N-terminal domain of a glycolipid-anchored prion protein is essential for its endocytosis via clathrin-coated pits
    • S.L. Shyng, K.L. Moulder, A. Lesko, and D.A. Harris The N-terminal domain of a glycolipid-anchored prion protein is essential for its endocytosis via clathrin-coated pits J. Biol. Chem. 270 1995 14793 14800
    • (1995) J. Biol. Chem. , vol.270 , pp. 14793-14800
    • Shyng, S.L.1    Moulder, K.L.2    Lesko, A.3    Harris, D.A.4
  • 11
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • P.C. Pauly, and D.A. Harris 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
  • 12
    • 18344403931 scopus 로고    scopus 로고
    • Effects of oxidative stress on prion protein expression in PC12 cells
    • D.R. Brown, B. Schmidt, and H.A. Kretzschmar Effects of oxidative stress on prion protein expression in PC12 cells Int. J. Dev. Neurosci. 15 1997 961 972
    • (1997) Int. J. Dev. Neurosci. , vol.15 , pp. 961-972
    • Brown, D.R.1    Schmidt, B.2    Kretzschmar, H.A.3
  • 14
    • 0035158321 scopus 로고    scopus 로고
    • Antioxidant activity related to copper binding of native prion protein
    • D.R. Brown, C. Clive, and S.J. Haswell Antioxidant activity related to copper binding of native prion protein J. Neurochem. 76 2001 69 76
    • (2001) J. Neurochem. , vol.76 , pp. 69-76
    • Brown, D.R.1    Clive, C.2    Haswell, S.J.3
  • 15
    • 0031194455 scopus 로고    scopus 로고
    • Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity
    • D.R. Brown, W.J. Schulz-Schaeffer, B. Schmidt, and H.A. Kretzschmar Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity Exp. Neurol. 146 1997 104 112
    • (1997) Exp. Neurol. , vol.146 , pp. 104-112
    • Brown, D.R.1    Schulz-Schaeffer, W.J.2    Schmidt, B.3    Kretzschmar, H.A.4
  • 18
    • 0034613113 scopus 로고    scopus 로고
    • Laminin-induced PC-12 cell differentiation is inhibited following laser inactivation of cellular prion protein
    • E. Graner, A.F. Mercadante, S.M. Zanata, V.R. Martins, D.G. Jay, and R.R. Brentani Laminin-induced PC-12 cell differentiation is inhibited following laser inactivation of cellular prion protein FEBS Lett. 482 2000 257 260
    • (2000) FEBS Lett. , vol.482 , pp. 257-260
    • Graner, E.1    Mercadante, A.F.2    Zanata, S.M.3    Martins, V.R.4    Jay, D.G.5    Brentani, R.R.6
  • 19
    • 0028820122 scopus 로고
    • Accumulation of proteinase K-resistant prion protein (PrP) is restricted by the expression level of normal PrP in mice inoculated with a mouse-adapted strain of the Creutzfeldt-Jakob disease agent
    • S. Sakaguchi, S. Katamine, K. Shigematsu, A. Nakatani, R. Moriuchi, N. Nishida, K. Kurokawa, R. Nakaoke, and H. Sato Accumulation of proteinase K-resistant prion protein (PrP) is restricted by the expression level of normal PrP in mice inoculated with a mouse-adapted strain of the Creutzfeldt-Jakob disease agent J. Virol. 69 1995 7586 7592
    • (1995) J. Virol. , vol.69 , pp. 7586-7592
    • Sakaguchi, S.1    Katamine, S.2    Shigematsu, K.3    Nakatani, A.4    Moriuchi, R.5    Nishida, N.6    Kurokawa, K.7    Nakaoke, R.8    Sato, H.9
  • 20
    • 0035298055 scopus 로고    scopus 로고
    • Transcriptional activation of prion protein gene in growth-arrested and differentiated mouse erythroleukemia and human neoplastic cells
    • D.D. Gougoumas, I.S. Vizirianakis, and A.S. Tsiftsoglou Transcriptional activation of prion protein gene in growth-arrested and differentiated mouse erythroleukemia and human neoplastic cells Exp. Cell. Res. 264 2001 408 417
    • (2001) Exp. Cell. Res. , vol.264 , pp. 408-417
    • Gougoumas, D.D.1    Vizirianakis, I.S.2    Tsiftsoglou, A.S.3
  • 21
    • 1642524321 scopus 로고    scopus 로고
    • Dual mechanisms for shedding of the cellular prion protein
    • E.T. Parkin, N.T. Watt, A.J. Turner, and N.M. Hooper Dual mechanisms for shedding of the cellular prion protein J. Biol. Chem. 279 2004 11170 11178
    • (2004) J. Biol. Chem. , vol.279 , pp. 11170-11178
    • Parkin, E.T.1    Watt, N.T.2    Turner, A.J.3    Hooper, N.M.4
  • 22
    • 0005453128 scopus 로고    scopus 로고
    • Expression of prostacyclin receptors in luteinizing hormone-releasing immortalized neurones, role in the control of hormone secretion
    • F. Pimpinelli, G.E. Rovati, V. Capra, F. Piva, L. Martini, and R. Maggi Expression of prostacyclin receptors in luteinizing hormone-releasing immortalized neurones, role in the control of hormone secretion Endocrinology 140 1999 171 177
    • (1999) Endocrinology , vol.140 , pp. 171-177
    • Pimpinelli, F.1    Rovati, G.E.2    Capra, V.3    Piva, F.4    Martini, L.5    Maggi, R.6
  • 24
    • 0035976894 scopus 로고    scopus 로고
    • Similar turnover and shedding of the cellular prion protein in primary lymphoid and neuronal cells
    • P. Parizek, C. Roeckl, J. Weber, E. Flechsig, A. Aguzzi, and A.J. Raeber Similar turnover and shedding of the cellular prion protein in primary lymphoid and neuronal cells J. Biol. Chem. 276 2001 44627 44632
    • (2001) J. Biol. Chem. , vol.276 , pp. 44627-44632
    • Parizek, P.1    Roeckl, C.2    Weber, J.3    Flechsig, E.4    Aguzzi, A.5    Raeber, A.J.6
  • 25
    • 0345714734 scopus 로고    scopus 로고
    • Copper binding to PrP(C) may inhibit prion disease propagation
    • N. Hijazi, Y. Shaked, H. Rosenmann, T. Ben-Hur, and R. Gabizon Copper binding to PrP(C) may inhibit prion disease propagation Brain Res. 993 2003 192 200
    • (2003) Brain Res. , vol.993 , pp. 192-200
    • Hijazi, N.1    Shaked, Y.2    Rosenmann, H.3    Ben-Hur, T.4    Gabizon, R.5
  • 26
    • 0032508637 scopus 로고    scopus 로고
    • Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae
    • L.J. Martins, L.T. Jensen, J.R. Simon, G.L. Keller, and D.R. Winge Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae J. Biol. Chem. 273 1998 23716 23721
    • (1998) J. Biol. Chem. , vol.273 , pp. 23716-23721
    • Martins, L.J.1    Jensen, L.T.2    Simon, J.R.3    Keller, G.L.4    Winge, D.R.5
  • 29
    • 0034474183 scopus 로고    scopus 로고
    • The molecular basis of copper transport diseases
    • J.F.B. Mercer The molecular basis of copper transport diseases Trends Mol. Med. 7 2001 64 69
    • (2001) Trends Mol. Med. , vol.7 , pp. 64-69
    • Mercer, J.F.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.