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Volumn 270, Issue 16, 2003, Pages 3368-3376

Mapping the functional domain of the prion protein

Author keywords

Copper; Creutzfeldt Jakob disease; Oxidative stress; Scrapie; Superoxide dismutase

Indexed keywords

BINDING PROTEIN; COPPER; COPPER BINDING PROTEIN; ISOPROTEIN; PRION PROTEIN; SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG;

EID: 0042477520     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03717.x     Document Type: Article
Times cited : (38)

References (67)
  • 1
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner, S.B. (1982) Novel proteinaceous infectious particles cause scrapie. Science 216, 136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 6
    • 0025641602 scopus 로고
    • Inherited human prion diseases
    • Hsiao, K. & Prusiner, S.B. (1990) Inherited human prion diseases. Neurology 40, 1820-1827.
    • (1990) Neurology , vol.40 , pp. 1820-1827
    • Hsiao, K.1    Prusiner, S.B.2
  • 7
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phosphatidylinositol glycolipid
    • Stahl, N., Borchelt, D.R., Hsiao, K. & Prusiner, S.B. (1987) Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 51, 229-240.
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Borchelt, D.R.2    Hsiao, K.3    Prusiner, S.B.4
  • 13
    • 0029997484 scopus 로고    scopus 로고
    • Role of microglia and host prion protein in neurotoxicity of a prion protein fragment
    • Brown, D.R., Schmidt, B. & Kretzschmar, H.A. (1996) Role of microglia and host prion protein in neurotoxicity of a prion protein fragment. Nature 380, 345-347.
    • (1996) Nature , vol.380 , pp. 345-347
    • Brown, D.R.1    Schmidt, B.2    Kretzschmar, H.A.3
  • 14
    • 0037080043 scopus 로고    scopus 로고
    • Lack of prion protein expression results in a neuronal phenotype sensitive to stress
    • Brown, D.R., St. Nicholas, R., J. & Canevari, L. (2002) Lack of prion protein expression results in a neuronal phenotype sensitive to stress. J. Neurosci. Res. 67, 211-224.
    • (2002) J. Neurosci. Res. , vol.67 , pp. 211-224
    • Brown, D.R.1    St. Nicholas, R.2    Canevari, L.3
  • 15
    • 0028844207 scopus 로고
    • Copper binding to the N-terminal repeat region of mammalian and avian prion protein: Structural studies using synthetic peptides
    • Hornshaw, M.P., McDermott, J.R., Candy, J.M. & Lakey, J.H., (1995) Copper binding to the N-terminal repeat region of mammalian and avian prion protein: structural studies using synthetic peptides. Biochem. Biophys. Res. Comm. 214, 993-999.
    • (1995) Biochem. Biophys. Res. Comm. , vol.214 , pp. 993-999
    • Hornshaw, M.P.1    McDermott, J.R.2    Candy, J.M.3    Lakey, J.H.4
  • 17
    • 0035158321 scopus 로고    scopus 로고
    • Anti-oxidant activity related to copper binding of native prion protein
    • Brown, D.R., Clive, C. & Haswell, S.J. (2001) Anti-oxidant activity related to copper binding of native prion protein. J. Neurochem. 76, 69-76.
    • (2001) J. Neurochem. , vol.76 , pp. 69-76
    • Brown, D.R.1    Clive, C.2    Haswell, S.J.3
  • 19
    • 0033515029 scopus 로고    scopus 로고
    • Copper binding to the prion protein: Structural implications of four identical cooperative binding sites
    • Viles, J.H., Cohen, F.E., Prusiner, S.B., Goodin, D.B., Wright, P.E. & Dyson, H.J. (1999) Copper binding to the prion protein: Structural implications of four identical cooperative binding sites. Proc. Natl Acad. Sci. USA 96, 2042-2047.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2042-2047
    • Viles, J.H.1    Cohen, F.E.2    Prusiner, S.B.3    Goodin, D.B.4    Wright, P.E.5    Dyson, H.J.6
  • 22
    • 0033485880 scopus 로고    scopus 로고
    • Prion protein expression aids cellular uptake and veratridine-induced release of copper
    • Brown, D.R. (1999) Prion protein expression aids cellular uptake and veratridine-induced release of copper. J. Neurosci. Res. 58, 717-725.
    • (1999) J. Neurosci. Res. , vol.58 , pp. 717-725
    • Brown, D.R.1
  • 23
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • Pauly, P.C. & Harris, D.A. (1998) Copper stimulates endocytosis of the prion protein. J. Biol. Chem. 273, 33107-33110.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 24
    • 0037018914 scopus 로고    scopus 로고
    • Plasminogen activation is stimulated by prion protein and regulated in a copper-dependent manner
    • Ellis, V., Daniels, M., Misra, R. & Brown, D.R. (2002) Plasminogen activation is stimulated by prion protein and regulated in a copper-dependent manner. Biochemistry 41, 6891-6896.
    • (2002) Biochemistry , vol.41 , pp. 6891-6896
    • Ellis, V.1    Daniels, M.2    Misra, R.3    Brown, D.R.4
  • 25
    • 0037113169 scopus 로고    scopus 로고
    • Cell surface prion protein interacts with glycosaminoglycans
    • Pan, T., Wong, B.S., Liu, T., Li, R., Petersen, R.B. & Sy, M.S. (2002) Cell surface prion protein interacts with glycosaminoglycans. Biochem. J. 368, 81-90.
    • (2002) Biochem. J. , vol.368 , pp. 81-90
    • Pan, T.1    Wong, B.S.2    Liu, T.3    Li, R.4    Petersen, R.B.5    Sy, M.S.6
  • 26
    • 0031194455 scopus 로고    scopus 로고
    • Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity
    • Brown, D.R., Schultz-Schaeffer, W.J., Schmidt, B. & Kretzschmar, H.A. (1997) Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity. Exp. Neurol. 146, 104-112.
    • (1997) Exp. Neurol. , vol.146 , pp. 104-112
    • Brown, D.R.1    Schultz-Schaeffer, W.J.2    Schmidt, B.3    Kretzschmar, H.A.4
  • 27
    • 0034709641 scopus 로고    scopus 로고
    • Differential contribution of superoxide dismutase activity by prion protein in vivo
    • Wong, B.S., Pan, T., Liu, T., Li, R.L., Gambetti, P. & Sy, M.S. (2000) Differential contribution of superoxide dismutase activity by prion protein in vivo. Biochem. Biophys. Res. Commun 273, 136-139.
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 136-139
    • Wong, B.S.1    Pan, T.2    Liu, T.3    Li, R.L.4    Gambetti, P.5    Sy, M.S.6
  • 28
    • 0033571055 scopus 로고    scopus 로고
    • Normal prion protein has an activity like that of superoxide dismutase
    • Brown, D.R., Wong, B.S., Hafiz, F., Clive, C., Haswell, S. & Jones, I.M. (1999) Normal prion protein has an activity like that of superoxide dismutase. Biochem. J. 344, 1-5.
    • (1999) Biochem. J. , vol.344 , pp. 1-5
    • Brown, D.R.1    Wong, B.S.2    Hafiz, F.3    Clive, C.4    Haswell, S.5    Jones, I.M.6
  • 31
    • 0037083888 scopus 로고    scopus 로고
    • Metal imbalance and compromised antioxidant function are early changes in prion disease
    • Thackray, A.M., Knight, R., Haswell, S.J., Bujdoso, R. & Brown, D.R. (2002) Metal imbalance and compromised antioxidant function are early changes in prion disease. Biochem. J. 362, 253-258.
    • (2002) Biochem. J. , vol.362 , pp. 253-258
    • Thackray, A.M.1    Knight, R.2    Haswell, S.J.3    Bujdoso, R.4    Brown, D.R.5
  • 32
    • 0034533064 scopus 로고    scopus 로고
    • Sc-like prion protein peptide inhibits the function of cellular prion protein
    • Sc-like prion protein peptide inhibits the function of cellular prion protein. Biochem. J. 352, 511-518.
    • (2000) Biochem. J. , vol.352 , pp. 511-518
    • Brown, D.R.1
  • 33
    • 0035213414 scopus 로고    scopus 로고
    • Toxicity of novel C-terminal prion protein fragments and peptides harbouring disease-related C-terminal mutations
    • Daniels, M., Cereghetti, G.M. & Brown, D.R. (2001) Toxicity of novel C-terminal prion protein fragments and peptides harbouring disease-related C-terminal mutations. Eur. J. Biochem. 268, 6155-6164.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6155-6164
    • Daniels, M.1    Cereghetti, G.M.2    Brown, D.R.3
  • 34
    • 0036312010 scopus 로고    scopus 로고
    • Heterogeneity of normal prion protein in two-dimensional immunoblot: Presence of various glycosylated and truncated forms
    • Pan, T., Li, R., Wong, B.S., Liu, T., Gambetti, P. & Sy, M.-S. (2002) Heterogeneity of normal prion protein in two-dimensional immunoblot: presence of various glycosylated and truncated forms. J. Neurochem. 81, 1092-1101.
    • (2002) J. Neurochem. , vol.81 , pp. 1092-1101
    • Pan, T.1    Li, R.2    Wong, B.S.3    Liu, T.4    Gambetti, P.5    Sy, M.-S.6
  • 35
    • 0035970784 scopus 로고    scopus 로고
    • Differential expression of cellular prion protein in mouse brain as detected with multiple anti-PrP monoclonal antibodies
    • Liu, T., Zwingman, T., Li, R., Pan, T., Wong, B.S., Petersen, R.B., Gambetti, P., Herrup, K. & Sy, M.S. (2001) Differential expression of cellular prion protein in mouse brain as detected with multiple anti-PrP monoclonal antibodies. Brain Res. 896, 118-129.
    • (2001) Brain Res. , vol.896 , pp. 118-129
    • Liu, T.1    Zwingman, T.2    Li, R.3    Pan, T.4    Wong, B.S.5    Petersen, R.B.6    Gambetti, P.7    Herrup, K.8    Sy, M.S.9
  • 39
    • 0037148129 scopus 로고    scopus 로고
    • Sleep deprivation in prion protein deficient mice sleep deprivation in prion protein deficient mice and control mice: Genotype dependent regional rebound
    • Hüber, R., Deboer, T. & Tobler, I. (2002) Sleep deprivation in prion protein deficient mice sleep deprivation in prion protein deficient mice and control mice: genotype dependent regional rebound. Neuroreport 13, 1-4.
    • (2002) Neuroreport , vol.13 , pp. 1-4
    • Hüber, R.1    Deboer, T.2    Tobler, I.3
  • 40
    • 0038399726 scopus 로고    scopus 로고
    • Age-Dependent Loss of PTP and LTP in the hippocampus of PrP-null Mice
    • Curtis, J., Errington, M., Bliss, T., Voss, K. & Macleod, N. (2003) Age-Dependent Loss of PTP and LTP in the hippocampus of PrP-null Mice. Neurobiol. Dis. 13, 55-62.
    • (2003) Neurobiol. Dis. , vol.13 , pp. 55-62
    • Curtis, J.1    Errington, M.2    Bliss, T.3    Voss, K.4    Macleod, N.5
  • 42
    • 0032724766 scopus 로고    scopus 로고
    • Prion protein-deficient neurons reveal lower glutathione reductase activity and increased susceptibility to hydrogen peroxide toxicity
    • White, A.R., Collins, S.J., Maher, F., Jobling, M.F., Stewart, L.R., Thyer, J.M., Beyreuther, K., Masters, C.L. & Cappai, R. (1999a) Prion protein-deficient neurons reveal lower glutathione reductase activity and increased susceptibility to hydrogen peroxide toxicity. Am. J. Pathol. 155, 1723-1730.
    • (1999) Am. J. Pathol. , vol.155 , pp. 1723-1730
    • White, A.R.1    Collins, S.J.2    Maher, F.3    Jobling, M.F.4    Stewart, L.R.5    Thyer, J.M.6    Beyreuther, K.7    Masters, C.L.8    Cappai, R.9
  • 43
    • 0037316675 scopus 로고    scopus 로고
    • Tethering the N-terminus of the prion protein compromises the cellular response to oxidative stress
    • Zeng, F., Watt, N.T., Walmsley, A.R. & Hooper, N.M. (2003) Tethering the N-terminus of the prion protein compromises the cellular response to oxidative stress. J. Neurochem. 84, 480-490.
    • (2003) J. Neurochem. , vol.84 , pp. 480-490
    • Zeng, F.1    Watt, N.T.2    Walmsley, A.R.3    Hooper, N.M.4
  • 44
    • 18344403931 scopus 로고    scopus 로고
    • Effects of oxidative stress on prion protein expression in PC12 cells
    • Brown, D.R., Schmidt, B. & Kretzschmar, H.A. (1997c) Effects of oxidative stress on prion protein expression in PC12 cells. Int. J. Dev Neurosci. 15, 961-972.
    • (1997) Int. J. Dev Neurosci. , vol.15 , pp. 961-972
    • Brown, D.R.1    Schmidt, B.2    Kretzschmar, H.A.3
  • 45
    • 0034654304 scopus 로고    scopus 로고
    • Consequences of manganese replacement of copper for prion protein function and proteinase resistance
    • Brown, D.R., Hafiz, F., Glasssmith, L.L., Wong, B.-S., Jones, I.M., Clive, C. & Haswell, S.J. (2000) Consequences of manganese replacement of copper for prion protein function and proteinase resistance. EMBO J. 19, 1180-1186.
    • (2000) EMBO J. , vol.19 , pp. 1180-1186
    • Brown, D.R.1    Hafiz, F.2    Glasssmith, L.L.3    Wong, B.-S.4    Jones, I.M.5    Clive, C.6    Haswell, S.J.7
  • 46
    • 0036291424 scopus 로고    scopus 로고
    • Ablation of cellular prion protein expression affects mitochondrial numbers and morphology
    • Miele, G., Jeffrey, M., Turnbull, D., Manson, J. & Clinton, M. (2002) Ablation of cellular prion protein expression affects mitochondrial numbers and morphology. Biochem. Biophys. Res. Commun. 291, 372-377.
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 372-377
    • Miele, G.1    Jeffrey, M.2    Turnbull, D.3    Manson, J.4    Clinton, M.5
  • 48
    • 0035194082 scopus 로고    scopus 로고
    • Prion diseases: Copper deficiency states associated with impaired nitrogen monoxide or carbon monoxide transduction and translocation
    • Sorenson, J.R. (2001) Prion diseases: copper deficiency states associated with impaired nitrogen monoxide or carbon monoxide transduction and translocation. J. Inorg. Biochem. 87, 125-127.
    • (2001) J. Inorg. Biochem. , vol.87 , pp. 125-127
    • Sorenson, J.R.1
  • 49
    • 0016414528 scopus 로고
    • Superoxide dismutases
    • Fridovich, I. (1975) Superoxide dismutases. Ann. Rev. Biochem. 44, 146-159.
    • (1975) Ann. Rev. Biochem. , vol.44 , pp. 146-159
    • Fridovich, I.1
  • 50
    • 0030836511 scopus 로고    scopus 로고
    • NMR characterization of the full-length recombinant murine prion protein mPrP (23-231)
    • Riek, R., Hornemann, S., Wider, G., Glockshuber, R. & Wüthrich, K. (1997) NMR characterization of the full-length recombinant murine prion protein mPrP (23-231). FEBS Lett. 413, 282-288.
    • (1997) FEBS Lett. , vol.413 , pp. 282-288
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Glockshuber, R.4    Wüthrich, K.5
  • 52
    • 0034682866 scopus 로고    scopus 로고
    • Identification of an epitope in the C terminus of normal prion protein whose expression is modulated by binding events in the N terminus
    • Li, R., Liu, T., Wong, B.S., Pan, T., Morillas, M., Swietnicki, W., O'Rourke, K., Gambetti, P., Surewicz, W.K. & Sy, M.S. (2000) Identification of an epitope in the C terminus of normal prion protein whose expression is modulated by binding events in the N terminus. J. Mol. Biol. 301, 567-573.
    • (2000) J. Mol. Biol. , vol.301 , pp. 567-573
    • Li, R.1    Liu, T.2    Wong, B.S.3    Pan, T.4    Morillas, M.5    Swietnicki, W.6    O'Rourke, K.7    Gambetti, P.8    Surewicz, W.K.9    Sy, M.S.10
  • 56
    • 0033980694 scopus 로고    scopus 로고
    • Prion protein peptides: Optimal toxicity and peptide blockade of toxicity
    • Brown, D.R. (2000) Prion protein peptides: Optimal toxicity and peptide blockade of toxicity. Mol. Cell Neurosci. 15, 66-78.
    • (2000) Mol. Cell Neurosci. , vol.15 , pp. 66-78
    • Brown, D.R.1
  • 59
    • 0034711569 scopus 로고    scopus 로고
    • Increased ferric iron content and iron-induced oxidative stress in the brains of scrapie-infected mice
    • Kim, N.H., Park, S., Jin, J., Kwon, M., Choi, E., Carp, R.I. & Kim, Y. (2000) Increased ferric iron content and iron-induced oxidative stress in the brains of scrapie-infected mice. Brain Res. 884, 98-103.
    • (2000) Brain Res. , vol.884 , pp. 98-103
    • Kim, N.H.1    Park, S.2    Jin, J.3    Kwon, M.4    Choi, E.5    Carp, R.I.6    Kim, Y.7
  • 63
  • 64
  • 66
    • 0031594587 scopus 로고    scopus 로고
    • Overexpression of non-convertable PrPcΔ114-121 in scrapie-infected mouse neuroblastoma cells leads to trans-dominant inhibition of wild-type PrPSc accumulation
    • Hölscher, C., Delius, H. & Bürkle, A. (1998) Overexpression of non-convertable PrPcΔ114-121 in scrapie-infected mouse neuroblastoma cells leads to trans-dominant inhibition of wild-type PrPSc accumulation. J. Virol. 72, 1153-1159.
    • (1998) J. Virol. , vol.72 , pp. 1153-1159
    • Hölscher, C.1    Delius, H.2    Bürkle, A.3
  • 67
    • 0028925377 scopus 로고
    • Prion protein peptide induces α-helix to β-sheet conformation transitions
    • Nguyen, J., Baldwin, M.A., CohE.N., F.E. & Prusiner, S.B. (1995) Prion protein peptide induces α-helix to β-sheet conformation transitions. Biochemistry 34, 4186-4192.
    • (1995) Biochemistry , vol.34 , pp. 4186-4192
    • Nguyen, J.1    Baldwin, M.A.2    Coh, E.N.3    Prusiner, S.B.4


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