메뉴 건너뛰기




Volumn 9, Issue 6, 2003, Pages 237-243

Is loss of function of the prion protein the cause of prion disorders?

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN;

EID: 0038603947     PISSN: 14714914     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1471-4914(03)00069-8     Document Type: Article
Times cited : (69)

References (61)
  • 1
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: Their causes and molecular basis
    • Collinge, J. (2001) Prion diseases of humans and animals: their causes and molecular basis. Annu. Rev. Neurosci. 24, 519-550
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 519-550
    • Collinge, J.1
  • 3
    • 0032076463 scopus 로고    scopus 로고
    • Prion protein biology
    • Prusiner, S.B. et al. (1998) Prion protein biology. Cell 93, 337-348
    • (1998) Cell , vol.93 , pp. 337-348
    • Prusiner, S.B.1
  • 4
    • 0031711595 scopus 로고    scopus 로고
    • Pathologic conformations of prion proteins
    • Cohen, F.E. and Prusiner, S.B. (1998) Pathologic conformations of prion proteins. Annu. Rev. Biochem. 67, 793-819
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 793-819
    • Cohen, F.E.1    Prusiner, S.B.2
  • 5
    • 0028876473 scopus 로고
    • Neuropathological diagnostic criteria for Creutzfeldt-Jakob disease (CJD) and other human spongiform encephalopathies (prion diseases)
    • Budka, H. et al. (1995) Neuropathological diagnostic criteria for Creutzfeldt-Jakob disease (CJD) and other human spongiform encephalopathies (prion diseases). Brain Pathol. 5, 459-466
    • (1995) Brain Pathol. , vol.5 , pp. 459-466
    • Budka, H.1
  • 6
    • 0029657958 scopus 로고    scopus 로고
    • Human prion diseases
    • Ironside, J.W. et al. (1996) Human prion diseases. J. Neural Transm. 47, 231-246
    • (1996) J. Neural Transm. , vol.47 , pp. 231-246
    • Ironside, J.W.1
  • 7
    • 0027757723 scopus 로고
    • Pathology of nonhuman spongiform encephalopathies: Variations and their implications for pathogenesis
    • Wells, G.A. (1993) Pathology of nonhuman spongiform encephalopathies: variations and their implications for pathogenesis. Dev. Biol. Stand. 80, 61-69
    • (1993) Dev. Biol. Stand. , vol.80 , pp. 61-69
    • Wells, G.A.1
  • 8
    • 0033598441 scopus 로고    scopus 로고
    • Vacuolation in murine prion disease: An informative artefact
    • Betmouni, S. et al. (1999) Vacuolation in murine prion disease: an informative artefact. Curr. Biol. 9, R677-R679
    • (1999) Curr. Biol. , vol.9
    • Betmouni, S.1
  • 9
    • 0345654322 scopus 로고    scopus 로고
    • Neuronal apoptosis in Creutzfeldt-Jakob disease
    • Gray, F. et al. (1999) Neuronal apoptosis in Creutzfeldt-Jakob disease. J. Neuropathol. Exp. Neurol. 58, 321-328
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , pp. 321-328
    • Gray, F.1
  • 10
    • 0029784248 scopus 로고    scopus 로고
    • Evidence for an early inflammatory response in the central nervous system of mice with scrapie
    • Betmouni, S. et al. (1996) Evidence for an early inflammatory response in the central nervous system of mice with scrapie. Neuroscience 74, 1-5
    • (1996) Neuroscience , vol.74 , pp. 1-5
    • Betmouni, S.1
  • 11
    • 15844415943 scopus 로고    scopus 로고
    • Prion protein amyloidosis
    • Ghetti, B. et al. (1996) Prion protein amyloidosis. Brain Pathol. 6, 127-145
    • (1996) Brain Pathol. , vol.6 , pp. 127-145
    • Ghetti, B.1
  • 12
    • 0029169770 scopus 로고
    • Pathology of the transmissible spongiform encephalopathies with special emphasis on ultrastructure
    • Jeffrey, M. et al. (1995) Pathology of the transmissible spongiform encephalopathies with special emphasis on ultrastructure. Micron 26, 277-298
    • (1995) Micron , vol.26 , pp. 277-298
    • Jeffrey, M.1
  • 13
    • 0032802332 scopus 로고    scopus 로고
    • Cellular biology of prion diseases
    • Harris, D.A. (1999) Cellular biology of prion diseases. Clin. Microbiol. Rev. 12, 429-444
    • (1999) Clin. Microbiol. Rev. , vol.12 , pp. 429-444
    • Harris, D.A.1
  • 14
    • 0034665847 scopus 로고    scopus 로고
    • Signal transduction through prion protein
    • Mouillet-Richard, S. et al. (2000) Signal transduction through prion protein. Science 289, 1925-1928
    • (2000) Science , vol.289 , pp. 1925-1928
    • Mouillet-Richard, S.1
  • 15
    • 0035977053 scopus 로고    scopus 로고
    • C directly interacts with proteins involved in signaling pathways
    • C directly interacts with proteins involved in signaling pathways. J. Biol. Chem. 276, 44604-44612
    • (2001) J. Biol. Chem. , vol.276 , pp. 44604-44612
    • Spielhaupter, C.1    Schatzl, H.M.2
  • 16
    • 18444397736 scopus 로고    scopus 로고
    • Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection
    • Zanata, S.M. et al. (2002) Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection. EMBO J. 21, 3307-3316
    • (2002) EMBO J. , vol.21 , pp. 3307-3316
    • Zanata, S.M.1
  • 17
    • 0027439595 scopus 로고
    • Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70
    • Smith, D.F. et al. (1993) Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70. Mol. Cell. Biol. 13, 869-876
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 869-876
    • Smith, D.F.1
  • 18
    • 0031036746 scopus 로고    scopus 로고
    • Stress-inducible, murine protein mSTI1. Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases
    • Lassle, M. et al. (1997) Stress-inducible, murine protein mSTI1. Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases. J. Biol. Chem. 272, 1876-1884
    • (1997) J. Biol. Chem. , vol.272 , pp. 1876-1884
    • Lassle, M.1
  • 19
    • 0036645677 scopus 로고    scopus 로고
    • Cellular prion protein transduces neuroprotective signals
    • Chiarini, L.B. et al. (2002) Cellular prion protein transduces neuroprotective signals. EMBO J. 21, 3317-3326
    • (2002) EMBO J. , vol.21 , pp. 3317-3326
    • Chiarini, L.B.1
  • 20
    • 0027483615 scopus 로고
    • Neurotoxicity of a prion protein fragment
    • Forloni, G. et al. (1993) Neurotoxicity of a prion protein fragment. Nature 362, 543-546
    • (1993) Nature , vol.362 , pp. 543-546
    • Forloni, G.1
  • 21
    • 0027259274 scopus 로고
    • Molecular characteristics of a protease-resistant, amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein
    • Selvaggini, C. et al. (1993) Molecular characteristics of a protease-resistant, amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. Biochem. Biophys. Res. Commun. 194, 1380-1386
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 1380-1386
    • Selvaggini, C.1
  • 22
    • 0028925377 scopus 로고
    • Prion protein peptides induce α-helix to β-sheet conformational transitions
    • Nguyen, J. et al. (1995) Prion protein peptides induce α-helix to β-sheet conformational transitions. Biochemistry 34, 4186-4192
    • (1995) Biochemistry , vol.34 , pp. 4186-4192
    • Nguyen, J.1
  • 23
    • 0028143841 scopus 로고
    • Mouse cortical cells lacking cellular PrP survive in culture with a neurotoxic PrP fragment
    • Brown, D.R. et al. (1994) Mouse cortical cells lacking cellular PrP survive in culture with a neurotoxic PrP fragment. Neuroreport 5, 2057-2060
    • (1994) Neuroreport , vol.5 , pp. 2057-2060
    • Brown, D.R.1
  • 24
    • 0033566067 scopus 로고    scopus 로고
    • Prions prevent neuronal cell-line death
    • Kuwahara, C. et al. (1999) Prions prevent neuronal cell-line death. Nature 400, 225-226
    • (1999) Nature , vol.400 , pp. 225-226
    • Kuwahara, C.1
  • 25
    • 0034931131 scopus 로고    scopus 로고
    • Interaction of prion proteins with cell surface receptors, molecular chaperones, and other molecules
    • Gauczynski, S. et al. (2001) Interaction of prion proteins with cell surface receptors, molecular chaperones, and other molecules. Adv. Protein Chem. 57, 229-272
    • (2001) Adv. Protein Chem. , vol.57 , pp. 229-272
    • Gauczynski, S.1
  • 26
    • 0029932071 scopus 로고    scopus 로고
    • Analysis of interaction sites in homo- and heteromeric complexes containing Bcl-2 family members and the cellular prion protein
    • Kurschner, C. and Morgan, J.I. (1996) Analysis of interaction sites in homo- and heteromeric complexes containing Bcl-2 family members and the cellular prion protein. Brain Res. Mol. Brain Res. 37, 249-258
    • (1996) Brain Res. Mol. Brain Res. , vol.37 , pp. 249-258
    • Kurschner, C.1    Morgan, J.I.2
  • 27
    • 0035914410 scopus 로고    scopus 로고
    • Prion protein protects human neurons against Bax-mediated apoptosis
    • Bounhar, Y. et al. (2001) Prion protein protects human neurons against Bax-mediated apoptosis. J. Biol. Chem. 276, 39145-39149
    • (2001) J. Biol. Chem. , vol.276 , pp. 39145-39149
    • Bounhar, Y.1
  • 28
    • 0033695126 scopus 로고    scopus 로고
    • Prion protein devoid of the octapeptide repeat region restores susceptibility to scrapie in PrP knockout mice
    • Flechsig, E. et al. (2000) Prion protein devoid of the octapeptide repeat region restores susceptibility to scrapie in PrP knockout mice. Neuron 27, 399-408
    • (2000) Neuron , vol.27 , pp. 399-408
    • Flechsig, E.1
  • 29
    • 0035872476 scopus 로고    scopus 로고
    • Copper and prion disease
    • Brown, D.R. (2001) Copper and prion disease. Brain Res. Bull. 55, 165-173
    • (2001) Brain Res. Bull. , vol.55 , pp. 165-173
    • Brown, D.R.1
  • 30
    • 0015589898 scopus 로고
    • Clinical and histological recovery from the scrapie-like spongiform encephalopathy produced in mice by feeding them with cuprizone
    • Pattison, I.H. and Jebbett, J.N. (1973) Clinical and histological recovery from the scrapie-like spongiform encephalopathy produced in mice by feeding them with cuprizone. J. Pathol. 109, 245-250
    • (1973) J. Pathol. , vol.109 , pp. 245-250
    • Pattison, I.H.1    Jebbett, J.N.2
  • 31
    • 0014530743 scopus 로고
    • Spongiform encephalopathy induced in rats and guinea pigs by cuprizone
    • Carlton, W.W. (1969) Spongiform encephalopathy induced in rats and guinea pigs by cuprizone. Exp. Mol. Pathol. 10, 274-287
    • (1969) Exp. Mol. Pathol. , vol.10 , pp. 274-287
    • Carlton, W.W.1
  • 32
    • 0035907363 scopus 로고    scopus 로고
    • Prion protein binds copper within the physiological concentration range
    • Kramer, M.L. et al. (2001) Prion protein binds copper within the physiological concentration range. J. Biol. Chem. 276, 16711-16719
    • (2001) J. Biol. Chem. , vol.276 , pp. 16711-16719
    • Kramer, M.L.1
  • 33
    • 0031444294 scopus 로고    scopus 로고
    • The cellular prion protein binds copper in vivo
    • Brown, D.R. et al. (1997) The cellular prion protein binds copper in vivo. Nature 390, 684-687
    • (1997) Nature , vol.390 , pp. 684-687
    • Brown, D.R.1
  • 34
    • 0033571055 scopus 로고    scopus 로고
    • Normal prion protein has an activity like that of superoxide dismutase
    • Brown, D.R. et al. (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
  • 35
    • 0034678023 scopus 로고    scopus 로고
    • Brain copper content and cuproenzyme activity do not vary with prion protein expression level
    • Waggoner, D.J. et al. (2000) Brain copper content and cuproenzyme activity do not vary with prion protein expression level. J. Biol. Chem. 275, 7455-7458
    • (2000) J. Biol. Chem. , vol.275 , pp. 7455-7458
    • Waggoner, D.J.1
  • 36
    • 0037083888 scopus 로고    scopus 로고
    • Metal imbalance and compromised antioxidant function are early changes in prion disease
    • Thackray, A.M. et al. (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
  • 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. (2001) Oxidative impairment in scrapie-infected mice is associated with brain metals perturbations and altered antioxidant activities. J. Neurochem. 79, 689-698
    • (2001) J. Neurochem. , vol.79 , pp. 689-698
    • Wong, B.S.1
  • 38
    • 0034810585 scopus 로고    scopus 로고
    • Aberrant metal binding by prion protein in human prion disease
    • Wong, B.S. et al. (2001) Aberrant metal binding by prion protein in human prion disease. J. Neurochem. 78, 1400-1408
    • (2001) J. Neurochem. , vol.78 , pp. 1400-1408
    • Wong, B.S.1
  • 39
    • 0027096137 scopus 로고
    • Synthesis and trafficking of prion proteins in cultured cells
    • Taraboulos, A. et al. (1992) Synthesis and trafficking of prion proteins in cultured cells. Mol. Biol. Cell 3, 851-863
    • (1992) Mol. Biol. Cell , vol.3 , pp. 851-863
    • Taraboulos, A.1
  • 40
    • 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, 33107-33110
    • (1998) J. Biol. Chem. , vol.273 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 41
    • 0034705438 scopus 로고    scopus 로고
    • Copper(II)-induced conformational changes and protease resistance in recombinant and cellular PrP. Effect of protein age and deamidation
    • Qin, K. et al. (2000) Copper(II)-induced conformational changes and protease resistance in recombinant and cellular PrP. Effect of protein age and deamidation. J. Biol. Chem. 275, 19121-19131
    • (2000) J. Biol. Chem. , vol.275 , pp. 19121-19131
    • Qin, K.1
  • 42
    • 0032488777 scopus 로고    scopus 로고
    • A transmembrane form of the prion protein in neurodegenerative disease
    • Hegde, R.S. et al. (1998) A transmembrane form of the prion protein in neurodegenerative disease. Science 279, 827-834
    • (1998) Science , vol.279 , pp. 827-834
    • Hegde, R.S.1
  • 43
    • 0033576323 scopus 로고    scopus 로고
    • Transmissible and genetic prion diseases share a common pathway of neurodegeneration
    • Hegde, R.S. et al. (1999) Transmissible and genetic prion diseases share a common pathway of neurodegeneration. Nature 402, 822-826
    • (1999) Nature , vol.402 , pp. 822-826
    • Hegde, R.S.1
  • 44
    • 0037195617 scopus 로고    scopus 로고
    • Sc-like conformation in the cytosol
    • Sc-like conformation in the cytosol. Science 298, 1785-1788
    • (2002) Science , vol.298 , pp. 1785-1788
    • Ma, J.1    Lindquist, S.2
  • 45
    • 0037195647 scopus 로고    scopus 로고
    • Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol
    • Ma, J. et al. (2002) Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298, 1781-1785
    • (2002) Science , vol.298 , pp. 1781-1785
    • Ma, J.1
  • 46
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh, H. et al. (2002) ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev. 16, 1345-1355
    • (2002) Genes Dev. , vol.16 , pp. 1345-1355
    • Nishitoh, H.1
  • 47
    • 0035865398 scopus 로고    scopus 로고
    • Onset of ataxia and Purkinje cell loss in PrP null mice inversely correlated with Dpl level in brain
    • Rossi, D. et al. (2001) Onset of ataxia and Purkinje cell loss in PrP null mice inversely correlated with Dpl level in brain. EMBO J. 20, 694-702
    • (2001) EMBO J. , vol.20 , pp. 694-702
    • Rossi, D.1
  • 49
    • 0026600865 scopus 로고
    • Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein
    • Bueler, H. 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
    • Bueler, H.1
  • 50
    • 0028420937 scopus 로고
    • 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal
    • Manson, J.C. et al. (1994) 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal. Mol. Neurobiol. 8, 121-127
    • (1994) Mol. Neurobiol. , vol.8 , pp. 121-127
    • Manson, J.C.1
  • 51
    • 13344282734 scopus 로고    scopus 로고
    • Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene
    • Sakaguchi, S. et al. (1996) Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene. Nature 380, 528-531
    • (1996) Nature , vol.380 , pp. 528-531
    • Sakaguchi, S.1
  • 52
    • 0033215478 scopus 로고    scopus 로고
    • Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel
    • Moore, R.C. et al. (1999) Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel. J. Mol. Biol. 292, 797-817
    • (1999) J. Mol. Biol. , vol.292 , pp. 797-817
    • Moore, R.C.1
  • 53
    • 0036304151 scopus 로고    scopus 로고
    • Differences between the prion protein and its homolog Doppel: A partially structured state with implications for scrapie formation
    • Nicholson, E.M. et al. (2002) Differences between the prion protein and its homolog Doppel: a partially structured state with implications for scrapie formation. J. Mol. Biol. 316, 807-815
    • (2002) J. Mol. Biol. , vol.316 , pp. 807-815
    • Nicholson, E.M.1
  • 54
    • 0035021524 scopus 로고    scopus 로고
    • The PrP-like protein Doppel gene in sheep and cattle: cDNA sequence and expression
    • Tranulis, M.A. et al. (2001) The PrP-like protein Doppel gene in sheep and cattle: cDNA sequence and expression. Mamm. Genome 12, 376-379
    • (2001) Mamm. Genome , vol.12 , pp. 376-379
    • Tranulis, M.A.1
  • 55
    • 0037099695 scopus 로고    scopus 로고
    • Absence of the prion protein homologue Doppel causes male sterility
    • Behrens, A. et al. (2002) Absence of the prion protein homologue Doppel causes male sterility. EMBO J. 21, 3652-3658
    • (2002) EMBO J. , vol.21 , pp. 3652-3658
    • Behrens, A.1
  • 56
    • 0035909931 scopus 로고    scopus 로고
    • Doppel-induced cerebellar degeneration in transgenic mice
    • Moore, R.C. et al. (2001) Doppel-induced cerebellar degeneration in transgenic mice. Proc. Natl. Acad. Sci. U. S. A. 98, 15288-15293
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 15288-15293
    • Moore, R.C.1
  • 57
    • 0035042258 scopus 로고    scopus 로고
    • Normal neurogenesis and scrapie pathogenesis in neural grafts lacking the prion protein homologue Doppel
    • Behrens, A. et al. (2001) Normal neurogenesis and scrapie pathogenesis in neural grafts lacking the prion protein homologue Doppel. EMBO Rep. 2, 347-352
    • (2001) EMBO Rep. , vol.2 , pp. 347-352
    • Behrens, A.1
  • 58
    • 0036184716 scopus 로고    scopus 로고
    • Expression of doppel in the CNS ofmice does not modulate transmissible spongiform encephalopathy disease
    • Tuzi, N.L. et al. (2002) Expression of doppel in the CNS ofmice does not modulate transmissible spongiform encephalopathy disease. J. Gen. Virol. 83, 705-711
    • (2002) J. Gen. Virol. , vol.83 , pp. 705-711
    • Tuzi, N.L.1
  • 59
    • 0001552281 scopus 로고    scopus 로고
    • Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions
    • Shmerling, D. 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
  • 60
    • 0036470471 scopus 로고    scopus 로고
    • Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration
    • Mallucci, G.R. et al. (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
  • 61
    • 0037080043 scopus 로고    scopus 로고
    • Lack of prion protein expression results in a neuronal phenotype sensitive to stress
    • Brown, D.R. et al. (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.