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E. N. Olson, H. H. Arnold, P. W. Rigby, and B. J. Wold, Know your neighbors: three phenotypes in null mutants of the myogenic bHLH gene MRF4. Cell 85, 1–4 (1996).
R. C. Moore, I. Y. Lee, G. L. Silverman, P. M. Harrison, R. Strome, C. Heinrich, A. Karunaratne, S. H. Pasternak, M. A. Chishti, Y. Liang, P. Mastrangelo, K. Wang, A. F. Smit, S. Katamine, G. A. Carlson, F. E. Cohen, S. B. Prusiner, D. W. Melton, P. Tremblay, L. E. Hood, and D. Westaway, 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).
A. Li, S. Sakaguchi, R. Atarashi, B. C. Roy, R. Nakaoke, K. Arima, N. Okimura, J. Kopacek, and K. Shigematsu, Identification of a novel gene encoding a PrP-like protein expressed as chimeric transcripts fused to PrP exon 1/2 in ataxic mouse line with a disrupted PrP gene. Cell Mol Neurobiol 20, 553–67 (2000).
B. Oesch, D. Westaway, M. Walchli, M. P. McKinley, S. B. Kent, R. Aebersold, R. A. Barry, P. Tempst, D. B. Teplow, L. E. Hood, and et al., A cellular gene encodes scrapie PrP 27–30 protein. Cell 40, 735–46 (1985).
S. B. Prusiner, Molecular biology of prion diseases. Science 252, 1515–22 (1991).
S. B. Prusiner, Prions. Proc Natl Acad Sci USA 95, 13363–83 (1998).
H. Bueler, A. Aguzzi, A. Sailer, R. A. Greiner, P. Autenried, M. Aguet, and C. Weissmann, Mice devoid of PrP are resistant to scrapie. Cell 73, 1339–47 (1993).
S. B. Prusiner, D. Groth, A. Serban, R. Koehler, D. Foster, M. Torchia, D. Burton, S. L. Yang, and S. J. DeArmond, Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies. Proc Natl Acad Sci USA 90, 10608–12 (1993).
J. C. Manson, A. R. Clarke, P. A. McBride, I. McConnell, and J. Hope, PrP gene dosage determines the timing but not the final intensity or distribution of lesions in scrapie pathology. Neurodegeneration 3, 331–40 (1994).
S. Sakaguchi, S. Katamine, K. Yamanouchi, M. Kishikawa, R. Moriuchi, N. Yasukawa, T. Doi, and T. Miyamoto, Kinetics of infectivity are dissociated from PrP accumulation in salivary glands of Creutzfeldt-Jakob disease agent-inoculated mice. J Gen Virol 74 (Pt 10), 2117–23 (1993).
H. Bueler, M. Fischer, Y. Lang, H. Bluethmann, H. P. Lipp, S. J. DeArmond, S. B. Prusiner, M. Aguet, and C. Weissmann, Normal developmentand behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 356, 577–82 (1992).
J. C. Manson, A. R. Clarke, M. L. Hooper, L. Aitchison, I. McConnell, and J. Hope, 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal. Mol Neurobiol 8, 121–7 (1994).
S. Sakaguchi, S. Katamine, N. Nishida, R. Moriuchi, K. Shigematsu, T. Sugimoto, A. Nakatani, Y Kataoka, T. Houtani, S. Shirabe, H. Okada, S. Hasegawa, T Miyamoto, and T. Noda, Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene. Nature 380, 528–31 (1996).
S. Sakaguchi, S. Katamine, K. Shigematsu, A. Nakatani, R. Moriuchi, N. Nishida, K. Kurokawa, R. Nakaoke, H. Sato, K. Jishage, and et al., 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, 7586–92 (1995).
D. Rossi, A. Cozzio, E. Flechsig, M. A. Klein, T Rulicke, A. Aguzzi, and C. Weissmann, Onset of ataxia and Purkinje cell loss in PrP null mice inversely correlated with Dpl level in brain. Embo J 20, 694–702 (2001).
J. Manson, J. D. West, V. Thomson, P. McBride, M. H. Kaufman, and J. Hope, The prion protein gene: a role in mouse embryogenesis? Development 115, 117–22 (1992).
S. J. DeArmond, W. C. Mobley, D. L. DeMott, R. A. Barry, J. H. Beckstead, and S. B. Prusiner, Changes in the localization of brain prion proteins during scrapie infection. Neurology 37, 1271–80 (1987).
R. Morris, Developments of a water-maze procedure forstudying spatial learning in the rat. J Neurosci Methods 11, 47–60 (1984).
A. L. Phinney, M. E. Calhoun, D. P. Wolfer, H. P. Lipp, and H. Zheng, No hippocampal neuron or synaptic bouton loss in learningimpaired aged beta-amyloid precursor protein-null mice. Neuroscience 90, 1207–1216 (1999).
H. P. Lipp, and H. Van der Loos, A computer-controlled Y-maze for the analysis of vibrissotactile discrimination learning in mice. Behav Brain Res 45, 135–145 (1991).
N. Nishida, S. Katamine, K. Shigematsu, A. Nakatani, N. Sakamoto, S. Hasegawa, R. Nakaoke, R. Atarashi, Y. Kataoka, and T Miyamoto, Prion protein is necessary for latent learning and long-term memory retention. Cell Mol Neurobiol 17, 537–45 (1997).
A. Ettenberg, M. L. Moal, G. F. Koob, and F. E. Bloom, Vasopressin potentiation in the performance of a learned appetitive task: Reversal by a pressor antagonist analog of vasopressin. Pharmacol Biochem Behav 18, 645–647 (1983).
H. P. Lipp, H. Schwegler, B. Heimrich, and P. Driscoll, Infrapyramidal mossy fibers and two-way avoidance learning: Developmental modification of hippocampal circuitry and adult behaviorof rats and mice. J Neurosci 8, 1905–1921 (1988).
J. Collinge, M. A. Whittington, K. C. Sidle, C. J. Smith, M. S. Palmer, A. R. Clarke, and J. G. Jefferys, Prion protein is necessary for normal synaptic function. Nature 370, 295–7 (1994).
M. A. Whittington, K. C. Sidle, I. Gowland, J. Meads, A. F. Hill, M. S. Palmer, J. G. Jefferys, and J. Collinge, Rescue of neurophysiological phenotype seen in PrP null mice by transgene encoding human prion protein. Nat Genet 9, 197–201 (1995).
J. Manson, J. Hope, A. R. Clarke, A. Johnston, C. Black, and N. MacLeod, PrP gene dosage and long term potentiation. Neurodegeneration 4, 113–115 (1995).
J. W. Herms, H. A. Kretzchmar, S. Titz, and B. U. Keller, Patch-clamp analysis of synaptic transmission to cerebellar purkinje cells of prion protein knockout mice. Eur J Neurosci 7, 2508–12 (1995).
P. M. Lledo, P. Tremblay, S. J. DeArmond, S. B. Prusiner, and R. A. Nicoll, Mice deficient for prion protein exhibit normal neuronal excitability and synaptic transmission in the hippocampus. Proc Natl Acad Sci USA 93, 2403–7 (1996).
I. Tobler, S. E. Gaus, T Deboer, P. Achermann, M. Fischer, T. Rulicke, M. Moser, B. Oesch, P. A. McBride, and J. C. Manson, Altered circadian activity rhythms and sleep in mice devoid of prion protein. Nature 380, 639–42 (1996).
N. Nishida, P. Tremblay, T. Sugimoto, K. Shigematsu, S. Shirabe, C. Petromilli, S. P. Erpel, R. Nakaoke, R. Atarashi, T. Houtani, M. Torchia, S. Sakaguchi, S. J. DeArmond, S. B. Prusiner, and S. Katamine, A mouse prion protein transgene rescues mice deficient for the prion protein gene from purkinje cell degeneration and demyelination. Lab Invest 79, 689–97 (1999).
D. R. Borchelt, V. E. Koliatsos, M. Guarnieri, C. A. Pardo, S. S. Sisodia, and D. L. Price, Rapid anterograde axonal transport of the cellular prion glycoprotein in the peripheral and central nervous systems. J Biol Chem 269, 14711–4 (1994).
R. Atarashi, S. Sakaguchi, K. Shigematsu, K. Arima, N. Okimura, N. Yamaguchi, A. Li, J. Kopacek, and S. Katamine, Abnormal activation of glial cells in the brains of prion protein-deficient mice ectopically expressing prion protein-like protein, PrPLP/Dpl. Mol Med 7, 803–9 (2001).
M. Moser, R. J. Colello, U. Pott, and B. Oesch, Developmental expression of the prion protein gene in glial cells. Neuron 14, 509–17 (1995).
D. R. Brown, A. Besinger, J. W. Herms, and H. A. Kretzschmar, Microglial expression of the prion protein. Neuroreport 9, 1425–9 (1998).
J. Follet, C. Lemaire-Vieille, F. Blanquet-Grossard, V. Podevin-Dimster, S. Lehmann, J. P. Chauvin, J. P. Decavel, R. Varea, J. Grassi, M. Fontes, and J. Y Cesbron, PrP expression and replication by Schwann cells: implications in prion spreading. J Virol 76, 2434–9 (2002).
E. J. Steinmetz, Pre-mRNA processing and the CTD of RNA polymerase II: The tail that wags the dog. Cell 89, 491–194 (1997).
R. C. Moore, P. Mastrangelo, E. Bouzamondo, C. Heinrich, G. Legname, S. B. Prusiner, L. Hood, D. Westaway, S. J. DeArmond, and P. Tremblay, Doppel-induced cerebellar degeneration in transgenic mice. Proc Natl Acad Sci USA 98, 15288–93 (2001).
A. Li, S. Sakaguchi, K. Shigematsu, R. Atarashi, B. C. Roy, R. Nakaoke, K. Arima, N. Okimura, J. Kopacek, and S. Katamine, Physiological expression of the gene for PrP-like protein, PrPLP/Dpl, by brain endothelial cells and its ectopic expression in neurons of PrP-deficient mice ataxic due to Purkinje cell degeneration. Am J Pathol 157, 1447–52 (2000).
G. L. Silverman, K. Qin, R. C. Moore, Y Yang, P. Mastrangelo, P. Tremblay, S. B. Prusiner, F. E. Cohen, and D. Westaway, Doppel is an N-glycosylated, glycosylphosphatidylinositol-anchored protein. Expression in testis and ectopic production in the brains of Prnp(0/0) mice predisposed to Purkinje cell loss. J Biol Chem 275, 26834–11 (2000).
H. Mo, R. C. Moore, F. E. Cohen, D. Westaway S. B. Prusiner, P. E. Wright, and H. J. Dyson, Two different neurodegenerative diseases caused by proteins with similar structures. Proc Natl Acad Sci USA 98, 2352–7 (2001).
Y. Shaked, N. Hijazi, and R. Gabizon, Doppel and PrP(C) do not share the same membrane microenvironment. FEBS Lett 530, 85–8 (2002).
A. Behrens, N. Genoud, H. Naumann, T. Rulicke, F. Janett, F. L. Heppner, B. Ledermann, and A. Aguzzi, Absence of the prion protein homologue Doppel causes male sterility. Embo J 21, 3652–8 (2002).
K. Peoc’h, C. Serres, Y Frobert, C. Martin, S. Lehmann, S. Chasseigneaux, V. Sazdovitch, J. Grassi, P. Jouannet, J. M. Launay, and J. L. Laplanche, The human “prion-like” protein Doppel is expressed in both Sertoli cells and spermatozoa. J Biol Chem 277, 43071–8 (2002).
N. Yamaguchi, S. Sakaguchi, K. Shigematsu, N. Okimura, and S. Katamine, Doppel-induced Purkinje cell death is stoichiometrically abrogated by prion protein. Biochem Biophys Res Commun 319, 1247–1252 (2004).
L. Anderson, D. Rossi, J. Linehan, S. Brandner, and C. Weissmann, Transgene-driven expression of the Doppel protein in Purkinje cells causes Purkinje cell degeneration and motor impairment. Proc Natl Acad Sci USA 101, 3644–3649 (2004).
R. Atarashi, N. Nishida, K. Shigematsu, S. Goto, T. Kondo, S. Sakaguchi, and S. Katamine, Deletion of N-terminal residues 23–88 from prion protein (PrP) abrogates the potentialto rescue PrP-deficient micefrom PrP-like protein/doppel-induced Neu-rodegeneration. J Biol Chem 278, 28944–9 (2003).
Y. Zhang, W. Swietnicki, M. G. Zagorski, W. K. Surewicz, and F. D. Sonnichsen, Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases. J Biol Chem 275, 33650–4 (2000).
D. Shmerling, I. Hegyi, M. Fischer, T. Blattler, S. Brandner, J. Gotz, T. Rulicke, E. Flechsig, A. Cozzio, C. von Mering, C. Hangartner, A. Aguzzi, and C. Weissmann, Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions. Cell 93, 203–14 (1998).
E. Flechsig, I. Hegyi, R. Leimeroth, A. Zuniga, D. Rossi, A. Cozzio, P. Schwarz, T. Rulicke, J. Gotz, A. Aguzzi, and C. Weissmann, Expression of truncated PrP targeted to Purkinje cells of PrP knockout mice causes Purkinje cell death and ataxia. Embo J 22, 3095–101 (2003).
C. Weissmann, and A. Aguzzi, Perspectives: neurobiology. PrP’s double causes trouble. Science 286, 914–5 (1999).
G. M. Cereghetti, A. Schweiger, R. Glockshuber, and S. Van Doorslaer, Electron paramagnetic resonance evidence for binding of Cu(2+) to the C-terminal domain of the murine prion protein. Biophys J 81, 516–25 (2001).
G. S. Jackson, I. Murray, L. L Hosszu, N. Gibbs, J. P. Waltho, A. R. Clarke, and J. Collinge, Location and properties of metal-binding sites on the human prion protein. Proc Natl Acad Sci USA 98, 8531–5 (2001).
K. Qin, J. Coomaraswamy, P. Mastrangelo, Y. Yang, S. Lugowski, C. Petromilli, S. B. Prusiner, P. E. Fraser, J. M. Goldberg, A. Chakrabartty, and D. Westaway, The PrP-like protein Doppel binds copper. J Biol Chem 278, 8888–96 (2003).
T. Muramoto, S. J. DeArmond, M. Scott, G. C. Telling, F. E. Cohen, and S. B. Prusiner, Heritable disorder resembling neuronal storage disease in mice expressing prion protein with deletion of an alpha-helix. Nat Med 3, 750–5 (1997).
S. M. Zanata, M. H. Lopes, A. F. Mercadante, G. N. Hajj, L. B. Chiarini, R. Nomizo, A. R. Freitas, A. L. Cabral, K. S. Lee, M. A. Juliano, E. de Oliveira, S. G. Jachieri, A. Burlingame, L. Huang, R. Linden, R. R. Brentani, and V. R. Martins, Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection. EMBO J 21, 3307–16 (2002).
R. G. Warner, C. Hundt, S. Weiss, and J. E. Turnbull, Identification of the heparan sulfate binding sites in the cellular prion protein. J Biol Chem 277, 18421–30 (2002).
B. S. Wong, T. Liu, D. Paisley, R. Li, T. Pan, S. G. Chen, G. Perry, R. B. Petersen, M. A. Smith, D. W. Melton, P. Gambetti, D. R. Brown, and M. S. Sy, Induction of HO-1 and NOS in doppel-expressing mice devoid of PrP: implications for doppel function. Mol Cell Neurosci 17, 768–75 (2001).
T. Cui, A. Holme, J. Sassoon, and D. R. Brown, Analysis of doppel protein toxicity. Mol Cell Neurosci 23, 144–55 (2003).
D. R. Brown, K. Qin, J. W. Herms, A. Madlung, J. Manson, R. Strome, P. E. Fraser, T. Kruck, A. von Bohlen, W. Schulz-Schaeffer, A. Giese, D. Westaway and H. Kretzschmar, The cellular prion protein binds copper in vivo. Nature 390, 684–7 (1997).
D. R. Brown, R. S. Nicholas, and L. Canevari, Lack of prion protein expression results in a neuronal phenotype sensitive to stress. J Neurosci Res 67, 211–24 (2002).
C. Kuwahara, A. M. Takeuchi, T. Nishimura, K. Haraguchi, A. Kubosaki, Y Matsumoto, K. Saeki, T. Yokoyama, S. Itohara, and T Onodera, Prions prevent neuronal cell-line death. Nature 400, 225–6 (1999).
Y. Bounhar, Y Zhang, C. G. Goodyer, and A. LeBlanc, Prion protein protects human neurons against Bax-mediated apoptosis. J Biol Chem 276, 39145–9 (2001).
S. J. DeArmond, and S. B. Prusiner, Etiology and pathogenesis of prion diseases. Am J Pathol 146, 785–811 (1995).
T. Yokoyama, K. M. Kimura, Y. Ushiki, S. Yamada, A. Morooka, T. Nakashiba, T. Sassa, and S. Itohara, In vivo conversion of cellular prion protein to pathogenic isoforms, as monitored by conformation-specific antibodies. J Biol Chem 276, 11265–71 (2001).
G. Forloni, N. Angeretti, R. Chiesa, E. Monzani, M. Salmona, O. Bugiani, and F. Tagliavini, Neurotoxicity of a prion protein fragment. Nature 362, 543–6 (1993).
T. Kitamoto, N. Amano, Y Terao, Y Nakazato, T. Isshiki, T. Mizutani, and J. Tateishi, A new inherited prion disease (PrP-P105L mutation) showing spastic paraparesis. Ann Neurol 34, 808–13 (1993).
M. Y Neufeld, J. Josiphov, and A. D. Korczyn, Demyelinating peripheral neuropathy in Creutzfeldt-Jakob disease. Muscle Nerve 15, 1234–9 (1992).
N. L. Tuzi, E. Gall, D. Melton, and J. C. Manson, Expression of doppel in the CNS of mice does not modulate transmissible spongiform encephalopathy disease. J Gen Virol 83, 705–11 (2002).
S. G. Chen, D. B. Teplow, P. Parchi, J. K. Teller, P. Gambetti, and L. Autilio-Gambetti, Truncated forms of the human prion protein in normal brain and in prion diseases. J Biol Chem 270, 19173–80 (1995).
R. Daoud, M. Da Penha Berzaghi, F. Siedler, M. Hubener, and S. Stamm, Activity-dependent regulation of alternative splicing patterns inthe rat brain. Eur J Neurosci 11, 788–802 (1999).
R. Daoud, G. Mies, A. Smialowska, L. Olah, K. A. Hossmann, and S. Stamm, Ischemia induces a translocation of the splicing factor tra2-beta 1 and changes alternative splicing patterns in the brain. J Neurosci 22, 5889–99 (2002).
D. Grisaru, M. Sternfeld, A. Eldor, D. Glick, and H. Soreq, Structural roles of acetyl-cholinesterase variants in biology and pathology. Eur J Biochem 264, 672–86 (1999).
Y. Imai, N. Matsuo, S. Ogawa, M. Tohyama, and T. Takagi, Cloning of a gene, YT521, for a novel RNA splicing-related protein induced by hypoxia/reoxygenation. Brain Res Mol Brain Res 53, 33–40 (1998).
K. L. Jin, S. H. Graham, X. O. Mao, X. He, T. Nagayama, R. P. Simon, and D. A. Greenberg, Bax kappa, a novel Bax splice variant from ischemic rat brain lacking an ART domain, promotes neuronal cell death. J Neurochem 77, 1508–19 (2001).
D. Kaufer, A. Friedman, S. Seidman, and H. Soreq, Acute stress facilitates long-lasting changes in cholinergic gene expression. Nature 393, 373–7 (1998).
J. Xie, and D. L. Black, A CaMK IV responsive RNA element mediates depolarization-induced alternative splicing of ion channels. Nature 410, 936–9 (2001).
J. R. Sarna, and R. Hawkes, Patterned Purkinje cell death in the cerebellum. Prog Neurobiol 70, 473–507 (2003).
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Sakaguchi, S. (2005). Prion Protein, Prion Protein-Like Protein, and Neurodegeneration. In: Brown, D.R. (eds) Neurodegeneration and Prion Disease. Springer, Boston, MA. https://doi.org/10.1007/0-387-23923-5_7
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