Biology of the prion gene complex

Biochemistry and Cell Biology

Volumn 79, Issue 5, 2001, Pages 613-628

  Mastrangelo, Peter ^a   Westaway, David ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

CJD; Neurodegenerative disease; Paralogs; Scrapie; Spongiform encephalopathy

Indexed keywords

ANIMALIA; ATAXIA; BOVINAE; MAMMALIA; MUS MUSCULUS;

ANIMAL; BIOLOGICAL MODEL; CELL DEATH; CHEMICAL STRUCTURE; CREUTZFELDT JAKOB DISEASE; DEGENERATIVE DISEASE; GENETIC POLYMORPHISM; GENETICS; HUMAN; METABOLISM; MOUSE; NERVE CELL; PRION; PRION DISEASE; PROTEIN BINDING; REVIEW; SCRAPIE;

ANIMALS; CELL DEATH; CREUTZFELDT-JAKOB SYNDROME; HUMANS; MICE; MODELS, GENETIC; MODELS, MOLECULAR; NEURODEGENERATIVE DISEASES; NEURONS; POLYMORPHISM, GENETIC; PRION DISEASES; PRIONS; PROTEIN BINDING; SCRAPIE;

EID: 85047684706     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o01-142     Document Type: Article

References (140)

1. Basler, K., Oesch, B., Scott, M., Westaway, D., Wälchli, M., Groth, D.F., McKinley, M.P., Prusiner, S.B., and Weissmann, C. 1986. Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell, 46: 417-428.
2. Bazan, J.F., Fletterick, R.J., McKinley, M.P., and Prusiner, S.B. 1987. Predicted secondary structure and membrane topology of the scrapie prion protein. Protein Eng. 1: 125-135.
3. Behrens, A., Brandner, S., Genoud, N., and Aguzzi, A. 2001. Normal neurogenesis and scrapie pathogenesis in neural grafts lacking the prion protein homologue Doppel. EMBO Rep. 2: 347-352.
4. Bessen, R.A., and Marsh, R.F. 1992. Identification of two biologically distinct strains of transmissible mink encephalopathy in hamsters. J. Gen. Virol. 73: 329-334.
5. Bessen, R.A., and Marsh, R.F. 1994. Distinct PrP properties suggest the molecular basis of strain variation in Transmissible Mink Encephalopathy. J. Virol. 68: 7859-7868.
6. Bessen, R.A., Kocisko, D.A., Raymond, G.J., Nandan, S., Lansbury, P.T., and Caughey, B. 1995. Non-genetic propagation of strain-specific properties of scrapie prion protein. Nature (London), 375: 698-700.
7. Bolton, D.C., Meyer, R.K., and Prusiner, S.B. 1985. Scrapie PrP 27-30 is a sialoglycoprotein. J. Virol. 53: 596-606.
8. Borchelt, D.R., Taraboulos, A., and Prusiner, S.B. 1992. Evidence for synthesis of scrapie prion proteins in the endocytic pathway. J. Biol. Chem. 267: 6188-6199.
9. Bordier, C. 1981. Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 256: 1604-1607.
10. Brown, D.R., Qin, K., Heims, J., Madlung, A., von Bohlen, A., Manson, J., Strome, R., Fraser, P.E., Knick, T., Schulz-Schaeffer, W., Giese, A., Westaway, D., and Kretzschmar, H.A. 1997a. The cellular isoform of the prion protein binds to copper in vivo. Nature (London), 390: 684-687.
11. Brown, D.R., Schulz-Schaeffer, B., Schmidt, B., and Krtezschmar, H.A. 1997b. Prion-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity. Exp. Neurol. 146: 104-112.
12. Brown, D.R., Schmidt, B., and Kretzschmar, H.A. 1998. Effects of copper on survival of prion protein knockout neurons and glia. J. Neurochem. 70: 1686-1693.
13. Brown, D.R., Wong, B.S., Hafiz, F., Clive, C., Haswell, S.J., and Jones, I.M. 1999. Normal prion protein has an activity like that of superoxide dismutase. Biochem. J. 344: 1-5.
14. Brown, D.R., Hafiz, F., Glasssmith, L.L., Wong, B.S., Jones, I.M., Clive, C., and Haswell, S.J. 2000. Consequences of manganese replacement of copper for prion protein function and proteinase resistance. EMBO J. 19: 1180-1186.
15. Brown, P., Gibbs, C.J., Jr., Rodgers-Johnson, P., Asher, D.M., Sulima, M.P., Bacote, A., Goldfarb, L.G., and Gajdusek, D.C. 1994. Human spongiform encephalopathy: the National Institutes of Health series of 300 cases of experimentally transmitted disease. Ann. Neurol. 35: 513-529.
16. Büeler, H., Fischer, M., Lang, Y., Bluethmann, H., Lipp, H.-P., DeArmond, S.J., Prusiner, S.B., Aguet, M., and Weissmann, C. 1992. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature (London), 356: 577-582.
17. Büeler, H., Aguzzi, A., Sailer, A., Greiner, R.-A., Autenried, P., Aguet, M., and Weissmann, C. 1993. Mice devoid of PrP are resistant to scrapie. Cell, 73: 1339-1347.
18. Cappai, R., Stewart, L., Jobling, M.F., Thyer, J.M., White, A.R., Beyreuther, K., Collins, S.J., Masters, C.L., and Barrow, C.J. 1999. Familial prion disease mutation alters the secondary structure of recombinant mouse prion protein: implications for the mechanism of prion formation. Biochemistry, 38: 3280-3284.
19. Carlson, G.A., Kingsbury, D.T., Goodman, P.A., Coleman, S., Marshall, S.T., DeArmond, S.J., Westaway, D., and Prusiner, S.B. 1986. Linkage of prion protein and scrapie incubation time genes. Cell, 46: 503-511.
20. Carlson, G.A., Goodman, P.A., Lovett, M., Taylor, B.A., Marshall, S.T., Peterson-Torchia, M., Westaway, D., and Prusiner, S.B. 1988. Genetics and polymorphism of the mouse prion gene complex: the control of scrapie incubation time. Mol. Cell. Biol. 8: 5528-5540.
21. Carlson, G., Ebeling, C., Yang, S.L., Telling, G., Torchia, M., Groth, D., Westaway, D., and Prusiner, S. 1994. Prion isolate specific allotypic interactions between cellular and scrapie prion proteins in congenic and transgenic mice. Proc. Natl. Acad. Sci. U.S.A. 91: 5690-5694.
22. Caughey, B., and Raymond, G.J. 1991. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive. J. Biol. Chem. 266: 18217 - 18223.
23. Chernoff, Y.O., Lindquist, S.L., Ono, B.-I., Inge-Vechtomov, S.G., and Liebman, S.W. 1995. Role of the chaperone protein HSP104 in propagation of the Yeast prion-like Factor [psi+]. Science (Washington, D.C.), 268: 880-884.
24. Chiesa, R., Piccardo, P., Ghetti, B., and Harris, D.A. 1998. Neurological illness in transgenic mice expressing a prion protein with an insertional mutation. Neuron, 21: 1339-1351.
25. Chiesa, R., Drisaldi, B., Quaglio, E., Migheli, A., Piccardo, P., Ghetti, B., and Harris, D.A. 2000. Accumulation of protease-resistant prion protein (PrP) and apoptosis of cerebellar granule cells in transgenic mice expressing a PrP insertional mutation. Proc. Natl. Acad. Sci. U.S.A. 97: 5574-5579.
26. Chiesa, R., Pestronk, A., Schmidt, R.E., Tourtellotte, W.G., Ghetti, B., Piccardo, P., and Harris, D.A. 2001. Primary myopathy and accumulation of PrPSc-like molecules in peripheral tissues of transgenic mice expressing a prion protein insertional mutation. Neurobiol. Dis. 8(2): 279-288.
27. Collinge, J. 2001. Prion diseases of humans and animals: their causes and molecular basis. Ann. Rev. Neurosci. 24: 519-550.
28. Collinge, J., Whittington, M.A., Sidle, K.C., Smith, C.J., Palmer, M.S., Clarke, A.R., and Jefferys, J.G.R. 1994. Prion protein is necessary for normal synaptic function. Nature (London), 370: 295-297.
29. Conzelmann, A., Spiazzi, A., Hyman, R., and Bron, C. 1986. Anchoring of membrane proteins via phosphatidylinositol is deficient in two classes of Thy-1 negative mutant lymphoma cells. EMBO J. 5: 3291-3296.
30. Coschigano, P.W., and Magasanik, B. 1991. The URE2 gene product of Saccharomyces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione 5-transferases. Mol. Cell. Biol. 11: 822-832.
31. Coustou, V., Deleu, C., Saupe, S., and Begueret, J. 1997. The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc. Natl. Acad. Sci. U.S.A. 94: 9773-9778.
32. - mutation which eliminates the Ψ factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene. Genetics, 137: 659-670.
33. Donne, D., Viles, J.H., Groth, D., Mehlhorn, I., James, T.L., Cohen, F.E., Prusiner, S.B., Wright, P.E., and Dyson, H.J. 1997. Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. Proc. Natl. Acad. Sci. U.S.A. 94: 13452 - 13 457.
34. Edenhofer, F., Rieger, R., Famulok, M., Wendler, W., Weiss, S., and Winnacker, E.-L. 1996. Prion protein PrPC interacts with molecular chaperones of the Hsp60 family. J. Virol. 70: 4724-4728.
35. Finckh, U., Muller-Thomsen, T., Mann, U., Eggers, C., Marksteiner, J., Meins, W., Binetti, G., Alberici, A., Hock, C., Nitsch, R.M., and Gal, A. 2000. High prevalence of pathogenic mutations in patients with early-onset dementia detected by sequence analyses of four different genes. Am. J. Hum. Genet. 66: 110-117.
36. Fischer, M., Rulicke, T., Raeber, A., Sailer, A., Moser, M., Oesch, B., Brandner, S., Aguzzi, A., and Weissmann, C. 1996. Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO J. 15: 1255-1264.
37. Flechsig, E., Shmerling, D., Hegyi, I., Raeber, A.J., Fischer, M., Cozzio, A., von Mering, C., Aguzzi, A., and Weissmann, C. 2000. Prion protein devoid of the octapeptide repeat region restores susceptibility to scrapie in PrP knockout mice. Neuron, 27: 399-408.
38. Gabriel, J.-M., Oesch, B., Kretzschmar, H., Scott, M., and Prusiner, S.B. 1992. Molecular cloning of a candidate chicken prion protein. Proc. Natl. Acad. Sci. U.S.A. 89: 9097-9101.
39. Ghetti, B., Piccardo, P., Spillantini, M.G., Ichimiya, Y., Porro, M., Perini, F., Kitamoto, T., Tateishi, J., Seiler, C., Frangione, B., Bugiani, O., Giaccone, G., Prelli, F., Goedert, M., Dlouhy, S.R., and Tagliavini, F. 1996. Vascular variant of prion protein cerebral amyloidosis with T-positive neurofibrillary tangles: the phenotype of a stop codon145 mutation in PRNP. Proc. Natl. Acad. Sci. U.S.A. 93: 744-748.
40. Goldmann, W., Hunter, N., Multhaup, G., Salbalm, J.M., Foster, J.D., Beyreuther, K.T., and Hope, J. 1988. The PrP gene in natural scrapie. Alzheimer Dis. Assoc. Disord. 2(Abstr. suppl.): 330.
41. Goldmann, W., Hunter, N., Foster, J.D., Salbaum, J.M., Beyreuther, K., and Hope, J. 1990. Two alleles of a neural protein gene linked to scrapie in sheep. Proc. Natl. Acad. Sci. U.S.A. 87: 2476-2480.
42. Goldmann, W., Hunter, N., Smith, G., Foster, J., and Hope, J. 1994. PrP genotype and agent effects in scrapie: change in allelic interaction with different isolates of agent in sheep, a natural host of scrapie. J. Gen. Virol. 75: 989-995.
43. Harries-Jones, R., Knight, R., Will, R.G., Cousens, S., Smith, P.G., and Matthews, W.B. 1988. Creutzfeldt-Jakob disease in England and Wales, 1980-1984: a case-control study of potential risk factors. J. Neurol. Neurosurg. Psychiatry, 51: 1113-1119.
44. Hay, B., Barry, R.A., Lieberburg, I., Prusiner, S.B., and Lingappa, V.R. 1987. Biogenesis and transmembrane orientation of the cellular isoform of the scrapie prion protein. Mol. Cell. Biol. 7: 914-920.
45. Hedge, R.S., Mastrianni, J.A., Scott, M.R., DeFea, K.A., Trembaly, P., Torchia, M., DeArmond, S.J., Prusiner, S.B., and Lingappa, V.R. 1998. A transmembrane form of the prion protein in neurodegenerative disease. Science (Washington, D.C.), 279: 827-834.
46. Herms, J.W., Kretzchmar, H.A., Titz, S., and Keller, B.U. 1995. Patch-clamp analysis of synaptic transmission to cerebellar purkinje cells of prion protein knockout mice. Eur. J. Neurosci. 7: 2508-2512.
47. Herms, J., Tings, T., Gall, S., Madlung, A., Giese, A., Siebert, H., Schurmann, P., Windl, O., Brose, N., and Kretzschmar, H. 1999. Evidence of presynaptic location and function of the prion protein. J. Neurosci. 19: 8866-8875.
48. Hornshaw, M.P., McDermott, J.R., and Candy, J.M. 1995. Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein. Biochem. Biophys. Res. Commun. 207: 621-629.
49. James, T.L., Liu, H., Ulyanov, N.B., Farr-Jones, S., Zhang, H., Donne, D.G., Kaneko, K., Groth, D., Mehlhorn, I., Prusiner, S.B., and Cohen, F.E. 1997. Solution structure of a 142-residue prion protein corresponding to the infectious fragment of the scrapie isoform. Proc. Natl. Acad. Sci. U.S.A. 94: 10086-10091.
50. Kaneko, K., Vey, M., Scott, M., Pilkuhn, S., Cohen, F.E., and Prusiner, S.B. 1997a. COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform. Proc. Natl. Acad. Sci. U.S.A. 94: 2333-2338.
51. Kaneko, K., Zulianello, L., Scott, M., Cooper, C.M., Wallace, A.C., James, T.L., Cohen, F.E., and Prusiner, S.B. 1997b. Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc. Natl. Acad. Sci. U.S.A. 94: 10 069 - 10 074.
52. Kramer, M.L., Kratzin, H.D., Schmidt, B., Romer, A., Windl, O., Liemann, S., Hornemann, S., and Kretzschmar, H. 2001. Prion protein binds copper within the physiological concentration range. J. Biol. Chem. 27: 27.
53. Kurschner, C., and Morgan, J.I. 1995. The cellular prion protein (PrP) selectively binds to Bcl-2 in the yeast two-hybrid system. Mol. Brain Res. 30: 165-168.
54. Kuwahara, C., Takeuchi, A.M., Nishimura, T., Haraguchi, K., Kubosaki, A., Matsumoto, Y., Saeki, K., Yokoyama, T., Itohara, S., and Onodera, T. 1999. Prions prevent neuronal cell-line death. Nature (London), 400: 225-226.
55. Laplanche, J.L., Chatelain, J., Westaway, D., Thomas, S., Dussaucy, M., Brugere-Picoux, J., and Launay, J.M. 1993. PrP polymorphisms associated with natural scrapie discovered by denaturing gradient gel electrophoresis. Genomics, 15: 30-37.
56. Lee, I., Westaway, D., Smit, A.F.A., Wang, K., Seto, J., Chen, L., Acharya, C., Ankener, M., Baskin, D., Cooper, C., Yao, H., Prusiner, S.B., and Hood, L. 1998. Complete genomic sequence and analysis of the prion protein gene region from three mammalian species. Genome Res. 8: 1022-1037.
57. Lehmann, S., and Harris, D.A. 1996. Mutant and infectious prion proteins display common biochemical properties in cultured cells. J. Biol. Chem. 271: 1633-1637.
58. Li, A., Sakaguchi, S., Atarashi, R., Roy, B.C., Nakaoke, R., Arima, K., Okimura, N., Kopacek, J., and Shigematsu, K. 2000a. 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 [In process citation]. Cell. Mol. Neurobiol. 20: 553-567.
59. Li, A., Sakaguchi, S., Shigematsu, K., Atarashi, R., Roy, B.C., Nakaoke, R., Arima, K., Okimura, N., Kopacek, J., and Katamine, S. 2000b. 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 [In process citation]. Am. J. Pathol. 157: 1447-1452.
60. Liemann, S., and Glockshuber, R. 1999. Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein. Biochemistry, 38: 3258-3267.
61. Lledo, P.-M., Tremblay, P., DeArmond, S.J., Prusiner, S.B., and Nicoll, R.A. 1996. Mice deficient for prion protein exhibit normal neuronal excitability and synaptic transmission in the hippocampus. Proc. Natl. Acad. Sci. U.S.A. 93: 2403-2407.
62. Loftus, B., and Rogers, M. 1997. Characterization of a prion protein (PrP) gene from rabbit; a species with apparent resistance to infection by prions. Gene, 184: 215-219.
63. Lopez, C.D., Yost, C.S., Prusiner, S.B., Myers, R.M., and Lingappa, V.R. 1990. Unusual topogenic sequence directs prion protein biogenesis. Science (Washington, D.C.), 248: 226-229.
64. Lopez Garcia, F., Zahn, R., Riek, R., and Wuthrich, K. 2000. NMR structure of the bovine prion protein. Proc. Natl. Acad. Sci. U.S.A. 97: 8334-8339.
65. Lu, K., Wang, W., Xie, Z., Wong, B.S., Li, R., Petersen, R.B., Sy, M.S., and Chen, S.G. 2000. Expression and structural characterization of the recombinant human doppel protein. [In process citation]. Biochemistry, 39: 13 575 - 13 583.
66. Ma, J., and Lindquist, S. 1999. De novo generation of a PrPSc-like conformation in living cells. Nat. Cell Biol. 1: 358-361.
67. Manson, J.C., Clarke, A.R., Hooper, M.L., Aitchison, L., McConnel, I., and Hope, J. 1994a. 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal. Mol. Neurobiol. 8: 121-127.
68. Manson, J.C., Clarke, A.R., McBride, P.A., McConnell, I., and Hope, J. 1994b. PrP gene dosage determines the timing but not the final intensity or distribution of lesions in scrapie pathology. Neurodegeneration, 3: 331-340.
69. Martins, V.R., Graner, E., Garcia-Abreu, J., De Souza, S.J., Mercadante, A.F., Veiga, S.S., Zanata, S.M., Neto, V.M., and Brentani, R.R. 1997. Complementary hydropathy identifies a cellular prion protein receptor. Nat. Med. 3: 1376-1382.
70. c and Doppel: insights from mutational analysis. Gene, 275: 1-18.
71. McMahon, H.E., Mange, A., Nishida, N., Creminon, C., Casanova, D., and Lehmann, S. 2001. Cleavage of the amino terminus of the prion protein by reactive oxygen species. J. Biol. Chem. 276: 2286-2291.
72. Mead, S., Beck, J., Dickinson, A., Fisher, E.M., and Collinge, J. 2000. Examination of the human prion protein-like gene doppel for genetic susceptibility to sporadic and variant Creutzfeldt-Jakob disease. Neurosci. Lett. 290: 117-120.
73. Mo, H., Moore, R.C., Cohen, F.E., Westaway, D., Prusiner, S.B., Wright, P.E., and Dyson, H.J. 2001. Two different neurodegenerative diseases caused by proteins with similar structures. Proc. Natl. Acad. Sci. U.S.A. 98(5): 2352-2357.
74. Moore, R.C., Hope, J., McBride, P.A., McConnell, I., Selfridge, J., Melton, D.W., and Manson, J.C. 1998. Mice with gene targetted prion protein alterations show that Prnp, Sinc and Prni are congruent. Nat. Genet. 18: 118-125.
75. Moore, R., Lee, I., Silverman, G.S., Harrison, P., Strome, R., Heinrich, C., Chishti, M.A., Karunaratne, A., Pasternak, S.H., Chishti, M.A., Liang, Y., Mastrangelo, P., Wang, K., Smit, A.F.A., Katamine, S., Carlson, G.A., Cohen, F.E., Prusiner, S.B., Melton, D.W., Tremblay, P., Hood, L.E., and Westaway, D. 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.
76. Moore, R., Mastrangelo, P., Tremblay, P., DeArmond, S., Westaway, D., and Prusiner, S.B. 2001. Overexpression of the prion-like protein Dpi causes an ataxic syndrome. Proc. Natl. Acad. Sci. U.S.A. In press.
77. Moran, P., Raab, H., Kohr, W.J., and Caras, I.W. 1991. Glycophospholipid membrane anchor attachment. Molecular analysis of the cleavage/attachment site. J. Biol. Chem. 266: 1250-1257.
78. Mouillet-Richard, S., Ermonval, M., Chebassier, C., Laplanche, J.L., Lehmann, S., Launay, J.M., and Kellermann, O. 2000. Signal transduction through prion protein. Science (Washington, D.C.), 289: 1925-1928.
79. Muramoto, T., DeArmond, S.J., Scott, M., Telling, G.C., Cohen, F.E., and Prusiner, S. 1997. Heritable disorder resembling neuronal storage disease in mice expressing prion protein with deletion of an alpha-helix. Nat. Med. 3: 750-755.
80. Neufeld, M.Y., Josiphov, J., and Korczyn, A.D. 1992. Demye- linating peripheral neuropathy in Creutzfeldt-Jakob disease. Muscle Nerve, 15: 1234-1239.
81. Oesch, B., Westaway, D., Wälchli, M., McKinley, M.P., Kent, S.B.H., Aebersold, R., Barry, R.A., Tempst, P., Teplow, D.B., Hood, L.E., Prusiner, S.B., and Weissmann, C. 1985. A cellular gene encodes scrapie PrP 27-30 protein. Cell, 40: 735-746.
82. Oesch, B., Teplow, D.B., Stahl, N., Serban, D., Hood, L.E., and Prusiner, S.B. 1990. Identification of cellular proteins binding to the scrapie prion protein. Biochemistry, 29: 5848-5855.
83. O'Rourke, K.I., Holyoak, G.R., Clark, W.W., Mickelson, J.R., Wang, S., Melco, R.P., Besser, T.E., and Foote, W.C. 1997. PrP genotypes and experimental scrapie in orally inoculated Suffolk sheep in the United States. J. Gen. Virol. 78: 975-978.
84. Palmer, M.S., Dryden, A.J., Hughes, J.T., and Collinge, J. 1991. Homozygous prion protein genotype predisposes to sporadic Creutzfeld-Jacob Disease. Nature (London), 352: 340-342.
85. Pauly, P.C., and Harris, D.A. 1998. Copper stimulates endocytosis of the Prion Protein. J. Biol. Chem. 273: 33 107 - 33 110.
86. Peoc'h, K., Guerin, C., Brandel, J.P., Launay, J.M., and Laplanche, J.L. 2000. First report of polymorphisms in the prion-like protein gene (PRND): implications for human prion diseases. Neurosci. Lett. 286: 144-148.
87. Priola, S.A., and Chesebro, B. 1995. A single hamster PrP amino acid blocks conversion to protease-resistant PrP in scrapie-infected mouse neuroblastoma cells. J. Virol. 69: 7754-7758.
88. Prusiner, S.B. 1997. Prion diseases and the BSE crisis. Science (Washington, D.C.), 278: 245-251.
89. Prusiner, S., Scott, M., Foster, D., Westaway, D., and DeArmond, S. 1990. Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell, 63: 673-686.
90. Prusiner, S.B., Groth, D., Serban, A., Koehler, R., Foster, D., Torchia, M., Burton, D., Yang, S.-L., and DeArmond, S.J. 1993. Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies. Proc. Natl. Acad. Sci. U.S.A. 90: 10 608 - 10 612.
91. Qin, K., Yang, D.S., Yang, Y., Chishti, M.A., Meng, L.J., Kretzschmar, H.A., Yip, C.M., Fraser, P.E., and Westaway, D. 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.
92. Race, R.E., Priola, S.A., Bessen, R.A., Ernst, D., Dockter, J., Rall, G.F., Mucke, L., Chesebro, B., and Oldstone, M.B. 1995. Neuron-specific expression of a hamster prion protein minigene in transgenic mice induces susceptibility to hamster scrapie agent. Neuron, 15: 1183-1191.
93. Rieger, R., Edenhofer, F., Lasmeza, C.I., and Weiss, S. 1997. The human 37-KDa laminin receptor precursor interacts with the prion protein in eukaryotic cells. Nat. Med. 3: 1383-1388.
94. Riek, R., Hornemann, S., Wider, G., Billeter, M., Glockshuber, R., and Wuthrich, K. 1996. NMR structure of the mouse prion protein domain PrP (121-231). Nature (London), 382: 180-183.
95. Riek, R., Hornemann, S., Wider, G., Glockshuber, R., and Wuthrich, K. 1997. NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett. 413: 282-288.
96. Riek, R., Wider, G., Billeter, M., Hornemann, S., Glockshuber, R., and Wuthrich, K. 1998. Prion protein NMR structure and familial human spongiform encephalopathies. Proc. Natl. Acad. Sci. U.S.A. 95: 11 667- 11 672.
97. Rosenthal, N.P., Keesey, J., Crandall, B., and Brown, W.J. 1976. Familial neurological disease associated with spongiform encephalopathy. Arch. Neurol. 33: 252-259.
98. Rossi, D., Cozzio, A., Flechsig, E., Klein, M.A., Rulicke, T., Aguzzi, A., and Weissmann, C. 2001. Onset of ataxia and Purkinje cell loss in PrP null mice inversely correlated with Dpl level in brain. EMBO J. 20: 694-702.
99. Sc molecules with different conformations. Nat. Med. 4: 1157-1165.
100. Sailer, A., Büeler, H., Fischer, M., Aguzzi, A., and Weissmann, C. 1994. No propagation of prions in mice devoid of PrP. Cell, 77: 967-968.
101. Sakaguchi, S., Katamine, S., Nishida, N., Moriuchi, R., Shigematsu, K., Sugimoto, T., Nakatani, A., Kataoka, Y., Houtani, T., Shirabe, S., Okada, H., Hasegawa, S., Miyamoto, T., and Noda, T. 1996. Loss of cerebellar purkinje cells in aged mice homozygous for a disrupted PrP gene. Nature (London), 380: 528-531.
102. Scott, M., Foster, D., Mirenda, C., Serban, D., Coufal, F., Wälchli, M., Torchia, M., Groth, D., Carlson, G., DeArmond, S.J., Westaway, D., and Prusiner, S.B. 1989. Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques. Cell, 59: 847-857.
103. Scott, M.R., Köhler, R., Foster, D., and Prusiner, S.B. 1992. Chimeric prion protein expression in cultured cells and transgenic mice. Protein Sci. 1: 986-997.
104. Shaked, Y., Rosenmann, H., Talmor, G., and Gabizon, R. 1999. A C-terminal-truncated PrP isoform is present in mature sperm. J. Biol. Chem. 274: 32 153 - 32 158.
105. Shibuya, S., Higuchi, J., Shin, R.W., Tateishi, J., and Kitamoto, T. 1998. Codon 219 Lys allele of PRNP is not found in sporadic Creutzfeldt-Jakob disease. Ann. Neurol. 43: 826-828.
106. Shmerling, D., Hegyi, I., Fischer, M., Blattler, T., Brandner, S., Gotz, J., Rulicke, T., Flechsig, E., Cozzio, A., von Mering, C., Hangartner, C., Aguzzi, A., and Weissmann, C. 1998. Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions. Cell, 93: 203-214.
107. Shyng, S.-L., Moulder, K.L., Lesko, A., and Harris, D.A. 1995. The N-terminal domain of a glycolipid-anchored prion protein is essential for its endocytosis via clathrin-coated pits. J. Biol. Chem. 270: 14 793 - 14 800.
108. 0/0 mice predisposed to Purkinje cell loss [In process citation]. J. Biol. Chem. 275: 26 834 - 26 841.
109. Spudich, S., Mastrianni, J.A., Wrensch, M., Gabizon, R., Meiner, Z., Kahana, I., Rosenmann, H., Kahana, E., and Prusiner, S.B. 1995. Complete penetrance of Creutzfeldt-Jakob Disease in Libyan Jews. Mol. Med. 1: 607-613.
110. Stahl, N., Borchelt, D.R., Hsiao, K., and Prusiner, S.B. 1987. Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell, 51: 229-240.
111. Supattapone, S., Bosque, P., Muramoto, T., Wille, H., Aagaard, C., Peretz, D., Nguyen, H.O., Heinrich, C., Torchia, M., Safar, J., Cohen, F.E., DeArmond, S.J., Prusiner, S.B., and Scott, M. 1999. Prion protein of 106 residues creates an artifical transmission barrier for prion replication in transgenic mice. Cell, 96: 869-878.
112. Swietnicki, W., Petersen, R.B., Gambetti, P., and Surewicz, W.K. 1998. Familial mutations and the thermodynamic stability of the recombinant human prion protein. J. Biol. Chem. 273: 31 048 - 31 052.
113. Tagliavini, F., Prelli, F., Ghisto, J., Bugiani, O., Serban, D., Prusiner, S.B., Farlow, M.R., Ghetti, B., and Frangione, B. 1991. Amyloid protein of Gerstmann-Sträussler-Scheinker disease (Indiana kindred) is an 11-kd fragment of prion protein with an N-terminal glycine at codon 58. EMBO J. 10: 513-519.
114. Tagliavini, F., Lievens, P.M., Tranchant, C., Warter, J.M., Mohr, M., Giaccone, G., Perini, F., Rossi, G., Salmona, M., Piccardo, P., Ghetti, B., Beavis, R.C., Bugiani, O., Frangione, B., and Prelli, F. 2001. A 7-kDa prion protein (PrP) fragment, an integral component of the PrP region required for infectivity, is the major amyloid protein in Gerstmann-Straussler-Scheinker disease A117V. J. Biol. Chem. 276: 6009-6015.
115. Tateishi, J., Brown, P., Kitamoto, T., Hoque, Z.M., Roos, R., Wollman, R., Cervenakova, L., and Gajdusek, D.C. 1995. First experimental transmission of fatal familial insomnia. Nature (London), 376: 434-435.
116. Telling, G.C., Scott, M., Foster, D., Yang, S.-L., Torchia, M., Sidle, K.C.L., Collinge, J., DeArmond, S.J., and Prusiner, S.B. 1994. Transmission of Creutzfeldt-Jakob disease from humans to transgenic mice expressing chimeric human-mouse prion protein. Proc. Natl. Acad. Sci. U.S.A. 91: 9936-9940.
117. Telling, G.C., Scott, M., Mastrianni, J., Gabizon, R., Torchia, M., Cohen, F.E., DeArmond, S.J., and Prusiner, S.B. 1995. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell, 83: 79-90.
118. Telling, G.C., Haga, T., Torchia, M., Tremblay, P., DeArmond, S.J., and Prusiner, S.B. 1996a. Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice. Genes Dev. 10: 1736-1750.
119. Telling, G.C., Parchi, P., DeArmond, S.J., Cortelli, P., Montagna, P., Gabizon, R., Mastriani, J., Lugaresi, E., Gambetti, P., and Prusiner, S.B. 1996b. Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. Science (Washington, D.C.), 274: 2079-2082.
120. Tobler, I., Gaus, S.E., DeBoer, T., Achermann, P., Fischer, M., Rulicke, T., Moser, M., Oesch, B., McBride, P.A., and Manson, J.C. 1996. Altered circadian activity rhythms and sleep in mice devoid of prion protein. Nature (London), 380: 639-642.
121. Tremblay, P., Meiner, Z., Galou, M., Heinrich, C., Petromilli, C., Lisse, T., Cayetano, J., Torchia, M., Mobley, W., Bujard, H., DeArmond, S.J., and Prusiner, S.B. 1998. Doxycycline control of prion protein transgene expression modulates prion disease in mice. Proc. Natl. Acad. Sci. U.S.A. 95: 12 580 - 12 585.
122. Turk, E., Teplow, D.B., Hood, L.E., and Prusiner, S.B. 1988. Purification and properties of the cellular and scrapie hamster prion proteins. Eur. J. Biochem. 176: 21-30.
123. Viles, J.H., Cohen, F.E., Prusiner, S.B., Goodin, D.B., Wright, P.E., and Dyson, H.J. 1999. Copper binding to the prion protein: structural implications of four identical cooperative binding sites. Proc. Natl. Acad. Sci. U.S.A. 96: 2042-2047.
124. Waggoner, D.J., Drisaldi, B., Bartnikas, T.B., Casareno, R.L., Prohaska, J.R., Gitlin, J.D., and Harris, D.A. 2000. Brain copper content and cuproenzyme activity do not vary with prion protein expression level. J. Biol. Chem. 275: 7455-7458.
125. Weissmann, C. 1991. Spongiform encephalopathies - the prion's progress. Nature (London), 349: 569-571.
126. Weissmann, C., and Aguzzi, A. 1999. Perspectives: neurobiology. PrP's double causes trouble [published erratum appears in Science (Washington, D.C.), 286(5447): 2086]. Science (Washington, D.C.), 286: 914-915.
127. Westaway, D., Goodman, P.A., Mirenda, C.A., McKinley, M.P., Carlson, G.A., and Prusiner, S.B. 1987. Distinct prion proteins in short and long scrapie incubation period mice. Cell, 51: 651-662.
128. Westaway, D., Mirenda, C.A., Foster, D., Zebarjadian, Y., Scott, M., Torchia, M., Yang, S.-L., Serban, H., DeArmond, S.J., Ebeling, C., Prusiner, S.B., and Carlson, G.A. 1991. Paradoxical shortening of scrapie incubation times by expression of prion protein transgenes derived from long incubation period mice. Neuron, 7: 59-68.
129. Westaway, D., Cooper, C., Turner, S., Da Costa, M., Carlson, G.A., and Prusiner, S.B. 1994a. Structure and polymorphism of the mouse prion protein gene. Proc. Natl. Acad. Sci. U.S.A. 91: 6418-6422.
130. Westaway, D., DeArmond, S.J., Cayetano-Canlas, J., Groth, D., Foster, D., Yang, S.-L., Torchia, M., Carlson, G.A., and Prusiner, S.B. 1994b. Degeneration of skeletal muscle, peripheral nerves, and central nervous system in transgenic mice overexpressing wild-type prion proteins. Cell, 76: 117-129.
131. Westaway, D., Zuliani, V., Cooper, C.M., Da Costa, M., Neuman, S., Jenny, A.L., Detwiler, L., and Prusiner, S.B. 1994c. Homozygosity for prion protein alleles encoding glutamine-171 renders sheep susceptible to natural scrapie. Genes Dev. 8: 959-969.
132. White, A.R., Collins, S.J., Maher, F., Jobling, M.F., Stewart, L.R., Thyer, J.M., Beyreuther, K., Masters, C.L., and Cappai, R. 1999. Prion protein-deficient neurons reveal lower glutathione reductase activity and increased susceptibility to hydrogen peroxide toxicity. Am. J. Pathol. 155: 1723-1730.
133. Whittal, R.M., Ball, H.L., Cohen, F.E., Burlingame, A.L., Prusiner, S.B., and Baldwin, M.A. 2000. Copper binding to octarepeat peptides of the prion protein monitored by mass spectrometry. Protein Sci. 9: 332-343.
134. Whittington, M.A., Sidle, K.C.L., Gowland, I., Meads, J., Hill, A.F., Palmer, M.S., Jefferys, J.G.R., and Collinge, J. 1995. Rescue of neurophysiological phenotype seen in PrP null mice by transgene encoding human prion protein. Nat. Genet. 9: 197-201.
135. Wickner, R.B. 1994. Evidence for a prion analog in S. cerevisiae: the [URE3] non-Mendelian genetic element as an altered URE2 protein. Science (Washington, D.C.), 264: 567-569.
136. Wong, B.S., Liu, T., Paisley, D., Li, R., Pan, T., Chen, S.G., Perry, G., Petersen, R.B., Smith, M.A., Melton, D.W., Gambetti, P., Brown, D.R., and Sy, M.S. 2001. Induction of ho-1 and nos in doppel-expressing mice devoid of prp: implications for doppel function. Mol. Cell. Neurosci. 17: 768-775.
137. Wong, N.K., Renouf, D.V., Lehmann, S., and Hounsell, E.F. 2000. Glycosylation of prions and its effects on protein conformation relevant to amino acid mutations. J. Mol. Graph. Model. 18: 126-134, 163-165.
138. Yehiely, F., Bamborough, P., Da Costa, M., Perry, B.J., Thinakaran, G., Cohen, F.E., Carlson, G.A., and Prusiner, S.B. 1997. Identification of candidate proteins binding to prion protein. Neurobiol. Dis. 3: 339-355.
139. Zahn, R., Liu, A., Luhrs, T., Riek, R., von Schroetter, C., Lopez Garcia, F., Billeter, M., Calzolai, L., Wider, G., and Wuthrich, K. 2000. NMR solution structure of the human prion protein. Proc. Natl. Acad. Sci. U.S.A. 97: 145-150.
140. Zhang, Y., Swietnicki, W., Zagorski, M.G., Surewicz, W.K., and Sonnichsen, F.D. 2000. Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases. J. Biol. Chem. 275: 33 650 - 33 654.