Neurological illness in transgenic mice expressing a prion protein with an insertional mutation

Neuron

Volumn 21, Issue 6, 1998, Pages 1339-1351

  Chiesa, Roberto ^a   Piccardo, Pedro ^b   Ghetti, Bernardino ^b   Harris, David A ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b INDIANA UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN; PROTEINASE K;

ANIMAL CELL; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; ATAXIA; BRAIN ATROPHY; BRAIN DISEASE; DEMENTIA; GENE INSERTION; MOUSE; NEUROPATHOLOGY; NONHUMAN; PHENOTYPE; PRION DISEASE; PRIORITY JOURNAL; PROTEIN EXPRESSION;

EID: 0032427904     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(00)80653-4     Document Type: Article

References (54)

1. Bessen, R.A., and Marsh, R.F. (1992). Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent. J. Virol. 66, 2096-2101.
2. Bolton, D.C., Seligman, S.J., Bablanian, G., Windsor, D., Scala, L.J., Kim, K.S., Chen, C.M., Kascsak, R.J., and Bendheim, P.E. (1991). Molecular location of a species-specific epitope on the hamster scrapie agent protein. J. Virol. 65, 3667-3675.
3. Borchelt, D.R., Davis, J., Fischer, M., Lee, M.K., Slunt, H.H., Ratovitsky, T., Regard, J., Copeland, N.G., Jenkins, N.A., Sisodia, S.S., and Price, D.L. (1996). A vector for expressing foreign genes in the brains and hearts of transgenic mice. Genet. Anal. Biomol. Eng. 13, 159-163.
4. Büeler, H., Fischer, M., Lang, Y., Fluethmann, H., Lipp, H.-P., DeArmond, S.J., Prusiner, S.B., Aguet, M., and Weissmann, C. (1992). Normal development and behavior of mice lacking the neuronal cell-surface PrP protein. Nature 356, 577-582.
5. Capellari, S., Vital, C., Parchi, P., Petersen, R.B., Ferrer, X., Jarnier, J., Pegoraro, E., Gambetti, P., and Julien, J. (1997). Familial prion disease with a novel 144-bp insertion in the prion protein gene in a Basque family. Neurology 49, 133-141.
6. 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.
7. Chen, S.G., Teplow, D.B., Parchi, P., Teller, J.K., Gambetti, P., and Autilio-Gambetti, L. (1995). Truncated forms of the human prion protein in normal brain and in prion diseases. J. Biol. Chem. 270, 19173-19180.
8. Chen, S.G., Parchi, P., Brown, P., Capellari, S., Zou, W.Q., Cochran, E.J., Vnencakjones, C.L., Julien, J., Vital, C., Mikol, J., et al. (1997). Allelic origin of the abnormal prion protein isoform in familial prion diseases. Nat. Med. 3, 1009-1015.
9. Chiesa, R., Piccardo, P., Ghetti, B., and Harris, D.A. (1998). A transgenic mouse model of a familial prion disease with an insertional mutation. Neurobiol. Aging 19, S300.
10. Cohen, F.E., Pan, K.M., Huang, Z., Baldwin, M., Fletterick, R.J., and Prusiner, S.B. (1994). Structural clues to prion replication. Science 264, 530-531.
11. Collinge, J., Brown, J., Hardy, J., Mullan, M., Rossor, M.N., Baker, H., Crow, T.J., Lofthouse, R., Poulter, M., Ridley, R., et al. (1992). Inherited prion disease with 144 base pair gene insertion: clinical and pathological features. Brain 115, 687-710.
12. Collinge, J., Sidle, K.C.L., Meads, J., Ironside, J., and Hill, A.F. (1996). Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature 383, 685-690.
13. Daude, N., Lehmann, S., and Harris, D.A. (1997). Identification of intermediate steps in the conversion of a mutant prion protein to a scrapie-like form in cultured cells. J. Biol. Chem. 272, 11604-11612.
14. Donne, D.G., 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. USA 94, 13452-13457.
15. Duchen, L.W., Poulter, M., and Harding, A.E. (1993). Dementia associated with a 216 base pair insertion in the prion protein gene: clinical and neuropathological features. Brain 116, 555-567.
16. Englund, P.T. (1993). The structure and biosynthesis of glycosyl phosphatidylinositol protein anchors. Annu. Rev. Biochem. 62, 121-138.
17. Fischer, M., Rülicke, 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.
18. Gabizon, R., Telling, G., Meiner, Z., Halimi, M., Kahana, I., and Prusiner, S.B. (1996). Insoluble wild-type and protease-resistant mutant prion protein in brains of patients with inherited prion disease. Nat. Med. 2, 59-64.
19. Harris, D.A., Huber, M.T., van Dijken, P., Shyng, S.-L., Chait, B.T., and Wang, R. (1993). Processing of a cellular prion protein: identification of N- and C-terminal cleavage sites. Biochemistry 32, 1009-1016.
20. Harrison, P.M., Bamborough, P., Daggett, V., Prusiner, S.B., and Cohen, F.E. (1997). The prion folding problem. Curr. Opin. Struct. Biol. 7, 53-59.
21. Hegde, R.S., Mastrianni, J.A., Scott, M.R., Defea, K.A., Tremblay, 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 279, 827-834.
22. Hsiao, K.K., Scott, M., Foster, D., Groth, D.F., DeArmond, S.J., and Prusiner, S.B. (1990). Spontaneous neurodegeneration in transgenic mice with mutant prion protein. Science 250, 1587-1590.
23. Hsiao, K.K., Groth, D., Scott, M., Yang, S.-L., Serban, H., Rapp, D., Foster, D., Torchia, M., DeArmond, S.J., and Prusiner, S.B. (1994). Serial transmission in rodents of neurodegeneration from transgenic mice expressing mutant prion protein. Proc. Natl. Acad. Sci. USA 91, 9126-9130.
24. Kitamoto, T., Shin, R.-W., Doh-ura, K., Tomokane, N., Miyazono, M., Muramoto, T., and Tateishi, J. (1992). Abnormal isoform of prion proteins accumulates in the synaptic structures of the central nervous system in patients with Creutzfeldt-Jakob disease. Am. J. Path. 140, 1285-1294.
25. Krasemann, S., Zerr, I., Weber, T., Poser, S., Kretzschmar, H., Hunsmann, G., and Bodemer, W. (1995). Prion disease associated with a novel nine octapeptide repeat insertion in the PRNP gene. Mol. Brain Res. 34, 173-176.
26. Lehmann, S., and Harris, D.A. (1995). A mutant prion protein displays an aberrant membrane association when expressed in cultured cells. J. Biol. Chem. 270, 24589-24597.
27. Lehmann, S., and Harris, D.A. (1996a). Mutant and infectious prion proteins display common biochemical properties in cultured cells. J. Biol. Chem. 271, 1633-1637.
28. Lehmann, S., and Harris, D.A. (1996b). Two mutant prion proteins expressed in cultured cells acquire biochemical properties reminiscent of the scrapie isoform. Proc. Natl. Acad. Sci. USA 93, 5610-5614.
29. Lehmann, S., and Harris, D.A. (1997). Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells. J. Biol. Chem. 272, 21479-21487.
30. Lehmann, S., Daude, N., and Harris, D.A. (1997). A wild-type prion protein does not acquire properties of the scrapie isoform when coexpressed with a mutant prion protein in cultured cells. Mol. Brain Res. 52, 139-145.
31. Manson, J., West, J.D., Thomson, V., McBride, P., Kaufman, M.H., and Hope, J. (1992). The prion protein gene: a role in mouse embryogenesis? Development 115, 117-122.
32. Muramoto, T., Dearmond, S.J., Scott, M., Telling, G.C., Cohen, F.E., and Prusiner, S.B. (1997). Heritable disorder resembling neuronal storage disease in mice expressing prion protein with deletion of an α-helix. Nat. Med. 3, 750-755.
33. Oesch, B., Westaway, D., Walchli, M., McKinley, M.P., Kent, S.B., Aebersold, R., Barry, R.A., Tempst, P., Teplow, D.B., Hood, L.E., et al. (1985). A cellular gene encodes scrapie PrP 27-30 protein. Cell 40, 735-746.
34. Owen, F., Poulter, M., Collinge, J., Leach, M., Lofthouse, R., Crow, T.J., and Harding, A.E. (1992). A dementing illness associated with a novel insertion in the prion protein gene. Mol. Brain Res. 13, 155-157.
35. Parchi, P., and Gambetti, P. (1995). Human prion diseases. Curr. Opin. Neurol. 8, 286-293.
36. Parchi, P., Castellani, R., Capellari, S., Ghetti, B., Young, K., Chen, S.G., Farlow, M., Dickson, D.W., Sima, A.A.F., Trojanowski, J.Q., et al. (1996). Molecular basis of phenotypic variability in sporadic Creutzfeldt-Jakob disease. Ann. Neurol. 39, 767-778.
37. Parchi, P., Gambetti, P., Piccardo, P., and Ghetti, B. (1998). Human prion diseases. In Progress in Pathology 4, N. Kirkham and N.R. Lemoine, eds. (Edinburgh: Churchill Livingstone), pp. 39-77.
38. Petersen, R.B., Parchi, P., Richardson, S.L., Urig, C.B., and Gambetti, P. (1996). Effect of the D178N mutation and the codon 129 polymorphism on the metabolism of the prion protein. J. Biol. Chem. 271, 12661-12668.
39. Piccardo, P., Langeveld, J.P.M., Hill, A.F., Dlouhy, S.R., Young, K., Giaccone, G., Rossi, G., Bugiani, O., Meloen, R.H., Collinge, J., et al. (1998). An antibody raised against a conserved sequence of the prion protein recognizes pathological isoforms in human and animal prion diseases, including Creutzfeldt-Jakob disease and bovine spongiform encephalopathy. Am. J. Pathol. 152, 1415-1420.
40. Priola, S.A., and Chesebro, B. (1998). Abnormal properties of prion protein with insertional mutations in different cell types. J. Biol. Chem. 273, 11980-11985.
41. Prusiner, S.B., and Hsiao, K.K. (1994). Human prion diseases. Ann. Neurol. 35, 385-395.
42. Prusiner, S.B., Scott, M.R., DeArmond, S.J., and Cohen, F.E. (1998). Prion protein biology. Cell 93, 337-348.
43. Riek, R., Hornemann, S., Wider, G., Glockshuber, R., and Wüthrich, K. (1997). NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett. 413, 282-288.
44. Rosenberry, T.L. (1991). A chemical modification that makes glycoinositol phospholipids resistant to phospholipase C cleavage: fatty acid acylation of inositol. Cell Biol. Int. Rep. 15, 1133-1150.
45. Sakaguchi, S., Katamine, S., Nishida, N., Moriuchi, R., Shigematsu, K., Sugimoto, T., Nakatani, A., Kataoka, Y., Houtani, T., Shirabe, S., et al. (1996). Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene. Nature 380, 528-531.
46. Scott, M., Groth, D., Foster, D., Torchia, M., Yang, S.L., DeArmond, S.J., and Prusiner, S.B. (1993). Propagation of prions with artificial properties in transgenic mice expressing chimeric PrP genes. Cell 73, 979-988.
47. Shmerling, D., Hegyi, I., Fischer, M., Blättler, T., Brandner, S., Götz, J., Rülicke, T., Flechsig, E., Cozzio, A., von Mering, et al. (1998). Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions. Cell 93, 203-214.
48. Singh, N., Zanusso, G., Chen, S.G., Fujioka, H., Richardson, S., Gambetti, P., and Petersen, R.B. (1997). Prion protein aggregation reverted by low temperature in transfected cells carrying a prion protein gene mutation. J. Biol. Chem. 272, 28461-28470.
49. Stahl, N., Borchelt, D.R., Hsiao, K., and Prusiner, S.B. (1987). Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 51, 229-249.
50. Stahl, N., Borchelt, D.R., and Prusiner, S.B. (1990). Differential release of cellular and scrapie prion proteins from cellular membranes by phosphatidylinositol-specific phospholipase C. Biochemistry 29, 5405-5412.
51. Telling, G.C., Haga, T., Torchia, M., Tremblay, P., DeArmond, S.J., and Prusiner, S.B. (1996). Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice. Genes Dev. 10, 1736-1750.
52. Westaway, D., DeArmond, S.J., Cayetano-Canlas, J., Groth, D., Foster, D., Yang, S.-L., Torchia, M., Carlson, G.A., and Prusiner, S.B. (1994). Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins. Cell 76, 117-129.
53. Wozniak, D.F., Brosnan-Watters, G., Nardi, A., McEwen, M., Corso, T.D., Olney, J.W., and Fix, A.S. (1996). MK-801 neurotoxicity in male mice: histologic effects and chronic impairment in spatial learning. Brain Res. 707, 165-179.
54. Young, K., Piccardo, P., Dlouhy, S., Bugiani, O., Tagliavini, F., and Ghetti, B. (1999). The human genetic prion diseases. In Prions: Molecular and Cellular Biology, D.A. Harris, ed. (Wymondham, U.K.: Horizon Scientific Press), 139-175.