Overexpression of Shadoo protein in transgenic mice does not impact the pathogenesis of scrapie

Neuroscience Letters

Volumn 496, Issue 1, 2011, Pages 1-4

  Wang, Haiying ^a,b,c   Wan, Jiayu ^b   Wang, Wei ^a,b   Wang, Dongxu ^a,b   Li, Sha ^a,b   Liao, Peng ^a,b   Hao, Zhuo ^a,b   Wu, Songbo ^a,b   Xu, Jing ^b   Li, Nan ^b   OuYang, Hongsheng ^a   Gao, Hongwei ^b  

^a JILIN UNIVERSITY   (China)

^b BEIJING INSTITUTE OF MICROBIOLOGY AND EPIDEMIOLOGY   (China)

^c UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE   (United States)

Author keywords

Incubation times; Mouse model; Overepression; Scrapie pathogenesis; Shadoo

Indexed keywords

GLYCOPROTEIN; PROTEIN SHADOO; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; BRAIN SPONGIOSIS; CELL LINE; CONTROLLED STUDY; DISEASE COURSE; GENE OVEREXPRESSION; MOUSE; NONHUMAN; NOTE; PATHOGENESIS; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN BLOOD LEVEL; PROTEIN EXPRESSION; SCRAPIE; TRANSGENIC MOUSE; WILD TYPE;

ANIMALS; BRAIN; DISEASE MODELS, ANIMAL; FEMALE; GLIAL FIBRILLARY ACIDIC PROTEIN; MALE; MICE; MICE, INBRED C57BL; MICE, TRANSGENIC; NERVE TISSUE PROTEINS; PHENOTYPE; PRPSC PROTEINS; SCRAPIE;

EID: 79955621862     PISSN: 03043940     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neulet.2011.03.073     Document Type: Note

References (24)

1. Behrens A., Genoud N., Naumann H., Rulicke T., Janett F., Heppner F.L., Ledermann B., Aguzzi A. Absence of the prion protein homologue Doppel causes male sterility. J. EMBO 2002, 21:3652-3658.
2. Bruce M.E., Dickinson A.G. Genetic control of amyloid plaque production and incubation period in scrapie-infected mice. J. Neuropathol. Exp. Neurol. 1985, 44:285-294.
3. Büeler H., Fischer M., Lang Y., Bluethmann H., Lipp H.P., DeArmond S.J., Prusiner S.B., Aquet M., Wessmann C. Normal development and behaviour of mice lacking the neuronal cell-surface prp protein. Nature 1992, 356:577-582.
4. Büeler H., Aguzzi A., sailer A., Greiner R.A., Autenried P., Aquet M., Wessimann C. Mice devoid of prp are resistant of scrapie. Cell 1993, 73:1339-1347.
5. Caughey B., Lansbury P.T. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 2003, 26:267-298.
6. Ersdal C., Goodsir C.M., Simmons M.M., McGovern G., Jeffrey M. Abnormal prion protein is associated with changes of plasma membranes and endocytosis in bovine spongiform encephalopathy (BSE)-affected cattle brains. Neuropathol. Appl. Neurobiol. 2009, 35:259-271.
7. Gabizon R., McKinley M.P., Prusiner S.B. Purified prion proteins and scrapie infectivity copartition into liposomes. Proc. Natl. Acad. Sci. USA. 1987, 4017-4021.
8. Ghetti B., Piccardo P., Frangione B., Bugiani O., Giaccone G., Young K., Prelli F., Farlow M.R., Dlouhy S.R., Taqliavini F. Prion protein amyloidosis. Brain Pathol. 1996, 6:127-145.
9. Giaccone G., Verga L., Bugiani O., Frangione B., Serban D., S.B Prusiner., M.R Farlow., Ghetti B., Taqliavini F. Prion protein preamyloid and amyloid deposits in Gerstmann-Sträussler-Scheinker disease. Proc. Natl. Acad. Sci. U.S.A. 1992, 9349-9353.
10. González L., Martin S., Begara-McGorum I., Hunter N., Houston F., Simmons M., Jeffrey M. Effects of agent strain and host genotype on PrP accumulation in the brain of sheep naturally and experimentally affected with scrapie. J. Comp. Pathol. 2002, 126:17-29.
11. Gossner A.G., Bennet N., Hunter N., Hopkins J. Differential expression of Prnp and Sprn in scrapie infected sheep also reveals Prnp genotype specific differences. Biochem. Biophys. Res. Commun. 2009, 378:862-866.
12. Jeffrey M., Goodsir C.M., Bruce M.E., McBride P.A., Scott J.R., Halliday W.G. Infection specific prion protein (PrP) accumulates on neuronal plasmalemma in scrapie infected mice. Neurosci. Lett. 1992, 147:106-109.
13. Jeffrey M., Goodsir C.M., Bruce M.E., McBride P.A., Fraser J.R. In vivo toxicity of prion protein in murine scrapie: ultrastructural and immunogold studies. Neuropathol. Appl. Neurobiol. 1997, 23:93-101.
14. Lloyd S.E., Grizenkova J., Pota H., Collinge J. Shadoo (Sprn) and prion disease incubation time in mice. Mamm. Genome 2009, 20:367-374.
15. Miyazawa K., Manuelidis L. Agent-specific Shadoo responses in transmissible encephalopathies. J. Neuroimmune Pharmacol. 2010, 5:155-163.
16. Moore R.C., Lee I.Y., Silverman G.L., Westaway D., Harrison P.M., Strome R., Heinrich C., Karunaratne A., Pasternak S.H., Chishti M.A., Liang Y., Mastrangelo P., Wang K., Smitv A.F., Katamine S., Carlson G.A., Cohen F.E., Prusiner S.B., Melton D.W., Tremblay P., Hood L.E. Ataxia in prion protein(PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel. J. Mol. Biol. 1999, 292:797-817.
17. Moore R.C., Mastrangelo P., Bouzamondo E., Heinrich C., Legname G., Prusiner S.B., Hood L., Westaway D., DeArmond S.J., Tremblay P. Doppel-induced cerebellar degeneration in transgenic mice. Proc. Natl. Acad. Sci. U.S.A. 2001, 15288-15293.
18. Parchi P., Chen S.G., Brown P., Zou W., Capellari S., Budka H., Hainfellner J., Reyes P.F., Golden G.T., Hauw J.J., Gajdusek D.C., Gambetti P. Different patterns of truncated prion protein fragments correlate with distinct phenotypes in P102L Gerstmann-Straussler-Scheinker disease. Proc. Natl. Acad. Sci. U.S.A. 1998, 8322-8327.
19. Piccardo P., Seiler C., Dlouhy S.R., Young K., Farlow M.R., Prelli F., Frangione B., Buqiani O., Taqliavini F., Ghetti B. Proteinase-K-resistant prion protein isoforms in Gerstmann-Sträussler-Scheinker disease (Indiana kindred). J. Neuropathol. Exp. Neurol. 1996, 55:1157-1163.
20. Piccardo P., Dlouhy S.R., Lievens P.M., Young K., Bird T.D., Nochlin D., Dickson D.W., Vinters H.V., Zimmerman T.R., Mackenzie I.R., Kish S.J., Ang L.C., Carli C.De., Pocchiari M., Brown P., Gibbs C.J., Gajdusek D.C., Bugiani O., Ironside J., Taqliavini F., Ghetti B. Phenotypic variability of Gerstmann-Sträussler-Scheinker disease is associated with prion protein heterogeneity. J. Neuropathol. Exp. Neurol. 1998, 57:979-988.
21. Premzl M., Sangiorgio L., Strumbo B., Marshall Graves J.A., Simonic T., Gready J.E. Shadoo, a new protein highly conserved from fish to mammals and with similarity to prion protein. Gene 2003, 314:89-102.
22. Prusiner S.B. Prions. Proc. Natl. Acad. Sci. U.S.A. 1998, 13363-13383.
23. Silveira J.R., Raymond G.J., Hughson A.G., Race R.E., Sim V.L., Hayes S.F., Caughey B. The most infectious prion protein particles. Nature 2005, 437:257-261.
24. Watts J.C, Drisaldi B., Ng V., Yang J., Strome B., Horne P., Sy.M.S., Yoony L., Young R., Mastrangelo P., Bergeron C., Fraser P.E., Carlson G.A., Mount H.T., Schmitt-ULms G., Westaway D. The CNS glycoprotein Shadoo has PrP (C)-like protective properties and displays reduced levels in prion infections. J. EMBO 2007, 26:4038-4050.