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Disease relevance of Scrapie


Psychiatry related information on Scrapie

  • The disease-specific amyloid fibrils comprise primarily a single protein, amyloid beta, in Alzheimer's disease, and the prion protein in scrapie [6].
  • New-variant Creutzfeldt-Jakob disease and scrapie are typically initiated by extracerebral exposure to the causative agent, and exhibit early prion replication in lymphoid organs [7].
  • These data suggest that both the noradrenergic and dopaminergic system are sensitive to the action of scrapie agent 87V and that changes in the catecholamine levels in the brains of scrapie-infected mice may contribute to some of the clinical symptoms of the diseases, such as ataxia and apraxia [8].

High impact information on Scrapie

  • Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins [6].
  • These results indicate that various PrP isoforms engage in a complex in vivo, whose distortion by PrP-Fc(2) affects prion propagation and scrapie pathogenesis [9].
  • Classical genetic analysis has identified Sinc/Prni as the major gene controlling mouse scrapie incubation time [10].
  • Similarly, Tg mice inoculated with Ha prions exhibited neuropathologic changes characteristic of hamsters with scrapie, while Mo prions produced changes similar to those in non-Tg mice [11].
  • Tg 81 brains also showed HaPrP amyloid plaques characteristic of Ha scrapie and contained integral of 10(9) ID50 units of Ha prions based on Ha bioassays [12].

Chemical compound and disease context of Scrapie

  • It was labeled with N-succinimidyl 3-(4-hydroxy-5-[125I]-iodophenyl) propionate, which did not alter the titer of the scrapie prion [13].
  • Amphotericin B treatment dissociates in vivo replication of the scrapie agent from PrP accumulation [14].
  • Chemical modification of the scrapie agent by diethyl pyrocarbonate reduced the titer 1000-fold [15].
  • Autoclaving does not decontaminate formol-fixed scrapie tissues [16].
  • This is a proteinase K-resistant glycoprotein of 27-30 kd that is derived from an abnormal isoform of a neuronal glycoprotein of 33-35 kd designated PrPSc and is a molecular marker of amyloid fibrils isolated from animals with scrapie and humans with related disorders [17].

Biological context of Scrapie

  • Mice devoid of PrP develop normally but are resistant to scrapie; introduction of a PrP transgene restores susceptibility to the disease [18].
  • A clone encoding PrP 27-30, the major protein in purified preparations of scrapie agent, was selected from a scrapie-infected hamster brain cDNA library by oligonucleotide probes corresponding to the N terminus of the protein [19].
  • On the other hand, because there are many different strains of scrapie agent with distinct phenotypes which can be propagated in animals homozygous for the PrPc gene, it has been suggested that a nucleic acid must be a component of the agent [20].
  • To study the effect of cell type-restricted hamster PrP expression on susceptibility to the hamster scrapie agent, we generated transgenic mice using a 1 kb hamster cDNA clone containing the 0.76 kb HPrP open reading frame under control of the neuron-specific enolase promoter [21].
  • Species specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrier [4].

Anatomical context of Scrapie


Gene context of Scrapie

  • After inoculation with hamster scrapie, these mice accumulated infectivity and PrPSc to high levels, developed severe disease after 227 +/- 5 days and died 7 +/- 4 days later [27].
  • However, TNFR1(-/-), TNFR2(-/-), and some TNFalpha(-/-) mice developed scrapie similarly to wild-type mice [28].
  • The results indicate that the accumulation of the scrapie prion protein in the CA1-3 region strongly inhibits NPY binding at the Y2-Rs, which, however, is only marginally due to reduced Y2-R mRNA expression [29].
  • In scrapie, a prion disease of animals, amyloid plaques have been shown to be composed of prion proteins (PrP), which form filaments of relatively uniform diameter [30].
  • In scrapie infected mice, cortical PV+ neurons were severely reduced while CB+ and CR+ neurons were well preserved [31].
  • PrP(Sc) was clearly distinct from BSE prions passaged in sheep and from atypical scrapie prions [32].

Analytical, diagnostic and therapeutic context of Scrapie


  1. The cellular prion protein binds copper in vivo. Brown, D.R., Qin, K., Herms, J.W., Madlung, A., Manson, J., Strome, R., Fraser, P.E., Kruck, T., von Bohlen, A., Schulz-Schaeffer, W., Giese, A., Westaway, D., Kretzschmar, H. Nature (1997) [Pubmed]
  2. Preclinical deposition of pathological prion protein PrPSc in muscles of hamsters orally exposed to scrapie. Thomzig, A., Schulz-Schaeffer, W., Kratzel, C., Mai, J., Beekes, M. J. Clin. Invest. (2004) [Pubmed]
  3. Relation between Carp (multiple-sclerosis associated) agent and multiple sclerosis. Adams, D.H. Lancet (1976) [Pubmed]
  4. Species specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrier. Kocisko, D.A., Priola, S.A., Raymond, G.J., Chesebro, B., Lansbury, P.T., Caughey, B. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  5. Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody. Enari, M., Flechsig, E., Weissmann, C. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  6. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Harper, J.D., Lansbury, P.T. Annu. Rev. Biochem. (1997) [Pubmed]
  7. Complement facilitates early prion pathogenesis. Klein, M.A., Kaeser, P.S., Schwarz, P., Weyd, H., Xenarios, I., Zinkernagel, R.M., Carroll, M.C., Verbeek, J.S., Botto, M., Walport, M.J., Molina, H., Kalinke, U., Acha-Orbea, H., Aguzzi, A. Nat. Med. (2001) [Pubmed]
  8. Extensive degeneration of catecholaminergic neurons to scrapie agent 87V in the brains of IM mice. Yun, S.W., Choi, E.K., Ju, W.K., Ahn, M.S., Carp, R.I., Wisniewski, H.M., Kim, Y.S. Mol. Chem. Neuropathol. (1998) [Pubmed]
  9. Soluble dimeric prion protein binds PrP(Sc) in vivo and antagonizes prion disease. Meier, P., Genoud, N., Prinz, M., Maissen, M., Rülicke, T., Zurbriggen, A., Raeber, A.J., Aguzzi, A. Cell (2003) [Pubmed]
  10. Mice with gene targetted prion protein alterations show that Prnp, Sinc and Prni are congruent. Moore, R.C., Hope, J., McBride, P.A., McConnell, I., Selfridge, J., Melton, D.W., Manson, J.C. Nat. Genet. (1998) [Pubmed]
  11. Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Prusiner, S.B., Scott, M., Foster, D., Pan, K.M., Groth, D., Mirenda, C., Torchia, M., Yang, S.L., Serban, D., Carlson, G.A. Cell (1990) [Pubmed]
  12. Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques. Scott, M., Foster, D., Mirenda, C., Serban, D., Coufal, F., Wälchli, M., Torchia, M., Groth, D., Carlson, G., DeArmond, S.J. Cell (1989) [Pubmed]
  13. A protease-resistant protein is a structural component of the scrapie prion. McKinley, M.P., Bolton, D.C., Prusiner, S.B. Cell (1983) [Pubmed]
  14. Amphotericin B treatment dissociates in vivo replication of the scrapie agent from PrP accumulation. Xi, Y.G., Ingrosso, L., Ladogana, A., Masullo, C., Pocchiari, M. Nature (1992) [Pubmed]
  15. Reversible chemical modification of the scrapie agent. McKinley, M.P., Masiarz, F.R., Prusiner, S.B. Science (1981) [Pubmed]
  16. Autoclaving does not decontaminate formol-fixed scrapie tissues. Taylor, D.M., McConnell, I. Lancet (1988) [Pubmed]
  17. 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. Tagliavini, F., Prelli, F., Ghiso, J., Bugiani, O., Serban, D., Prusiner, S.B., Farlow, M.R., Ghetti, B., Frangione, B. EMBO J. (1991) [Pubmed]
  18. Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions. Shmerling, D., Hegyi, I., Fischer, M., Blättler, T., Brandner, S., Götz, J., Rülicke, T., Flechsig, E., Cozzio, A., von Mering, C., Hangartner, C., Aguzzi, A., Weissmann, C. Cell (1998) [Pubmed]
  19. A cellular gene encodes scrapie PrP 27-30 protein. Oesch, B., Westaway, D., Wälchli, M., McKinley, M.P., Kent, S.B., Aebersold, R., Barry, R.A., Tempst, P., Teplow, D.B., Hood, L.E. Cell (1985) [Pubmed]
  20. A 'unified theory' of prion propagation. Weissmann, C. Nature (1991) [Pubmed]
  21. Neuron-specific expression of a hamster prion protein minigene in transgenic mice induces susceptibility to hamster scrapie agent. Race, R.E., Priola, S.A., Bessen, R.A., Ernst, D., Dockter, J., Rall, G.F., Mucke, L., Chesebro, B., Oldstone, M.B. Neuron (1995) [Pubmed]
  22. Temporary depletion of complement component C3 or genetic deficiency of C1q significantly delays onset of scrapie. Mabbott, N.A., Bruce, M.E., Botto, M., Walport, M.J., Pepys, M.B. Nat. Med. (2001) [Pubmed]
  23. Scrapie replication in lymphoid tissues depends on prion protein-expressing follicular dendritic cells. Brown, K.L., Stewart, K., Ritchie, D.L., Mabbott, N.A., Williams, A., Fraser, H., Morrison, W.I., Bruce, M.E. Nat. Med. (1999) [Pubmed]
  24. Sympathetic innervation of lymphoreticular organs is rate limiting for prion neuroinvasion. Glatzel, M., Heppner, F.L., Albers, K.M., Aguzzi, A. Neuron (2001) [Pubmed]
  25. Conversion of truncated and elongated prion proteins into the scrapie isoform in cultured cells. Rogers, M., Yehiely, F., Scott, M., Prusiner, S.B. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  26. Separation and properties of cellular and scrapie prion proteins. Meyer, R.K., McKinley, M.P., Bowman, K.A., Braunfeld, M.B., Barry, R.A., Prusiner, S.B. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  27. Astrocyte-specific expression of hamster prion protein (PrP) renders PrP knockout mice susceptible to hamster scrapie. Raeber, A.J., Race, R.E., Brandner, S., Priola, S.A., Sailer, A., Bessen, R.A., Mucke, L., Manson, J., Aguzzi, A., Oldstone, M.B., Weissmann, C., Chesebro, B. EMBO J. (1997) [Pubmed]
  28. Lymph nodal prion replication and neuroinvasion in mice devoid of follicular dendritic cells. Prinz, M., Montrasio, F., Klein, M.A., Schwarz, P., Priller, J., Odermatt, B., Pfeffer, K., Aguzzi, A. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  29. Marked decrease of neuropeptide Y Y2 receptor binding sites in the hippocampus in murine prion disease. Diez, M., Koistinaho, J., Dearmond, S.J., Groth, D., Prusiner, S.B., Hökfelt, T. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  30. Amyloid plaques in Creutzfeldt-Jakob disease stain with prion protein antibodies. Kitamoto, T., Tateishi, J., Tashima, T., Takeshita, I., Barry, R.A., DeArmond, S.J., Prusiner, S.B. Ann. Neurol. (1986) [Pubmed]
  31. Severe, early and selective loss of a subpopulation of GABAergic inhibitory neurons in experimental transmissible spongiform encephalopathies. Guentchev, M., Groschup, M.H., Kordek, R., Liberski, P.P., Budka, H. Brain Pathol. (1998) [Pubmed]
  32. Classic scrapie in sheep with the ARR/ARR prion genotype in Germany and France. Groschup, M.H., Lacroux, C., Buschmann, A., Lühken, G., Mathey, J., Eiden, M., Lugan, S., Hoffmann, C., Espinosa, J.C., Baron, T., Torres, J.M., Erhardt, G., Andreoletti, O. Emerging Infect. Dis. (2007) [Pubmed]
  33. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Jarrett, J.T., Lansbury, P.T. Cell (1993) [Pubmed]
  34. Molecular cloning and complete sequence of prion protein cDNA from mouse brain infected with the scrapie agent. Locht, C., Chesebro, B., Race, R., Keith, J.M. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  35. Molecular mass, biochemical composition, and physicochemical behavior of the infectious form of the scrapie precursor protein monomer. Safar, J., Wang, W., Padgett, M.P., Ceroni, M., Piccardo, P., Zopf, D., Gajdusek, D.C., Gibbs, C.J. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  36. Neuropathological diagnostic criteria for Creutzfeldt-Jakob disease (CJD) and other human spongiform encephalopathies (prion diseases). Budka, H., Aguzzi, A., Brown, P., Brucher, J.M., Bugiani, O., Gullotta, F., Haltia, M., Hauw, J.J., Ironside, J.W., Jellinger, K. Brain Pathol. (1995) [Pubmed]
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