1. Anchorless prion protein results in infectious amyloid disease without clinical scrapie
- Author
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Chesebro, Bruce, Trifilo, Matthew, Race, Richard, Meade-White, Kimberly, Teng, Chao, LaCasse, Rachel, Raymond, Lynne, Favara, Cynthia, Baron, Gerald, Priola, Suzette, Caughey, Byron, Masliah, Eliezer, and Oldstone, Michael
- Subjects
Prion diseases -- Research -- Analysis ,Science and technology ,Analysis ,Research - Abstract
In prion and Alzheimer's diseases, the roles played by amyloid versus nonamyIoid deposits in brain damage remain unresolved. In scrapie-infected transgenic mice expressing prion protein (PrP) lacking the glycosylphosphatidylinositol (GPI) membrane anchor, abnormal protease-resistant PrPres was deposited as amyloid plaques, rather than the usual nonamyloid form of PrPres. Although PrPres amyloid plaques induced brain damage reminiscent of Alzheimer's disease, clinical manifestations were minimal. In contrast, combined expression of anchorless and wild-type PrP produced accelerated clinical scrapie. Thus, the PrP GPI anchor may play a role in the pathogenesis of prion diseases., Transmissible spongiform encephalopathies (TSEs) or prion diseases (1) include CreutzfeldtJakob disease (CJD) in humans, bovine spongiform encephalopathy or 'mad cow dissease' in cattle, scrapie in sheep, and chronic wasting disease [...]
- Published
- 2005