Anchorless prion protein results in infectious amyloid disease without clinical scrapie |
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| Authors: | 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 Oldstone Michael |
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| Institution: | Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, Hamilton, MT 59840, USA. bchesebro@niaid.nih.gov |
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| Abstract: | In prion and Alzheimer's diseases, the roles played by amyloid versus nonamyloid 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. |
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