Publication Date:
2005-06-04
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉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 -- AG004342/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2005 Jun 3;308(5727):1435-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, Hamilton, MT 59840, USA. bchesebro@niaid.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15933194" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Brain/metabolism/pathology/ultrastructure
;
Glycosylphosphatidylinositols/genetics/*metabolism
;
Mice
;
Mice, Inbred C57BL
;
Mice, Transgenic
;
Plaque, Amyloid/metabolism/pathology
;
PrPSc Proteins/chemistry/metabolism
;
Prion Diseases/etiology/metabolism/pathology
;
Prions/biosynthesis/chemistry/genetics/*metabolism
;
Scrapie/*etiology/metabolism/pathology
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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