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Synthetic amyloid-{beta} oligomers impair long-term memory independently of cellular prion protein.

著者 Balducci C , Beeg M , Stravalaci M , Bastone A , Sclip A , Biasini E , Tapella L , Colombo L , Manzoni C , Borsello T , Chiesa R , Gobbi M , Salmona M , Forloni G
Proc Natl Acad Sci U S A.2010 Feb 2 ; 107(5):2295-300.
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Department of Neuroscience and Department of Biochemistry and Molecular Pharmacology, Mario Negri Institute for Pharmacological Research, Milan 20156, Italy.

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Inability to form new memories is an early clinical sign of Alzheimer's disease (AD). There is ample evidence that the amyloid-beta (Abeta) peptide plays a key role in the pathogenesis of this disorder. Soluble, bio-derived oligomers of Abeta are proposed as the key mediators of synaptic and cognitive dysfunction, but more tractable models of Abeta-mediated cognitive impairment are needed. Here we report that, in mice, acute intracerebroventricular injections of synthetic Abeta(1-42) oligomers impaired consolidation of the long-term recognition memory, whereas mature Abeta(1-42) fibrils and freshly dissolved peptide did not. The deficit induced by oligomers was reversible and was prevented by an anti-Abeta antibody. It has been suggested that the cellular prion protein (PrP(C)) mediates the impairment of synaptic plasticity induced by Abeta. We confirmed that Abeta(1-42) oligomers interact with PrP(C), with nanomolar affinity. However, PrP-expressing and PrP knock-out mice were equally susceptible to this impairment. These data suggest that Abeta(1-42) oligomers are responsible for cognitive impairment in AD and that PrP(C) is not required.
PMID: 20133875 [PubMed - in process]
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