Abstract：
:Increased levels of brain amyloid-beta, a secreted peptide cleavage product of amyloid precursor protein (APP), is believed to be critical in the aetiology of Alzheimer's disease. Increased amyloid-beta can cause synaptic depression, reduce the number of spine protrusions (that is, sites of synaptic contacts) and block long-term synaptic potentiation (LTP), a form of synaptic plasticity; however, the receptor through which amyloid-beta produces these synaptic perturbations has remained elusive. Laurén et al. suggested that binding between oligomeric amyloid-beta (a form of amyloid-beta thought to be most active) and the cellular prion protein (PrP(C)) is necessary for synaptic perturbations. Here we show that PrP(C) is not required for amyloid-beta-induced synaptic depression, reduction in spine density, or blockade of LTP; our results indicate that amyloid-beta-mediated synaptic defects do not require PrP(c).
journal_name
Naturejournal_title
Natureauthors
Kessels HW,Nguyen LN,Nabavi S,Malinow Rdoi
10.1038/nature09217subject
Has Abstractpub_date
2010-08-12 00:00:00pages
E3-4; discussion E4-5issue
7308eissn
0028-0836issn
1476-4687pii
nature09217journal_volume
466pub_type
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