The prion protein as a receptor for amyloid-β

Helmut W. Kessels (), Louis N. Nguyen (), Sadegh Nabavi () and Roberto Malinow ()
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Helmut W. Kessels: Center for Neural Circuits and Behavior, 9500 Gilman Drive 0634, University of California at San Diego
Louis N. Nguyen: Center for Neural Circuits and Behavior, 9500 Gilman Drive 0634, University of California at San Diego
Sadegh Nabavi: Center for Neural Circuits and Behavior, 9500 Gilman Drive 0634, University of California at San Diego
Roberto Malinow: Center for Neural Circuits and Behavior, 9500 Gilman Drive 0634, University of California at San Diego

Nature, 2010, vol. 466, issue 7308, E3-E4

Abstract: Abstract Arising from: J. Laurén et al. Nature 457, 1128–1132 (2009)10.1038/nature07761 ; Laurén et al. reply Increased levels of brain amyloid-β, a secreted peptide cleavage product of amyloid precursor protein (APP), is believed to be critical in the aetiology of Alzheimer’s disease1. Increased amyloid-β can cause synaptic depression2,3, reduce the number of spine protrusions (that is, sites of synaptic contacts)4,5 and block long-term synaptic potentiation (LTP)6,7, a form of synaptic plasticity; however, the receptor through which amyloid-β produces these synaptic perturbations has remained elusive. Laurén et al.8 suggested that binding between oligomeric amyloid-β (a form of amyloid-β thought to be most active5,6,9,10,11) and the cellular prion protein (PrPC)8 is necessary for synaptic perturbations. Here we show that PrPC is not required for amyloid-β-induced synaptic depression, reduction in spine density, or blockade of LTP; our results indicate that amyloid-β-mediated synaptic defects do not require PrPc.

Date: 2010
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DOI: 10.1038/nature09217

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