The prion protein as a receptor for amyloid-β


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.

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Figure 1: PrP C is not required for amyloid-β-induced synaptic deficits.


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Author information

Experimental work was conducted by H.W.K., L.N.N. and S.N.; designed by H.W.K., L.N.N., S.N. and R.M. The manuscript was written by R.M., H.W.K. and L.N.N.

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Kessels, H., Nguyen, L., Nabavi, S. et al. The prion protein as a receptor for amyloid-β. Nature 466, E3–E4 (2010).

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