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The prion protein as a receptor for amyloid-β

Nature volume 466, pages E3–E4 (2010)Cite this article

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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.

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

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Authors and Affiliations

  1. Center for Neural Circuits and Behavior, 9500 Gilman Drive 0634, University of California at San Diego, La Jolla, 92093, California, USA

    Helmut W. Kessels, Louis N. Nguyen, Sadegh Nabavi & Roberto Malinow

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  1. Helmut W. Kessels
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  2. Louis N. Nguyen
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  3. Sadegh Nabavi
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  4. Roberto Malinow
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Contributions

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). https://doi.org/10.1038/nature09217

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