Laurén et al. reply.

Replying to: H. W. Kessels, L. N. Nguyen, S. Nabavi & R. Malinow 466, 10.1038/nature09217 (2010)Amyloid-? oligomers are correlated with Alzheimer’s disease progression and suppress synaptic plasticity. Through unbiased expression cloning, we identified cellular prion protein (PrPC) as an amyloid-? oligomer binding protein. PrPC was necessary for acute amyloid-?(1?42) (A?42) oligomer suppression of synaptic plasticity; thus, it becomes critical to explore the importance of PrPC in a range of Alzheimer’s-disease-related deficits. Transgenic Alzheimer’s disease model mice show deficits of spatial learning and memory, so the most direct assessment of PrPC will monitor memory in transgenic Alzheimer’s disease model mice deficient for PrPC. In this paradigm, amyloid-? species are produced endogenously and the brain is exposed chronically over months. Recently, we have found that deletion of PrPC from APPswe/PSen1?E9 transgenic mice restores spatial learning and memory without altering amyloid-?. Furthermore, the early death, synapse loss and serotonin axonal degeneration of transgenic Alzheimer’s disease mice require PrPC (ref. 6). Kessels et al. examine PrPC in alternative paradigms. [ABSTRACT FROM AUTHOR]