title: The prion protein as a receptor for amyloid-beta.
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).
authors: Center for Neural Circuits and Behavior, 9500 Gilman Drive 0634, University of California at San Diego, La Jolla, California 92093, USA.
authors: Helmut W
authors: HW
authors: Kessels
authors: Louis N
authors: LN
authors: Nguyen
authors: Sadegh
authors: S
authors: Nabavi
authors: Roberto
authors: R
authors: Malinow
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism / Q000473:pathology; D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D007858:Learning / Q000502:physiology; D051379:Mice; D008810:Mice, Inbred C57BL; D008822:Mice, Transgenic; D018621:PrPC Proteins / Q000172:deficiency / Q000235:genetics / Q000378:metabolism*; D015203:Reproducibility of Results; D012701:Serotonin / Q000378:metabolism; D013569:Synapses / Q000378:metabolism* / Q000473:pathology*; D009435:Synaptic Transmission
chemical_list: D016229:Amyloid beta-Peptides; D018621:PrPC Proteins; D012701:Serotonin