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prnp / mice ( edinburgh strain)21 on an inbred c57bl6 background were obtained from dr .
chesebro of the rocky mountain laboratories and prnp / mice ( zurich i)20 on a mixed strain background from the european mutant mouse archive .
for binding assays , cos-7 cells were transiently transfected with cdna expression plasmids or isolated hippocampal neurons were cultured from e18 embryos .
hippocampal slices ( 400 m ) from c57bl6j or prnp/ mice were bathed in oxygenated artificial cerebrospinal fluid .
the schaffer collateral pathway was stimulated at 0.033 hz at levels that evoked less than 50% of maximal field epsps .
evoked ca1 field potentials were recorded and the slope of the epsp determined ( clampfit , molecular devices ) .
a42 or antibodies were bath applied for 2040 minutes before inducing ltp with ten 100 hz trains at five pulses delivered at 5 hz .
prnp / mice ( edinburgh strain)21 on an inbred c57bl6 background were obtained from dr .
chesebro of the rocky mountain laboratories and prnp / mice ( zurich i)20 on a mixed strain background from the european mutant mouse archive .
a42 oligomer preparations were generated from synthetic peptide4 . for binding assays , cos-7 cells were transiently transfected with cdna expression plasmids or isolated hippocampal neurons were cultured from e18 embryos .
hippocampal slices ( 400 m ) from c57bl6j or prnp/ mice were bathed in oxygenated artificial cerebrospinal fluid .
the schaffer collateral pathway was stimulated at 0.033 hz at levels that evoked less than 50% of maximal field epsps .
evoked ca1 field potentials were recorded and the slope of the epsp determined ( clampfit , molecular devices ) .
a42 or antibodies were bath applied for 2040 minutes before inducing ltp with ten 100 hz trains at five pulses delivered at 5 hz .
a pathological hallmark of alzheimer s disease ( ad ) is an accumulation of insoluble plaque containing the amyloid- peptide ( a ) of 4042 aa residues1 . 
 prefibrillar , soluble oligomers of a have been recognized to be early and key intermediates in ad - related synaptic dysfunction29 . at nanomolar concentrations , 
 soluble a-oligomers block hippocampal long - term potentiation7 , cause dendritic spine retraction from pyramidal cells5,8 and impair rodent spatial memory2 . 
 soluble a-oligomers have been prepared from chemical syntheses , from transfected cell culture supernatants , from transgenic mouse brain and from human ad brain2,4,7,9 . 
 together , these data imply a high affinity cell surface receptor for soluble a-oligomers on neurons , one that is central to the pathophysiological process in ad . here , we identify the cellular prion protein ( prpc ) as an a-oligomer receptor by expression cloning . 
 a-oligomers bind with nanomolar affinity to prpc , but the interaction does not require the infectious prpsc conformation . 
 synaptic responsiveness in hippocampal slices from young adult prp null mice is normal , but the a-oligomer blockade of long - term potentiation is absent . 
 anti - prp antibodies prevent a-oligomer binding to prpc and rescue synaptic plasticity in hippocampal slices from oligomeric . thus , prpc is a mediator of aoligomer induced synaptic dysfunction , and prpc - specific pharmaceuticals may have therapeutic potential for alzheimer s disease .