Fig. 2

Ten nanomolar of soluble recombinant Aη-α and Aη-β lower LTP. a Diagram explaining the production of soluble HIS-tagged recAη-α and recAη-β samples used in c and d (see the “Methods” section for details of Ni-NTA purification and sample quantification). b Commassie stain of 1 μg of Aη peptides. Synthetic Aη peptides or recombinant CHO cell-expressed glycosylated purified Aη peptides were separated in SDS-PAGE and stained with GelCode Blue. c, d LTP was analyzed ex vivo at CA3-CA1 synapse in hippocampal slices of RjOrl:SWISS mice. Summary graphs of c fEPSP slope (% baseline) pre- and post-LTP induction (time 0) and d fEPSP magnitude 45–60 min after LTP induction in control (aCSF only) or in presence of 10 nM recAη–α or recAη–β throughout the recording (n= slices, N= mice), *p< 0.05. Detailed statistics are shown in Supplementary Table S2