Amyloid-b1-42 Disrupts Synaptic Plasticity by Altering XXXX Recycling at the Synapse.

@entity2227 @entity308 @entity1399 @entity535 @entity16 @entity3072 @entity179 @entity143 @entity367 @entity195 @entity528 @entity13069
UNASSIGNED: @entity195 ( @entity195 ) is the most prevalent form of @entity179 characterized by neuritic plaques containing amyloid-b peptide (Ab) and @entity3072 . Evidence has been reported that Ab1-42 plays an essential pathogenic role in decreased spine density, impairment of synaptic plasticity, and @entity528 with disruption of memory-related synapse function, all associated with @entity195 . Experimentally, Ab1-42 oligomers perturb hippocampal long-term potentiation (LTP), an electrophysiological correlate of learning and memory. Ab was also reported to perturb synaptic @entity2227 ( @entity367 )-recycling by inhibiting excitatory- @entity535 -transporters. Elevated level of extracellular @entity367 leads to activation of perisynaptic receptors, including @entity13069 subunit containing NMDARs. These receptors were shown to induce impaired LTP and enhanced long-term @entity308 and proapoptotic pathways, all central features of @entity195 . In the present study, we investigated the role of @entity367 -recycling on Ab1-42-induced LTP deficit in the @entity1399 . We found that Ab-induced @entity16 , which was mimicked by the @entity367 -reuptake inhibitor TBOA, could be rescued by blocking the @entity13069 subunit of @entity143 receptors. Furthermore, decreasing the level of extracellular @entity367 using a @entity367 scavenger also restores TBOA or Ab induces @entity16 . Overall, these results suggest that reducing ambient @entity367 in the brain can be protective against Ab-induced synaptic disruption.
