Synaptic and memory dysfunction induced by tau oligomers is rescued by up-regulation of the nitric oxide cascade.

ABSTRACT:

Background

Soluble aggregates of oligomeric forms of tau protein (oTau) have been associated with impairment of synaptic plasticity and memory in Alzheimer's disease. However, the molecular mechanisms underlying the synaptic and memory dysfunction induced by elevation of oTau are still unknown.

Methods

This work used a combination of biochemical, electrophysiological and behavioral techniques. Biochemical methods included analysis of phosphorylation of the cAMP-responsive element binding (CREB) protein, a transcriptional factor involved in memory, histone acetylation, and expression immediate early genes c-Fos and Arc. Electrophysiological methods included assessment of long-term potentiation (LTP), a type of synaptic plasticity thought to underlie memory formation. Behavior

SUBMITTER: Acquarone E 

PROVIDER: S-EPMC6598340 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature