Tau oligomers impair memory and synaptic plasticity through the cellular prion protein.

ABSTRACT: Deposition of abnormally phosphorylated tau aggregates is a central event leading to neuronal dysfunction and death in Alzheimer's disease (AD) and other tauopathies. Among tau aggregates, oligomers (TauOs) are considered the most toxic. AD brains show significant increase in TauOs compared to healthy controls, their concentration correlating with the severity of cognitive deficits and disease progression. In vitro and in vivo neuronal TauO exposure leads to synaptic and cognitive dysfunction, but their mechanisms of action are unclear. Evidence suggests that the cellular prion protein (PrP^C) may act as a mediator of TauO neurotoxicity, as previously proposed for β-amyloid and α-synuclein oligomers. To investigate whether PrP^C mediates TauO detrimental activities, we

SUBMITTER: Balducci C 

PROVIDER: S-EPMC11773831 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature