Spreading of Tau Protein Does Not Depend on Aggregation Propensity.

ABSTRACT: The stereotypical progression of Tau pathology during Alzheimer disease has been attributed to trans-neuronal spreading of misfolded Tau proteins, followed by prion-like templated aggregation of Tau. The nature of Tau and the cellular mechanisms of Tau spreading are still under debate. We hypothesized that Tau's propensity for aggregation would correlate with its ability to spread across synapses and propagate pathology. To study the progressive propagation of Tau proteins in brain regions relevant for Alzheimer disease, we used mice expressing near-physiological levels of full-length human Tau protein carrying pro-aggregant (TauΔK280, Tau^ΔK) or anti-aggregant (TauΔK280-PP, Tau^ΔK-PP) mutations in the entorhinal cortex (EC). To enhance Tau expression in the EC, we perf

SUBMITTER: Rodrigues S 

PROVIDER: S-EPMC10694122 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature