Cellular prion protein and calcium ions trigger the neurotoxicity of α-synuclein aggregates.

ABSTRACT:

Background

The aggregation of α-Synuclein (αS) into amyloid fibrils and their deposition in intraneuronal Lewy bodies are hallmark features of Parkinson's disease (PD) and other synucleinopathies. Among the molecular players implicated in αS toxicity, the cellular prion protein (PrP^C) has emerged as a potential modulator of αS-neuron interactions.

Results

Using confocal microscopy, colocalization analysis and both siRNA-induced PrP^C silencing and antibody-based blockade, we investigated the contribution of PrP^C to αS-induced neurotoxicity in human iPSC-derived dopaminergic neurons, primary rat cortical neurons and human SH-SY5Y neuroblastoma cells. We show that PrP^C facilitated the early recruitment of αS prefibrillar type B* oligo

SUBMITTER: Bigi A 

PROVIDER: S-EPMC12687500 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature