Lack of cellular prion protein causes Amyloid β accumulation, increased extracellular vesicle abundance, and changes to exosome biogenesis proteins.

ABSTRACT: Alzheimer's disease (AD) progression is closely linked to the propagation of pathological Amyloid β (Aβ), a process increasingly understood to involve extracellular vesicles (EVs), namely exosomes. The specifics of Aβ packaging into exosomes remain elusive, although evidence suggests an ESCRT (Endosomal Sorting Complex Required for Transport)-independent origin to be responsible in spreading of AD pathogenesis. Intriguingly, PrP^C, known to influence exosome abundance and bind oligomeric Aβ (oAβ), can be released in exosomes via both ESCRT-dependent and ESCRT-independent pathways, raising questions about its role in oAβ trafficking. Thus, we quantified Aβ levels within EVs, cell medium, and intracellularly, alongside exosome biogenesis-related proteins, following deletion or over

SUBMITTER: Johansson L 

PROVIDER: S-EPMC11842432 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature