Short-chain polyphosphates induce tau fibrillation and neurotoxicity in human iPSC-derived retinal neurons.

ABSTRACT: The onset of Alzheimer's Disease and Frontotemporal Dementia is closely associated with the aggregation of tau, a multifunctional protein essential for neuronal stability and function. Given the role of tau aggregation in neurodegeneration, understanding the mechanisms behind its fibril formation is crucial for developing therapeutic interventions to halt or reverse disease progression. However, the structural complexity and diverse aggregation pathways of tau present significant challenges, requiring comprehensive experimental studies. In this research, we demonstrate that short-chain polyphosphates, specifically sodium tripolyphosphate (NaTPP), effectively induce tau fibril formation in vitro using the microtubule-binding domain fragment (K18). NaTPP-induced fibrils display unique struct

SUBMITTER: Barolo L 

PROVIDER: S-EPMC12064648 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature