Soluble and Insoluble Lysates from the Human A53T Mutant α-Synuclein Transgenic Mouse Model Induces α-Synucleinopathy Independent of Injection Site.

ABSTRACT: Pathological aggregation of α-synuclein (αS) is implicated in the pathogenesis of Parkinson's disease (PD) and other α-synucleinopathies. The current view is that neuron-to-neuron spreading of αS pathology contributes to the progression of α-synucleinopathy. We used an A53T mutant human αS transgenic mouse model (TgA53T) to examine whether the site of pathogenic αS inoculation affects the pattern of neuropathology and whether soluble and insoluble fractions derived from crude pathogenic tissue lysates exhibit differential capacities to initiate αS pathology. To test whether the inoculation site impacts the ultimate spatial/temporal patterns of αS pathology, αS preformed fibrils (PFFs), or brain homogenates from TgA53T mice with α-synucleinopathy, were injected into the cortex

SUBMITTER: Barnes J 

PROVIDER: S-EPMC12249840 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature