Age-dependent Progression from Clearance to Vulnerability in the Early Response of Periventricular Microglia to α-synuclein Toxic Species

Cytoplasmic alpha-synuclein (αSyn) aggregates are a typical feature of Parkinson’s disease (PD). Extracellular insoluble αSyn can induce pathology in healthy neurons suggesting that PD neurodegeneration may spread through cell-to-cell transfer of αSyn proteopathic seeds. Early pro-homeostatic reacti...

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Detalles Bibliográficos
Autores: Sirerol Piquer, Mª Salomé, Pérez Villalba, Ana, Duart Abadía, Pere, Belenguer, Germán, Gómez Pinedo, Ulises, Blasco Chamarro, Laura, Carrillo Barberà, Pau, Pérez Cañamás, Azucena, Navarro Garrido, Victoria, Dehay, Benjamin, Vitorica Ferrández, Francisco Javier, Fariñas, Isabel
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2025
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/172097
Acceso en línea:https://hdl.handle.net/11441/172097
https://doi.org/10.1186/s13024-025-00816-1
Access Level:acceso abierto
Palabra clave:Aging
Alpha-synuclein
CSF
Lewy bodies
Microglia
Parkinson’s disease
PFFs
Descripción
Sumario:Cytoplasmic alpha-synuclein (αSyn) aggregates are a typical feature of Parkinson’s disease (PD). Extracellular insoluble αSyn can induce pathology in healthy neurons suggesting that PD neurodegeneration may spread through cell-to-cell transfer of αSyn proteopathic seeds. Early pro-homeostatic reaction of microglia to toxic forms of αSyn remains elusive, which is especially relevant considering the recently uncovered microglial molecular diversity. Here, we show that periventricular microglia of the subependymal neurogenic niche monitor the cerebrospinal fluid and can rapidly phagocytize and degrade different aggregated forms of αSyn delivered into the lateral ventricle. However, this clearing ability worsens with age, leading to an increase in microglia with aggregates in aged treated mice, an accumulation also observed in human PD samples. We also show that exposure of aged microglia to aggregated αSyn isolated from human PD samples results in the phosphorylation of the endogenous protein and the generation of αSyn seeds that can transmit the pathology to healthy neurons. Our data indicate that while microglial phagocytosis rapidly clears toxic αSyn, aged microglia can contribute to synucleinopathy spreading.