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- W3011845531 abstract "Alzheimer's disease is the world's most common neurodegenerative disorder. It is associated with neuroinflammation involving activation of microglia by β-amyloid (Aβ) deposits. Based on previous studies showing apoptosis-associated speck-like protein containing a CARD (ASC) binding and cross-seeding extracellular Aβ, we investigate the propagation of ASC between primary microglia and the effects of ASC-Aβ composites on microglial inflammasomes and function. Indeed, ASC released by a pyroptotic cell can be functionally built into the neighboring microglia NOD-like receptor protein (NLRP3) inflammasome. Compared with protein-only application, exposure to ASC-Aβ composites amplifies the proinflammatory response, resulting in pyroptotic cell death, setting free functional ASC and inducing a feedforward stimulating vicious cycle. Clustering around ASC fibrils also compromises clearance of Aβ by microglia. Together, these data enable a closer look at the turning point from acute to chronic Aβ-related neuroinflammation through formation of ASC-Aβ composites." @default.
- W3011845531 created "2020-03-23" @default.
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- W3011845531 date "2020-03-01" @default.
- W3011845531 modified "2023-10-16" @default.
- W3011845531 title "β-Amyloid Clustering around ASC Fibrils Boosts Its Toxicity in Microglia" @default.
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- W3011845531 doi "https://doi.org/10.1016/j.celrep.2020.02.025" @default.
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