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000151661 037__ $$aDZNE-2020-01240
000151661 041__ $$aEnglish
000151661 082__ $$a610
000151661 1001_ $$aFriker, Lea L.$$b0
000151661 245__ $$aβ-Amyloid Clustering around ASC Fibrils Boosts Its Toxicity in Microglia
000151661 260__ $$a[New York, NY]$$bElsevier$$c2020
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000151661 520__ $$aAlzheimer’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.
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000151661 650_2 $$2MeSH$$aAmyloid beta-Peptides: metabolism
000151661 650_2 $$2MeSH$$aAmyloid beta-Peptides: toxicity
000151661 650_2 $$2MeSH$$aAmyloid beta-Peptides: ultrastructure
000151661 650_2 $$2MeSH$$aAnimals
000151661 650_2 $$2MeSH$$aCARD Signaling Adaptor Proteins: metabolism
000151661 650_2 $$2MeSH$$aCaspase 1: metabolism
000151661 650_2 $$2MeSH$$aCells, Cultured
000151661 650_2 $$2MeSH$$aHumans
000151661 650_2 $$2MeSH$$aInflammasomes: metabolism
000151661 650_2 $$2MeSH$$aInterleukin-1beta: metabolism
000151661 650_2 $$2MeSH$$aMice, Inbred C57BL
000151661 650_2 $$2MeSH$$aMicroglia: drug effects
000151661 650_2 $$2MeSH$$aMicroglia: metabolism
000151661 650_2 $$2MeSH$$aMicroglia: pathology
000151661 650_2 $$2MeSH$$aModels, Biological
000151661 650_2 $$2MeSH$$aNLR Family, Pyrin Domain-Containing 3 Protein: metabolism
000151661 650_2 $$2MeSH$$aProteolysis: drug effects
000151661 650_2 $$2MeSH$$aPyroptosis: drug effects
000151661 650_2 $$2MeSH$$aSignal Transduction: drug effects
000151661 650_2 $$2MeSH$$aToll-Like Receptor 2: metabolism
000151661 650_2 $$2MeSH$$aToll-Like Receptor 4: metabolism
000151661 7001_ $$0P:(DE-HGF)0$$aScheiblich, Hannah$$b1
000151661 7001_ $$aHochheiser, Inga V.$$b2
000151661 7001_ $$aBrinkschulte, Rebecca$$b3
000151661 7001_ $$aRiedel, Dietmar$$b4
000151661 7001_ $$0P:(DE-HGF)0$$aLatz, Eicke$$b5
000151661 7001_ $$aGeyer, Matthias$$b6
000151661 7001_ $$0P:(DE-2719)2000008$$aHeneka, Michael T.$$b7$$eLast author$$udzne
000151661 773__ $$0PERI:(DE-600)2649101-1$$a10.1016/j.celrep.2020.02.025$$gVol. 30, no. 11, p. 3743 - 3754.e6$$n11$$p3743 - 3754.e6$$tCell reports$$v30$$x2211-1247$$y2020
000151661 8564_ $$uhttps://www.sciencedirect.com/science/article/pii/S2211124720301868
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