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How inflammation interacts with other disease pathways and how protein aggregation increases during disease are not clear. We used single-molecule imaging approaches and membrane permeabilization assays to determine the effect of chronic exposure to tumour necrosis factor, a master proinflammatory cytokine, on protein aggregation in human-induced pluripotent stem cell-derived neurons harbouring monogenic Alzheimer\u2019s disease mutations. We report that exposure of Alzheimer\u2019s disease neurons, but not control neurons, to tumour necrosis factor induces substantial production of extracellular protein aggregates. Aggregates from Alzheimer\u2019s disease neurons are composed of amyloid-\u03b2 and \u03b1-synuclein and induce significant permeabilization of lipid membranes in an assay of pathogenicity. These findings provide support for a causal relationship between two crucial processes in Alzheimer\u2019s disease pathogenesis and suggest that targeting inflammation, particularly tumour necrosis factor, may have beneficial downstream effects on ameliorating aberrant protein aggregation and accumulation.<\/jats:p>","DOI":"10.1093\/braincomms\/fcaa146","type":"journal-article","created":{"date-parts":[[2020,9,15]],"date-time":"2020-09-15T18:38:40Z","timestamp":1600195120000},"source":"Crossref","is-referenced-by-count":28,"title":["Tumour necrosis factor induces increased production of extracellular amyloid-\u03b2- and \u03b1-synuclein-containing aggregates by human Alzheimer\u2019s disease neurons"],"prefix":"10.1093","volume":"2","author":[{"given":"Daniel R","family":"Whiten","sequence":"first","affiliation":[{"name":"Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philip 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