Lactylation—a New Protein Modification That Slows Alzheimer’s?
In mice, lactylation of APP reduces amyloid deposits and slows disease progression.
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In mice, lactylation of APP reduces amyloid deposits and slows disease progression.
Recent genetic and mechanistic studies on SORL1 place the endolysosomal system, in both neurons and microglia, front and center in the pathogenesis of AD.
In models of amyloidosis and tauopathy, the noble gas curbed inflammation and made microglia more phagocytic, resulting in fewer aggregates and healthier neurons.
Survey of post-translationally modified and noncoding RNA identified more than 25,000 differences between AD and control brain.
In AD brain, cells ramp up expression of herpes virus proteins. In cultured neurons, these proteins boost p-tau, which then suppresses viral proteins.
In mice, eliminating the NPC1 gene from microglia recapitulated aspects of the lysosomal storage disorder.
In lab animals, lithocholic acid replicates life-extending benefits of caloric restriction.
Dennis Selkoe offers a closing response.
In postmortem tissue, nearly half of AD patients had HCMV infections in the brain and gut. In cerebral organoids, HCMV triggered accumulation of Aβ and p-tau212.
With age, this coupling erodes, making synapses sluggish. Rekindling it lessens synaptic deficits and memory loss in old mice.
Scott Small offers a closing argument.
Dennis Selkoe replies to Scott Small.
Scott Small reacts to a recent perspective paper and the discussion it engendered.
In mice, crippling PSEN2 worsened amyloid deposition, synaptic dysfunction, and deficit in working memory.
A Tolstoy-inspired method identifies AD variants that exert similar effects, pinpointing causal AD proteins—six known, plus a new one, RET.