Lysosomal Protein TMEM106b Is Tightly Linked to TDP-43, Tau Pathology
Neurons with TMEM106B aggregates lose nuclear TDP-43 in ALS models. In tauopathy models, they accumulate no p-tau.
Neurons with TMEM106B aggregates lose nuclear TDP-43 in ALS models. In tauopathy models, they accumulate no p-tau.
The fateful pairing may happen in microglial lysosomes, where ApoE forms fibrillar aggregates.
In certain regions of the brain, microglia internalize proteins from the plasma. At least one of them—ApoA-I—supports microglial phagocytosis.
Combining isotopic labeling and transcriptomics, scientists found that mature plaques in mice wreaked more havoc on surrounding synapses than immature ones.
Glia need exactly the right amount of tau for lipid droplets to bud from the endoplasmic reticulum. The droplets soak up toxic lipids spilled by stressed neurons.
In a head-to-head comparison with aducanumab, gantenerumab, and donanemab, lecanemab had the highest affinity, especially for smaller aggregates.
In two hospital systems, people who received heparin were diagnosed with AD a year later than people who never took the anticoagulant.
The NIH removed Masliah from his post after an investigation found two publications with falsified data. At least 130 more papers with 500 co-authors face allegations.
Most scientists agree that for amyloidosis to ignite, both ApoE and microglia need to be present. A new study presents a mechanistic link between the two. Scientists report that ApoE and Aβ both aggregate within microglial lysosomes, and that these intracellular liaisons ultimately seed amyloid plaques.
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