How Vesicles Shuttle Tau Filaments Throughout the Brain in Alzheimer's Disease
Post by Lila Metko
The takeaway
Many cell types, including neurons, release compartments called extracellular vesicles (EVs) for signaling and transportation. The cell’s transportation of tau, a protein that misfolds and propagates in Alzheimer’s disease, is carried out through these EVs. This research reveals that impairments in the function of lysosomes, organelles involved in breaking down cellular waste, may be involved in the association of tau with EVs and shows that tau filaments in EVs are short and tethered to their membranes.
What's the science?
Tau is a protein that maintains the structural integrity of neurons in healthy individuals but becomes hyperphosphorylated, misfolded and aggregated in the brains of people with Alzheimer’s disease. Tau has a greater ability to seed new misfolded proteins when associated with EVs. It is unknown which types of tau associate with EVs, which EVs contain tau, and how tau associates with EVs. This November in Nature Neuroscience, Fowler and colleagues investigate how EVs shuttle tau throughout the brain.
How did they do it?
The authors analyzed frontal and temporal lobe tissue that had been obtained from Alzheimer’s disease patients post-mortem. They separated the tissue using density gradient centrifugation, a type of analysis that separates molecules by density. This allows for the different subtypes of EVs to be separated into different fractions. The fractions were then analyzed by liquid chromatography-tandem mass spectrometry and immunoblotting to determine the protein content of the EV types. Additionally, they confirmed the ability of the EVs to seed further tau aggregation using cell culture and a transgenic mouse line, expressing human tau. Cryo-electron microscopy and Cryo-electron tomography were used to analyze the structure of the tau filaments found in the EVs.
What did they find?
The authors found that only fractions 4-6, fractions with medium to high density, contained EVs with tau filaments and that these fractions also had the highest amount of lysosomal proteins. Further analysis showed that there were two types of tau filaments within the EVs, one with a symmetrical organization of its subcomponents and another with a non-symmetrical organization that was shorter than those found in neurofibrillary tangles (aggregated tau protein deposits seen in Alzheimer’s disease). Shorter tau filaments have a greater ability to seed tau assembly in animal models. The authors also found that tau filaments within EVs were either tethered to the EV membrane or tethered to a tau filament that was connected to the membrane. Additionally, these filaments were all tethered at their ends. This gives researchers insight into the tethering process of tau filaments to EVs and could potentially inform therapeutic interventions.
What's the impact?
This research provides further insight into how tau filaments are transported out of the cell through EVs and propagate through the brain in Alzheimer’s disease. These findings can help us to develop therapeutics that target tau propagation.