Human tau seeds trigger disease-specific shapes in mouse brains, new study finds
Tau is a protein that occurs naturally in the brain. It is essential for proper neuron development and for how neurons communicate with each other. The same protein, however, when misshapen or misfolded, can act as a driver of neurodegenerative diseases. Abnormal buildup of tau is a hallmark of Alzheimer's disease, and scientists have also found an association between misfolded tau and more than…
Human tau proteins, crucial for neuron function, can become misshapen and contribute to neurodegenerative diseases. Misfolded tau is a key factor in Alzheimer's disease and more than 20 other neurodegenerative conditions. A recent study explored how these misfolded tau proteins, dubbed "tau seeds," spread and altered the shape of normal tau proteins in mouse brains.
By injecting human tau seeds from Alzheimer's disease (AD) or corticobasal degeneration (CBD) into healthy mice, researchers observed the normal mouse tau adopting the exact 3D structure of the diseased seeds. Despite vanishing within a week, the human seeds triggered a chain reaction, causing mouse tau to form fibers with the same disease-specific folds for nine to 12 months.
These findings support the prion-like seeding hypothesis, where misfolded proteins force normal proteins to misfold into the same structure. The research revealed that AD seeds produced tau aggregates only in neurons, while CBD seeds caused aggregates in both neurons and glial cells. This study provides evidence that distinct tau folds function as prion strains, maintaining their unique structure as they disseminate through the brain, potentially aiding in the development of new diagnostic tools and treatments.
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