New details about AD aggregates

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Scientists have provided new details about how proteins involved in the origin and development of Alzheimer's Disease (AD) form harmful aggregates.

AD, the most common type of dementia, is characterized by progressive cognitive deterioration and declining daily activities. One of AD's pathological hallmarks is the abnormal aggregation of a protein called tau within nerve cells. Scientists have long suspected that this process contributes to the progressive damage or death of neurons but, until now, they have had difficulty testing this hypothesis in cultured cells because tau proteins do not aggregate easily under normal conditions.

To address this problem, Jeff Kuret and colleagues have developed drug-like chemicals that cross cell membranes and drive efficient tau aggregation over a period of days. They noticed that when tau proteins within cells were treated with this chemical, they separated from other proteins - called microtubules - to which they naturally attach and then started aggregating.

The scientists then showed that cells in which tau proteins aggregated could not grow and function properly. These results suggest that tau aggregation is toxic to cells and could directly contribute to the progressive damage or death of neurons in AD. The results also show that by further understanding the toxic effects of tau aggregation, scientists may be able to devise treatments to prevent or slow down AD in the future.

Article: "Tau Aggregation and Toxicity in a Cell Culture Model of Tauopathy" by Bhaswati Bandyopadhyay, Guibin Li, Haishan Yin, and Jeff Kuret