New research in humans published today reveals that the so-called FKBP52 protein may prevent the Tau protein from turning pathogenic. This may prove significant for the development of new Alzheimer's drugs and for detecting the disease before the onset of clinical symptoms.
A study published online today in the Journal of Alzheimer's Disease (1), for the first time demonstrates that the FKBP52 protein, discovered by Prof. Etienne BAULIEU twenty years ago, may prevent hyperphosphorylation of Tau protein, which has been shown to characterise a number of cerebral neurodegenerative diseases, including Alzheimer's Disease (AD).
This work has been carried out by Professor Etienne Baulieu and his research team at Inserm (National Institute for medical research in France) with the support of philanthropists who help the Institut Baulieu, based in France.
Limited research exists on Tau and its role in the development of AD, but it is known that many neurodegenerative diseases are characterised by the deposition of pathological hyperphosphorylated forms of Tau protein, into structures known as 'Tau tangles'. The mechanism of Tau toxicity is unclear and there are currently no drug treatments targeting Tau, nor any biomarkers that predict the risk of a future "Tauopathy". Professor Baulieu decided to focus on Tau abnormalities and was the first to discover in 2010, an interaction between Tau, and the FKBP52 protein (2).
The new research takes his previous research to the next level. It demonstrates a direct correlation between high levels of hyperphosphorylated Tau protein and reduced levels of FKBP52, in brain cells from patients who have died following Alzheimer's Disease, compared with normal brain cells. This suggests that FKBP52 could control the aberrant production of pathogenic Tau. When FKBP52 is reduced in the nerve cells of AD patients, pathogenic Tau is free to accumulate and contribute to the degeneration of brain cell
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