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2014 New Investigator Research Grant (NIRG)

A pathogenic role for tau acetylation in Alzheimer's disease

Todd Cohen, Ph.D.
The University of North Carolina at Chapel Hill
Chapel Hill, NC - United States

Tau protein plays a major role in Alzheimer’s disease. It normally functions to help maintain the structure of nerve cells and transport nutrients throughout the cell. In Alzheimer’s disease, however, tau becomes abnormally modified, leading it to form neurofibrillary tangles, one of the characteristic features of the disease.

Scientists have known for many years that tau becomes abnormally modified by the addition of chemical phosphate groups; the process is called phosphorylation and has been extensively studied. More recently, it has been reported that tau can also be modified by the addition of an acetyl group in a process known as acetylation. The abnormal acetylation of tau protein may contribute to some of the brain changes associated with Alzheimer’s disease.

Todd Cohen, Ph.D., and colleagues are studying the acetylation of tau and have observed that it can initiate the formation of tau neurofibrillary tangles. Dr. Cohen and colleagues have proposed more extensive studies of tau acetylation and its possible role in the formation of neurofibrillary tangles in Alzheimer’s disease. The researchers plan to study this process in samples of brain tissue from people who had Alzheimer’s disease. They will determine if the parts of the brain containing acetylated tau correspond to the locations of neurofibrillary tangles. These studies will help to determine if acetylation of tau is an important event in the development of Alzheimer’s disease, possibly paving the way for future studies exploring ways to prevent tau acetylation as a potential novel treatment for Alzheimer’s disease.

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