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2007 Grant - Johnson
Tau Oligomerization and Aggregation Analysis: A Novel Approach
Gail V. W. Johnson, Ph.D.
University of Rochester
Rochester, New York
2007 Investigator-Initiated Research Grant
The tau protein is found in normal, healthy neurons in the brain. But in Alzheimer's disease, tau proteins undergo abnormal chemical alterations that cause them to aggregate, or assemble themselves, into abnormal structures. The final stage of this aggregation process is the neurofibrillary tangle, one of the key pathological features of Alzheimer's disease.
Increasing evidence suggests that small aggregates of the tau protein have properties that are toxic to nerve cells, but that the longer aggregates forming neurofibrillary tangles are not toxic.
Gail V. W. Johnson, Ph.D., and colleagues plan to study the aggregation of tau and the effect of these aggregates on the cell's survival. They will use a laboratory procedure in which tau appears fluorescent when it forms into small aggregates but then decreases in fluorescence as tau forms into large neurofibrillary tangles. Using this technique, the researchers can follow the time course of tau aggregation in living cells and correlate that time course with measures of cell viability and survival.
They also plan to study specific drugs that cause tau aggregation and determine how those drugs affect cell survival. These studies may help characterize the mechanisms of tau aggregation and the mechanisms by which these aggregates lead to the death of neurons.