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- W2025796656 abstract "Tau proteins normally interact with microtubules in the nervous system. During the course of neurodegenerative diseases such as Alzheimer's disease (AD) and tauopathies, these proteins dissociate from the microtubule and begin to aggregate. The resultant tau filaments are thought by many to be toxic although the nature of this toxicity is, as yet, unknown. The tau molecule aggregates by association with its repeat region; this area of the molecule that normally mediates tau's association with microtubules. We have discovered that the carboxy and amino regions of the molecule constitute control elements in tau aggregation with the carboxy tail region being inhibitory and the amino region being facilitative of the filament assembly process. For the past several years, we have been studying mechanisms by which the cell modulates these regions of the molecule in disease. Using molecular biological, biochemical and immunological procedures, we have discovered that these regions can be nitrated on tyrosines or truncated by enzymes such as caspases. The result of changes such as these are modeled in vitro to assess their affect on tau filament formation and assayed in situ in AD and tauopathies using appropriately targeted monoclonal antibodies. Additionally, we have used different tau isoforms and modified polymers to assess their affect on axonal transport in isolated axoplasm from the squid giant axon. Tau filaments and certain non-canonical isoforms of tau that contain only the amino region of the molecule inhibit anterograde but not retrograde transport through a signal transduction cascade involving specific phosphatases and GSK3β. Taken together, our results indicate that the amino terminal region of tau may be a primary site of toxicity in neurodegenerative disease. Supported by Grants AG14453, AG09466, AG021184, and AG021661." @default.
- W2025796656 created "2016-06-24" @default.
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- W2025796656 date "2008-07-01" @default.
- W2025796656 modified "2023-09-27" @default.
- W2025796656 title "PL-02-01: Tau modifications, aggregation and toxicity" @default.
- W2025796656 doi "https://doi.org/10.1016/j.jalz.2008.05.265" @default.
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