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Item Type: | Article |
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Title: | The green tea polyphenol (-)-epigallocatechin gallate prevents the aggregation of tau protein into toxic oligomers at substoichiometric ratios |
Creators Name: | Wobst, H.J., Sharma, A., Diamond, M.I., Wanker, E.E. and Bieschke, J. |
Abstract: | The accumulation of amyloid-beta (Abeta) and tau aggregates is a pathological hallmark of Alzheimer's disease. Both polypeptides form fibrillar deposits, but several lines of evidence indicate that Abeta and tau form toxic oligomeric aggregation intermediates. Depleting such structures could thus be a powerful therapeutic strategy. We generated a fragment of tau (His-K18DeltaK280) that forms stable, toxic, oligomeric tau aggregates in vitro. We show that (-)-epigallocatechin gallate (EGCG), a green tea polyphenol that was previously found to reduce Abeta aggregation, inhibits the aggregation of tau K18DeltaK280 into toxic oligomers at ten- to hundred-fold substoichiometric concentrations, thereby rescuing toxicity in neuronal model cells. |
Keywords: | Tau Protein, Tau Oligomers, Aggregation Inhibitors, EGCG, Alzheimer's Disease, Polyphenol, Animals, Rats |
Source: | FEBS Letters |
ISSN: | 0014-5793 |
Publisher: | Wiley-Blackwell |
Volume: | 589 |
Number: | 1 |
Page Range: | 77-83 |
Date: | 2 January 2015 |
Official Publication: | https://doi.org/10.1016/j.febslet.2014.11.026 |
PubMed: | View item in PubMed |
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