Amyloid-binding compounds maintain protein homeostasis during ageing and extend lifespan

Silvestre Alavez (), Maithili C. Vantipalli, David J. S. Zucker, Ida M. Klang and Gordon J. Lithgow ()
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Silvestre Alavez: Buck Institute for Research on Aging, 8001 Redwood Blvd
Maithili C. Vantipalli: Buck Institute for Research on Aging, 8001 Redwood Blvd
David J. S. Zucker: Buck Institute for Research on Aging, 8001 Redwood Blvd
Ida M. Klang: Buck Institute for Research on Aging, 8001 Redwood Blvd
Gordon J. Lithgow: Buck Institute for Research on Aging, 8001 Redwood Blvd

Nature, 2011, vol. 472, issue 7342, 226-229

Abstract: Healthy proteins for a longer life The amyloid-binding histological dye thioflavin T (ThT) is known to slow protein aggregation in vitro. Experiments in Caenorhabditis elegans, commonly used as a model system for the study of ageing, now show that ThT also extends lifespan and slows ageing in the nematode. It inhibits the pathology caused by worm-specific toxic proteins and human β-amyloid expression. These beneficial effects depend on heat shock factor 1 (HSF-1), transcription factor SKN-1, molecular chaperones, autophagy and proteosomal functions. This work shows that the ageing rate in worms can be modulated by pharmacological maintenance of protein homeostasis.

Date: 2011
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DOI: 10.1038/nature09873

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