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

Author

Listed:
  • 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
    Dominican University of California)

  • Ida M. Klang

    (Buck Institute for Research on Aging, 8001 Redwood Blvd
    Karolinska Institute, Center for Biosciences at NOVUM, Hälsovägen 7)

  • Gordon J. Lithgow

    (Buck Institute for Research on Aging, 8001 Redwood Blvd)

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.

Suggested Citation

  • Silvestre Alavez & Maithili C. Vantipalli & David J. S. Zucker & Ida M. Klang & Gordon J. Lithgow, 2011. "Amyloid-binding compounds maintain protein homeostasis during ageing and extend lifespan," Nature, Nature, vol. 472(7342), pages 226-229, April.
    • Handle: RePEc:nat:nature:v:472:y:2011:i:7342:d:10.1038_nature09873
    DOI: 10.1038/nature09873
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    Cited by:

    1. Donghai Cui & Zixiang Wang & Qianli Dang & Jing Wang & Junchao Qin & Jianping Song & Xiangyu Zhai & Yachao Zhou & Ling Zhao & Gang Lu & Hongbin Liu & Gang Liu & Runping Liu & Changshun Shao & Xiyu Zha, 2023. "Spliceosome component Usp39 contributes to hepatic lipid homeostasis through the regulation of autophagy," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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