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The Ancient Drug Salicylate Directly Activates AMP-Activated Protein Kinase

The Ancient Drug Salicylate Directly Activates AMP-Activated Protein Kinase

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  • Simon A Hawley
  • Morgan D Fullerton
  • Fiona A Ross
  • Jonathan D Schertzer
  • Cyrille Chevtzoff
  • Katherine J Walker
  • Mark W Peggie
  • Darya Zibrova
  • Kevin A Green
  • Kirsty J. Mustard
  • Bruce E Kemp
  • Kei Sakamoto
  • Gregory R Steinberg
  • D Grahame Hardie (Lead / Corresponding author)

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Original languageEnglish
Pages (from-to)918-922
Number of pages5
Issue number6083
Early online date19 Apr 2012
StatePublished - 18 May 2012


Salicylate, a plant product, has been in medicinal use since ancient times. More recently, it has been replaced by synthetic derivatives such as aspirin and salsalate, both rapidly broken down to salicylate in vivo. At concentrations reached in plasma following administration of salsalate, or aspirin at high doses, salicylate activates adenosine monophosphate-activated protein kinase (AMPK), a central regulator of cell growth and metabolism. Salicylate binds at the same site as the synthetic activator, A-769662, to cause allosteric activation and inhibition of dephosphorylation of the activating phosphorylation site, Thr172. In AMPK knockout mice, effects of salicylate to increase fat utilization and lower plasma fatty acids in vivo were lost. Our results suggest that AMPK activation could explain some beneficial effects of salsalate and aspirin in humans.

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