Journal
SCIENCE
Volume 336, Issue 6083, Pages 918-922Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1215327
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Funding
- Wellcome Trust [080982]
- Medical Research Council
- AstraZeneca
- Boehringer-Ingelheim
- GlaxoSmithKline
- Merck Serono
- Pfizer
- Canadian Institutes of Health Research (CIHR)
- Canadian Diabetes Association
- National Health and Medical Research Council of Australia
- Australian Research Council
- Victorian Government
- Medical Research Council [MC_U127088492] Funding Source: researchfish
- MRC [MC_U127088492] Funding Source: UKRI
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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 More recently, it has been replaced by synthetic derivatives such as aspirin and salsalate, both of which are rapidly broken down to salicylate in vivo. At concentrations reached in plasma after administration of salsalate or of 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, threonine-172. In AMPK knockout mice, effects of salicylate to increase fat utilization and to 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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