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This version published online on September 4, 2003
Endocrinology, doi:10.1210/en.2003-0982
A more recent version of this article appeared on December 1, 2003
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Submitted on July 31, 2003
Accepted on August 25, 2003

The AMP-activated protein kinase cascade: the key sensor of cellular energy status

D. Grahame Hardie1*

1 Division of Molecular Physiology, University of Dundee, Wellcome Trust Biocentre, Dundee, DD1 5EH, Scotland, UK

* To whom correspondence should be addressed. E-mail: d.g.hardie{at}dundee.ac.uk.

All cells must maintain a high ratio of cellular ATP:ADP to survive. Because of the adenylate kinase reaction (2ADP {leftrightarrow} ATP + AMP), AMP rises whenever the ATP:ADP falls, and a high cellular ratio of AMP:ATP is a signal that the energy status of the cell is compromised. The AMP-activated protein kinase (AMPK) is the downstream component of a protein kinase cascade that is switched on by a rise in the AMP:ATP ratio, via a complex mechanism that results in an exquisitely sensitive system. AMPK is switched on by cellular stresses that either interfere with ATP production (e.g. hypoxia, glucose deprivation or ischemia) or by stresses that increase ATP consumption (e.g. muscle contraction). It is also activated hormones that act via Gq-coupled receptors, and by leptin and adiponectin, via mechanisms that remain unclear. Once activated, the system switches on catabolic pathways that generate ATP, while switching off ATP consuming processes that are not essential for short-term cell survival, such as the synthesis of lipids, carbohydrates and proteins. The AMPK cascade is the probable target for the anti-diabetic drug, metformin, and current indications are that is responsible for many of the beneficial effects of exercise in the treatment and prevention of Type 2 diabetes and the metabolic syndrome.




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