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

      1
      Endocrinology
      The Endocrine Society

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          Abstract

          All cells must maintain a high ratio of cellular ATP:ADP to survive. Because of the adenylate kinase reaction (2ADP <--> ATP + AMP), AMP rises whenever the ATP:ADP ratio 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 by 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 antidiabetic drug metformin, and current indications are that it 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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          Author and article information

          Journal
          Endocrinology
          Endocrinology
          The Endocrine Society
          0013-7227
          0013-7227
          Dec 2003
          : 144
          : 12
          Affiliations
          [1 ] Division of Molecular Physiology, University of Dundee, Wellcome Trust Biocentre, Dundee DD1 5EH, Scotland, United Kingdom. d.g.hardie@dundee.ac.uk.
          Article
          en.2003-0982
          10.1210/en.2003-0982
          12960015
          b3fc9b5f-6e8d-40df-b42c-9fa521f1b229
          History

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