Stress signaling in the heart by AMP-activated protein kinase.
The stress-signaling protein, adenosine monophosphate-activated protein kinase (AMPK), regulates a variety of pathways in cells that 1) increase the provision and utilization of energy-providing substrates such as glucose and fatty acids, 2) inhibit energy-requiring pathways such as cholesterol biosynthesis and protein synthesis, and 3) increase the transcription of genes involved in energy metabolism and mitochondrial biogenesis. In the heart, AMPK therefore becomes very important in protecting against ischemia-reperfusion injury and regulating substrate metabolism in the face of changes in workload. This review summarizes the regulation of AMPK activity in the heart and discusses the effects of AMPK activation.
Russell
Raymond
R
Section of Cardiovascular Medicine, Yale University School of Medicine, 333 Cedar Street, FMP 3, New Haven, CT 06510, USA. raymond.russell@yale.edu
D055372:AMP-Activated Protein Kinases; D000241:Adenosine / Q000031:analogs & derivatives; D004730:Endothelium, Vascular / Q000378:metabolism; D004734:Energy Metabolism / Q000502:physiology; D004789:Enzyme Activation / Q000502:physiology; D005227:Fatty Acids / Q000378:metabolism; D006321:Heart / Q000502:physiology*; D006801:Humans; D009097:Multienzyme Complexes / Q000378:metabolism*; D017202:Myocardial Ischemia / Q000201:enzymology; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D011736:Pyridoxine / Q000031:analogs & derivatives
D005227:Fatty Acids; D009097:Multienzyme Complexes; C058697:adenosine-N(6)-diethylthioether-N'-pyridoximine 5'-phosphate; D017346:Protein Serine-Threonine Kinases; D055372:AMP-Activated Protein Kinases; D000241:Adenosine; D011736:Pyridoxine