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      AMP-activated protein kinase phosphorylation of endothelial NO synthase.

      Febs Letters
      AMP-Activated Protein Kinases, Amino Acid Sequence, Animals, Aorta, Calmodulin, metabolism, Cattle, Endothelium, Vascular, cytology, enzymology, Enzyme Activation, Kinetics, Liver, Molecular Sequence Data, Multienzyme Complexes, Myocardial Ischemia, Myocardium, Nitric Oxide Synthase, Nitric Oxide Synthase Type III, Phosphorylation, Precipitin Tests, Protein Binding, Protein Kinases, Protein-Serine-Threonine Kinases, Rats, Recombinant Proteins, Serine, Threonine

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          Abstract

          The AMP-activated protein kinase (AMPK) in rat skeletal and cardiac muscle is activated by vigorous exercise and ischaemic stress. Under these conditions AMPK phosphorylates and inhibits acetyl-coenzyme A carboxylase causing increased oxidation of fatty acids. Here we show that AMPK co-immunoprecipitates with cardiac endothelial NO synthase (eNOS) and phosphorylates Ser-1177 in the presence of Ca2+-calmodulin (CaM) to activate eNOS both in vitro and during ischaemia in rat hearts. In the absence of Ca2+-calmodulin, AMPK also phosphorylates eNOS at Thr-495 in the CaM-binding sequence, resulting in inhibition of eNOS activity but Thr-495 phosphorylation is unchanged during ischaemia. Phosphorylation of eNOS by the AMPK in endothelial cells and myocytes provides a further regulatory link between metabolic stress and cardiovascular function.

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