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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1999-3-11
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pubmed:abstractText |
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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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/AMP-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase Type III,
http://linkedlifedata.com/resource/pubmed/chemical/Nos3 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Threonine
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
443
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
285-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10025949-AMP-Activated Protein Kinases,
pubmed-meshheading:10025949-Amino Acid Sequence,
pubmed-meshheading:10025949-Animals,
pubmed-meshheading:10025949-Aorta,
pubmed-meshheading:10025949-Calmodulin,
pubmed-meshheading:10025949-Cattle,
pubmed-meshheading:10025949-Endothelium, Vascular,
pubmed-meshheading:10025949-Enzyme Activation,
pubmed-meshheading:10025949-Kinetics,
pubmed-meshheading:10025949-Liver,
pubmed-meshheading:10025949-Molecular Sequence Data,
pubmed-meshheading:10025949-Multienzyme Complexes,
pubmed-meshheading:10025949-Myocardial Ischemia,
pubmed-meshheading:10025949-Myocardium,
pubmed-meshheading:10025949-Nitric Oxide Synthase,
pubmed-meshheading:10025949-Nitric Oxide Synthase Type III,
pubmed-meshheading:10025949-Phosphorylation,
pubmed-meshheading:10025949-Precipitin Tests,
pubmed-meshheading:10025949-Protein Binding,
pubmed-meshheading:10025949-Protein Kinases,
pubmed-meshheading:10025949-Protein-Serine-Threonine Kinases,
pubmed-meshheading:10025949-Rats,
pubmed-meshheading:10025949-Recombinant Proteins,
pubmed-meshheading:10025949-Serine,
pubmed-meshheading:10025949-Threonine
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pubmed:year |
1999
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pubmed:articleTitle |
AMP-activated protein kinase phosphorylation of endothelial NO synthase.
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pubmed:affiliation |
St. Vincent's Institute of Medical Research, St. Vincent's Hospital, Fitzroy, Vic., Australia.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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