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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2004-4-2
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pubmed:abstractText |
The cardiac ryanodine receptor (RyR2)/calcium release channel on the sarcoplasmic reticulum is required for muscle excitation-contraction coupling. Using site-directed mutagenesis, we identified the specific Ca2+/calmodulin-dependent protein kinase II (CaMKII) phosphorylation site on recombinant RyR2, distinct from the site for protein kinase A (PKA) that mediates the "fight-or-flight" stress response. CaMKII phosphorylation increased RyR2 Ca2+ sensitivity and open probability. CaMKII was activated at increased heart rates, which may contribute to enhanced Ca2+-induced Ca2+ release. Moreover, rate-dependent CaMKII phosphorylation of RyR2 was defective in heart failure. CaMKII-mediated phosphorylation of RyR2 may contribute to the enhanced contractility observed at higher heart rates. The full text of this article is available online at http://circres.ahajournals.org.
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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/Adrenergic beta-Agonists,
http://linkedlifedata.com/resource/pubmed/chemical/Benzylamines,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Isoproterenol,
http://linkedlifedata.com/resource/pubmed/chemical/KN 93,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoserine,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ryanodine Receptor Calcium Release...,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfonamides,
http://linkedlifedata.com/resource/pubmed/chemical/Tacrolimus Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/tacrolimus binding protein 1B
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1524-4571
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
2
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pubmed:volume |
94
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
e61-70
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:15016728-Adrenergic beta-Agonists,
pubmed-meshheading:15016728-Amino Acid Sequence,
pubmed-meshheading:15016728-Animals,
pubmed-meshheading:15016728-Benzylamines,
pubmed-meshheading:15016728-Calcium-Calmodulin-Dependent Protein Kinase Type 2,
pubmed-meshheading:15016728-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:15016728-Cardiac Pacing, Artificial,
pubmed-meshheading:15016728-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:15016728-Enzyme Inhibitors,
pubmed-meshheading:15016728-Heart Failure,
pubmed-meshheading:15016728-Heart Rate,
pubmed-meshheading:15016728-Humans,
pubmed-meshheading:15016728-Isoproterenol,
pubmed-meshheading:15016728-Molecular Sequence Data,
pubmed-meshheading:15016728-Mutagenesis, Site-Directed,
pubmed-meshheading:15016728-Myocardial Infarction,
pubmed-meshheading:15016728-Myocardium,
pubmed-meshheading:15016728-Phosphorylation,
pubmed-meshheading:15016728-Phosphoserine,
pubmed-meshheading:15016728-Protein Processing, Post-Translational,
pubmed-meshheading:15016728-Rabbits,
pubmed-meshheading:15016728-Rats,
pubmed-meshheading:15016728-Rats, Sprague-Dawley,
pubmed-meshheading:15016728-Recombinant Fusion Proteins,
pubmed-meshheading:15016728-Ryanodine Receptor Calcium Release Channel,
pubmed-meshheading:15016728-Sequence Alignment,
pubmed-meshheading:15016728-Sequence Homology, Amino Acid,
pubmed-meshheading:15016728-Sulfonamides,
pubmed-meshheading:15016728-Tacrolimus Binding Proteins
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pubmed:year |
2004
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pubmed:articleTitle |
Ca2+/calmodulin-dependent protein kinase II phosphorylation regulates the cardiac ryanodine receptor.
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pubmed:affiliation |
Department of Physiology and Cellular Biophysics, Columbia University College of Physicians and Surgeons, 630 W 168th St, P&S 9-401, Box 65, New York, NY 10032, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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