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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1987-11-9
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pubmed:abstractText |
Canine cardiac sarcoplasmic reticulum is phosphorylated by an endogenous calcium X calmodulin-dependent protein kinase and phosphorylation occurs mainly on a 27 kDa proteolipid, called phospholamban. To determine whether this phosphorylation has any effect on Ca2+ release, sarcoplasmic reticulum vesicles were phosphorylated by the calcium X calmodulin-dependent protein kinase, while non-phosphorylated vesicles were preincubated under identical conditions but in the absence of ATP to avoid phosphorylation. Both non-phosphorylated and phosphorylated vesicles were centrifuged to remove calmodulin, and subsequently used for Ca2+ release studies. Calcium loading was carried out either by the active calcium pump or by incubation with high (5 mM) calcium for longer periods. Phosphorylation of sarcoplasmic reticulum by calcium X calmodulin-dependent protein kinase had no appreciable effect on the initial rates of Ca2+ released from cardiac sarcoplasmic reticulum vesicles loaded under passive conditions and on the apparent 45Ca2+-40Ca2+ exchange from cardiac sarcoplasmic reticulum vesicles loaded under active conditions. Thus, it appears that calcium X calmodulin-dependent protein kinase mediated phosphorylation of cardiac sarcoplasmic reticulum is not involved in the regulation of Ca2+ release and 45Ca2+-40Ca2+ exchange.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/phospholamban
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
903
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
333-40
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:2443173-Animals,
pubmed-meshheading:2443173-Biological Transport, Active,
pubmed-meshheading:2443173-Calcium,
pubmed-meshheading:2443173-Calcium Radioisotopes,
pubmed-meshheading:2443173-Calcium-Binding Proteins,
pubmed-meshheading:2443173-Calmodulin,
pubmed-meshheading:2443173-Dogs,
pubmed-meshheading:2443173-Ion Channels,
pubmed-meshheading:2443173-Myocardium,
pubmed-meshheading:2443173-Phosphoproteins,
pubmed-meshheading:2443173-Phosphorylation,
pubmed-meshheading:2443173-Protein Kinases,
pubmed-meshheading:2443173-Sarcoplasmic Reticulum
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pubmed:year |
1987
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pubmed:articleTitle |
Lack of effects of calcium X calmodulin-dependent phosphorylation on Ca2+ release from cardiac sarcoplasmic reticulum.
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pubmed:affiliation |
Department of Pharmacology and Cell Biophysics, University of Cincinnati College of Medicine, OH 45267.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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