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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1991-4-17
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pubmed:abstractText |
Effects of troponin phosphorylation on Ca2(+)-stimulated MgATPase activity of bovine cardiac actomyosin were examined. Phosphorylation by protein kinase C of troponin I and troponin T subunits in troponin or troponin-tropomyosin complex resulted in a decreased Ca2(+)-stimulated MgATPase activity in reconstituted actomyosin, and this effect was reversed by subsequent dephosphorylation by protein phosphatase 1. It was further observed that protein kinase C phosphorylation of either troponin I or troponin T subunits led to a similar inhibition of Ca2(+)-stimulated actomyosin MgATPase activity. In all cases, EC50 values (concentrations causing 50% stimulation) for Ca2+ were not appreciably affected by troponin phosphorylation by protein kinase C. Data from phosphorylation site analysis suggests that phosphorylation of threonine 144 in troponin I and possibly threonine 280 or threonine 199 in troponin T might be important for the observed decrease of Ca2(+)-stimulated actomyosin MgATPase. It is suggested that inhibition of actomyosin MgATPase caused by protein kinase C phosphorylation of troponin I and/or troponin T represents a new mechanism that can account for in part the reported negative inotropic effect of phorbol esters on various cardiac preparations.
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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/Actomyosin,
http://linkedlifedata.com/resource/pubmed/chemical/Ca(2 ) Mg(2 )-ATPase,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Troponin,
http://linkedlifedata.com/resource/pubmed/chemical/Troponin I,
http://linkedlifedata.com/resource/pubmed/chemical/Troponin T
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
266
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4974-8
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1825828-Actomyosin,
pubmed-meshheading:1825828-Animals,
pubmed-meshheading:1825828-Ca(2+) Mg(2+)-ATPase,
pubmed-meshheading:1825828-Calcium,
pubmed-meshheading:1825828-Cattle,
pubmed-meshheading:1825828-Kinetics,
pubmed-meshheading:1825828-Myocardium,
pubmed-meshheading:1825828-Phosphorylation,
pubmed-meshheading:1825828-Protein Kinase C,
pubmed-meshheading:1825828-Troponin,
pubmed-meshheading:1825828-Troponin I,
pubmed-meshheading:1825828-Troponin T
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pubmed:year |
1991
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pubmed:articleTitle |
Protein kinase C phosphorylation of cardiac troponin I or troponin T inhibits Ca2(+)-stimulated actomyosin MgATPase activity.
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pubmed:affiliation |
Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia 30322.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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