Source:http://linkedlifedata.com/resource/pubmed/id/11158984
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2001-2-22
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| pubmed:abstractText |
To determine the in vivo functional significance of troponin I (TnI) protein kinase C (PKC) phosphorylation sites, we created a transgenic mouse expressing mutant TnI, in which PKC phosphorylation sites at serines-43 and -45 were replaced by alanine. When we used high-perfusate calcium as a PKC activator, developed pressures in transgenic (TG) perfused hearts were similar to wild-type (WT) hearts (P = not significant, NS), though there was a 35% and 32% decrease in peak-systolic intracellular calcium (P < 0.01) and diastolic calcium (P < 0.005), respectively. The calcium transient duration was prolonged in the TG mice also (12-27%, ANOVA, P < 0.01). During global ischemia, TG hearts developed ischemic contracture to a greater extent than WT hearts (41 +/- 18 vs. 69 +/- 10 mmHg, perfusate calcium 3.5 mM, P < 0.01). In conclusion, expression of mutant TnI lacking PKC phosphorylation sites results in a marked alteration in the calcium-pressure relationship, and thus susceptibility to ischemic contracture. The reduced intracellular calcium and prolonged calcium transients suggests that a potent feedback mechanism exists between the myofilament and the processes controlling calcium homeostasis.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alanine,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Troponin I
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
0363-6135
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
280
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
H835-43
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| pubmed:dateRevised |
2007-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11158984-Alanine,
pubmed-meshheading:11158984-Animals,
pubmed-meshheading:11158984-Binding Sites,
pubmed-meshheading:11158984-Calcium,
pubmed-meshheading:11158984-Feedback,
pubmed-meshheading:11158984-Female,
pubmed-meshheading:11158984-Homeostasis,
pubmed-meshheading:11158984-Mice,
pubmed-meshheading:11158984-Mice, Transgenic,
pubmed-meshheading:11158984-Mutagenesis,
pubmed-meshheading:11158984-Myocardial Ischemia,
pubmed-meshheading:11158984-Myocardial Reperfusion Injury,
pubmed-meshheading:11158984-Myocardium,
pubmed-meshheading:11158984-Organ Size,
pubmed-meshheading:11158984-Oxygen Consumption,
pubmed-meshheading:11158984-Phosphorylation,
pubmed-meshheading:11158984-Protein Kinase C,
pubmed-meshheading:11158984-Protein Structure, Tertiary,
pubmed-meshheading:11158984-Serine,
pubmed-meshheading:11158984-Troponin I,
pubmed-meshheading:11158984-Ventricular Pressure
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| pubmed:year |
2001
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| pubmed:articleTitle |
Ischemic dysfunction in transgenic mice expressing troponin I lacking protein kinase C phosphorylation sites.
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| pubmed:affiliation |
Pittsburgh Nuclear Magnetic Resonance Center for Biomedical Research, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA. macgowanga@msx.upmc.edu
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| pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|