| pubmed-article:19655190 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19655190 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:19655190 | lifeskim:mentions | umls-concept:C0027061 | lld:lifeskim |
| pubmed-article:19655190 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:19655190 | lifeskim:mentions | umls-concept:C0041199 | lld:lifeskim |
| pubmed-article:19655190 | lifeskim:mentions | umls-concept:C0256371 | lld:lifeskim |
| pubmed-article:19655190 | lifeskim:mentions | umls-concept:C0312418 | lld:lifeskim |
| pubmed-article:19655190 | lifeskim:mentions | umls-concept:C0033621 | lld:lifeskim |
| pubmed-article:19655190 | lifeskim:mentions | umls-concept:C0242210 | lld:lifeskim |
| pubmed-article:19655190 | lifeskim:mentions | umls-concept:C0392756 | lld:lifeskim |
| pubmed-article:19655190 | lifeskim:mentions | umls-concept:C1149266 | lld:lifeskim |
| pubmed-article:19655190 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:19655190 | lifeskim:mentions | umls-concept:C0036667 | lld:lifeskim |
| pubmed-article:19655190 | lifeskim:mentions | umls-concept:C0439098 | lld:lifeskim |
| pubmed-article:19655190 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:19655190 | pubmed:dateCreated | 2010-1-19 | lld:pubmed |
| pubmed-article:19655190 | pubmed:abstractText | Previous studies indicated that the increase in protein kinase C (PKC)-mediated myofilament protein phosphorylation observed in failing myocardium might be detrimental for contractile function. This study was designed to reveal and compare the effects of PKCalpha- and PKCepsilon-mediated phosphorylation on myofilament function in human myocardium. Isometric force was measured at different [Ca2+] in single permeabilized cardiomyocytes from failing human left ventricular tissue. Activated PKCalpha and PKCepsilon equally reduced Ca2+ sensitivity in failing cardiomyocytes (DeltapCa50 = 0.08 +/- 0.01). Both PKC isoforms increased phosphorylation of troponin I- (cTnI) and myosin binding protein C (cMyBP-C) in failing cardiomyocytes. Subsequent incubation of failing cardiomyocytes with the catalytic subunit of protein kinase A (PKA) resulted in a further reduction in Ca2+ sensitivity, indicating that the effects of both PKC isoforms were not caused by cross-phosphorylation of PKA sites. Both isozymes showed no effects on maximal force and only PKCalpha resulted in a modest significant reduction in passive force. Effects of PKCalpha were only minor in donor cardiomyocytes, presumably because of already saturated cTnI and cMyBP-C phosphorylation levels. Donor tissue could therefore be used as a tool to reveal the functional effects of troponin T (cTnT) phosphorylation by PKCalpha. Massive dephosphorylation of cTnT with alkaline phosphatase increased Ca2+ sensitivity. Subsequently, PKCalpha treatment of donor cardiomyocytes reduced Ca2+ sensitivity (DeltapCa50 = 0.08 +/- 0.02) and solely increased phosphorylation of cTnT, but did not affect maximal and passive force. PKCalpha- and PKCepsilon-mediated phosphorylation of cMyBP-C and cTnI as well as cTnT decrease myofilament Ca2+ sensitivity and may thereby reduce contractility and enhance relaxation of human myocardium. | lld:pubmed |
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| pubmed-article:19655190 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19655190 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19655190 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19655190 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19655190 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19655190 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19655190 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19655190 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19655190 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19655190 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19655190 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19655190 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:19655190 | pubmed:issn | 1435-1803 | lld:pubmed |
| pubmed-article:19655190 | pubmed:author | pubmed-author:JaquetKorneli... | lld:pubmed |
| pubmed-article:19655190 | pubmed:author | pubmed-author:van der... | lld:pubmed |
| pubmed-article:19655190 | pubmed:author | pubmed-author:StienenGer... | lld:pubmed |
| pubmed-article:19655190 | pubmed:author | pubmed-author:ZarembaRuudR | lld:pubmed |
| pubmed-article:19655190 | pubmed:author | pubmed-author:dos... | lld:pubmed |
| pubmed-article:19655190 | pubmed:author | pubmed-author:KooijViolaV | lld:pubmed |
| pubmed-article:19655190 | pubmed:author | pubmed-author:BoontjeNickyN | lld:pubmed |
| pubmed-article:19655190 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19655190 | pubmed:volume | 105 | lld:pubmed |
| pubmed-article:19655190 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19655190 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19655190 | pubmed:pagination | 289-300 | lld:pubmed |
| pubmed-article:19655190 | pubmed:dateRevised | 2010-9-27 | lld:pubmed |
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| pubmed-article:19655190 | pubmed:year | 2010 | lld:pubmed |
