pubmed-article:16513777 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16513777 | lifeskim:mentions | umls-concept:C0025914 | lld:lifeskim |
pubmed-article:16513777 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
pubmed-article:16513777 | lifeskim:mentions | umls-concept:C0027061 | lld:lifeskim |
pubmed-article:16513777 | lifeskim:mentions | umls-concept:C0547070 | lld:lifeskim |
pubmed-article:16513777 | lifeskim:mentions | umls-concept:C1527148 | lld:lifeskim |
pubmed-article:16513777 | lifeskim:mentions | umls-concept:C0441722 | lld:lifeskim |
pubmed-article:16513777 | pubmed:issue | 11 | lld:pubmed |
pubmed-article:16513777 | pubmed:dateCreated | 2006-5-15 | lld:pubmed |
pubmed-article:16513777 | pubmed:abstractText | Myosin-binding protein-C (MyBP-C) is a thick filament-associated protein that binds tightly to myosin. Given that cMyBP-C may act to modulate cooperative activation of the thin filament by constraining the availability of myosin cross-bridges for binding to actin, we investigated the role of MyBP-C in the regulation of cardiac muscle contraction. We assessed the Ca(2+) sensitivity of force (pCa(50)) and the activation dependence of the rate of force redevelopment (k(tr)) in skinned myocardium isolated from wild-type (WT) and cMyBP-C null (cMyBP-C(-/-)) mice. Mechanical measurements were performed at 22 degrees C in the absence and presence of a strong-binding, nonforce-generating analog of myosin subfragment-1 (NEM-S1). In the absence of NEM-S1, maximal force and k(tr) and the pCa(50) of isometric force did not differ between WT and cMyBP-C(-/-) myocardium; however, ablation of cMyBP-C-accelerated k(tr) at each submaximal force. Treatment of WT and cMyBP-C(-/-) myocardium with 3 muM NEM-S1 elicited similar increases in pCa(50,) but the effects of NEM-S1 to increase k(tr) at submaximal forces and thereby markedly reduce the activation dependence of k(tr) occurred to a greater degree in cMyBP-C(-/-) myocardium. Together, these results support the idea that cMyBP-C normally acts to constrain the interaction between myosin and actin, which in turn limits steady-state force development and the kinetics of cross-bridge interaction. | lld:pubmed |
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pubmed-article:16513777 | pubmed:language | eng | lld:pubmed |
pubmed-article:16513777 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16513777 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:16513777 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16513777 | pubmed:month | Jun | lld:pubmed |
pubmed-article:16513777 | pubmed:issn | 0006-3495 | lld:pubmed |
pubmed-article:16513777 | pubmed:author | pubmed-author:MossRichard... | lld:pubmed |
pubmed-article:16513777 | pubmed:author | pubmed-author:FitzsimonsDan... | lld:pubmed |
pubmed-article:16513777 | pubmed:author | pubmed-author:StelzerJulian... | lld:pubmed |
pubmed-article:16513777 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16513777 | pubmed:day | 1 | lld:pubmed |
pubmed-article:16513777 | pubmed:volume | 90 | lld:pubmed |
pubmed-article:16513777 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16513777 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16513777 | pubmed:pagination | 4119-27 | lld:pubmed |
pubmed-article:16513777 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:16513777 | pubmed:year | 2006 | lld:pubmed |
pubmed-article:16513777 | pubmed:articleTitle | Ablation of myosin-binding protein-C accelerates force development in mouse myocardium. | lld:pubmed |
pubmed-article:16513777 | pubmed:affiliation | Department of Physiology, University of Wisconsin School of Medicine and Public Health, 1300 University Avenue, Madison, WI 53706, USA. stelzer@physiology.wisc.edu | lld:pubmed |
pubmed-article:16513777 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16513777 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:16513777 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:16513777 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
entrez-gene:17868 | entrezgene:pubmed | pubmed-article:16513777 | lld:entrezgene |
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