rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2006-5-15
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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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16513777-10024460,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16513777-9734469
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-3495
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
90
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4119-27
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:16513777-Actins,
pubmed-meshheading:16513777-Animals,
pubmed-meshheading:16513777-Biomechanics,
pubmed-meshheading:16513777-Calcium,
pubmed-meshheading:16513777-Carrier Proteins,
pubmed-meshheading:16513777-Mice,
pubmed-meshheading:16513777-Mice, Knockout,
pubmed-meshheading:16513777-Myocardial Contraction,
pubmed-meshheading:16513777-Myocardium,
pubmed-meshheading:16513777-Myosin Subfragments,
pubmed-meshheading:16513777-Myosins,
pubmed-meshheading:16513777-Protein Binding
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pubmed:year |
2006
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pubmed:articleTitle |
Ablation of myosin-binding protein-C accelerates force development in mouse myocardium.
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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
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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