rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 1
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pubmed:dateCreated |
2003-11-17
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pubmed:abstractText |
We have explored the role of the giant elastic protein titin in the Frank-Starling mechanism of the heart by measuring the sarcomere length (SL) dependence of activation in skinned cardiac muscles with different titin-based passive stiffness characteristics. We studied muscle from the bovine left ventricle (BLV), which expresses a high level of a stiff titin isoform, and muscle from the bovine left atrium (BLA), which expresses more compliant titin isoforms. Passive tension was also varied in each muscle type by manipulating the pre-history of stretch prior to activation. We found that the SL-dependent increases in Ca2+ sensitivity and maximal Ca2+-activated tension were markedly more pronounced when titin-based passive tension was high. Small-angle X-ray diffraction experiments revealed that the SL dependence of reduction of interfilament lattice spacing is greater in BLV than in BLA and that the lattice spacing is coupled with titin-based passive tension. These results support the notion that titin-based passive tension promotes actomyosin interaction by reducing the lattice spacing. This work indicates that titin may be a factor involved in the Frank-Starling mechanism of the heart by promoting actomyosin interaction in response to stretch.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12963792-10371696,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12963792-10625306,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12963792-10625312,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12963792-11045995,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12963792-11112991,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12963792-3312367,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12963792-9530220
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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 |
Nov
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pubmed:issn |
0022-3751
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
553
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
147-54
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12963792-Algorithms,
pubmed-meshheading:12963792-Animals,
pubmed-meshheading:12963792-Cattle,
pubmed-meshheading:12963792-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:12963792-Heart,
pubmed-meshheading:12963792-Heart Atria,
pubmed-meshheading:12963792-Heart Ventricles,
pubmed-meshheading:12963792-Isomerism,
pubmed-meshheading:12963792-Muscle Proteins,
pubmed-meshheading:12963792-Myocardial Contraction,
pubmed-meshheading:12963792-Myocardium,
pubmed-meshheading:12963792-Protein Kinases,
pubmed-meshheading:12963792-Sarcomeres,
pubmed-meshheading:12963792-Ventricular Function,
pubmed-meshheading:12963792-X-Ray Diffraction
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pubmed:year |
2003
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pubmed:articleTitle |
Titin isoform variance and length dependence of activation in skinned bovine cardiac muscle.
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pubmed:affiliation |
Department of Veterinary and Comparative Anatomy, Pharmacology and Physiology, Washington State University, Pullman, WA 99164-6520, USA.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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