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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1998-5-28
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pubmed:abstractText |
1. The composition of myosin heavy chains (MHCs) was investigated in young (1- to 8-week-old) and mature (9- to 26-week-old) guinea-pigs using two monoclonal antibodies directed specifically against alpha-MHC and beta-MHC. In addition, maximum force and the rate of ATP consumption during isometric contraction were measured in chemically skinned trabeculae taken from the same hearts. 2. An age-dependent shift in the MHC composition was found. The alpha-MHC fraction decreased from 0.17 +/- 0.02 (mean +/- S.E.M.; n = 24) in young to 0.04 +/- 0.01 (n = 43) in mature hearts. This shift was correlated with a decrease in tension cost (i.e. ATP consumption per second per trabecula volume/force per cross-sectional area) from 4.1 +/- 0.2 mmol kN-1 m-1 s-1 (n = 23) in young to 2.5 +/- 0.1 mmol kN-1 m-1 s-1 (n = 57) in mature hearts. 3. From the results it follows that the slow beta-MHC isoform, which predominates in hearts of mature guinea-pigs, is about 5 times more economical than the fast alpha-MHC isoform. Calcium sensitivity of force and ATP consumption decreased with age, but stabilized within a few weeks after birth. The pronounced dependence of cardiac energetics on MHC composition should be taken into account in long-term studies of cardiac overload.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-13485191,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-13860702,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-1533346,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-1742869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-1934353,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-2146490,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-2172555,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-2523412,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-2782621,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-2932264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-2942954,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-2952364,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-2964793,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-3182811,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-3618771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-6119365,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-6189421,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-6212048,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-6222846,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-6232394,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-6448166,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-6454511,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-6456085,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-6459193,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-6461437,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-6796647,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-722801,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-7328666,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-7614728,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-7943406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-8057257,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-8729055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9518708-9038957
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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 |
Mar
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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 |
1
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pubmed:volume |
507 ( Pt 2)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
497-510
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9518708-Adenosine Triphosphatases,
pubmed-meshheading:9518708-Adenosine Triphosphate,
pubmed-meshheading:9518708-Aging,
pubmed-meshheading:9518708-Animals,
pubmed-meshheading:9518708-Antibodies, Monoclonal,
pubmed-meshheading:9518708-Blotting, Western,
pubmed-meshheading:9518708-Calcium,
pubmed-meshheading:9518708-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:9518708-Energy Metabolism,
pubmed-meshheading:9518708-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:9518708-Female,
pubmed-meshheading:9518708-Guinea Pigs,
pubmed-meshheading:9518708-Heart,
pubmed-meshheading:9518708-Heart Ventricles,
pubmed-meshheading:9518708-Myocardial Contraction,
pubmed-meshheading:9518708-Myocardium,
pubmed-meshheading:9518708-Myosin Heavy Chains,
pubmed-meshheading:9518708-Myosins,
pubmed-meshheading:9518708-Ventricular Function
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pubmed:year |
1998
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pubmed:articleTitle |
Age-dependent changes in myosin composition correlate with enhanced economy of contraction in guinea-pig hearts.
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pubmed:affiliation |
Laboratory for Physiology, Institute for Cardiovascular Research, Free University, Amsterdam, The Netherlands. J.van_der_Velden.physiol@med.vu.nl
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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