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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2008-10-30
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pubmed:abstractText |
Myosin binding protein C (MyBP-C) is a component of the thick filament of striated muscle. The importance of this protein is revealed by recent evidence that mutations in the cardiac gene are a major cause of familial hypertrophic cardiomyopathy. Here we investigate the distribution of MyBP-C in the A-bands of cardiac and skeletal muscles and compare this to the A-band structure in cardiac muscle of MyBP-C-deficient mice. We have used a novel averaging technique to obtain the axial density distribution of A-bands in electron micrographs of well-preserved specimens. We show that cardiac and skeletal A-bands are very similar, with a length of 1.58+/-0.01 mum. In normal cardiac and skeletal muscle, the distributions are very similar, showing clearly the series of 11 prominent accessory protein stripes in each half of the A-band spaced axially at 43-nm intervals and starting at the edge of the bare zone. We show by antibody labelling that in cardiac muscle the distal nine stripes are the location of MyBP-C. These stripes are considerably suppressed in the knockout mouse hearts as expected. Myosin heads on the surface of the thick filament in relaxed muscle are thought to be arranged in a three-stranded quasi-helix with a mean 14.3-nm axial cross bridge spacing and a 43 nm helix repeat. Extra "forbidden" meridional reflections, at orders of 43 nm, in X-ray diffraction patterns of muscle have been interpreted as due to an axial perturbation of some levels of myosin heads. However, in the MyBP-C-deficient hearts these extra meridional reflections are weak or absent, suggesting that they are due to MyBP-C itself or to MyBP-C in combination with a head perturbation brought about by the presence of MyBP-C.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-10860988,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-11227795,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-11909824,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-12386147,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-12707239,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-12713950,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-12899839,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-12946354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-1453458,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-15059932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-15166115,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-16061384,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-16731006,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-17239393,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-17656749,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-17993479,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-18252826,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-18472277,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-2035614,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-263692,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-2805252,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-3265158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-3344552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-3543050,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-4103927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-4269687,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-4802,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-5586931,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-7706420,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-7744002,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-7918996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-839534,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18817784-9344751
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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 |
Dec
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pubmed:issn |
1089-8638
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
5
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pubmed:volume |
384
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
60-72
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:18817784-Animals,
pubmed-meshheading:18817784-Carrier Proteins,
pubmed-meshheading:18817784-Fourier Analysis,
pubmed-meshheading:18817784-Microscopy, Electron,
pubmed-meshheading:18817784-Muscle, Skeletal,
pubmed-meshheading:18817784-Myocardium,
pubmed-meshheading:18817784-Myocytes, Cardiac,
pubmed-meshheading:18817784-Protein Structure, Tertiary
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pubmed:year |
2008
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pubmed:articleTitle |
Understanding the organisation and role of myosin binding protein C in normal striated muscle by comparison with MyBP-C knockout cardiac muscle.
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pubmed:affiliation |
Molecular Medicine Section, National Heart and Lung Institute, Faculty of Medicine, Imperial College London, London SW72AZ, UK. p.luther@imperial.ac.uk
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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