Cardiff University | Prifysgol Caerdydd ORCA
Online Research @ Cardiff 
WelshClear Cookie - decide language by browser settings

Understanding the organisation and role of Myosin binding protein C in normal striated muscle by comparison with MyBP-C knockout cardiac muscle

Luther, Pradeep K., Bennett, Pauline M., Knupp, Carlo, Craig, Roger, Padrón, Raúl, Harris, Samantha P., Patel, Jitendrakumar and Moss, Richard L. 2008. Understanding the organisation and role of Myosin binding protein C in normal striated muscle by comparison with MyBP-C knockout cardiac muscle. Journal of Molecular Biology 384 (1) , pp. 60-72. 10.1016/j.jmb.2008.09.013

Full text not available from this repository.


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 μm. 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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Optometry and Vision Sciences
Subjects: Q Science > QP Physiology
R Medicine > R Medicine (General)
R Medicine > RE Ophthalmology
Uncontrolled Keywords: cardiac muscle ; electron microscopy ; cryosections; myosin-binding protein C
Publisher: Elsevier
ISSN: 0022-2836
Last Modified: 17 Jun 2017 04:48

Citation Data

Cited 57 times in Google Scholar. View in Google Scholar

Cited 82 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item Edit Item