Expression of slow skeletal myosin binding C-protein in normal adult mammalian heart
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Updated: Aug 17, 2026

Analysis of Cardiomyocyte Development using Immunofluorescence in Embryonic Mouse Heart
Published on: March 26, 2015
Gurtej K Dhoot1, Samuel V Perry
1Department of Basic Sciences, The Royal Veterinary College, London, NW1 OTU, UK. tdhoot@rvc.ac.uk
Insights
Skeletal muscle C-protein, typically absent in adult hearts, was detected in human, rabbit, rat, and bovine atria. This finding reveals a previously unreported presence of slow skeletal muscle C-protein in the vertebrate heart.
Area of Science:
- Muscle biology
- Cardiac physiology
- Protein expression analysis
Background:
- Myosin binding C-protein has three main isoforms in striated muscle.
- Cardiac C-protein expression is found in fetal skeletal muscle.
- Skeletal muscle C-protein isoforms have not been reported in the vertebrate heart.
Purpose of the Study:
- To investigate the presence of skeletal muscle isoforms of C-protein in the adult vertebrate heart.
- To determine if slow skeletal muscle C-protein is expressed in cardiac tissues.
Main Methods:
- Immunocytochemistry was used to localize C-protein.
- Immunoblotting was employed to detect and quantify C-protein.
- Samples from adult human, rabbit, rat, and bovine hearts were analyzed.
Main Results:
- Slow skeletal muscle type C-protein was detected in moderate amounts.
- Expression was observed in the right atrium and interatrial septum of all species studied.
- This indicates a novel expression pattern for skeletal muscle C-protein.
Conclusions:
- Slow skeletal muscle C-protein is present in specific regions of the adult vertebrate heart.
- This challenges previous assumptions about the compartmentalization of C-protein isoforms.
- Further research is needed to understand the functional implications of this finding.
Abstract:
Myosin binding C-protein exists in three main isoforms in striated muscle. While expression of cardiac muscle type C-protein is detected in skeletal muscle during early fetal development, there have not so far been any reports of the expression of the skeletal muscle isoforms of this protein in either developing or adult vertebrate heart. The present study demonstrates slow skeletal muscle type C-protein in moderate amount in right atrium and interatrial septum of adult human, rabbit, rat and bovine hearts using both immunocytochemical and immunoblotting procedures.
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