Cardiac myosin binding protein-C plays no regulatory role in skeletal muscle structure and function
UMass Chan Affiliations
Department of Cell and Developmental BiologyDocument Type
Journal ArticlePublication Date
2013-07-31Keywords
AnimalsBlotting, Western
Carrier Proteins
Mice
Mice, Inbred C57BL
Mice, Inbred mdx
Mice, Knockout
Microscopy, Electron
Muscle Contraction
Muscle Fibers, Fast-TwitchMuscle Fibers, Slow-TwitchMuscle, SkeletalMyocardiumPromoter Regions, GeneticProtein IsoformsSarcomeresCell BiologyCellular and Molecular Physiology
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Myosin binding protein-C (MyBP-C) exists in three major isoforms: slow skeletal, fast skeletal, and cardiac. While cardiac MyBP-C (cMyBP-C) expression is restricted to the heart in the adult, it is transiently expressed in neonatal stages of some skeletal muscles. However, it is unclear whether this expression is necessary for the proper development and function of skeletal muscle. Our aim was to determine whether the absence of cMyBP-C alters the structure, function, or MyBP-C isoform expression in adult skeletal muscle using a cMyBP-C null mouse model (cMyBP-C((t/t))). Slow MyBP-C was expressed in both slow and fast skeletal muscles, whereas fast MyBP-C was mostly restricted to fast skeletal muscles. Expression of these isoforms was unaffected in skeletal muscle from cMyBP-C((t/t)) mice. Slow and fast skeletal muscles in cMyBP-C((t/t)) mice showed no histological or ultrastructural changes in comparison to the wild-type control. In addition, slow muscle twitch, tetanus tension, and susceptibility to injury were all similar to the wild-type controls. Interestingly, fMyBP-C expression was significantly increased in the cMyBP-C((t/t)) hearts undergoing severe dilated cardiomyopathy, though this does not seem to prevent dysfunction. Additionally, expression of both slow and fast isoforms was increased in myopathic skeletal muscles. Our data demonstrate that i) MyBP-C isoforms are differentially regulated in both cardiac and skeletal muscles, ii) cMyBP-C is dispensable for the development of skeletal muscle with no functional or structural consequences in the adult myocyte, and iii) skeletal isoforms can transcomplement in the heart in the absence of cMyBP-C.Source
Lin B, Govindan S, Lee K, Zhao P, Han R, Runte KE, Craig R, Palmer BM, Sadayappan S. Cardiac myosin binding protein-C plays no regulatory role in skeletal muscle structure and function. PLoS One. 2013 Jul 31;8(7):e69671. doi:10.1371/journal.pone.0069671. Link to article on publisher's siteDOI
10.1371/journal.pone.0069671Permanent Link to this Item
http://hdl.handle.net/20.500.14038/27676PubMed ID
23936073Related Resources
Link to Article in PubMedRights
Copyright 2013 Lin et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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