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Cardiac Myosin Binding Protein-C Plays No Regulatory Role in Skeletal Muscle Structure and Function

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...

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Autores principales: Lin, Brian, Govindan, Suresh, Lee, Kyounghwan, Zhao, Piming, Han, Renzhi, Runte, K. Elisabeth, Craig, Roger, Palmer, Bradley M., Sadayappan, Sakthivel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3729691/
https://www.ncbi.nlm.nih.gov/pubmed/23936073
http://dx.doi.org/10.1371/journal.pone.0069671
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author Lin, Brian
Govindan, Suresh
Lee, Kyounghwan
Zhao, Piming
Han, Renzhi
Runte, K. Elisabeth
Craig, Roger
Palmer, Bradley M.
Sadayappan, Sakthivel
author_facet Lin, Brian
Govindan, Suresh
Lee, Kyounghwan
Zhao, Piming
Han, Renzhi
Runte, K. Elisabeth
Craig, Roger
Palmer, Bradley M.
Sadayappan, Sakthivel
author_sort Lin, Brian
collection PubMed
description 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.
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spelling pubmed-37296912013-08-09 Cardiac Myosin Binding Protein-C Plays No Regulatory Role in Skeletal Muscle Structure and Function Lin, Brian Govindan, Suresh Lee, Kyounghwan Zhao, Piming Han, Renzhi Runte, K. Elisabeth Craig, Roger Palmer, Bradley M. Sadayappan, Sakthivel PLoS One Research Article 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. Public Library of Science 2013-07-31 /pmc/articles/PMC3729691/ /pubmed/23936073 http://dx.doi.org/10.1371/journal.pone.0069671 Text en © 2013 Lin et al http://creativecommons.org/licenses/by/4.0/ 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 properly credited.
spellingShingle Research Article
Lin, Brian
Govindan, Suresh
Lee, Kyounghwan
Zhao, Piming
Han, Renzhi
Runte, K. Elisabeth
Craig, Roger
Palmer, Bradley M.
Sadayappan, Sakthivel
Cardiac Myosin Binding Protein-C Plays No Regulatory Role in Skeletal Muscle Structure and Function
title Cardiac Myosin Binding Protein-C Plays No Regulatory Role in Skeletal Muscle Structure and Function
title_full Cardiac Myosin Binding Protein-C Plays No Regulatory Role in Skeletal Muscle Structure and Function
title_fullStr Cardiac Myosin Binding Protein-C Plays No Regulatory Role in Skeletal Muscle Structure and Function
title_full_unstemmed Cardiac Myosin Binding Protein-C Plays No Regulatory Role in Skeletal Muscle Structure and Function
title_short Cardiac Myosin Binding Protein-C Plays No Regulatory Role in Skeletal Muscle Structure and Function
title_sort cardiac myosin binding protein-c plays no regulatory role in skeletal muscle structure and function
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3729691/
https://www.ncbi.nlm.nih.gov/pubmed/23936073
http://dx.doi.org/10.1371/journal.pone.0069671
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