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:	Brian Lin, Suresh Govindan, Kyounghwan Lee, Piming Zhao, Renzhi Han, K Elisabeth Runte, Roger Craig, Bradley M Palmer, Sakthivel Sadayappan
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/4d1264bd714f4b1d9f939002124a1319
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spelling	oai:doaj.org-article:4d1264bd714f4b1d9f939002124a13192021-11-18T09:01:51ZCardiac myosin binding protein-C plays no regulatory role in skeletal muscle structure and function.1932-620310.1371/journal.pone.0069671https://doaj.org/article/4d1264bd714f4b1d9f939002124a13192013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23936073/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Myosin 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.Brian LinSuresh GovindanKyounghwan LeePiming ZhaoRenzhi HanK Elisabeth RunteRoger CraigBradley M PalmerSakthivel SadayappanPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 7, p e69671 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Brian Lin Suresh Govindan Kyounghwan Lee Piming Zhao Renzhi Han K Elisabeth Runte Roger Craig Bradley M Palmer Sakthivel Sadayappan Cardiac myosin binding protein-C plays no regulatory role in skeletal muscle structure and function.
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.
format	article
author	Brian Lin Suresh Govindan Kyounghwan Lee Piming Zhao Renzhi Han K Elisabeth Runte Roger Craig Bradley M Palmer Sakthivel Sadayappan
author_facet	Brian Lin Suresh Govindan Kyounghwan Lee Piming Zhao Renzhi Han K Elisabeth Runte Roger Craig Bradley M Palmer Sakthivel Sadayappan
author_sort	Brian Lin
title	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_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_sort	cardiac myosin binding protein-c plays no regulatory role in skeletal muscle structure and function.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/4d1264bd714f4b1d9f939002124a1319
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Cardiac myosin binding protein-C plays no regulatory role in skeletal muscle structure and function.

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