Cardiac myosin binding protein-C: redefining its structure and function Journal Article

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Authors: Sadayappan, S; de Tombe, P. P.
Article Title: Cardiac myosin binding protein-C: redefining its structure and function
Abstract: Mutations of cardiac myosin binding protein-C (cMyBP-C) are inherited by an estimated 60 million people worldwide, and the protein is the target of several kinases. Recent evidence further suggests that cMyBP-C mutations alter Ca(2+) transients, leading to electrophysiological dysfunction. Thus, while the importance of studying this cardiac sarcomere protein is clear, preliminary data in the literature have raised many questions. Therefore, in this article, we propose to review the structure and function of cMyBP-C with particular respect to the role(s) in cardiac contractility and whether its release into the circulatory system is a potential biomarker of myocardial infarction. We also discuss future directions and experimental designs that may lead to expanding the role(s) of cMyBP-C in the heart. In conclusion, we suggest that cMyBP-C is a regulatory protein that could offer a broad clinical utility in maintaining normal cardiac function.
Journal Title: Biophysical reviews
Volume: 4
Issue: 2
ISSN: 1867-2450
Publisher: Unknown  
Date Published: 2012
Start Page: 93
End Page: 106
Language: ENG
DOI/URL:

10.1007/s12551-012-0067-x
Notes: GR: K02 HL114749/HL/NHLBI NIH HHS/United States; GR: P01 HL062426/HL/NHLBI NIH HHS/United States; GR: P30 HL101297/HL/NHLBI NIH HHS/United States; GR: R01 HL075494/HL/NHLBI NIH HHS/United States; GR: R01 HL105826/HL/NHLBI NIH HHS/United States; JID: 101498573; NIHMS380700; ppublish