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    Ablation of cardiac myosin binding protein-C disrupts the super-relaxed state of myosin in murine cardiomyocytes

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    JMCC9853R2_final.pdf
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    Description:
    Final Accepted Manuscript
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    Author
    McNamara, James W. cc
    Li, Amy
    Smith, Nicola J.
    Lal, Sean
    Graham, Robert M.
    Kooiker, Kristina Bezold
    van Dijk, Sabine J.
    Remedios, Cristobal G. dos
    Harris, Samantha P.
    Cooke, Roger
    Affiliation
    Univ Arizona, Dept Cellular & Mol Med
    Issue Date
    2016-05
    Keywords
    Cardiac SRX
    Hypertrophic cardiomyopathy
    Myosin binding protein-C (MyBP-C)
    Myosin II ATPase
    Thick filament structure
    Cardiac energetics
    
    Metadata
    Show full item record
    Publisher
    ELSEVIER SCI LTD
    Citation
    Ablation of cardiac myosin binding protein-C disrupts the super-relaxed state of myosin in murine cardiomyocytes 2016, 94:65 Journal of Molecular and Cellular Cardiology
    Journal
    Journal of Molecular and Cellular Cardiology
    Rights
    Crown Copyright © 2016 Published by Elsevier Ltd. All rights reserved.
    Collection Information
    This item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.
    Abstract
    Cardiac myosin binding protein-C (cMyBP-C) is a structural and regulatory component of cardiac thick filaments. It is observed in electron micrographs as seven to nine transverse stripes in the central portion of each half of the A band. Its C-terminus binds tightly to the myosin rod and contributes to thick filament structure, while the N-terminus can bind both myosin S2 and actin, influencing their structure and function. Mutations in the MYBPC3 gene (encoding cMyBP-C) are commonly associated with hypertrophic cardiomyopathy (HCM). In cardiac cells there exists a population of myosin heads in the super-relaxed (SRX) state, which are bound to the thick filament core with a highly inhibited ATPase activity. This report examines the role cMyBP-C plays in regulating the population of the SRX state of cardiac myosin by using an assay that measures single ATP turnover of myosin. We report a significant decrease in the proportion of myosin heads in the SRX state in homozygous cMyBP-C knockout mice, however heterozygous cMyBP-C knockout mice do not significantly differ from the wild type. A smaller, non-significant decrease is observed when thoracic aortic constriction is used to induce cardiac hypertrophy in mutation negative mice. These results support the proposal that cMyBP-C stabilises the thick filament and that the loss of cMyBP-C results in an untethering of myosin heads. This results in an increased myosin ATP turnover, further consolidating the relationship between thick filament structure and the myosin ATPase. Crown Copyright (C) 2016 Published by Elsevier Ltd. All rights reserved.
    Note
    Available online 26 March 2016. 12 month embargo.
    ISSN
    00222828
    PubMed ID
    27021517
    DOI
    10.1016/j.yjmcc.2016.03.009
    Version
    Final accepted manuscript
    Sponsors
    NG Macintosh Memorial Fund; National Heart Foundation [GNT1093852, PB 12S 6939]; NIH [R01 HL080367]; American Heart Association [13POST14780089]
    Additional Links
    http://linkinghub.elsevier.com/retrieve/pii/S0022282816300566
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.yjmcc.2016.03.009
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