scholarly journals Effects of the N-terminal Domains of Myosin Binding Protein-C in anin VitroMotility Assay

2006 ◽  
Vol 281 (47) ◽  
pp. 35846-35854 ◽  
Author(s):  
Maria V. Razumova ◽  
Justin F. Shaffer ◽  
An-Yue Tu ◽  
Galina V. Flint ◽  
Michael Regnier ◽  
...  
Keyword(s):  
Protein C ◽  
Binding Protein ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Myosin Binding ◽  
Terminal Domains

scholarly journals Human Cardiac Myosin-Binding Protein C N-Terminal Domains Cooperatively Impact Actin Structural Dynamics

2019 ◽  
Vol 116 (3) ◽  
pp. 266a
Author(s):  
Rhye-Samuel Kanassatega ◽  
Thomas A. Bunch ◽  
Victoria C. Lepak ◽  
Brett A. Colson
Keyword(s):  
Structural Dynamics ◽  
Protein C ◽  
Binding Protein ◽  
Cardiac Myosin ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Myosin Binding ◽  
Terminal Domains

scholarly journals The N-Terminal Domains of Myosin Binding Protein C Can Bind Polymorphically to F-Actin

2011 ◽  
Vol 412 (3) ◽  
pp. 379-386 ◽  
Author(s):  
Albina Orlova ◽  
Vitold E. Galkin ◽  
Cy M.J. Jeffries ◽  
Edward H. Egelman ◽  
Jill Trewhella
Keyword(s):  
Protein C ◽  
Binding Protein ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Myosin Binding ◽  
Terminal Domains

scholarly journals N-Terminal Domains of Cardiac Myosin Binding Protein C Cooperatively Activate the Thin Filament

Structure ◽  
2018 ◽  
Vol 26 (12) ◽  
pp. 1604-1611.e4 ◽  
Author(s):  
Cristina Risi ◽  
Betty Belknap ◽  
Eva Forgacs-Lonart ◽  
Samantha P. Harris ◽  
Gunnar F. Schröder ◽  
...  
Keyword(s):  
Protein C ◽  
Thin Filament ◽  
Binding Protein ◽  
Cardiac Myosin ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Myosin Binding ◽  
Terminal Domains

scholarly journals Activation of Myocardial Contraction by the N-Terminal Domains of Myosin Binding Protein-C

2006 ◽  
Vol 98 (10) ◽  
pp. 1290-1298 ◽  
Author(s):  
Todd J. Herron ◽  
Elena Rostkova ◽  
Gudrun Kunst ◽  
Rajiv Chaturvedi ◽  
Mathias Gautel ◽  
...  
Keyword(s):  
Protein C ◽  
Binding Protein ◽  
Myocardial Contraction ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Myosin Binding ◽  
Terminal Domains

scholarly journals The N terminus of myosin-binding protein C extends toward actin filaments in intact cardiac muscle

2021 ◽  
Vol 153 (3) ◽  
Author(s):  
Sheema Rahmanseresht ◽  
Kyoung H. Lee ◽  
Thomas S. O’Leary ◽  
James W. McNamara ◽  
Sakthivel Sadayappan ◽  
...  
Keyword(s):  
Actin Filaments ◽  
Protein C ◽  
Myosin Head ◽  
Binding Protein ◽  
Myosin Filament ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
N Terminus ◽  
Myosin Binding ◽  
Terminal Domains

Myosin and actin filaments are highly organized within muscle sarcomeres. Myosin-binding protein C (MyBP-C) is a flexible, rod-like protein located within the C-zone of the sarcomere. The C-terminal domain of MyBP-C is tethered to the myosin filament backbone, and the N-terminal domains are postulated to interact with actin and/or the myosin head to modulate filament sliding. To define where the N-terminal domains of MyBP-C are localized in the sarcomere of active and relaxed mouse myocardium, the relative positions of the N terminus of MyBP-C and actin were imaged in fixed muscle samples using super-resolution fluorescence microscopy. The resolution of the imaging was enhanced by particle averaging. The images demonstrate that the position of the N terminus of MyBP-C is biased toward the actin filaments in both active and relaxed muscle preparations. Comparison of the experimental images with images generated in silico, accounting for known binding partner interactions, suggests that the N-terminal domains of MyBP-C may bind to actin and possibly the myosin head but only when the myosin head is in the proximity of an actin filament. These physiologically relevant images help define the molecular mechanism by which the N-terminal domains of MyBP-C may search for, and capture, molecular binding partners to tune cardiac contractility.

Biological variation of cardiac myosin-binding protein C in healthy individuals

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Bashir Alaour ◽  
Torbjørn Omland ◽  
Janniche Torsvik ◽  
Thomas E. Kaier ◽  
Marit S. Sylte ◽  
...  
Keyword(s):  
Risk Stratification ◽  
Protein C ◽  
Myocardial Injury ◽  
Binding Protein ◽  
Biological Variation ◽  
Cardiac Myosin ◽  
Analytical Quality ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Myosin Binding

Abstract Objectives Cardiac myosin-binding protein C (cMyC) is a novel biomarker of myocardial injury, with a promising role in the triage and risk stratification of patients presenting with acute cardiac disease. In this study, we assess the weekly biological variation of cMyC, to examine its potential in monitoring chronic myocardial injury, and to suggest analytical quality specification for routine use of the test in clinical practice. Methods Thirty healthy volunteers were included. Non-fasting samples were obtained once a week for ten consecutive weeks. Samples were tested in duplicate on the Erenna® platform by EMD Millipore Corporation. Outlying measurements and subjects were identified and excluded systematically, and homogeneity of analytical and within-subject variances was achieved before calculating the biological variability (CVI and CVG), reference change values (RCV) and index of individuality (II). Results Mean age was 38 (range, 21–64) years, and 16 participants were women (53%). The biological variation, RCV and II with 95% confidence interval (CI) were: CVA (%) 19.5 (17.8–21.6), CVI (%) 17.8 (14.8–21.0), CVG (%) 66.9 (50.4–109.9), RCV (%) 106.7 (96.6–120.1)/−51.6 (−54.6 to −49.1) and II 0.42 (0.29–0.56). There was a trend for women to have lower CVG. The calculated RCVs were comparable between genders. Conclusions cMyC exhibits acceptable RCV and low II suggesting that it could be suitable for disease monitoring, risk stratification and prognostication if measured serially. Analytical quality specifications based on biological variation are similar to those for cardiac troponin and should be achievable at clinically relevant concentrations.

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