Myosin-Binding Protein C (MyBP-C) in Cardiac Muscle and Contractility

2003 ◽  
pp. 31-41 ◽  
Author(s):  
Saul Winegrad
Keyword(s):  
Cardiac Muscle ◽  
Protein C ◽  
Binding Protein ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Myosin Binding

scholarly journals Hypercontractile Properties of Cardiac Muscle Fibers in a Knock-in Mouse Model of Cardiac Myosin-binding Protein-C

2000 ◽  
Vol 276 (7) ◽  
pp. 5353-5359 ◽  
Author(s):  
Christian C. Witt ◽  
Brenda Gerull ◽  
Michael J. Davies ◽  
Thomas Centner ◽  
Wolfgang A. Linke ◽  
...  
Keyword(s):  
Mouse Model ◽  
Cardiac Muscle ◽  
Protein C ◽  
Binding Protein ◽  
Muscle Fibers ◽  
Cardiac Myosin ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Myosin Binding ◽  
Cardiac Muscle Fibers

scholarly journals Roles of phosphorylation of myosin binding protein-C and troponin I in mouse cardiac muscle twitch dynamics

2004 ◽  
Vol 558 (3) ◽  
pp. 927-941 ◽  
Author(s):  
Carl W. Tong ◽  
Robert D. Gaffin ◽  
David C. Zawieja ◽  
Mariappan Muthuchamy
Keyword(s):  
Cardiac Muscle ◽  
Protein C ◽  
Troponin I ◽  
Binding Protein ◽  
Muscle Twitch ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Myosin Binding

Effect of Extracellular CA on the Phosphorylation of Myosin Binding Protein C. In Cardiac Muscle and the Phosphorylation on Force Generation

2000 ◽  
Vol 6 (S2) ◽  
pp. 74-75
Author(s):  
S. Winegrad ◽  
I. Kulikavskaya ◽  
G. McClellan
Keyword(s):  
Cardiac Muscle ◽  
Binding Sites ◽  
Protein C ◽  
Contractile Activity ◽  
Binding Protein ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Myosin Binding ◽  
Physiological Reactions ◽  
Binding Subunit

The affinity of the binding sites on troponin C (TNC) for Ca is sensitive to the state of phosporylation of troponin 1 (TN1). Two and possibly three other myofilament proteins can be phosphorylated by physiological reactions: the mosin binding protein C (MyBP-C), the regulatory light chain of myosin (RLC), and the tropomyosin binding subunit of troponin (TNT). In MyBP-C, the phosphorylation sites are specific for cardiac muscle, an occurrence that suggests a function unique to cardiac muscle. Phosphorylation of MyBP-C and RLC can be produced by Ca regulated kinases present in the myofibrils. Phosphorylation of RLC produces an increase in Ca sensitivity of contraction at submaximal concentrations of Ca without alteration of the maximum Ca activated force (Fmax). Absence of contractile activity decreases phosphorylation of RLC. One to two hours of quiescence in normal extracellular Ca reduces phophorylation substantially, and the level rises slowly when contractile activity is resumed.

scholarly journals In the eye of the STORM: Tracking the myosin-binding protein C N terminus in heart muscle

2021 ◽  
Vol 153 (3) ◽  
Author(s):  
Brett A. Colson
Keyword(s):  
Cardiac Muscle ◽  
Heart Muscle ◽  
Protein C ◽  
Binding Protein ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Storm Tracking ◽  
N Terminus ◽  
Myosin Binding

Colson discusses a recent investigation of the localization of N-terminal myosin-binding protein C in cardiac muscle.

scholarly journals Orientation of Myosin Binding Protein C in the Cardiac Muscle Sarcomere Determined by Domain-Specific Immuno-EM

2015 ◽  
Vol 427 (2) ◽  
pp. 274-286 ◽  
Author(s):  
Kyounghwan Lee ◽  
Samantha P. Harris ◽  
Sakthivel Sadayappan ◽  
Roger Craig
Keyword(s):  
Cardiac Muscle ◽  
Protein C ◽  
Binding Protein ◽  
Domain Specific ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Myosin Binding

Abstract 123: Study Of The Role Of Myosin-binding Protein C In The Structure-function Of Intact Cardiac Muscles Through The Use Of A Sarcomere Activation Biosensor

2021 ◽  
Vol 129 (Suppl_1) ◽  
Author(s):  
Ashley A Martin ◽  
Brian R Thompson ◽  
Joseph M Metzger
Keyword(s):  
Cardiac Muscle ◽  
Real Time ◽  
Knockout Mice ◽  
Protein C ◽  
Binding Protein ◽  
Muscle Performance ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Biosensor System ◽  
Myosin Binding

Cardiomyopathies affect as many as 1 in 500 adults, with hypertrophic cardiomyopathy (HCM) being the most commonly inherited heart disease. Although there are various genetic mutations which cause HCM, 40-50% of mutations identified in patients with this disease are found in the cardiac myosin-binding protein C (MyBP-C) gene. Thus, understanding this protein's role in sarcomere activation is critical for the development of effective therapeutic strategies. Previous work has identified MyBP-C as a key modulator of the sarcomere through inter-myofilament signaling. Although these studies have provided valuable information on the function of MyBP-C protein, the bulk of this work has been done with either in vitro protein recombination or permeabilized muscle. Unfortunately, these systems lack significant physiological features of muscle, such as load and intact excitation-contraction coupling mechanisms. Therefore, a large gap exists in the ability to monitor muscle sarcomere activation in an intact system in real time. In order to further advance the study of sarcomere activation in HCM disease models, specifically those targeting MyBP-C, a cardiac specific myofilament-targeted FRET based biosensor has been designed and validated. This new sarcomere activation biosensor reports real-time myofilament dynamics during physiological twitch contractions in live cardiac muscle. This allows for the in vivo biophysical tracking of FRET-detected conformation changes in TnC, which reflect the ensemble of regulatory events which lead to sarcomere activation. Currently, the biosensor is being utilized to investigate changes in sarcomere activation in MyBP-C knockout mice. We find that intact cardiac muscle under load shows slowed isometric twitch relaxation kinetics in MyBP-C knockout mice versus controls. In concert with thin and thick filament modifying small molecules, this biosensor system will be used to investigate sarcomere-based mechanisms of intact cardiac muscle performance in health and disease.

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