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

scholarly journals The Interplay between S-glutathionylation and Phosphorylation of Cardiac Troponin I and Myosin Binding Protein C in End-Stage Human Failing Hearts

Antioxidants ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 1134
Author(s):  
Heidi Budde ◽  
Roua Hassoun ◽  
Melina Tangos ◽  
Saltanat Zhazykbayeva ◽  
Melissa Herwig ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Protein C ◽  
Troponin I ◽  
Reduced Glutathione ◽  
Binding Protein ◽  
Enzyme Treatment ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Myosin Binding ◽  
End Stage

Oxidative stress is defined as an imbalance between the antioxidant defense system and the production of reactive oxygen species (ROS). At low levels, ROS are involved in the regulation of redox signaling for cell protection. However, upon chronical increase in oxidative stress, cell damage occurs, due to protein, DNA and lipid oxidation. Here, we investigated the oxidative modifications of myofilament proteins, and their role in modulating cardiomyocyte function in end-stage human failing hearts. We found altered maximum Ca2+-activated tension and Ca2+ sensitivity of force production of skinned single cardiomyocytes in end-stage human failing hearts compared to non-failing hearts, which was corrected upon treatment with reduced glutathione enzyme. This was accompanied by the increased oxidation of troponin I and myosin binding protein C, and decreased levels of protein kinases A (PKA)- and C (PKC)-mediated phosphorylation of both proteins. The Ca2+ sensitivity and maximal tension correlated strongly with the myofilament oxidation levels, hypo-phosphorylation, and oxidative stress parameters that were measured in all the samples. Furthermore, we detected elevated titin-based myocardial stiffness in HF myocytes, which was reversed by PKA and reduced glutathione enzyme treatment. Finally, many oxidative stress and inflammation parameters were significantly elevated in failing hearts compared to non-failing hearts, and corrected upon treatment with the anti-oxidant GSH enzyme. Here, we provide evidence that the altered mechanical properties of failing human cardiomyocytes are partially due to phosphorylation, S-glutathionylation, and the interplay between the two post-translational modifications, which contribute to the development of heart failure.

scholarly journals Regulation of Contraction by PKA Phosphorylation of Myosin Binding Protein C and Troponin I in Murine Skinned Myocardium

2010 ◽  
Vol 98 (3) ◽  
pp. 554a
Author(s):  
Peter P. Chen ◽  
Jitandrakumar R. Patel ◽  
Jeffrey W. Walker ◽  
Richard L. Moss
Keyword(s):  
Protein C ◽  
Troponin I ◽  
Binding Protein ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Regulation Of Contraction ◽  
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 Cardiac Myosin-binding Protein C and Troponin-I Phosphorylation Independently Modulate Myofilament Length-dependent Activation

2015 ◽  
Vol 290 (49) ◽  
pp. 29241-29249 ◽  
Author(s):  
Mohit Kumar ◽  
Suresh Govindan ◽  
Mengjie Zhang ◽  
Ramzi J. Khairallah ◽  
Jody L. Martin ◽  
...  
Keyword(s):  
Protein C ◽  
Troponin I ◽  
Binding Protein ◽  
Cardiac Myosin ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Myosin Binding ◽  
Length Dependent Activation

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.

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