Cardiac myosin binding protein C phosphorylation in cardiac disease.

Abstract

Perturbations in sarcomeric function may in part underlie systolic and diastolic dysfunction of the failing heart. Sarcomeric dysfunction has been ascribed to changes in phosphorylation status of sarcomeric proteins caused by an altered balance between intracellular kinases and phosphatases during the development of cardiac disease. In the present review we discuss changes in phosphorylation of the thick filament protein myosin binding protein C (cMyBP-C) reported in failing myocardium, with emphasis on phosphorylation changes observed in familial hypertrophic cardiomyopathy caused by mutations in MYBPC3. Moreover, we will discuss assays which allow to distinguish between functional consequences of mutant sarcomeric proteins and (mal)adaptive changes in sarcomeric protein phosphorylation.

• Authors: Diederik W D Kuster, Amira Cholid Bawazeer, Ruud Zaremba, Max Goebel, Nicky M Boontje, Jolanda van der Velden
• Journal: Journal of muscle research and cell motility (J Muscle Res Cell Motil) Vol. 33 Issue 1 Pg. 43-52 (May 2012) ISSN: 1573-2657 [Electronic] Netherlands
• PMID: 22127559 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)

Chemical References

• Carrier Proteins
• myosin-binding protein C
• Cyclic AMP-Dependent Protein Kinases
• Phosphoric Monoester Hydrolases
• Calcium

Topics

• Animals
• Calcium (metabolism)
• Cardiomyopathy, Hypertrophic, Familial (genetics, metabolism, pathology)
• Carrier Proteins (genetics, metabolism)
• Cyclic AMP-Dependent Protein Kinases (metabolism)
• Heart Failure, Systolic (metabolism, pathology)
• Humans
• Mice
• Mice, Transgenic
• Mutation
• Myocardium (metabolism, pathology)
• Myocytes, Cardiac (metabolism, pathology)
• Phosphoric Monoester Hydrolases (metabolism)
• Phosphorylation
• Sarcomeres (metabolism, pathology)