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. 2007 Aug;43(2):223-9.
doi: 10.1016/j.yjmcc.2007.05.003. Epub 2007 May 13.

Decreased phosphorylation levels of cardiac myosin-binding protein-C in human and experimental heart failure

Ali El-Armouche  1 , Lutz Pohlmann, Saskia Schlossarek, Jutta Starbatty, Yung-Hsin Yeh, Stanley Nattel, Dobromir Dobrev, Thomas Eschenhagen, Lucie Carrier
Affiliations

Decreased phosphorylation levels of cardiac myosin-binding protein-C in human and experimental heart failure

Ali El-Armouche et al. J Mol Cell Cardiol. 2007 Aug.

Abstract

Cardiac myosin-binding protein-C (cMyBP-C) is an important regulator of cardiac contractility, and its phosphorylation by PKA is a mechanism that contributes to increased cardiac output in response to beta-adrenergic stimulation. It is presently unknown whether heart failure alters cMyBP-C phosphorylation. The present study determined the level of phosphorylated cMyBP-C in failing human hearts and in a canine model of pacing-induced heart failure. A polyclonal antibody directed against the major phosphorylation site of cMyBP-C (Ser-282) was generated and its specificity was confirmed by PKA phosphorylation with isoprenaline in cardiomyocytes and Langendorff-perfused mouse hearts. Left ventricular myocardial tissue from (i) patients with terminal heart failure (hHF; n=12) and nonfailing donor hearts (hNF; n=6) and (ii) dogs with rapid-pacing-induced end-stage heart failure (dHF; n=10) and sham-operated controls (dNF; n=10) were used for quantification of total cMyBP-C and phospho-cMyBP-C by Western blotting. Total cMyBP-C protein levels were similar in hHF and hNF as well as in dHF and dNF. In contrast, the ratio of phospho-cMyBP-C to total cMyBP-C levels were >50% reduced in hHF and >40% reduced in dHF. In summary, cMyBP-C phosphorylation levels are markedly decreased in human and experimental heart failure. Thus, the compromised contractile function of the failing heart might be in part attributable to reduced cMyBP-C phosphorylation levels.

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