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pubmed-article:16380103pubmed:abstractTextBeta-adrenergic stimulation modulates cardiac contractility through protein kinase A (PKA), which phosphorylates proteins such as troponin I (cTnI) and C-protein (cMyBP-C). The relative contributions of cTnI and cMyBP-C to the regulation of myofilament Ca(2+) sensitivity are still controversial because of difficulty in targeting specific protein phosphorylation. Recently, impaired relaxation was found in cMyBP-C-deficient mice (KO) in vivo under basal conditions and after beta-adrenergic stimulation. The goal of this study was to analyse the length-dependent and PKA-dependent modulations of the cardiac contractile machinery in a mouse model lacking cMyBP-C.lld:pubmed
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pubmed-article:16380103pubmed:articleTitleLength and protein kinase A modulations of myocytes in cardiac myosin binding protein C-deficient mice.lld:pubmed
pubmed-article:16380103pubmed:affiliationINSERM U-637, CHU Arnaud de Villeneuve, F-34295 Montpellier, France. cazorla@montp.inserm.frlld:pubmed
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