Fink et al., Circ Res 2001
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The increase in PKA dependent phosphorylation of troponin I and myosin binding protein C on isoproterenol stimulation was significantly reduced in Ht31 expressing cells compared with controls
Herron et al., Circ Res 2001
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Consistent with previous studies, PKA increased phosphorylation levels of myosin binding protein C and troponin I, and reduced Ca ( 2+ ) sensitivity of force
Konhilas et al., J Physiol 2003
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To clarify the role of PKA dependent phosphorylation of TnI and MyBP-C on LDA in the heart, we examined LDA in skinned myocytes from a non-transgenic ( NTG ) and a transgenic murine model in which the native cardiac isoform ( cTnI ) was completely replaced by the slow skeletal isoform of TnI ( ssTnI-TG ) lacking the phosphorylation sites for PKA, while retaining PKA sites on MyBP-C
Hanft et al., Am J Physiol Heart Circ Physiol 2009
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PKA increased the phosphorylation of myosin binding protein C and cardiac troponin I, as assessed by autoradiography