Key result
PKC phospho-mimetic cMyBP-C exhibited a significant decrease in active force, cross-bridge kinetics, Mg2+-ATPase activity, and myofilament Ca2+ sensitivity in vitro compared to controls.
Population
Recombinant proteins, yeast-2-hybrid clones expressing cMyBP-C variants, and skinned ventricular fibers
Comparison
PKC-mediated phosphorylation at Ser273/302 vs Controls (cMyBP-CWT, cMyBP-CADA)
Design
Preclinical
Authors
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PKC-cMyBP-C phosphorylation may modulate contractility; hypothesis-generating in animal models, clinical relevance remains open pending in vivo data.
PKC-mediated phosphorylation of cMyBP-C at Ser273/302 decreases its interaction with actin and reduces active force and cross-bridge kinetics, highlighting its role in regulating sarcomere contractility.
Govindan et al. (2014) studied this question. PKC phospho-mimetic cMyBP-CDAD vs. Controls (cMyBP-CWT, cMyBP-CADA) was evaluated on Active force, cross-bridge kinetics, Mg2+-ATPase activity, and myofilament Ca2+ sensitivity. PKC phospho-mimetic cMyBP-C exhibited a significant decrease in active force, cross-bridge kinetics, Mg2+-ATPase activity, and myofilament Ca2+ sensitivity in vitro compared to controls.
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