Key result
Serine-to-aspartate substitutions in cMyBP-C failed to mimic the effects of tris-phosphorylation on thin filament activation, though they did mimic effects on myosin S2 binding.
Population
Ventricular trabeculae of rat heart and the expressed C1mC2 region of cMyBP-C
Comparison
Serine-to-aspartate substitutions in the… vs Tris-phosphorylation of the m-domain
Design
Preclinical
Authors
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Ser-Asp substitutions inadequately model phosphorylation effects; leaves open optimal phosphomimetics for cardiac thick filament studies.
Absolute Event Rate: 57% vs 0%
Serine-to-aspartate substitutions do not fully mimic the structural and functional effects of cMyBP-C phosphorylation in heart muscle, suggesting previous inferences based on these substitutions should be reconsidered.
Kampourakis et al. (2018) studied Cardiac muscle regulation. Serine-to-aspartate (S-D) substitutions in C1mC2 vs. Tris-phosphorylated C1mC2 and unphosphorylated C1mC2 was evaluated on Activation of contraction (isometric force) in the absence of calcium. Serine-to-aspartate substitutions in cMyBP-C failed to mimic the effects of tris-phosphorylation on thin filament activation, though they did mimic effects on myosin S2 binding.
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