Key result
Phosphorylation of cardiac troponin I at serines 23/24 shifted shallow length-tension relationships to steep relationships in striated muscle preparations.
Population
Rat cardiac myocyte preparation or skinned slow-twitch skeletal muscle fibre
Comparison
Exchange with unphosphorylated recombinant… vs Unphosphorylated recombinant cTn
Design
Preclinical
Authors
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May inform length-dependent force in animal models; leaves open human relevance and therapeutic targeting.
Phosphorylation of cardiac troponin I at serines 23/24 is a key regulator of the length dependence of force generation in striated muscle, providing a molecular basis for the Frank-Starling relationship.
Hanft et al. (2013) studied this question. PKA treatment or cTnI serines 23/24 mutation to aspartic acids vs. Unphosphorylated recombinant cTn was evaluated on Length-tension relationship steepness. Phosphorylation of cardiac troponin I at serines 23/24 shifted shallow length-tension relationships to steep relationships in striated muscle preparations.
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