Key result
Amino acid substitutions causing hydrophobic imbalance in the cytoplasmic domain of phospholamban resulted in loss of function and dominant negative effects on SERCA.
Population
Preclinical model (in vitro study of phospholamban and SERCA)
Comparison
Amino acid substitutions in the cytoplasmic… vs Wild-type phospholamban (PLN)
Design
Preclinical
Authors
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Supports hydrophobic imbalance as driver of phospholamban dysfunction in models; leaves open translation to human dilated cardiomyopathy.
Hydrophobic imbalance in the cytoplasmic domain of phospholamban explains the loss of function and dominant negative effect on SERCA seen in mutations associated with lethal dilated cardiomyopathy.
Ceholski et al. (2012) studied Dilated cardiomyopathy. Amino acid substitutions in the cytoplasmic domain of phospholamban (PLN) vs. Wild-type PLN was evaluated on Ability to inhibit SERCA. Amino acid substitutions causing hydrophobic imbalance in the cytoplasmic domain of phospholamban resulted in loss of function and dominant negative effects on SERCA.
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