Key result
Deletion of muscle LIM protein in mice led to significantly increased peak systolic intracellular Ca2+ (603 vs 349 nM) and diminished fractional shortening despite normal or enhanced SR Ca2+ function.
Why the study?
Does deletion of muscle LIM protein alter myocyte contractility and calcium handling in mice?
Population
Left ventricular myocytes from mice deficient in muscle LIM protein (MLPKO) and wild-type (WT) mice
Comparison
Deletion of muscle LIM protein (MLPKO) vs Wild-type (WT) mice
Design
Preclinical
Authors
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MLP deletion uncouples Ca2+ from contractility via myofilament effects in mice; leaves open relevance to human cardiomyopathy mechanisms.
Does deletion of muscle LIM protein alter myocyte contractility and calcium handling in mice?
Absolute Event Rate: 603% vs 349%
Deletion of muscle LIM protein in mice leads to depressed contractility due to reduced Ca2+-induced shortening and myofibril disorganization, despite normal or enhanced SR Ca2+ handling.
Su et al. (2001) studied Dilated cardiomyopathy. Deletion of muscle LIM protein (MLPKO) vs. Wild-type (WT) was evaluated on Peak systolic intracellular Ca2+ concentration ([Ca2+]i). Deletion of muscle LIM protein in mice led to significantly increased peak systolic intracellular Ca2+ (603 vs 349 nM) and diminished fractional shortening despite normal or enhanced SR Ca2+ function.
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