Key result
Familial hypertrophic cardiomyopathy mutations in human cardiac myosin regulatory light chains dramatically alter Ca2+ binding and phosphorylation compared to wild-type.
Population
Human cardiac myosin regulatory light chains with familial hypertrophic cardiomyopathy mutations
Comparison
Mutations and phosphorylation vs Wild-type human cardiac myosin regulatory light…
Design
Preclinical
Authors
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May underlie contractile dysfunction in familial HCM; hypothesis-generating for mechanism-targeted therapies pending human studies.
Mutations in the regulatory light chain of human cardiac myosin associated with familial hypertrophic cardiomyopathy significantly alter calcium binding and phosphorylation, providing a molecular basis for the disease.
Szczȩsna et al. (2001) studied Familial hypertrophic cardiomyopathy. Familial hypertrophic cardiomyopathy mutations (A13T, F18L, E22K, R58Q, P95A) vs. Wild-type light chain was evaluated on Ca2+ binding properties, phosphorylation, and alpha-helical content. Familial hypertrophic cardiomyopathy mutations in human cardiac myosin regulatory light chains dramatically alter Ca2+ binding and phosphorylation compared to wild-type.
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