Key result
Cardiac myosin in asymmetric septal hypertrophy shows no structural or enzymatic differences versus normal controls.
Why the study?
The genetic defect in subjects with asymmetric septal hypertrophy may affect structural and functional characteristics of cardiac myosin, which required investigation.
Observational
Myosin properties unchanged in ASH; leaves open whether other sarcomeric defects drive the phenotype in this low-evidence comparison.
Human cardiac myosin isolated from operatively obtained samples of ventricular septum and left ventricular free wall of subjects with asymmetric septal hypertrophy (ASH) was compared, with respect to structural and enzymatic properties, to myosin isolated from hearts of subjects without heart disease. The following parameters were studied: (1) activation of myosin ATPase activity by K+-EDTA and Ca2+, (2) molecular weight of the heavy and light chains of myosin as determined by electrophoretic migration in polyacrylamide-sodium dodecyl sulfate (SDS) gels and (3) ability to form bipolar aggregates at low ionic strength, as examined by electron microscopy. No difference was present in any of these parameters between human cardiac myosin from subjects with ASH and from subjects without heart disease. Thus, the genetic defect present in subjects with ASH is not expressed in the particular structural and functional characteristics of myosin evaluated in this study.
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Maron et al. (1977) conducted an observational in Asymmetric septal hypertrophy (ASH). Asymmetric septal hypertrophy (ASH) vs. Subjects without heart disease was evaluated on Structural and enzymatic properties of cardiac myosin (ATPase activity, molecular weight, bipolar aggregate formation). Cardiac myosin from subjects with asymmetric septal hypertrophy showed no differences in structural or enzymatic properties compared to myosin from subjects without heart disease.
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