Myosin isoenzymes in human hypertrophic hearts. Shift in atrial myosin heavy chains and in ventricular myosin light chains.

The myosin light chain complement and proteolytic peptide patterns of myosin heavy chains were studied by two-dimensional and one-dimensional electrophoretic techniques respectively, in a total of 57 samples from ventricular and atrial tissues of normal and hypertrophied human hearts. Hypertrophies were classified haemodynamically as due to pressure-overload and volume-overload. In addition to the occurrence of ventricular light chains in hypertrophied atria we also observed the atrial light chain-1 (ALC-1) in hypertrophied ventricular tissues. On average over 6% of total light-chain-1 comprised ALC-1 in pressure-overloaded ventricles and around 3% in volume-overloaded ventricles. In single cases of pressure-overload ALC-1 amounted up to over 20% of total light chain-1. With regard to the myosin heavy chains limited digestion by two different proteinases produced over 200 clearly resoluble peptides. The absence of any detectable differences in the peptide patterns between myosin heavy chains from normal and hypertrophic tissues of left or right ventricle is in line with the findings of J. J. Schier and R. S. Adelstein (J Clin Invest 1982; 69: 816-825). In atrial tissues however, reproducible qualitative differences in the peptide patterns indicated that during hypertrophy a different type of myosin heavy chains becomes expressed. No differences were seen between the myosin heavy chains from normal left and right atria.