Comparison of myosin heavy chains in atria and ventricles from hyperthyroid, hypothyroid, and euthyroid rabbits.

The structural similarities of the heavy chains (HC) of myosin isolated from atria and ventricles of hyper-, hypo-, and euthyroid rabbits were compared by immunological analysis, by one- and two-dimensional peptide mapping, and by electrophoresis under nondenaturing conditions. Monoclonal and polyclonal antibodies, which are specific for HC alpha of ventricular myosin, cross-reacted equally with the HCs of euthyroid atrial myosin. Our immunological analysis identified multiple epitopes common to euthyroid atrial HC and ventricular HC alpha. One- and two-dimensional gel electrophoretic analysis of peptides produced by partial proteolytic digestion of each type of HC reveal no differences between euthyroid atrial HCs and ventricular HC alpha, whereas marked differences are apparent between atrial HC and ventricular HC beta. Nondenaturing gel electrophoresis separates ventricular myosin from hyper- and hypothyroid rabbits into two forms, V1 and V3, respectively. In euthyroid atria, two isomyosins, A1 and A2, were resolved; with the slower moving A2 isomyosin having the same mobility as that of the V1 isomyosin. After cross-hybridization of light chains of ventricular myosin with euthyroid atrial HCs, only a single band having a mobility identical with that of the V1 isomyosin was seen. Furthermore, atrial myosin HCs isolated from hyper- and hypothyroid rabbits were indistinguishable from euthyroid atrial HC and from ventricular HC alpha by these procedures. We conclude that ventricular HC alpha and atrial HC are indistinguishable proteins, and that the type of HC expressed in the atria is unaffected by the thyroid state of the rabbit.