Myosin heavy chain isoform expression in the failing and nonfailing human heart

In the heart, the relative proportions of the 2 forms of the motor protein myosin heavy chain (MyHC) have been shown to be affected by a wide variety of pathological and physiological stimuli. Hearts that express the faster M yHC motor protein, alpha, produce more power than those expressing the slow er MyHC motor protein, beta, leading to the hypothesis that MyHC isoforms p lay a major role in the determination of cardiac contractility. We showed p reviously that a significant amount of alpha MyHC mRNA is expressed in nonf ailing human ventricular myocardium and that alpha MyHC mRNA expression is decreased 15-fold in end-stage failing left ventricles. In the present stud y, we determined the MyHC protein isoform content of human heart samples of known MyHC mRNA composition. We demonstrate that alpha MyHC protein was ea sily detectable in 12 nonfailing hearts. alpha MyHC protein represented 7.2 +/-3.2% of total MyHC protein (compared with approximate to 35% of the MyHC mRNA), suggesting that translational regulation may be operative; in contr ast, there was effectively no detectable alpha MyHC protein in the left ven tricles of 10 end-stage failing human hearts.