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© 2000 American Heart Association, Inc.
Clinical Research |
Myosin Heavy Chain Isoform Expression in the Failing and Nonfailing Human Heart
From the Department of Molecular, Cellular and Developmental Biology (S.M., L.A.L.), University of Colorado (Boulder); and Division of Cardiology (W.M., M.B.), University of Colorado Health Science Center (Denver).
Correspondence to Dr Leslie A. Leinwand, Department of Molecular, Cellular and Developmental Biology, University of Colorado at Boulder, Campus Box 347, Boulder, CO 80309-0347. E-mail Leslie.Leinwand{at}colorado.edu
Abstract—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 MyHC motor protein, 
, produce more power than
those expressing the slower MyHC motor protein, ß, leading to the
hypothesis that MyHC isoforms play a major role in the determination of
cardiac contractility. We showed previously that a
significant amount of MyHC mRNA is expressed in nonfailing human
ventricular myocardium and that MyHC mRNA
expression is decreased 15-fold in end-stage failing left ventricles.
In the present study, we determined the MyHC protein isoform
content of human heart samples of known MyHC mRNA composition. We
demonstrate that MyHC protein was easily detectable in 12 nonfailing
hearts. MyHC protein represented 7.2±3.2% of total
MyHC protein (compared with 
35% of the MyHC mRNA), suggesting that
translational regulation may be operative; in contrast, there was
effectively no detectable MyHC protein in the left ventricles of 10
end-stage failing human hearts.
Key Words: myosin • heart failure • isoforms
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