Circulation Research. 2002;90:1150-1152
Published online before print May 23, 2002, doi: 10.1161/01.RES.0000022879.57270.11
Published online before print May 23, 2002, doi: 10.1161/01.RES.0000022879.57270.11
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© 2002 American Heart Association, Inc.
Reports |
Small Amounts of 
-Myosin Heavy Chain Isoform Expression Significantly Increase Power Output of Rat Cardiac Myocyte Fragments
From the Department of Physiology, University of Missouri School of Medicine, Columbia, Mo. Dr Herron’s present address is Centre for Cardiovascular Biology & Medicine, King’s College London, The Rayne Institute, St Thomas Hospital, London SE1 7EH, UK.
Correspondence to Kerry S. McDonald, PhD, Department of Physiology, School of Medicine, University of Missouri, Columbia, MO. E-mail mcdonaldks{at}health.missouri.edu
Abstract
Myocardial performance is likely affected by the relative expression of the two myosin heavy chain (MyHC) isoforms, namely 
-MyHC and ß-MyHC. The relative expression of each isoform is regulated developmentally and in pathophysiological states. Many pathophysiological states are associated with small shifts in the relative expression of each MyHC isoform, yet the functional consequence of these shifts remains unclear. The purpose of this study was to determine the functional effect of a small shift in the relative expression of -MyHC. To this end, power output was measured in rat cardiac myocyte fragments that expressed 
12% -MyHC and in myocyte fragments that expressed 0% -MyHC, as determined in the same cells by SDS-PAGE analysis after mechanical experiments. Myocyte fragments expressing 12% -MyHC developed 52% greater peak normalized power output than myocyte fragments expressing 0% -MyHC. These results indicate that small amounts of -MyHC expression significantly augment myocyte power output.
Key Words: myosin heavy chain • cardiac myocytes • power output • sarcomeric proteins • myocardial performance
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