Myosin heavy chain composition and the economy of contraction in healthy and diseased human myocardium

• DOI: 10.1007/s10974-005-9005-x
• Publication Date: 2005-08-08T03:31:33Z
• Authors: N.A. Narolska; S. Eiras; R.B. van Loon; N.M. Boontje; R. Zaremba; S.R. Spiegelen berg; W. Stooker; M.A.J.M. Huybregts; F.C. Visser; J. van der Velden; G.J.M. Stienen
• Keywords: Male; 0303 health sciences; Myosin Heavy Chains; Biopsy; Myocardium; Heart; Myocardial Contraction; 03 medical and health sciences; Adenosine Triphosphate; Atrial Fibrillation; Chronic Disease; Humans; Protein Isoforms; Arrhythmia, Sinus; Electrophoresis, Polyacrylamide Gel; Female

Changes in myosin heavy chain (MHC) isoform expression and protein composition occur during cardiac disease and it has been suggested that even a minor shift in MHC composition may exert a considerable effect on myocardial energetics and performance. Here an overview is provided of the cellular basis of the energy utilisation in cardiac tissue and novel data are presented concerning the economy of myocardial contraction in diseased atrial and ventricular human myocardium. ATP utilisation and force development were measured at various Ca(2+) concentrations during isometric contraction in chemically skinned atrial trabeculae from patients in sinus rhythm (SR) or with chronic atrial fibrillation (AF) and in ventricular muscle strips from non-failing donor or end-stage failing hearts. Contractile protein composition was analysed by one-dimensional gel electrophoresis. Atrial fibrillation was accompanied by a significant shift from the fast alpha-MHC isoform to the slow beta-MHC isoform, whereas both donor and failing ventricular tissue contained almost exclusively the beta-MHC isoform. Simultaneous measurements of force and ATP utilisation indicated that economy of contraction is preserved in atrial fibrillation and in end-stage human heart failure.