Modulation of crossbridge kinetics by myosin isoenzymes in skinned human heart fibers.
Skinned fibers from the normal human heart with the beta-myosin heavy chain (ventricular fibers) revealed both a higher force generation per cross section and a higher Ca2+ sensitivity than skinned fibers with the alpha-myosin heavy chain (atrial fibers). The relation between isometric ATPase activity and isometric tension of atrial fibers was higher than that of ventricular fibers. Since the ATPase-tension relation equals the rate constant for the transition from force-generating into non-force-generating crossbridge states (g(app)), myosin heavy chain isoenzymes seem to have different crossbridge turnover kinetics. Modulation of g(app) by myosin heavy chain isoenzymes could explain the different contractile behavior of atrial and ventricular fibers. g(app) was independent of Ca2+.
Morano
I
I
Department of Physiology II, University of Heidelberg, FRG.
Bletz
C
C
Wojciechowski
R
R
Rüegg
J C
JC
D000251:Adenosine Triphosphatases / Q000378:metabolism; D002118:Calcium / Q000378:metabolism; D006321:Heart / Q000502:physiology*; D006325:Heart Atria; D006352:Heart Ventricles; D006652:Histological Techniques; D006801:Humans; D007700:Kinetics; D008955:Models, Cardiovascular; D009200:Myocardial Contraction; D009206:Myocardium / Q000378:metabolism; D009218:Myosins / Q000502:physiology*; D009994:Osmolar Concentration
D000251:Adenosine Triphosphatases; D009218:Myosins; D002118:Calcium