Modelling the mechanical properties of cardiac muscle
Progress in Biophysics and Molecular BiologyPublished 1 March 1998
Peter Hunter, Andrew D. McCulloch, Henk E.D.J. ter Keurs
Citations461
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Abstract
A model of passive and active cardiac muscle mechanics is presented, suitable for use in continuum mechanics models of the whole heart. The model is based on an extensive review of experimental data from a variety of preparations (intact trabeculae, skinned fibres and myofibrils) and species (mainly rat and ferret) at temperatures from 20 to 27°C. Experimental tests include isometric tension development, isotonic loading, quick-release/restretch, length step and sinusoidal perturbations. We show that all of these experiments can be interpreted with a four state variable model which includes (i) the passive elasticity of myocardial tissue, (ii) the rapid binding of Ca2+ to troponin C and its slower tension-dependent release, (iii) the kinetics of tropomyosin movement and availability of crossbridge binding sites and the length dependence of this process and (iv) the kinetics of crossbridge tension development under perturbations of myofilament length.
Keywords
Medicine
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47 Citations1998Bruno D. Stuyvers, Makoto Miura +2 more
Results are consistent with the hypothesis that the Ca(2+)-sensitivity of the sarcomeres at [Ca2+] < 200 nM, i.e. where the myocytes in intact muscle operate during diastole, involves an association between titin molecules and the thin filament.
Biophysical JournalPhosphate release and force generation in cardiac myocytes investigated with caged phosphate and caged calcium
47 Citations1996Alexandre Herculano Borges Araújo, Jeffery W. Walker
Data from both types of measurements suggest that kinetic transitions associated with P(i) dissociation are modulated by the Ca(2+) regulatory system and partially limit the physiological rate of tension development in cardiac muscle.
American Journal of Physiology-Heart and Circulatory PhysiologyKinetics of tension development in skinned cardiac myocytes measured by photorelease of Ca2+
47 Citations1994Alexandre Herculano Borges Araújo, Jeffery W. Walker
It is concluded that significant differences exist between cardiac and fast-twitch skeletal muscles in terms of the effects of Ca2+ and Mg2+ on contraction kinetics and that these differences cannot be attributed solely to differences in TNC isoforms.
Circulation ResearchPositive Inotropy Mediated by Diacylglycerol in Rat Ventricular Myocytes
46 Citations1997YeQing Pi, R. Sreekumar +2 more
The data provide evidence that diacylglycerol can induce a strong positive inotropic effect in mammalian ventricular muscle, possibly by activating protein kinase C, and postulate that diC8 has distinct physiological actions at intracellular and extracellular sites.
Journal of Muscle Research and Cell MotilityCalcium binding and fluorescence measurements of dansylaziridine-labelled troponin C in reconstituted thin filaments
43 Citations1987Henry G. Zot, James D. Potter
The binding of Ca2+ to either low-affinity site is concluded to produce the fluorescence change of thin filaments reconstituted with TnCDANZ, in comparison with the low-Affinity sites of isolated Troponin and troponin-tropomyosin complex.
Circulation ResearchCa2+ and segment length dependence of isometric force kinetics in intact ferret cardiac muscle.
43 Citations1993William O. Hancock, Donald A. Martyn +1 more
Differences in the activation dependence of the force redevelopment rate between cardiac and skeletal muscle suggest that there are fundamental differences in the mechanism of Ca2+ activation between these two muscle types.
Advances in experimental medicine and biologyMyocardial Constitutive Laws for Continuum Mechanics Models of the Heart
43 Citations1995Peter Hunter
Biophysical JournalContinuum rheology of muscle contraction and its application to cardiac contractility
40 Citations1985Aydın Tözeren
The present analysis introduces a new interpretation of the index of contractility (dP/dt)/P used in cardiac literature and shows that this index may not be related at all to the maximum speed of shortening and that it may be dependent on both preload and afterload.
Modeling Mechanical-Electrical Transduction in the Heart
38 Citations1994Frederick Sachs
The rate and rhythm of the heart is sensitive to mechanical deformation and stretching alters action potential configuration and can cause quiescent tissue to become spontaneously active and cause the generation of extra systoles.
Journal of Biological ChemistryFast skeletal muscle skinned fibers and myofibrils reconstituted with N-terminal fluorescent analogues of troponin C.
38 Citations1986Henry G. Zot, K. Gūth +1 more
The results presented suggest that the Ca2+ affinity of theCa2+-specific sites of Troponin are reduced in the thin filament compared to that of troponin in solution.
Journal of BiomechanicsMechanics of cardiac muscle, based on Huxley's model: Simulation of active state and force-velocity relation
35 Citations1972Alan Y.K. Wong
Hill's three-component model for cardiac muscle, incorporating Huxley's sliding filament theory for the contractile element (CE) is extended to study the forcevelocity relation, finding the hyperbolic relation is not found in force-velocity curve obtained by afterloaded isotonic contraction.
Biophysical JournalRelaxation from rigor of skinned trabeculae of the guinea pig induced by laser photolysis of caged ATP
34 Citations1994Hunter Martin, Robert Barsotti
Results are consistent with the hypothesis that the presence of MgADP bound cross-bridges suppresses the inhibition normally imposed by the thin filament regulatory system in the absence of calcium ions and allows cross-bridge rebinding and force production during relaxation from rigor.
Biophysical JournalInfluence of Ca2+ on force redevelopment kinetics in skinned rat myocardium
32 Citations1996William O. Hancock, Donald A. Martyn +2 more
The lack of activation dependence of ktr contrasts with results from fast skeletal fibers, in which ktr varies 10-fold from low to high activation levels, and suggests that Ca2+ does not modulate the kinetics of cross-bridge attachment or detachment in mammalian cardiac muscle.
PhysiologyMechanical Modulation of the Ca2+ Regulatory Protein Complex in Cardiac Muscle
23 Citations1995Franklin Fuchs
The regulatory protein complex of cardiac myofilaments serves as a pathway through which changes in load or length can modify Ca2+ regulation, and may be an important component of the steep force-length relationship in the myocardium.
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