Abstract
A comprehensive dynamic model of the excitation contraction coupling, developed for a single cardiac muscle, is extended to a multi-cell system (duplex). The model defines the mechanical activation level based on calcium kinetics and crossbridge cycling and emphasizes the central role of the troponin regulatory proteins in regulating muscle activity. The intracellular control mechanism includes two feedback loops that affect the affinity of troponin for calcium and the crossbridge cycling. The model is used to simulate the basic mechanical characteristics of the cardiac muscle, i. e. the force-length and the force-velocity relationships, and describes their dependence on the mechanical activation level. The two-cell duplex unit is used to study the influence of inter-cellular interactions and the effect of inhomogeneity on muscle performance, due to non-uniformity in the electrical stimulation or inhomogeneity in calcium kinetics. Better understanding of the performance of the inhomogeneous muscle is obtained due to our ability to describe the control of the activation level in each cell.
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References
Beyar R, Sideman S. A computer study of the left ventricular performance based on fiber structure, sarcomere dynamics, and transmural electrical propagation velocity. Circ Res 1984; 55: 358–375.
Pietrabissa R, Montevecchi FM, Fumero R. Mechanical characterization of a model of a multicomponent cardiac fiber. J Biomed Eng 1991; 13: 407–414.
Wong ALK. Mechanics of cardiac muscle, based on Huxley’s model: mathematical simulation of isometric contraction. J Biomechanics 1971; 4: 529–540.
Ford EL. Mechanical manifestations of activation in cardiac muscle. Circ Res 1991; 68: 621–637.
Zahalak IG, Shi-ping MA. Muscle activation and contraction: constitutive relations based directly on crossbridge kinetics. J Biomechan Eng 1990; 112: 52–62.
Beyar R, Sideman S. Atrioventricular interaction: a computer study. Am J Physiol 1987; 252: H653–H665.
Huxley AF. Muscle structure and theories of contraction. Prog Biophys Biophys Chem 1957; 7: 255–318.
Eisenberg E, Hill TL. Muscle contraction and free energy transduction in biological system. Science 1985; 227: 999–1006.
Landesberg A, Sideman S. Coupling calcium binding to Troponin-C and crossbridge cycling kinetics in skinned cardiac cells. Am J Physiol 1992; submitted.
Hofmann PA, Fuchs F. Effect of length and crossbridge attachment on Ca2+ binding to cardiac troponin-C. Am J Physiol 1987; 253: C90–C96.
Hofmann PA, Fuchs F. Evidence for force-dependent component of calcium binding to cardiac troponin-C. Am J Physiol 1987; 253: C541–0546.
Kentish JC, ter Keurs HED, Noble MIM, Ricciardi L. The relationship between force, calcium and sarcomere length in skinned trabeculae from rat ventricle. J Physiol 1983; 345: 24P.
Hibberd MG, Jewell BR. Calcium and length-dependent force production in rat ventricular muscle. J Physiol 1982; 329: 527–540.
Brenner B, Eisenberg E. The mechanism of muscle contraction. Biochemical, mechanical, and structural approaches to elucidate crossbridge action in muscle. Basic Res Cardiol 1987; 82(Suppl. 2): 2–16.
Brenner B, Eisenberg E. Rate of force generation in muscle: correlation with actomyosin Atpase activity in solution. Proc Nall Acad Sci 1986; 83: 3542–3546.
Chalovich JM, Eisenberg E. The effect of troponin - tropomyosin on the binding of heavy meromyosin to actin in the presence of ATP. J Biol Chem 1986; 261: 5088–5093.
Grabarek Z, Grabarek J, Leavis PJ, Gergely J. Cooperative binding to Ca - specific sites of troponin C in regulated actin and actomyosin. J Biol Chem 1983; 258: 14098–14102.
Greene LE, Eisenberg E. Relationship between regulated actomyosin ATPase activity and cooperative binding of myosin to regulated actin. Cell Biophys 1988; 12: 59–71.
Guth K, Potter JD. Effect of rigor and cycling crossbridges on the structure of troponin-C and on the Ca2+ affinity of the Ca2+-specific regulatory sites in skinned rabbit spoas fibers. J Biol Chem 1987; 262: 15883–15890.
Williams DL, Greene LE, Eisenberg E. Cooperative turning on of myosin subfragment-1 ATPase activity by the troponin-tropomyosin-actin complex. Biochemistry 1988; 27: 6987–6993.
Stephenson DG, Stewart AW, Wilson GJ. Dissociation of force from myofibrillar MgATPase and stiffness at short sarcomere length in rat and toad skeletal muscle. J Physiol 1989; 410: 351–366.
Brenner B. Rapid dissociation and reassociation of actomyosin crossbridge during force generation: A newly observed facet of crossbridges action in muscle. Proc Natl Acad Sci 1991; 88: 10490–10494.
Lee JA, Allen DG. EMD 53998 Sensitizes the contractile proteins to calcium in intact ferret ventricular muscle. Circ Res 1991; 69: 927–936.
Allen DG, Smith GL. The first calcium transient following shortening in isolated ferret ventricular muscle. J Physiol 1985; 366: 83P.
Allen DG, Kurihara S. The effect of muscle length on intracellular calcium transient in mammalian cardiac muscle. J Physiol 1981; 327: 79–94.
Allen DG, Kentish JC. The cellular basis of the length-tension regulation in cardiac muscle. J Mol and Cellular Biol 1985; 17: 821–840.
Braunwald E. Heart Disease, A Textbook of Cardiovascular Medicine, third, edition. 1988; pp 394–401.
ter Keurs HEDJ, de Tombe PP. The velocity of sarcomere shortening in mammalian myocardium (abstract). The 10th Int Conf Cardiovasc System Dynamics Soc, Japan, September 1992.
Brutsaert DL, Sys SU, Rademakers FE. Triple control of relaxation: implications in cardiac disease. Circulation 1984; 69: 190–196.
Lab MJ, Allen DG, Orchard CH. The effect of shortening on myoplasmic calcium concentration and on action potential in mammalian ventricular muscle. Circ Res 1984; 55: 825–829.
Blink JR, Endo M. Modification of myofibrillar responsiveness to Ca++as an inotropic mechanism. Circulation 1986; 73: suppl-III, 85–98.
Blanchard EM, Solaro J. Inhibition of the activation and troponin calcium binding of dog cardiac myofibrils by acid pH. Circ Res 1984; 55: 382–391.
Wiegner AW, Allen GJ, Bing OHL. Weak and strong myocardium in series: implications for segmental dysfunction. Am J Physiol 1978; 4(6): H776–H783.
Zahalak IG. Modeling muscle mechanics (and energetics). In: Multiple Muscle System: Biomechanics and Movement Organization, Winters JM and Woo SLY (eds). Springer-Verlag: NY. 1990, pp 1–23.
Zahalak IG. A distribution-moment approximation for kinetic theories of muscle contraction. Mathematical Biosience, kinetics. Mathematical Biosience 1981; 55: 89–114.
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Landesberg, A., Sideman, S. (1993). Calcium Kinetic and Mechanical Regulation of the Cardiac Muscle. In: Sideman, S., Beyar, R. (eds) Interactive Phenomena in the Cardiac System. Advances in Experimental Medicine and Biology, vol 346. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2946-0_7
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DOI: https://doi.org/10.1007/978-1-4615-2946-0_7
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