Abstract
In order to study the mechanical contraction and energy consumption by the cardiomyocytes we further developed an actomyosin model of Vendelin et al. (Ann. Biomed. Eng. 28:629–640, 2000). The model is of a self-consistent Huxley-type and is based on Hill formalism linking the free energy profile of reactions and mechanical force. In several experimental studies it has been shown that the dependency between oxygen consumption and stress-strain area is linear and is the same for isometric and shortening contractions. We analyzed the free energy profiles of actomyosin interaction by changing free energies of intermediate states and activation of different reactions. The model is able to replicate the linear dependence between oxygen consumption and stress-strain area together with other important mechanical properties of a cardiac muscle.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Similar content being viewed by others
References
Boudina S, Laclau M, Tariosse L, Daret D, Gouverneur G, Bonoron-Adèle S, Saks V, Santos PD (2002) Alteration of mitochondrial function in a model of chronic ischemia in vivo in rat heart. Am J Physiol, Heart Circ Physiol 282:821–831
Brutsaert DL, Clerck NMD, Goethals MA, Housmans PR (1978) Relaxation of ventricular cardiac muscle. J Physiol (Lond) 283:469–480
Cooke R, Pate E (1985) The effects of ADP and phosphate on the contraction of muscle fibers. Biophys J 48:789–798
Delhaas T, Arts T, Prinzen FW, Reneman RS (1994) Regional fibre stress-fibre strain area as an estimate of regional blood flow and oxygen demand in the canine heart. J Physiol (Lond) 477:481–496
Eisenberg E, Hill TL, Chen Y (1980) Cross-bridge model of muscle contraction. Quantitative analysis. Biophys J 29:195–227
Gibbs CL, Barclay CJ (1995) Cardiac efficiency. Cardiovasc Res 30:627–634
Hill TL (1974) Theoretical formalism for the sliding filament model of contraction of striated muscle. Part I. Prog Biophys Mol Biol 28:267–340
Hisano R, Cooper G (1987) Correlation of force-length area with oxygen consumption in ferret papillary muscle. Circ Res 61:318–328
Janssen PM, Hunter WC (1995) Force, not sarcomere length, correlates with prolongation of isosarcometric contraction. Am J Physiol 269:676–685
Jepihhina N, Beraud N, Sepp M, Birkedal R, Vendelin M (2011) Permeabilized rat cardiomyocyte response demonstrates intracellular origin of diffusion obstacles. Biophys J 101:2112–2121
Jewell BR (1977) A reexamination of the influence of muscle length on myocardial performance. Circ Res 40:221–230
Kaasik A, Veksler V, Boehm E, Novotova M, Minajeva A, Ventura-Clapier R (2001) Energetic crosstalk between organelles: architectural integration of energy production and utilization. Circ Res 89:153–159
Kay L, Saks VA, Rossi A (1997) Early alteration of the control of mitochondrial function in myocardial ischemia. J Mol Cell Cardiol 29:3399–3411
Landesberg A, Sideman S (2000) Force-velocity relationship and biochemical-to-mechanical energy conversion by the sarcomere. Am J Physiol, Heart Circ Physiol 278:1274–1284
Månsson A (2010) Actomyosin-ADP states, interhead cooperativity, and the force-velocity relation of skeletal muscle. Biophys J 98:1237–1246
Pate E, Cooke R (1989) A model of crossbridge action: the effects of ATP, ADP and Pi. J Muscle Res Cell Motil 29:181–196
Ramay H, Vendelin M (2009) Diffusion restrictions surrounding mitochondria: a mathematical model of heart muscle fibers. Biophys J 97:443–452
Saks V, Kuznetsov A, Andrienko T, Usson Y, Appaix F, Guerrero K, Kaambre T, Sikk P, Lemba M, Vendelin M (2003) Heterogeneity of ADP diffusion and regulation of respiration in cardiac cells. Biophys J 84:3436–3456
Sepp M, Vendelin M, Vija H, Birkedal R (2010) ADP compartmentation analysis reveals coupling between pyruvate kinase and ATPases in heart muscle. Biophys J 98:2785–2793
Suga H (1990) Ventricular energetics. Physiol Rev 70:247–277
Taylor TW, Goto Y, Hata K, Takasago T, Saeki A, Nishioka T, Suga H (1993a) Comparison of the cardiac force-time integral with energetics using a cardiac muscle model. J Biomech 26:1217–1225
Taylor TW, Goto Y, Suga H (1993b) Variable cross-bridge cycling-ATP coupling accounts for cardiac mechanoenergetics. Am J Physiol 264:994–1004
Tobacman LS, Sawyer D (1990) Calcium binds cooperatively to the regulatory sites of the cardiac thin filament. J Biol Chem 265:931–939
Tran K, Smith N, Loiselle D, Crampin E (2010) A metabolite-sensitive, thermodynamically constrained model of cardiac cross-bridge cycling: implications for force development during ischemia. Biophys J 98:267–276
Velden JV, Moorman AF, Stienen GJ (1998) Age-dependent changes in myosin composition correlate with enhanced economy of contraction in guinea-pig hearts. J Physiol (Lond) 507:497–510
Vendelin M, Birkedal R (2008) Anisotropic diffusion of fluorescently labeled ATP in rat cardiomyocytes determined by raster image correlation spectroscopy. Am J Physiol, Cell Physiol 295:1302–1315
Vendelin M, Bovendeerd PHM, Arts T, Engelbrecht J, van Campen DH (2000) Cardiac mechanoenergetics replicated by cross-bridge model. Ann Biomed Eng 28:629–640
Vendelin M, Bovendeerd PHM, Engelbrecht J, Arts T (2002) Optimizing ventricular fibers: uniform strain or stress, but not ATP consumption, leads to high efficiency. Am J Physiol, Heart Circ Physiol 283:H1072–H1081
Vendelin M, Eimre M, Seppet E, Peet N, Andrienko T, Lemba M, Engelbrecht J, Seppet E, Saks V (2004). Intracellular diffusion of adenosine phosphates is locally restricted in cardiac muscle. Mol Cell Biochem 256–257:229–241
Vendelin M, Hoerter J, Mateo P, Soboll S, Gillet B, Mazet J (2010). Modulation of energy transfer pathways between mitochondria and myofibrils by changes in performance of perfused heart. J Biol Chem 285:37240–37250
Ventura-Clapier R, Mekhfi H, Vassort G (1987) Role of creatine kinase in force development in chemically skinned rat cardiac muscle. J Gen Physiol 89:815–837
Zahalak GI, Ma SP (1990) Muscle activation and contraction: constitutive relations based directly on cross-bridge kinetics. J Biomech Eng 112:52–62
Acknowledgements
This research was supported by the European Union through the European Regional Development Fund and by the Estonian Science Foundation (Grant nr. 7344).
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2013 Springer Science+Business Media Dordrecht
About this paper
Cite this paper
Kalda, M., Peterson, P., Engelbrecht, J., Vendelin, M. (2013). A Cross-Bridge Model Describing the Mechanoenergetics of Actomyosin Interaction. In: Holzapfel, G., Kuhl, E. (eds) Computer Models in Biomechanics. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-5464-5_7
Download citation
DOI: https://doi.org/10.1007/978-94-007-5464-5_7
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-007-5463-8
Online ISBN: 978-94-007-5464-5
eBook Packages: EngineeringEngineering (R0)