5. Summary
During muscle contraction and relaxation, Ca2+ moves through a cycle. About 20 to 40% of the ATP utilized in a twitch or a tetanus is utilized by the SR Ca2+ pump to sequester Ca2+. Parvalbumin is a soluble Ca2+ binding protein that functions in parallel with the SR Ca2+ pump to promote relaxation in rapidly contracting and relaxing skeletal muscles, especially at low temperatures. The rate of Ca2+ dissociation from troponin C, once thought to be much more rapid than the rate of relaxation, is likely to be similar to the rate of cross-bridge detachment and to the rate of muscle relaxation under some conditions. During the past fifty years, great progress has been made in understanding the Ca2+ cycle during skeletal muscle contraction and relaxation. Nonetheless, there are still mysteries waiting to be unraveled.
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6. References
A.V. Hill, The heat of activation and the heat of shortening in a muscle twitch, Proc. Roy. Soc. B 136, 195–211(1949).
S. Ebashi, M. Endo, and I. Ohtsuki, Control of muscle contraction, Quat. Rev. Biophys. 2, 351–384 (1969).
E. Homsher, W.F.H.M. Mommaerts, N.V. Ricchiuti, and A. Wallner, Activation heat, activation metabolism and tension-related heat in frog semintendinosus muscles, J. Physiol. 220, 601–625 (1972).
A.F. Huxley and R. Niedergerke, Structural changes in muscle during contraction, Nature 173, 971–973 (1954).
H.E. Huxley and J. Hanson, Changes in the cross-striations of muscle during contraction and stretch and their structural interpretations, Nature 173, 973–976 (1954).
I.C.H. Smith, Energetics of activation in frog and toad muscle, J. Physiol. 220, 583–599 (1972).
J.A. Rall and B.A. Schottelius, Energetics of contraction in phasic and tonic skeletal muscles of the chicken, J. Gen. Physiol. 62, 303–323 (1973).
I.R. Wendt and C.L. Oibbs, Energy production of rat extensor digitorum longus muscle, Am. J. Physiol. 224, 1081–1086(1973).
C.L. Gibbs and W.R. Gibson, Energy production of rat soleus muscle, Am. J. Physiol. 223 864–871 (1972).
M.T. Crow and M.J. Kushmerick, Correlated reduction of velocity of shortening and the rate of energy utilization in mouse fast-twitch muscle during a continuous tetanus, J. Gen. Physiol. 82, 703–720 (1983).
L.C. Rome and A.A. Klimov, Superfast contractions without superfast energetics: ATP usage by SR-Ca2+ pumps and crossbridges in toadfish swimbladder muscle, J. Physiol. 526, 279–286 (2000).
J.A. Rall, Energetics of Ca2+ cycling during skeletal muscle contraction, Fed. Proc. 41, 155–160 (1982).
J.A. Rall, Effects of previous activity on the energetics of activation in frog skeletal muscle, J. Gen. Physiol. 75, 617–631(1980).
N.R. Alpert, E.M. Blanchard, and L.A. Mulieri, Tension-independent heat in rabbit papillary muscle, J. Physiol. 414, 433–453 (1989).
G.J.M. Stienen, R. Zaremba, and G. Elzinga, ATP utilization for calcium uptake and force production in skinned muscle fibres of Xenopus laevis, J. Physiol. 482, 109–122 (1995).
A.V. Hill, Trails and Trials in Physiology (The Williams & Wilkins Company, Baltimore, 1965).
R.C. Woledge, N.A. Curtin, and E. Homsher, Energetics Aspects of Muscle Contraction (Academic Press, London, 1985).
N.A. Curtin and R.C. Woledge, Chemical change and energy production during contraction of frog muscle: how are their time courses related? J. Physiol. 288, 353–366 (1979).
E. Homsher, C.J. Kean, A. Wallner, and V. Garibian-Sarian, The time-course of energy balance in an isometric tetanus, J. Gen. Physiol. 73, 553–567 (1979).
N.A. Curtin and R.C. Woldege, The effect of muscle length on energy balance in frog skeletal muscle, J. Physiol. 316, 453–468 (1981).
C. Gerday and J.M. Gillis, Possible role of parvalbumin in the control of contraction, J. Physiol. 258, 96–97P (1976).
J.-F. Pechere, J. Derancourt, and J. Haiech, The participation of parvalbumins in the activation-relaxation cycle of vertebrate fast skeletal-muscle, FEBS Letters 75, 111–114 (1977).
N.A. Curtin and R.C. Woledge, Energy changes and muscular contraction, Physiol. Rev. 58, 690–761 (1978).
S.J. Smith and R.C. Woledge, Thermodyamic analysis of calcium binding to frog parvalbumin, J. Muscle Res. Cell Mot. 6, 757–768 (1985).
M. Tanokura and K. Yamada, A calorimetric study of Ca2+ binding to two major isotypes of bullfrog parvalbumin, FEBS 185, 165–169 (1985).
C.W. Heinzman, Parvalbumin, an intracellular calcium-binding protein; distribution, properties and possible roles in mammalian cells, Experientia Basel 40, 910–921 (1984).
J.A. Rall, Role of parvalbumin in skeletal muscle relaxation, News Physiol. Sci. 11, 249–255 (1996).
J.M. Gillis, D. Thomason, J. Lefevre, and R.H. Kretsinger, Parvalbumins and muscle relaxation: a computer simulation study, J. Muscle Res. Cell Mot. 3, 377–398 (1982).
M. Cannell and D.G. Allen, Model of calcium movements during activation in the sarcomere of frog skeletal muscle, Biophys. J. 45, 913–925 (1984).
T. Hou, J.D. Johnson, and J.A. Rall, Parvalbumin content and Ca2+ and Mg2+ dissociation rates correlated with changes in relaxation rate of frog muscle fibres, J. Physiol. 441, 285–304 (1991).
T. Hou, J.D. Johnson, and J.A. Rall, Effect of temperature on relaxation rate and Ca2+, Mg2+ dissociation rates from parvalbumin of frog muscle fibres, J. Physiol. 449, 399–410 (1992).
Y. Jiang, J.D. Johnson, and J.A. Rall, Parvalbumin relaxes frog skeletal muscle when the sarcoplasmic reticulum Ca-ATPase is inhibited, Am. J. Physiol. 270, C411–C417 (1996).
M.B. Cannell, Effect of tetanus duration on the free calcium during the relaxation of frog skeletal muscle fibres, J. Physiol. 376, 203–218 (1986).
J.M. Raymackers, P. Gailly, M.C. Schoor, D. Pette, B. Schwaller, W. Hunziker, M.R. Celio, and J.M. Gillis, Tetanus relaxation of fast skeletal muscles of the mouse made parvalbumin deficient by gene inactivation, J. Physiol. 527, 355–364 (2000).
B. Schwaller, J. Dick, G. Dhoot, S. Carroll, G. Vrbova, P. Nicotera, D. Pette, A. Wyss, H. Bluethmann, W. Hunziker, and M.R. Celio, Prolonged contraction-relaxation cycle of fast-twitch muscles in parvalbumin knockout mice, Am. J. Physiol. 276, C395–C403 (1999).
M. Muntener, L. Kaser, J. Weber, and M.W. Berchtold, Increase of skeletal muscle relaxation speed by direct injection of parvalbumin cDNA, Proc. Nat. Acad. Sci. 92, 6504–6508 (1995).
P.A. Wahr, D.E. Michele, and J.M. Metzger, Parvalbumin gene transfer corrects diastolic dysfunction in diseased cardiac myocytes, Proc. Nat. Acad. Sci. 96, 11982–11985 (1999).
E.R. Chin, R.W. Grange, F. Viau, A.R. Simard, C. Humphries, J. Shelton, R. Bassel-Duby, R.S. Williams, and R.N. Michel, Alterations in slow-twitch muscle phenotype in transgenic mice overexpressing the Ca2+ buffering protein parvalbumin, J. Physiol. 547, 649–663 (2003).
J.D. Johnson, Y. Jiang, and M. Flynn, Modulation of Ca2+ transients and tension by intracellular EGTA in intact frog muscle fibers, Am. J. Physiol. 272, C1437–C1444 (1997).
J.D. Johnson, S.C. Charlton, and J.D. Potter, A fluorescence stopped flow analysis of Ca2+ exchange with troponin C, J. Biol. Chem. 254, 3497–3502 (1979).
J.D. Potter and J.D. Johnson, Troponin, in: Calcium and Cell Function, Vol II, edited by W.Y. Cheung (Academic Press, New York, 1982), pp. 145–172.
S.B. Tikunova, J.A. Rall, and J.P. Davis, Effect of hydrophobic residue substitutions with glutamine on Ca2+ binding and exchange with the N-domain of troponin C, Biochem. 41: 6697–6705 (2002).
J.P. Davis, J.A. Rall, C. Alionte, and S.B. Tikunova, Mutations of hydrophobic residues in the N-domain of troponin C affect calcium binding and exchange with the troponin C-troponin I(96–148) complex and muscle force production, J. Biol. Chem, in press (2004).
Y. Luo, J.P. Davis, L.B. Smillie, and J.A. Rall, Determinants of relaxation rate in rabbit skinned skeletal muscle fibres, J. Physiol. 545, 887–901 (2002).
J.P. Davis, S.B. Tikunova, D.R. Swartz, and J.A. Rall, Measurement of Ca2+ dissociation rates from troponin C (TnC) in skeletal myofibrils, Biophys. J. 86, 218a (2004).
S.B. Tikunova, J.P. Davis, and J.A. Rall, Engineering cardiac troponin C (cTnC) mutants with dramatically altered Ca2+ dissociation rates as molecular tools to study cardiac muscle relaxation, Biophys. J. 86, 394a (2004).
S.P. Robertson, J.D. Johnson, M.J. Holroyde, E.G. Kranias, J.D. Porter, and R.J. Solaro, The effect of troponin I phosphorylation on the Ca2+-binding properties of the Ca2+-regulatory site of bovine cardiac troponin, J. Biol. Chem. 257, 260–263 (1982).
R. Zhang and J.D. Potter, Cardiac troponin I phosphorylation increases the rate of cardiac muscle relaxation, Circ. Res. 76, 1028–1035 (1995).
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Rall, J.A. (2005). Energetics, Mechanics and Molecular Engineering of Calcium Cycling in Skeletal Muscle. In: Sugi, H. (eds) Sliding Filament Mechanism in Muscle Contraction. Advances in Experimental Medicine and Biology, vol 565. Springer, Boston, MA. https://doi.org/10.1007/0-387-24990-7_14
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DOI: https://doi.org/10.1007/0-387-24990-7_14
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