Abstract
Microcalorimetric titration studies of EF-hand Ca-binding proteins (troponin C, calmodulin and parvalbumins) resulted in the notion that Ca binding to the “active” Ca site, which is involved in the regulation of contraction, induces a characteristic anomalous enthalpy and heat-capacity changes indicating an exposure of hydrophobic residues to the solvent, which enables the proteins to interact with their targets. There is a good agreement between the results of the calorimetric and the structural studies in frog and chicken skeletal troponin C. In both species one of the N-terminal low-affinity Ca-sites is the “active” Ca site regulating muscle contraction. The results from calorimetry have shown, however, that the situation in rabbit skeletal troponin C may be more complex. Moreover, in both calorimetric and structural studies, the situation in cardiac troponin C is quite different. These results suggest the need for further studies to elucidate the mechanism of regulation by Ca. These characteristic changes do not occur in Ca-buffering proteins.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Ebashi, S., and Endo, M., 1968, Calcium and muscle contraction. Prog. Biophys Mol. Biol. 18: 123.
van Eerd, J.-P, and Takahashi, K. 1975, The amino acid sequence of bovine cardiac troponin-C. Comparison with rabbit skeletal troponin-C. Biochem. Biophys. Res. Commun. 64: 122.
van Eerd, J.-R, Canopy J.-P., Ferraz, C, and Pechere, J.-F., 1978, The amino-acid sequence of troponin C from frog skeletal muscsle. Eur. J. Biochem. 91: 231.
Gagne, S.M., Tsudsa, S., Li, M.X., Smillie, L.B., and Sykes, B.D., 1995, Structures of the troponin C regulatory domains in the apo and calcium-saturated states. Nat. Struct. Biol. 2: 784.
Herzberg, O., Moult, J., and James, M.N.G., 1896, A model for the Ca2+-induced conformational transition of troponin C. J. Biol. Chem. 261: 2638.
Herzberg, O., and James, M.N.G., 1988, Refined crystal structure of troponin C from turkey skeletal muscle at 2.0 A resoltion. J. Mol. Biol. 203: 761.
Imaizumi, M., and Tanokura, M., 1990, Heat capacity and entropy changes of troponin C from bullfrog skeletal muscle induced by calcium binding. Eur. J. Biochem. 192: 275.
Imaizumi, M, Tanokura, M., and Yamada, K., 1987, A calorimetric study on calcium binding by troponin C from bullfrog skeletal muscle. J. Biol. Chem. 262: 7963.
Imaizumi, M, Tanokura, M., and Yamada, K., 1990, Calorimetric studies on calcium and magnesium binding by troponin C from bullfrog skeletal muscle. J. Biochem. 107: 127.
Kometani, K., and Yamada, K., 1983, Enthalpy, entropy and heat capacity changes induced by binding of calcium ions to cardiac troponin C Biochem. Biophys. Res. Commun. 114: 162.
Li, M.X., Gagne, S.M., Tsuda, S., Kay, CM., Smillie, L.B., and Sykes, B.D., 1995, Calcium binding to the regulatory N-domain of skeletal muscle troponin C occurs in a stepwise manner. Biochemistry, 34: 8330.
Potter, J.D., and Gergley, J., 1975, The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrilar ATPase. J. Biol. Chem. 250: 4628.
Sia, S.K., Li, M.X., Spyracopoulos, L, Gagne, S.M., Liu, W., Putkey, J.A., and Sykes, B.D., 1997, Structure of cardiac muscle troponin C unexpectredly reveals a closed regulatory domain. J. Biol. Chem. 272: 18216.
Skelton, M.J., Kordel, J., Akke, M, Forsen, S., and Chazin, W.J. 1994, Signal tranduction versus buffering activity in Ca2+-binding proteins. Nat. Struct. Biol. 1: 239.
Slupsky, CM., Kay, CM., Reinach, F.C, Smillie, L.B., and Sykes, B.D., 1995, Calcium-induced dimerization of troponin C: Mode of interaction and use of trifluoroethanol as a dénaturant of quaternary structure. Biochemistry, 34: 7365.
Tanokura, M., Imaizumi, M., and Yamada, K., 1986, A calorimetric study of Ca binding by parvalbumin of the toad (Bufo): distinguishable binding sites in the molecule. FEBS Lett. 209: 77.
Tanokura, M., and Yamada, K., 1983, A calorimetric study of Ca and Mg binding by calmodulin. J. Biochem. 94: 607.
Tanokura, M., and Yamada, K., 1984, Heat capacity and entropy changes of calmodulin induced by calcium binding. J. Biochem. 95: 643.
Tanokura, M., and Yamada, K. 1985a,A calorimetric study of Ca binding to two major isotypes of bullfrog parvalbumin. FEBS Lett. 185: 165.
Tanokura, M., and Yamada, K., 1985b,Effects of trifluoperazine on calcium binding by calmodulin. A microcalorimetric study. J. Biol. Chem. 260: 8680.
Tanokura, M., and Yamada, K., 1986, Effects of trifluoperazine on calcium binding by calmodulin. Heat capacity and entropy changes. J. Biol. Chem. 261: 10749.
Tanokura, M., and Yamada, K. 1987, Heat capacity and entropy changes of the two major isotypes of bullfrog (Rana catesbeiana) parvalbumins induced by calcium binding. Biochemistry 26: 7668.
Tanokura, M., and Yamada, K., 1993. A calorimetric study of Ca2+ binding by wheat germ calmodulin. Regulatory steps driven by entropy. J. Biol. Chem. 268: 7090.
Yamada, K., 1978, The enthalpy titration of troponin C with calcium. Biochim. Biophys. Acta 535: 342.
Yamada, K., 1999, Thermodynamic analyses of calcium binding to troponin C, calmodulin and parvalubumins by using microcaloimetry. Molec. Cell. Biochem. 190: 39.
Yamada, K., and Kometani, K., 1983, The changes in heat capacity and entropy of troponin C induced by calcium binding. J. Biochem. 92: 1505.
Yamada, K., Mashima, H., and Ebashi, S., 1976, The enthalpy changes accompanying the binding of calcium to troponin relating to the activation heat production of muscle. Proc. Japan Acad. 52: 252.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2003 Springer Science+Business Media New York
About this paper
Cite this paper
Yamada, K. (2003). Calcium Binding to Troponin C as a Primary Step of the Regulation of Contraction. In: Sugi, H. (eds) Molecular and Cellular Aspects of Muscle Contraction. Advances in Experimental Medicine and Biology, vol 538. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-9029-7_19
Download citation
DOI: https://doi.org/10.1007/978-1-4419-9029-7_19
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-4764-4
Online ISBN: 978-1-4419-9029-7
eBook Packages: Springer Book Archive