Abstract
The exact details of how calcium regulates muscle contraction is still an important problem in the motility field. Actin filaments in muscle have additional proteins, troponins and tropomyosin, which regulate how myosin interacts with actin. Various chapters in this volume, by S. Lehrer and M. Geeves, R. Craig, M. Miki, T. Wakabayashi and L. Tobacman, as well as recent reviews (e.g., Farah and Reinach 1995; Tobacman 1996; Squire and Morris 1998; Gordon et al. 2000) describe the structural and biochemical changes accompanying calcium regulation at the actomyosin interface. X-ray diffraction and electron micrographic data show that calcium induces changes may be ascribed to movement of either tropomyosin (Tm) alone or to both troponin (Tn) and tropomyosin (Squire and Morris 1998). Biochemical studies (Lehrer and Morris 1982; Williams et al. 1988) show that binding of myosin to actin can be cooperative in the presence of troponin, tropomyosin and calcium. Skinned fiber studies show that the calcium activation at steady force appears cooperative (Brandt et al. 1984), but that the calcium dependence of the rate of force development can be explained with little cooperativity on the basis of control of attachment (Regnier et al. 1998). Does calcium merely control the number of cross-bridges that can bind to actin or does it also control the kinetics of the of the actomyosin interaction? How is this control implemented on the molecular level?
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LaMadrid, M.A., Chase, P.B., Gordon, A.M. (2002). Motility Assays of Calcium Regulation of Actin Filaments. In: Thomas, D.D., Dos Remedios, C.G. (eds) Molecular Interactions of Actin. Results and Problems in Cell Differentiation, vol 36. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-46558-4_11
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DOI: https://doi.org/10.1007/978-3-540-46558-4_11
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