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Regulatory Mechanisms of Striated Muscle Contraction (Advances in Experimental Medicine and Biology)

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The discovery of troponin by Professor Setsuro Ebashi opened a new era for research into the regulation of striated muscle contraction. This volume is the proceedings of the symposium held at Okazaki, Japan, in 2005 celebrating the 40th anniversary of that discovery.

Professor Ebashi started his work on muscle contraction when he was a young researcher, immediately after World War II, having been inspired by the book Chemistry of Muscular Contraction by Albert Szent-Györgyi. He was fascinated by the dynamic features of the contractile processes performed by the two contractile proteins, myosin and actin, in the presence of ATP. However, he wondered about the mechanism by which muscle relaxes after contraction. He proceeded with biochemical studies of muscle relaxation and found in 1952 that a factor present in the supernatant of the suspension of minced frog skeletal muscle caused relaxation of glycerinated muscle fibers. Based on this finding and succeeding work, he came to the conclusion that the relaxation of contracted muscle was caused by the uptake of calcium ions from the cytosol into the relaxing factor (sarcoplasmic reticulum). His work greatly contributed to elucidating the entire processes of excitation–contraction coupling, particularly the role of calcium ions in triggering the contractile response of myofibrils.

Then he found that superprecipitation of actomyosin, i.e., an in vitro contraction model, became sensitive to calcium ion concentration in the presence of a protein factor other than myosin and actin. This factor showed some similarity to tropomyosin, which had been reported by Bailey, and thus was called native tropomyosin.

When I started working in Professor Ebashi’s laboratory in 1963 as a graduate student, he was working very hard with his wife to characterize the biochemical properties of native tropomyosin. Tropomyosin, reported by Bailey, was actually isolated by isoelectric precipitation from native tropomyosin, but it did not confer any calcium sensitivity to actomyosin. In 1965, Professor Ebashi succeeded in isolating a new protein named “troponin” from native tropomyosin, which, in association with tropomyosin, made actomyosin sensitive to calcium ions. With a series of studies in the 1960s, the molecular basis for the regulation of muscle contraction was established. Since that time, troponin has been the central object in research on the regulation of striated muscle contraction. Properties of troponin, which consists of three different components, have been extensively investigated as revealing insights into a representative calcium-receptive and calcium-regulatory protein.

Professor Ebashi and I sincerely hoped that this volume would become a milestone for future developments in the study of the regulation of muscle contraction and related biomedical sciences. I would like to express my profound gratitude to all contributors for their heartfelt cooperation.
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