alexa Visualization and Recording of Structural Changes in Hydrated, Living Muscle Myofilaments using the Gas Environmental Chamber
ISSN: 2157-7439

Journal of Nanomedicine & Nanotechnology
Open Access

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Review Article

Visualization and Recording of Structural Changes in Hydrated, Living Muscle Myofilaments using the Gas Environmental Chamber

Haruo Sugi1*, Takuya Miyakawa2, Suguru Tanokura2, Shigeru Chaen3, Hiroki Minoda4 and Tsuyoshi Akimoto1

1 Department of Physiology, School of Medicine, Teikyo University, Tokyo, Japan

2 Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo, Japan

3Department of Integrated Sciences in Physics and Biology, College of Humanities and Sciences, Nihon University, Tokyo, Japan

4Department of Applied Physics, Tokyo University of Agriculture and Technology, Tokyo, Japan

*Corresponding Author:
Haruo Sugi
Department of Physiology
School of Medicine, Teikyo University
Tokyo, Japan
Tel/Fax: +81 484 78 4079
E-mail: [email protected]

Received Date: December 13, 2013; Accepted Date: February 10, 2014; Published Date: February 12, 2014

Citation: Sugi H, Miyakawa T, Tanokura S, Chaen S, Minoda H, et al. (2014) Visualization and Recording of Structural Changes in Hydrated, Living Muscle Myofilaments using the Gas Environmental Chamber. J Nanomed Nanotechol S5:005. doi:10.4172/2157-7439.S5-005

Copyright: © 2014 Sugi H, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

 

Abstract

Although more than 50 years have passed since the monumental discovery of ATP-dependent sliding filament mechanism in muscle contraction, the mechanism of cyclic attachment-detachment cycle between myosin heads extending from myosin filaments and corresponding sites on actin filaments still remains to be a matter for debate and speculation. Using the gas environmental chamber (EC) attached to an electron microscope, we have succeeded in recording images of hydrated myosin filaments, with gold particle position markers attached to individual myosin heads. In the absence of ATP, the position of individual myosin heads does not change appreciably with time, indicating stability of time-averaged myosin head mean position. On ATP application, individual myosin heads move parallel to the filament axis by ~6 nm. At both sides of the filament bare region, across which myosin head polarity is reversed, individual myosin heads move away from, but not towards, the bare region, indicating that the observed myosin head movement
corresponds to the recovery stroke, associated with reaction, M + ATP → M·ADP·Pi. After exhaustion of applied ATP, individual myosin heads return towards their initial position. Recently, we have further succeeded in recording ATPinduced myosin head power stroke in the presence of actin filaments, and have found that the amplitude of power stroke in the isometric condition is ~3 nm, and increases to ~5 nm at low ionic strength, in accordance with the physiological experiments that Ca2+-activated force increases ~two fold at low ionic strength. These findings about the novel features of ATP-induced myosin head movement indicate that the EC is an extremely powerful tool, which enables us to visualize and investigate behavior of individual myosin heads in living, hydrated myosin filaments, retaining their physiological function. Finally, we emphasize that our EC work still remains to be the only attempt to investigate function of hydrated
macromolecules.

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