A critical analysis is presented of the experimental findings that led to the sliding filament model and to its offspring--the swinging (by rotating or tilting) crossbridge theory of muscle contraction (SCBT). Several principles that have been taken for granted implicitly and explicitly by the creators of these dogmas are discussed. The failure of numerous efforts to verify predictions of the SCBT, particularly the idea that the myosin molecules undergo a major conformational change, is critically reviewed. Analysis of various experimental data suggests that water may play an active role in muscular contraction. Examination of both the experiments that do not fulfill the expectations of the SCBT and the measurements of water liberation during the "contractile" process suggests a new outlook according to which tension development and movement are not due to major conformational changes but rather to restructuring of the hydration shells of actin and myosin.
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http://dx.doi.org/10.3109/10409239709082575 | DOI Listing |
Am J Physiol Cell Physiol
February 2025
Department of Evolution, Ecology, and Organismal Biology, University of California, Riverside, California, United States.
The optimum length for force generation () increases as activation is reduced, challenging classic theories of muscle contraction. Although the activation dependence of is seemingly consistent with length-dependent Ca sensitivity, this mechanism cannot explain the apparent force dependence of or the effect of series compliance on activation-related shifts in . We have tested a theory proposing that the activation dependence of relates to force depression resulting from shortening against series elasticity.
View Article and Find Full Text PDFAppl Microsc
August 2024
Department of Biochemistry, College of Natural Sciences, Kangwon National University, Chuncheon, 24341, Republic of Korea.
The sliding filament theory and the cross-bridge model have been fundamental in understanding muscle contraction. While the cross-bridge model explains the interaction between a single myosin head and actin filament, the native myosin molecule consists of two heads. This review explores the possibility and mechanism of two-headed binding in myosin II to the actin.
View Article and Find Full Text PDFBiomed Rep
January 2024
College of Physical Education, Qufu Normal University, Jining, Shandong 273165, P.R. China.
Intense and unaccustomed eccentric exercise has been extensively studied for its ability to induce muscle damage. However, the underlying mechanism of this phenomenon still requires further clarification. This knowledge gap arises from the need for explanation of the eccentric contraction through the sliding filament theory.
View Article and Find Full Text PDFAdv Physiol Educ
March 2024
Human Performance Laboratory, Faculty of Kinesiology, University of Calgary, Calgary, Alberta, Canada.
Given the recently proposed three-filament theory of muscle contraction, we present a low-cost physical sarcomere model aimed at illustrating the role of titin in the production of active force in skeletal muscle. With inexpensive materials, it is possible to illustrate actin-myosin cross-bridge interactions between the thick and thin filaments and demonstrate the two different mechanisms by which titin is thought to contribute to active and passive muscle force. Specifically, the model illustrates how titin, a molecule with springlike properties, may increase its stiffness by binding free calcium upon muscle activation and reducing its extensible length by attaching itself to actin, resulting in the greater force-generating capacity after an active than a passive elongation that has been observed experimentally.
View Article and Find Full Text PDFSci Rep
October 2023
Laboratorio de Acústica Ultrasonora, Facultad de Ciencias, Universidad de la República, Iguá 4225, 11400, Montevideo, Uruguay.
The skeletal muscle contraction is determined by cross-bridge formation between the myosin heads and the actin active sites. When the muscle contracts, it shortens, increasing its longitudinal shear elastic modulus ([Formula: see text]). Structurally, skeletal muscle can be considered analogous to the molecular receptors that form receptor-ligand complexes and exhibit specific ligand-binding dynamics.
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