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Molecular Studies of Muscle Contraction

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biophysics".

Deadline for manuscript submissions: 20 October 2025 | Viewed by 1013

Special Issue Editor


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Guest Editor
Dipartimento di Medicina Sperimentale e Clinica, Università degli Studi di Firenze, Florence, Italy
Interests: muscle physiology; mathematical modelling of muscle contraction; mechanics and structure of molecular motors
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Special Issue Information

Dear Colleagues,

The main function of muscle is to shorten and generate force through the cyclic interaction between actin and myosin, fuelled by ATP hydrolysis. Many other proteins are involved in the regulation of the contraction and in preserving the architecture of the contractile machinery. These functions are brought about through protein-protein interactions, in a complex interplay that can be investigated with both experimental and theoretical approaches.

The aim of this Special Issue is to host original research papers and reviews on the proteins at work in muscle, both striated and smooth, and on their role in promoting, assisting and regulating the contractile function.

Without intending to be exclusive, the papers collected in this issue could report studies on topics such as actomyosin interactions, thin and thick filament-based regulation, cytoskeletal anchoring proteins, and physiological or pharmacological modulation of muscle performance. Any of these investigations should be aimed at understanding the molecular mechanisms underlying either the normal muscle functioning or pathological condition.

Dr. Massimo Reconditi
Guest Editor

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Keywords

  • muscle contraction
  • actin
  • myosin
  • thin and thick filament
  • cytoskeletal anchoring protein

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Published Papers (1 paper)

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Research

16 pages, 1362 KiB  
Article
The Mechanism of Modulation of Cardiac Force by Temperature
by Ilaria Morotti, Matteo Marcello, Giulia Sautariello, Irene Pertici, Pasquale Bianco, Gabriella Piazzesi, Marco Linari, Vincenzo Lombardi, Massimo Reconditi and Marco Caremani
Int. J. Mol. Sci. 2025, 26(2), 469; https://doi.org/10.3390/ijms26020469 - 8 Jan 2025
Cited by 1 | Viewed by 760
Abstract
In maximally Ca2+-activated demembranated fibres from the mammalian skeletal muscle, the depression of the force by lowering the temperature below the physiological level (~35 °C) is explained by the reduction of force in the myosin motor. Instead, cooling is reported to [...] Read more.
In maximally Ca2+-activated demembranated fibres from the mammalian skeletal muscle, the depression of the force by lowering the temperature below the physiological level (~35 °C) is explained by the reduction of force in the myosin motor. Instead, cooling is reported to not affect the force per motor in Ca2+-activated cardiac trabeculae from the rat ventricle. Here, the mechanism of the cardiac performance depression by cooling is reinvestigated with fast sarcomere-level mechanics. We determine the changes in the half-sarcomere compliance of maximally Ca2+-activated demembranated rat trabeculae in the range of temperatures of 10–30 °C and analyse the data in terms of a simplified mechanical model of the half-sarcomere to extract the contribution of myofilaments and myosin motors. We find that the changes in the ensemble force are due to changes in the force per motor, while the fraction of actin-attached motors remains constant independent of temperature. The results demonstrate that in the cardiac myosin, as in the skeletal muscle myosin, the force-generating transition is endothermic. The underlying large heat absorption indicates the interaction of extended hydrophobic surfaces within the myosin motor, like those suggested by the crystallographic model of the working stroke. Full article
(This article belongs to the Special Issue Molecular Studies of Muscle Contraction)
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