1. Varying thin filament activation in the framework of the Huxley'57 model
- Author
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François Kimmig, Matthieu Caruel, Dominique Chapelle, Mathematical and Mechanical Modeling with Data Interaction in Simulations for Medicine (M3DISIM), Laboratoire de mécanique des solides (LMS), École polytechnique (X)-Mines Paris - PSL (École nationale supérieure des mines de Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-École polytechnique (X)-Mines Paris - PSL (École nationale supérieure des mines de Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Inria Saclay - Ile de France, Institut National de Recherche en Informatique et en Automatique (Inria)-Institut National de Recherche en Informatique et en Automatique (Inria), Laboratoire Modélisation et Simulation Multi-Echelle (MSME), and Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12)-Centre National de la Recherche Scientifique (CNRS)-Université Gustave Eiffel
- Subjects
Sarcomeres ,Applied Mathematics ,Biomedical Engineering ,[SPI.MECA.BIOM]Engineering Sciences [physics]/Mechanics [physics.med-ph]/Biomechanics [physics.med-ph] ,Cardiac modeling ,Actins ,Actin Cytoskeleton ,Computational Theory and Mathematics ,Thick and thin filament activation ,Modeling and Simulation ,Huxley'57 model ,Calcium ,Mathematical modeling ,Molecular Biology ,Software ,Muscle Contraction - Abstract
International audience; Muscle contraction is triggered by the activation of the actin sites of the thin filament by calcium ions. It results that the thin filament activation level varies over time. Moreover, this activation process is also used as a regulation mechanism of the developed force. Our objective is to build a model of varying actin site activation level within the classical Huxley'57 two-state framework. This new model is obtained as an enhancement of a previously proposed formulation of the varying thick filament activation within the same framework [1]. We assume that the state of an actin site depends on whether it is activated and whether it forms a cross-bridge with the associated myosin head, which results in four possible states. The transitions between the actin site states are controlled by the global actin sites activation level and the dynamics of these transitions is coupled with the attachment-detachment process. A preliminary calibration of the model with experimental twitch contraction data obtained at varying sarcomere lengths is performed.
- Published
- 2022
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