Literature DB >> 33610561

Force-velocity and tension transient measurements from Drosophila jump muscle reveal the necessity of both weakly-bound cross-bridges and series elasticity in models of muscle contraction.

Katelyn J Jarvis1, Kaylyn M Bell2, Amy K Loya3, Douglas M Swank4, Sam Walcott5.   

Abstract

Muscle contraction is a fundamental biological process where molecular interactions between the myosin molecular motor and actin filaments result in contraction of a whole muscle, a process spanning size scales differing in eight orders of magnitude. Since unique behavior is observed at every scale in between these two extremes, to fully understand muscle function it is vital to develop multi-scale models. Based on simulations of classic measurements of muscle heat generation as a function of work, and shortening rate as a function of applied force, we hypothesize that a model based on molecular measurements must be modified to include a weakly-bound interaction between myosin and actin in order to fit measurements at the muscle fiber or whole muscle scales. This hypothesis is further supported by the model's need for a weakly-bound state in order to qualitatively reproduce the force response that occurs when a muscle fiber is rapidly stretched a small distance. We tested this hypothesis by measuring steady-state force as a function of shortening velocity, and the force transient caused by a rapid length step in Drosophila jump muscle fibers. Then, by performing global parameter optimization, we quantitatively compared the predictions of two mathematical models, one lacking a weakly-bound state and one with a weakly-bound state, to these measurements. Both models could reproduce our force-velocity measurements, but only the model with a weakly-bound state could reproduce our force transient measurements. However, neither model could concurrently fit both measurements. We find that only a model that includes weakly-bound cross-bridges with force-dependent detachment and an elastic element in series with the cross-bridges is able to fit both of our measurements. This result suggests that the force response after stretch is not a reflection of distinct steps in the cross-bridge cycle, but rather arises from the interaction of cross-bridges with a series elastic element. Additionally, the model suggests that the curvature of the force-velocity relationship arises from a combination of the force-dependence of weakly- and strongly-bound cross-bridges. Overall, this work presents a minimal cross-bridge model that has predictive power at the fiber level.
Copyright © 2021 Elsevier Inc. All rights reserved.

Entities:  

Keywords:  Multi-scale modeling; Muscle mechanics; Myosin; Stretch-activation; Weak binding

Mesh:

Year:  2021        PMID: 33610561      PMCID: PMC7986577          DOI: 10.1016/j.abb.2021.108809

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN: 0003-9861            Impact factor:   4.013


  81 in total

1.  Filament compliance effects can explain tension overshoots during force development.

Authors:  Kenneth S Campbell
Journal:  Biophys J       Date:  2006-09-01       Impact factor: 4.033

2.  Tension responses to sudden length change in stimulated frog muscle fibres near slack length.

Authors:  L E Ford; A F Huxley; R M Simmons
Journal:  J Physiol       Date:  1977-07       Impact factor: 5.182

3.  Mechanical coupling between myosin molecules causes differences between ensemble and single-molecule measurements.

Authors:  Sam Walcott; David M Warshaw; Edward P Debold
Journal:  Biophys J       Date:  2012-08-08       Impact factor: 4.033

4.  Fluorescent actin filaments move on myosin fixed to a glass surface.

Authors:  S J Kron; J A Spudich
Journal:  Proc Natl Acad Sci U S A       Date:  1986-09       Impact factor: 11.205

5.  Structures of actomyosin crossbridges in relaxed and rigor muscle fibers.

Authors:  L C Yu; B Brenner
Journal:  Biophys J       Date:  1989-03       Impact factor: 4.033

Review 6.  Models for the specific adhesion of cells to cells.

Authors:  G I Bell
Journal:  Science       Date:  1978-05-12       Impact factor: 47.728

7.  Mechanism of adenosine triphosphate hydrolysis by actomyosin.

Authors:  R W Lymn; E W Taylor
Journal:  Biochemistry       Date:  1971-12-07       Impact factor: 3.162

8.  Nonlinear elasticity and an 8-nm working stroke of single myosin molecules in myofilaments.

Authors:  Motoshi Kaya; Hideo Higuchi
Journal:  Science       Date:  2010-08-06       Impact factor: 47.728

Review 9.  Residual Force Enhancement Following Eccentric Contractions: A New Mechanism Involving Titin.

Authors:  W Herzog; G Schappacher; M DuVall; T R Leonard; J A Herzog
Journal:  Physiology (Bethesda)       Date:  2016-07

10.  Smooth muscle heavy meromyosin phosphorylated on one of its two heads supports force and motion.

Authors:  Sam Walcott; Patricia M Fagnant; Kathleen M Trybus; David M Warshaw
Journal:  J Biol Chem       Date:  2009-05-06       Impact factor: 5.157

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  2 in total

1.  Mathematical modeling of myosin, muscle contraction, and movement.

Authors:  Kenneth Tran; Bertrand C W Tanner; Kenneth S Campbell
Journal:  Arch Biochem Biophys       Date:  2021-06-24       Impact factor: 4.114

Review 2.  From the Matrix to the Nucleus and Back: Mechanobiology in the Light of Health, Pathologies, and Regeneration of Oral Periodontal Tissues.

Authors:  Martin Philipp Dieterle; Ayman Husari; Thorsten Steinberg; Xiaoling Wang; Imke Ramminger; Pascal Tomakidi
Journal:  Biomolecules       Date:  2021-05-31
  2 in total

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