Literature DB >> 24703982

Electrostatic forces or structural scaffolding: what stabilizes the lattice spacing of relaxed skinned muscle fibers?

David A Smith1.   

Abstract

The filament lattice in relaxed striated muscle is thought to be stabilized by electrostatic forces between charged filaments; electrostatic theories based on known filament charge densities do predict that the lattice spacing drops slightly with sarcomere length when actin and myosin filaments overlap. However, at sarcomere lengths with no overlap, electrostatic forces are reduced to a very low level and electrostatic models predict that the lattice collapses to a much smaller spacing. This collapse is not observed, which suggests that the A-band and I-band lattices are stabilized mechanically by the M-band and Z-line. To determine which mechanisms operate, consider a model where charged-filament interactions are supplemented by elastic titin filaments and radially elastic M-bands and Z-lines. To make progress, this model is simplified by assuming that the areas of A-band and Z-line unit cells are equal. Published data for the length-dependence of the lattice spacing, in and out of overlap, can be fitted to a mechanical model with known titin elasticity and very weak M-band or Z-line stiffness (≈0.15 pN/nm per unit cell), which implies that electrostatic interactions cannot be ignored. A better fit is obtained when electrostatic interactions are restored. Electrostatic interactions also explain why the lattice spacing of relaxed muscle is a decreasing function of temperature.
Copyright © 2014 Elsevier Ltd. All rights reserved.

Entities:  

Keywords:  M-band; Muscle lattice; Sarcomere length; Titin; Z-line

Mesh:

Year:  2014        PMID: 24703982     DOI: 10.1016/j.jtbi.2014.03.037

Source DB:  PubMed          Journal:  J Theor Biol        ISSN: 0022-5193            Impact factor:   2.691


  4 in total

1.  In vivo X-ray diffraction and simultaneous EMG reveal the time course of myofilament lattice dilation and filament stretch.

Authors:  Sage A Malingen; Anthony M Asencio; Julie A Cass; Weikang Ma; Thomas C Irving; Thomas L Daniel
Journal:  J Exp Biol       Date:  2020-09-03       Impact factor: 3.312

2.  Muscle active force-length curve explained by an electrophysical model of interfilament spacing.

Authors:  Robert Rockenfeller; Michael Günther; Scott L Hooper
Journal:  Biophys J       Date:  2022-04-21       Impact factor: 3.699

3.  A mechanism for sarcomere breathing: volume change and advective flow within the myofilament lattice.

Authors:  Julie A Cass; C David Williams; Thomas C Irving; Eric Lauga; Sage Malingen; Thomas L Daniel; Simon N Sponberg
Journal:  Biophys J       Date:  2021-08-10       Impact factor: 3.699

4.  Titin stiffness modifies the force-generating region of muscle sarcomeres.

Authors:  Yong Li; Patrick Lang; Wolfgang A Linke
Journal:  Sci Rep       Date:  2016-04-15       Impact factor: 4.379

  4 in total

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