Multi-scale striated muscle contraction model linking sarcomere length-dependent cross-bridge kinetics to macroscopic deformation

2020 ◽  
Vol 39 ◽  
pp. 101062
Author(s):  
Boban Stojanovic ◽  
Marina Svicevic ◽  
Ana Kaplarevic-Malisic ◽  
Richard J. Gilbert ◽  
Srboljub M. Mijailovich
Keyword(s):  
Muscle Contraction ◽  
Sarcomere Length ◽  
Striated Muscle ◽  
Multi Scale ◽  
Cross Bridge ◽  
Macroscopic Deformation

Length dependence of active force production in skeletal muscle

1999 ◽  
Vol 86 (5) ◽  
pp. 1445-1457 ◽  
Author(s):  
D. E. Rassier ◽  
B. R. MacIntosh ◽  
W. Herzog
Keyword(s):  
Skeletal Muscle ◽  
Muscle Contraction ◽  
Sarcomere Length ◽  
Length Change ◽  
In Vivo Studies ◽  
Active Force ◽  
Moment Arm ◽  
Cross Bridge ◽  
Length Relationship

The sliding filament and cross-bridge theories of muscle contraction provide discrete predictions of the tetanic force-length relationship of skeletal muscle that have been tested experimentally. The active force generated by a maximally activated single fiber (with sarcomere length control) is maximal when the filament overlap is optimized and is proportionally decreased when overlap is diminished. The force-length relationship is a static property of skeletal muscle and, therefore, it does not predict the consequences of dynamic contractions. Changes in sarcomere length during muscle contraction result in modulation of the active force that is not necessarily predicted by the cross-bridge theory. The results of in vivo studies of the force-length relationship suggest that muscles that operate on the ascending limb of the force-length relationship typically function in stretch-shortening cycle contractions, and muscles that operate on the descending limb typically function in shorten-stretch cycle contractions. The joint moments produced by a muscle depend on the moment arm and the sarcomere length of the muscle. Moment arm magnitude also affects the excursion (length change) of a muscle for a given change in joint angle, and the number of sarcomeres arranged in series within a muscle fiber determines the sarcomere length change associated with a given excursion.

scholarly journals Sarcomere mechanics in striated muscles: from molecules to sarcomeres to cells

2017 ◽  
Vol 313 (2) ◽  
pp. C134-C145 ◽  
Author(s):  
Dilson E. Rassier
Keyword(s):  
Muscle Contraction ◽  
Sarcomere Length ◽  
Muscle Fibers ◽  
Strong Support ◽  
Common Mechanism ◽  
Striated Muscles ◽  
Cross Bridge ◽  
The Cross ◽  
Sliding Filament Theory ◽  
Permeabilized Fibers

Muscle contraction is commonly associated with the cross-bridge and sliding filament theories, which have received strong support from experiments conducted over the years in different laboratories. However, there are studies that cannot be readily explained by the theories, showing 1) a plateau of the force-length relation extended beyond optimal filament overlap, and forces produced at long sarcomere lengths that are higher than those predicted by the sliding filament theory; 2) passive forces at long sarcomere lengths that can be modulated by activation and Ca2+, which changes the force-length relation; and 3) an unexplained high force produced during and after stretch of activated muscle fibers. Some of these studies even propose “new theories of contraction.” While some of these observations deserve evaluation, many of these studies present data that lack a rigorous control and experiments that cannot be repeated in other laboratories. This article reviews these issues, looking into studies that have used intact and permeabilized fibers, myofibrils, isolated sarcomeres, and half-sarcomeres. A common mechanism associated with sarcomere and half-sarcomere length nonuniformities and a Ca2+-induced increase in the stiffness of titin is proposed to explain observations that derive from these studies.

Sarcomere length control in striated muscle

1982 ◽  
Vol 242 (3) ◽  
pp. H411-H420 ◽  
Author(s):  
R. van Heuningen ◽  
W. H. Rijnsburger ◽  
H. E. ter Keurs
Keyword(s):  
Sarcomere Length ◽  
Striated Muscle ◽  
Feedforward Control ◽  
Muscle Length ◽  
Transient Behavior ◽  
Loop Filter ◽  
Internal Position ◽  
Optimal Damping ◽  
Internal Velocity ◽  
Muscle Responses

A system that makes control of muscle length (ML), sarcomere length (SL), and force (F) possible in striated muscle preparations is described. SL was measured by light diffraction techniques and two diffractometers. Control was performed by influencing ML with a penmotor system with a frequency response of 190 Hz. SL or F could be controlled by interrupting the internal position (i.e., ML) feedback of the motor and by closing the respective loop. Velocity feedback of the motor through an internal velocity coil was maintained in all cases for optimal damping. Steady-state error of the system was minimized by an integrating loop filter. The feedback path was selected by means of potentiometers or analog switches. Electronic stops in the circuit protected the muscle against excessive stretch and load. A microprocessor-based average-response computer could be used for feedforward control to eliminate noise or to analyze longitudinal uniformity of the muscle. Responses of rat cardiac trabeculae during SL and F control are shown. Transient behavior of SL and F during control and measures to eliminate the transients are discussed.

The Filament Lattice of Striated Muscle

1998 ◽  
Vol 78 (2) ◽  
pp. 359-391 ◽  
Author(s):  
BARRY M. MILLMAN
Keyword(s):  
Muscle Contraction ◽  
Structural Changes ◽  
Striated Muscle ◽  
Muscle Fibers ◽  
Lattice Stability ◽  
X Ray Diffraction ◽  
Thin Filaments ◽  
Intact Muscle ◽  
Radial Forces ◽  
Speed Of Shortening

Millman, Barry M. The Filament Lattice of Striated Muscle. Physiol. Rev. 78: 359–391, 1998. — The filament lattice of striated muscle is an overlapping hexagonal array of thick and thin filaments within which muscle contraction takes place. Its structure can be studied by electron microscopy or X-ray diffraction. With the latter technique, structural changes can be monitored during contraction and other physiological conditions. The lattice of intact muscle fibers can change size through osmotic swelling or shrinking or by changing the sarcomere length of the muscle. Similarly, muscle fibers that have been chemically or mechanically skinned can be compressed with bathing solutions containing very large inert polymeric molecules. The effects of lattice change on muscle contraction in vertebrate skeletal and cardiac muscle and in invertebrate striated muscle are reviewed. The force developed, the speed of shortening, and stiffness are compared with structural changes occurring within the lattice. Radial forces between the filaments in the lattice, which can include electrostatic, Van der Waals, entropic, structural, and cross bridge, are assessed for their contributions to lattice stability and to the contraction process.

Limulus Striated Muscle Provides an Unusual Model for Muscle Contraction

1984 ◽  
pp. 67-87 ◽  
Author(s):  
M. M. Dewey ◽  
P. Brink ◽  
D. E. Colflesh ◽  
B. Gaylinn ◽  
S.-F. Fan ◽  
...  
Keyword(s):  
Muscle Contraction ◽  
Striated Muscle

scholarly journals Phosphate has dual roles in cross-bridge kinetics in rabbit psoas single myofibrils

2021 ◽  
Vol 153 (3) ◽  
Author(s):  
Masataka Kawai ◽  
Robert Stehle ◽  
Gabriele Pfitzer ◽  
Bogdan Iorga
Keyword(s):  
Rate Constants ◽  
Striated Muscle ◽  
Intrinsic Rate ◽  
Isometric Tension ◽  
Force Generation ◽  
Skinned Fibers ◽  
Sinusoidal Analysis ◽  
Rabbit Psoas ◽  
Cross Bridge

In this study, we aimed to study the role of inorganic phosphate (Pi) in the production of oscillatory work and cross-bridge (CB) kinetics of striated muscle. We applied small-amplitude sinusoidal length oscillations to rabbit psoas single myofibrils and muscle fibers, and the resulting force responses were analyzed during maximal Ca2+ activation (pCa 4.65) at 15°C. Three exponential processes, A, B, and C, were identified from the tension transients, which were studied as functions of Pi concentration ([Pi]). In myofibrils, we found that process C, corresponding to phase 2 of step analysis during isometric contraction, is almost a perfect single exponential function compared with skinned fibers, which exhibit distributed rate constants, as described previously. The [Pi] dependence of the apparent rate constants 2πb and 2πc, and that of isometric tension, was studied to characterize the force generation and Pi release steps in the CB cycle, as well as the inhibitory effect of Pi. In contrast to skinned fibers, Pi does not accumulate in the core of myofibrils, allowing sinusoidal analysis to be performed nearly at [Pi] = 0. Process B disappeared as [Pi] approached 0 mM in myofibrils, indicating the significance of the role of Pi rebinding to CBs in the production of oscillatory work (process B). Our results also suggest that Pi competitively inhibits ATP binding to CBs, with an inhibitory dissociation constant of ∼2.6 mM. Finally, we found that the sinusoidal waveform of tension is mostly distorted by second harmonics and that this distortion is closely correlated with production of oscillatory work, indicating that the mechanism of generating force is intrinsically nonlinear. A nonlinear force generation mechanism suggests that the length-dependent intrinsic rate constant is asymmetric upon stretch and release and that there may be a ratchet mechanism involved in the CB cycle.

The Frank-Starling mechanism is not mediated by changes in rate of cross-bridge detachment

1997 ◽  
Vol 273 (5) ◽  
pp. H2428-H2435 ◽  
Author(s):  
Thomas Wannenburg ◽  
Paul M. L. Janssen ◽  
Dongsheng Fan ◽  
Pieter P. De Tombe
Keyword(s):  
Cardiac Muscle ◽  
Maximum Rate ◽  
Sarcomere Length ◽  
Myosin Head ◽  
Isometric Force ◽  
Force Development ◽  
Cross Bridge ◽  
Average Slope ◽  
The Cross ◽  
Kinetics Of

We tested the hypothesis that the Frank-Starling relationship is mediated by changes in the rate of cross-bridge detachment in cardiac muscle. We simultaneously measured isometric force development and the rate of ATP consumption at various levels of Ca2+ activation in skinned rat cardiac trabecular muscles at three sarcomere lengths (2.0, 2.1, and 2.2 μm). The maximum rate of ATP consumption was 1.5 nmol ⋅ s−1 ⋅ μl fiber vol−1, which represents an estimated adenosinetriphosphatase (ATPase) rate of ∼10 s−1 per myosin head at 24°C. The rate of ATP consumption was tightly and linearly coupled to the level of isometric force development, and changes in sarcomere length had no effect on the slope of the force-ATPase relationships. The average slope of the force-ATPase relationships was 15.5 pmol ⋅ mN−1 ⋅ mm−1. These results suggest that the mechanisms that underlie the Frank-Starling relationship in cardiac muscle do not involve changes in the kinetics of the apparent detachment step in the cross-bridge cycle.

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