scholarly journals Estimation of Forces on Actin Filaments in Living Muscle from X-ray Diffraction Patterns and Mechanical Data

2019 ◽  
Vol 20 (23) ◽  
pp. 6044
Author(s):  
Srboljub M. Mijailovich ◽  
Momcilo Prodanovic ◽  
Thomas C. Irving
Keyword(s):  
Muscle Contraction ◽  
Striated Muscle ◽  
Thin Filaments ◽  
X Ray ◽  
Cytoskeletal Network ◽  
Molecular Events ◽  
Mechanisms Of Adaptation ◽  
Length Changes ◽  
Diffraction Patterns ◽  
Intracellular Forces

Many biological processes are triggered or driven by mechanical forces in the cytoskeletal network, but these transducing forces have rarely been assessed. Striated muscle, with its well-organized structure provides an opportunity to assess intracellular forces using small-angle X-ray fiber diffraction. We present a new methodology using Monte Carlo simulations of muscle contraction in an explicit 3D sarcomere lattice to predict the fiber deformations and length changes along thin filaments during contraction. Comparison of predicted diffraction patterns to experimental meridional X-ray reflection profiles allows assessment of the stepwise changes in intermonomer spacings and forces in the myofilaments within living muscle cells. These changes along the filament length reflect the effect of forces from randomly attached crossbridges. This approach enables correlation of the molecular events, such as the current number of attached crossbridges and the distributions of crossbridge forces to macroscopic measurements of force and length changes during muscle contraction. In addition, assessments of fluctuations in local forces in the myofilaments may reveal how variations in the filament forces acting on signaling proteins in the sarcomere M-bands and Z-discs modulate gene expression, protein synthesis and degradation, and as well to mechanisms of adaptation of muscle in response to changes in mechanical loading.

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.

scholarly journals Poorly Understood Aspects of Striated Muscle Contraction

2015 ◽  
Vol 2015 ◽  
pp. 1-28 ◽  
Author(s):  
Alf Månsson ◽  
Dilson Rassier ◽  
Georgios Tsiavaliaris
Keyword(s):  
Muscle Contraction ◽  
Structural Changes ◽  
Striated Muscle ◽  
Three Dimensional ◽  
Skeletal Muscle Function ◽  
Tension Development ◽  
Atomic Structures ◽  
Molecular Events ◽  
Physiological Properties

Muscle contraction results from cyclic interactions between the contractile proteins myosin and actin, driven by the turnover of adenosine triphosphate (ATP). Despite intense studies, several molecular events in the contraction process are poorly understood, including the relationship between force-generation and phosphate-release in the ATP-turnover. Different aspects of the force-generating transition are reflected in the changes in tension development by muscle cells, myofibrils and single molecules upon changes in temperature, altered phosphate concentration, or length perturbations. It has been notoriously difficult to explain all these events within a given theoretical framework and to unequivocally correlate observed events with the atomic structures of the myosin motor. Other incompletely understood issues include the role of the two heads of myosin II and structural changes in the actin filaments as well as the importance of the three-dimensional order. We here review these issues in relation to controversies regarding basic physiological properties of striated muscle. We also briefly consider actomyosin mutation effects in cardiac and skeletal muscle function and the possibility to treat these defects by drugs.

Hand-held model of a sarcomere to illustrate the sliding filament mechanism in muscle contraction

2009 ◽  
Vol 33 (4) ◽  
pp. 297-301 ◽  
Author(s):  
Karnyupha Jittivadhna ◽  
Pintip Ruenwongsa ◽  
Bhinyo Panijpan
Keyword(s):  
Muscle Contraction ◽  
Striated Muscle ◽  
Computer Graphic ◽  
Alternative Conceptions ◽  
Two Dimensional ◽  
Thin Filaments ◽  
Transverse Expansion ◽  
Thin Elements ◽  
Common Items ◽  
Graphic Displays

From our teaching of the contractile unit of the striated muscle, we have found limitations in using textbook illustrations of sarcomere structure and its related dynamic molecular physiological details. A hand-held model of a striated muscle sarcomere made from common items has thus been made by us to enhance students' understanding of the sliding filament mechanism as well as their appreciation of the spatial arrangements of the thick and thin filaments. The model proves to be quite efficacious in dispelling some alternative conceptions held by students exposed previously only to two-dimensional textbook illustrations and computer graphic displays. More importantly, after being taught by this hand-held device, electronmicrographic features of the A and I bands, H zone, and Z disk can be easily correlated by the students to the positions of the thick and thin elements relatively sliding past one another. The transverse expansion of the sarcomere and the constancy of its volume upon contraction are also demonstrable by the model.

Rapid small-angle X-ray diffraction of a tonically contracting molluscan smooth muscle recorded with imaging plates

1989 ◽  
Vol 22 (1) ◽  
pp. 72-74 ◽  
Author(s):  
Y. Tajima ◽  
K. Okada ◽  
O. Yoshida ◽  
T. Seto ◽  
Y. Amemiya
Keyword(s):  
Small Angle ◽  
Structural Changes ◽  
High Sensitivity ◽  
Imaging Plate ◽  
Layer Line ◽  
X Ray Diffraction ◽  
Thin Filaments ◽  
X Ray ◽  
Area Detector ◽  
Diffraction Patterns

Small-angle X-ray diffraction patterns from the anterior byssus retractor muscles of Mytilus edulis contracting tonically in response to stimulation with acetylcholine were recorded in a 30 s exposure with synchrotron radiation and a high-sensitivity X-ray area detector called an imaging plate. The 190 Å layer line from the thin filaments increased in intensity with increase in tonic tension up to 6 x 104 kg m−2. Above this value, the layer-line intensity remained almost constant and comparable to that for a contracting skeletal muscle, indicating that the same structural changes of the thin filaments occur in both muscles.

scholarly journals X-ray diffraction evidence for the existence of 102.0- and 230.0-nm transverse periodicities in striated muscle.

1987 ◽  
Vol 105 (3) ◽  
pp. 1311-1318 ◽  
Author(s):  
J Bordas ◽  
G R Mant ◽  
G P Diakun ◽  
C Nave
Keyword(s):  
Electron Density ◽  
Striated Muscle ◽  
Diffraction Theory ◽  
Optical Microscope ◽  
Sartorius Muscle ◽  
X Ray Diffraction ◽  
X Ray ◽  
Density Maps ◽  
Diffraction Patterns ◽  
Integrated Intensities

Synchrotron radiation techniques have enabled us to record meridional x-ray diffraction patterns from frog sartorius muscle at resolutions ranging from approximately 2,800 to 38 nm (i.e., overlapping with the optical microscope and the region normally accessible with low angle diffraction cameras). These diffraction patterns represent the transform of the low resolution structure of muscle projected on the sarcomere axis and sampled by its repeat. Altering the sarcomere length results in the sampling of different parts of this transform, which induces changes in the positions and the integrated intensities of the diffraction maxima. This effect has been used to determine the transform of the mass projection on the muscle axis in a quasicontinuous fashion. The results reveal the existence of maxima arising from long-range periodicities in the structure. Determination of the zeroes in the transforms has been used to obtain phase information from which electron density maps have been calculated. The x-ray diffraction diagrams and the resulting electron density maps show the existence of a series of mass bands, disposed transversely to the sarcomere axis and distributed at regular intervals. A set of these transverse structures is associated with thin filaments, and their 102.0-nm repeat suggests a close structural relationship with their known molecular components. A second set, spaced by approximately 230.0 nm, is also present; from diffraction theory one has to conclude that this repeat simultaneously exists in thick and thin filament regions.

scholarly journals Comparative Biomechanics of Thick Filaments and Thin Filaments with Functional Consequences for Muscle Contraction

2010 ◽  
Vol 2010 ◽  
pp. 1-14 ◽  
Author(s):  
Mark S. Miller ◽  
Bertrand C. W. Tanner ◽  
Lori R. Nyland ◽  
Jim O. Vigoreaux
Keyword(s):  
Mechanical Properties ◽  
Muscle Contraction ◽  
Material Properties ◽  
Muscle Function ◽  
Striated Muscle ◽  
Muscle Performance ◽  
Thin Filaments ◽  
Thick Filaments ◽  
Functional Consequences

The scaffold of striated muscle is predominantly comprised of myosin and actin polymers known as thick filaments and thin filaments, respectively. The roles these filaments play in muscle contraction are well known, but the extent to which variations in filament mechanical properties influence muscle function is not fully understood. Here we review information on the material properties of thick filaments, thin filaments, and their primary constituents; we also discuss ways in which mechanical properties of filaments impact muscle performance.

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