scholarly journals Nanoscopic changes in the lattice structure of striated muscle sarcomeres involved in the mechanism of spontaneous oscillatory contraction (SPOC)

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Fumiaki Kono ◽  
Seitaro Kawai ◽  
Yuta Shimamoto ◽  
Shin’ichi Ishiwata
Keyword(s):  
Structural Changes ◽  
Striated Muscle ◽  
Lattice Structure ◽  
Three Dimensional ◽  
Force Balance ◽  
Dynamic Force ◽  
Structural Requirement ◽  
Oscillatory Dynamics ◽  
Contractile System ◽  
Wide Range

Abstract Muscles perform a wide range of motile functions in animals. Among various types are skeletal and cardiac muscles, which exhibit a steady auto-oscillation of force and length when they are activated at an intermediate level of contraction. This phenomenon, termed spontaneous oscillatory contraction or SPOC, occurs devoid of cell membranes and at fixed concentrations of chemical substances, and is thus the property of the contractile system per se. We have previously developed a theoretical model of SPOC and proposed that the oscillation emerges from a dynamic force balance along both the longitudinal and lateral axes of sarcomeres, the contractile units of the striated muscle. Here, we experimentally tested this hypothesis by developing an imaging-based analysis that facilitates detection of the structural changes of single sarcomeres at unprecedented spatial resolution. We found that the sarcomere width oscillates anti-phase with the sarcomere length in SPOC. We also found that the oscillatory dynamics can be altered by osmotic compression of the myofilament lattice structure of sarcomeres, but they are unchanged by a proteolytic digestion of titin/connectin—the spring-like protein that provides passive elasticity to sarcomeres. Our data thus reveal the three-dimensional mechanical dynamics of oscillating sarcomeres and suggest a structural requirement of steady auto-oscillation.

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.

scholarly journals Development of synchrotron X-ray micro-tomography under extreme conditions of pressure and temperature

2017 ◽  
Vol 24 (1) ◽  
pp. 240-247 ◽  
Author(s):  
M. Álvarez-Murga ◽  
J. P. Perrillat ◽  
Y. Le Godec ◽  
F. Bergame ◽  
J. Philippe ◽  
...  
Keyword(s):  
High Pressure ◽  
Structural Changes ◽  
Three Dimensional ◽  
Crystallographic Structure ◽  
Three Dimensional Imaging ◽  
X Ray ◽  
Wide Range ◽  
Micro Tomography ◽  
Non Destructive

X-ray tomography is a non-destructive three-dimensional imaging/microanalysis technique selective to a wide range of properties such as density, chemical composition, chemical states and crystallographic structure with extremely high sensitivity and spatial resolution. Here the development of in situ high-pressure high-temperature micro-tomography using a rotating module for the Paris–Edinburgh cell combined with synchrotron radiation is described. By rotating the sample chamber by 360°, the limited angular aperture of ordinary high-pressure cells is surmounted. Such a non-destructive high-resolution probe provides three-dimensional insight on the morphological and structural evolution of crystalline as well as amorphous phases during high pressure and temperature treatment. To demonstrate the potentials of this new experimental technique the compression behavior of a basalt glass is investigated by X-ray absorption tomography, and diffraction/scattering tomography imaging of the structural changes during the polymerization of C60 molecules under pressure is performed. Small size and weight of the loading frame and rotating module means that this apparatus is portable, and can be readily installed on most synchrotron facilities to take advantage of the diversity of three-dimensional imaging techniques available at beamlines. This experimental breakthrough should open new ways for in situ imaging of materials under extreme pressure–temperature–stress conditions, impacting diverse areas in physics, chemistry, geology or materials sciences.

scholarly journals Mechanical Spectroscopy: Some Applications On Structural Changes And Relaxation Dynamics In Soft Matter

2015 ◽  
Vol 60 (3) ◽  
pp. 2077-2084
Author(s):  
Xuebang Wu ◽  
Changsong Liu
Keyword(s):  
Soft Matter ◽  
Structural Changes ◽  
Three Dimensional ◽  
Low Frequency ◽  
Soft Materials ◽  
Large Temperature ◽  
Relaxation Dynamics ◽  
Mechanical Spectroscopy ◽  
Frequency Scale ◽  
Wide Range

Abstract The general trend in soft matter is to study systems of increasing complexity covering a wide range in time and frequency. Mechanical spectroscopy is a powerful tool for understanding the structure and relaxation dynamics of these materials over a large temperature range and frequency scale. In this work, we collect a few recent applications using low-frequency mechanical spectroscopy for elucidating the structural changes and relaxation dynamics in soft matter, largely based on the author’s group. We illustrate the potential of mechanical spectroscopy with three kinds of soft materials: colloids, polymers and granular systems. Examples include structural changes in colloids, segmental relaxations in amorphous polymers, and resonant dissipation of grain chains in three-dimensional media. The present work shows that mechanical spectroscopy has been applied as a necessary and complementary tool to study the dynamics of such complex systems.

scholarly journals Directing multicellular organization by varying the aspect ratio of soft hydrogel microwells

2021 ◽  
Author(s):  
Gayatri Jayant Pahapale ◽  
Jiaxiang Tao ◽  
Milos Nikolic ◽  
Sammy Gao ◽  
Giuliano Scarcelli ◽  
...  
Keyword(s):  
Aspect Ratio ◽  
Three Dimensional ◽  
Force Balance ◽  
Substrate Stiffness ◽  
Self Organization ◽  
Balance Model ◽  
Physical Factors ◽  
Biological Processes ◽  
Chemical Patterning ◽  
Wide Range

Multicellular organization with precise spatial definition is an essential step in a wide range of biological processes, including morphogenesis, development, and healing. Gradients and patterns of chemoattractants are well-described guides of multicellular organization, but the influences of three-dimensional geometry of soft hydrogels on multicellular organization are less well defined. Here, we report the discovery of a new mode of self-organization of endothelial cells in ring-like patterns on the perimeters of hydrogel microwells that is independent of protein or chemical patterning and is driven only by geometry and substrate stiffness. We observe quantitatively striking influences of both the microwell aspect ratio (ε = perimeter/depth) and the hydrogel modulus. We systematically investigate the physical factors of cells and substrates that drive this multicellular behavior and present a mathematical model that explains the multicellular organization based upon balancing extracellular and cytoskeletal forces. These forces are determined in part by substrate stiffness, geometry, and cell density. The force balance model predicts the direction and distance of translational cell migration based on the dynamic interaction between tangential cytoskeletal tension and cell-cell and cell-substrate adhesion. We further show that the experimental observations can be leveraged to drive customized multicellular self-organization. Our observation of this multicellular behavior demonstrates the importance of the combinatorial effects of geometry and stiffness in complex biological processes. It also provides a new methodology for direction of cell organization that may facilitate the engineering of bionics and integrated model organoid systems.

SIMULATION OF SOLID STRUCTURE FORMATION IN AN ELECTRORHEOLOGICAL FLUID

1994 ◽  
Vol 08 (20n21) ◽  
pp. 2721-2730
Author(s):  
R. TAO ◽  
QI JIANG
Keyword(s):  
Temporal Evolution ◽  
Lattice Structure ◽  
Three Dimensional ◽  
Electrorheological Fluid ◽  
Dimensional Structure ◽  
Local Energy Minimum ◽  
Wide Range ◽  
Brownian Force ◽  
Er Fluid ◽  
Landau Instability

The temporal evolution of three-dimensional structure in an electrorheological (ER) fluid is examined by a computer simulation. A parameter B characterizing the ratio of the Brownian force to the dipolar force is introduced. For a wide range of B, the ER fluid was a rapid chain formation followed by aggregation of chains to form thick columns, which has a body-centered tetragonal (bct) lattice structure. The Peierls–Landau instability of single chains helps the formation of thick columns. If B is very small, the ER system will be trapped in some local energy-minimum state.

scholarly journals Inferring cellular forces from image stacks

2017 ◽  
Vol 372 (1720) ◽  
pp. 20160261 ◽  
Author(s):  
Jim H. Veldhuis ◽  
Ahmad Ehsandar ◽  
Jean-Léon Maître ◽  
Takashi Hiiragi ◽  
Simon Cox ◽  
...  
Keyword(s):  
Cancer Metastasis ◽  
Three Dimensional ◽  
Synthetic Data ◽  
Cellular Systems ◽  
Force Balance ◽  
Three Dimensions ◽  
Surface Evolver ◽  
Force Microscopy ◽  
Wide Range ◽  
Cellular Forces

Although the importance of cellular forces to a wide range of embryogenesis and disease processes is widely recognized, measuring these forces is challenging, especially in three dimensions. Here, we introduce CellFIT-3D, a force inference technique that allows tension maps for three-dimensional cellular systems to be estimated from image stacks. Like its predecessors, video force microscopy and CellFIT, this cell mechanics technique assumes boundary-specific interfacial tensions to be the primary drivers, and it constructs force-balance equations based on triple junction (TJ) dihedral angles. The technique involves image processing, segmenting of cells, grouping of cell outlines, calculation of dihedral planes, averaging along three-dimensional TJs, and matrix equation assembly and solution. The equations tend to be strongly overdetermined, allowing indistinct TJs to be ignored and solution error estimates to be determined. Application to clean and noisy synthetic data generated using Surface Evolver gave tension errors of 1.6–7%, and analyses of eight-cell murine embryos gave estimated errors smaller than the 10% uncertainty of companion aspiration experiments. Other possible areas of application include morphogenesis, cancer metastasis and tissue engineering. This article is part of the themed issue ‘Systems morphodynamics: understanding the development of tissue hardware’.

Application of stereological analysis of cell volume to isolated myocytes in culture with and without adrenergic innervation

1990 ◽  
Vol 48 (3) ◽  
pp. 416-417
Author(s):  
Jane K. Rosenthal ◽  
Dianne L. Atkins ◽  
William J. Marvin ◽  
Penny A. Krumm
Keyword(s):  
Cardiac Myocytes ◽  
Structural Changes ◽  
Three Dimensional ◽  
Adrenergic Innervation ◽  
Culture Cell ◽  
Serial Sections ◽  
Newborn Rats ◽  
Primary Culture Cell ◽  
Biological Studies ◽  
Cell Volumes

To comprehend structural changes in cardiac myocytes accompanying adrenergic innervation, it is essential that a three dimensional analysis be performed. To date, biological studies which utilize stereological methods have been limited to cells in tissue and in organs. Our laboratory has utilized current stereological techniques for measuring absolute volumes of individual myocytes in primary culture. Cell volumes are calculated for two distinct groups of cells at 96 hours in culture: isolated myocytes and myocytes innervated with adrenergic neurons (Figure 1).Cardiac myocytes are cultured from the ventricular apices of newborn rats. Cells are plated directly onto tissue culture dishes with or without preplated explants from the paravertebral thoracolumbar sympathetic chain. On day four cultures are photographed and marked for one-to-one cell location. Following conventional fixation and embeddment in eponate-12, the cells are relocated and mounted for microtomy. The cells are completely sectioned at 120nm in their parallel orientation to the surface of the dish (Figure 2). Serial sections are collected on formvar coated slotted grids and are recorded in sequence.

Going Beyond 3-D Imaging: Automated 3-D Montaged image Analysis of Cytological Specimens

1996 ◽  
Vol 54 ◽  
pp. 282-283
Author(s):  
Badrinath Roysam ◽  
Hakan Ancin ◽  
Douglas E. Becker ◽  
Robert W. Mackin ◽  
Matthew M. Chestnut ◽  
...  
Keyword(s):  
Image Analysis ◽  
Structural Changes ◽  
Sampling Methods ◽  
Spatial Clustering ◽  
Three Dimensional ◽  
Field Of View ◽  
Cell Counting ◽  
Depth Of Field ◽  
Tissue Cell ◽  
Tissue Organization

This paper summarizes recent advances made by this group in the automated three-dimensional (3-D) image analysis of cytological specimens that are much thicker than the depth of field, and much wider than the field of view of the microscope. The imaging of thick samples is motivated by the need to sample large volumes of tissue rapidly, make more accurate measurements than possible with 2-D sampling, and also to perform analysis in a manner that preserves the relative locations and 3-D structures of the cells. The motivation to study specimens much wider than the field of view arises when measurements and insights at the tissue, rather than the cell level are needed.The term “analysis” indicates a activities ranging from cell counting, neuron tracing, cell morphometry, measurement of tracers, through characterization of large populations of cells with regard to higher-level tissue organization by detecting patterns such as 3-D spatial clustering, the presence of subpopulations, and their relationships to each other. Of even more interest are changes in these parameters as a function of development, and as a reaction to external stimuli. There is a widespread need to measure structural changes in tissue caused by toxins, physiologic states, biochemicals, aging, development, and electrochemical or physical stimuli. These agents could affect the number of cells per unit volume of tissue, cell volume and shape, and cause structural changes in individual cells, inter-connections, or subtle changes in higher-level tissue architecture. It is important to process large intact volumes of tissue to achieve adequate sampling and sensitivity to subtle changes. It is desirable to perform such studies rapidly, with utmost automation, and at minimal cost. Automated 3-D image analysis methods offer unique advantages and opportunities, without making simplifying assumptions of tissue uniformity, unlike random sampling methods such as stereology.12 Although stereological methods are known to be statistically unbiased, they may not be statistically efficient. Another disadvantage of sampling methods is the lack of full visual confirmation - an attractive feature of image analysis based methods.

Conformational characterization of nucleosome structure by Electron Microscopy

1993 ◽  
Vol 51 ◽  
pp. 194-195
Author(s):  
Gregory J. Czarnota
Keyword(s):  
Electron Microscopy ◽  
Structural Changes ◽  
Physiological State ◽  
Gene Activation ◽  
Three Dimensional ◽  
Macromolecular Complex ◽  
Ultrastructural Studies ◽  
Ionic Environment ◽  
Nucleosome Structure ◽  
Dimensional Reconstruction

Chromatin structure at the fundamental level of the nucleosome is important in vital cellular processes. Recent biochemical and genetic analyses show that nucleosome structure and structural changes are very active participants in gene expression, facilitating or inhibiting transcription and reflecting the physiological state of the cell. Structural states and transitions for this macromolecular complex, composed of DNA wound about a heterotypic octamer of variously modified histone proteins, have been measured by physico-chemical techniques and by enzyme-accessibility and are recognized to occur with various post-translational modifications, gene activation, transformation and with ionic-environment. In spite of studies which indicate various forms of nucleosome structure, all current x-ray and neutron diffraction studies have consistently resulted in only one structure, suggestive of a static conformation. In contrast, two-dimensional electron microscopy studies and three-dimensional reconstruction techniques have yielded different structures. These fundamental differences between EM and other ultrastructural studies have created a long standing quandary, which I have addressed and resolved using spectroscopic electron microscopy and statistical analyses of nucleosome images in a study of nucleosome structure with ionic environment.

Structural Studies of Fibrinolysis by Electron and Light Microscopy

1999 ◽  
Vol 82 (08) ◽  
pp. 277-282 ◽  
Author(s):  
Yuri Veklich ◽  
Jean-Philippe Collet ◽  
Charles Francis ◽  
John W. Weisel
Keyword(s):  
Electron Microscopy ◽  
Light Microscopy ◽  
Plasminogen Activator ◽  
Structural Changes ◽  
Molecular Mechanisms ◽  
Degradation Products ◽  
Molecular Model ◽  
Three Dimensional ◽  
Tissue Type ◽  
Type Plasminogen Activator

IntroductionMuch is known about the fibrinolytic system that converts fibrin-bound plasminogen to the active protease, plasmin, using plasminogen activators, such as tissue-type plasminogen activator (t-PA) and urokinase-type plasminogen activator. Plasmin then cleaves fibrin at specific sites and generates soluble fragments, many of which have been characterized, providing the basis for a molecular model of the polypeptide chain degradation.1-3 Soluble degradation products of fibrin have also been characterized by transmission electron microscopy, yielding a model for their structure.4 Moreover, high resolution, three-dimensional structures of certain fibrinogen fragments has provided a wealth of information that may be useful in understanding how various proteins bind to fibrin and the overall process of fibrinolysis (Doolittle, this volume).5,6 Both the rate of fibrinolysis and the structures of soluble derivatives are determined in part by the fibrin network structure itself. Furthermore, the activation of plasminogen by t-PA is accelerated by the conversion of fibrinogen to fibrin, and this reaction is also affected by the structure of the fibrin. For example, clots made of thin fibers have a decreased rate of conversion of plasminogen to plasmin by t-PA, and they generally are lysed more slowly than clots composed of thick fibers.7-9 Under other conditions, however, clots made of thin fibers may be lysed more rapidly.10 In addition, fibrin clots composed of abnormally thin fibers formed from certain dysfibrinogens display decreased plasminogen binding and a lower rate of fibrinolysis.11-13 Therefore, our increasing knowledge of various dysfibrinogenemias will aid our understanding of mechanisms of fibrinolysis (Matsuda, this volume).14,15 To account for these diverse observations and more fully understand the molecular basis of fibrinolysis, more knowledge of the physical changes in the fibrin matrix that precede solubilization is required. In this report, we summarize recent experiments utilizing transmission and scanning electron microscopy and confocal light microscopy to provide information about the structural changes occurring in polymerized fibrin during fibrinolysis. Many of the results of these experiments were unexpected and suggest some aspects of potential molecular mechanisms of fibrinolysis, which will also be described here.

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