scholarly journals The mechanical properties of oesophageal striated muscle in the cat and sheep.

1975 ◽  
Vol 248 (3) ◽  
pp. 717-724 ◽  
Author(s):  
K Floyd ◽  
J F Morrison
2018 ◽  
Vol 114 (3) ◽  
pp. 135a-136a
Author(s):  
Joseph D. Powers ◽  
C. David Williams ◽  
Michael Regnier ◽  
Thomas L. Daniel

2010 ◽  
Vol 2010 ◽  
pp. 1-14 ◽  
Author(s):  
Mark S. Miller ◽  
Bertrand C. W. Tanner ◽  
Lori R. Nyland ◽  
Jim O. Vigoreaux

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.


Author(s):  
Gary A. Monteiro ◽  
David I. Shreiber

The long-term objective of this research is to develop tunable collagen-based biomaterial scaffolds for directed stem cell differentiation into neural lineages to aid in CNS diseases and trauma. Type I collagen is a ubiquitous protein that provides mechanostructural and ligand-induced biochemical cues to cells that attach to the protein via integrin receptors. Previous studies have demonstrated that the mechanical properties of a substrate or tissue can be an important regulator of stem cell differentiation. For example, the mechanical properties polyacrylamide gels can be tuned to induce neural differentiation from stem cells [1, 2]. Mesenchymal stem cells (MSCs) cultured on ployacrylamide gels with low elastic modulus (0.1–1 kPa) resulted in a neural like population. MSCs on 10-fold stiffer matrices that mimic striated muscle elasticity (Emuscle ∼8–17 kPa) lead to spindle-shaped cells similar in shape to myoblasts. Still stiffer gels (25–40 kPa) resulted in osetoblast differentiation. Based on these observations, collagen gels may provide an ideal material for differentiation into neural lineages because of their low compliance.


1993 ◽  
Vol 265 (2) ◽  
pp. H469-H475 ◽  
Author(s):  
R. K. Strumpf ◽  
J. D. Humphrey ◽  
F. C. Yin

The architecture, vascular supply, and ease of tetanization make the diaphragm an ideal structure in which to assess multidimensional mechanical properties of active and passive striated muscle. We developed an isolated, perfused canine diaphragm preparation suitable for the assessment of biaxial stress-strain relations in both the resting state and during tetanization. Each of 33 specimens had a wide, flat region (approximately 3 x 3 cm) wherein there was a single predominant fiber direction. Simultaneous, equal stretchings were imposed in the fiber and perpendicular cross-fiber directions over the same strain ranges in both the passive state and during tetanic contraction. Highly nonlinear behavior was seen in the passive state with a limit of extensibility in both directions. The specimens were also markedly anisotropic, with the cross-fiber direction being stiffer than the fiber direction (slopes of the regression line for the stresses in each direction averaged 3.97). Moreover, 31 of the 33 specimens were stiffer in the cross-fiber direction, one was isotropic, and one was stiffer in the fiber direction. During tetanization, the extent and distribution of anisotropy were significantly altered (regression slope averaged 1.08, and 18 specimens were now either isotropic or stiffer in the fiber direction). Disrupting the membranes covering each surface increased extensibility and decreased the anisotropy, thereby suggesting that these membranes bear most of the passive load and contribute greatly to the cross-fiber stiffness and anisotropy of the intact diaphragm. Both before and after disruption of the surface membranes, there was still a consistent increase in cross-fiber stress during tetanization, implying active force generation perpendicular to the fiber direction.(ABSTRACT TRUNCATED AT 250 WORDS)


2003 ◽  
Vol 465 (1-2) ◽  
pp. 153-161 ◽  
Author(s):  
Fumiko Sekiguchi ◽  
Kyoko Kawata ◽  
Mayumi Komori ◽  
Satoru Sunano

2001 ◽  
Vol 280 (1) ◽  
pp. C46-C52 ◽  
Author(s):  
Aladin M. Boriek ◽  
Y. Capetanaki ◽  
Willy Hwang ◽  
Todd Officer ◽  
Muffasir Badshah ◽  
...  

Striated muscle is a linear motor whose properties have been defined in terms of uniaxial structures. The question addressed here is what contribution is made to the properties of this motor by extramyofilament cytoskeletal structures that are not aligned in parallel with the myofilaments. This question arose from observations that transverse loads increase muscle force production in diaphragm but not in the hindlimb muscle, thereby indicating the presence of structures that couple longitudinal and transverse properties of diaphragmatic muscle. Furthermore, we find that the diaphragms of null mutants for the cytoskeletal protein desmin show 1) significant reductions in coupling between the longitudinal and transverse properties, indicating for the first time a role for a specific protein in integrating the three-dimensional mechanical properties of muscle, 2) significant reductions in the stiffness and viscoelasticity of muscle, and 3) significant increases in tetanic force production. Thus desmin serves a complex mechanical function in diaphragm muscle by contributing both to passive stiffness and viscoelasticity and to modulation of active force production in a three-dimensional structural network. Our finding changes the paradigm of force transmission among cells by placing our understanding of the function of the cytoskeleton in the context of the structural and mechanical complexity of muscles.


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