scholarly journals Effects on shortening velocity of rabbit skeletal muscle due to variations in the level of thin-filament activation.

1986 ◽  
Vol 377 (1) ◽  
pp. 487-505 ◽  
Author(s):  
R L Moss
Keyword(s):  
Skeletal Muscle ◽  
Thin Filament ◽  
Rabbit Skeletal Muscle ◽  
Shortening Velocity ◽  
Filament Activation

scholarly journals Influence of enhanced troponin C Ca2+-binding affinity on cooperative thin filament activation in rabbit skeletal muscle

2007 ◽  
Vol 583 (1) ◽  
pp. 337-350 ◽  
Author(s):  
Kareen L. Kreutziger ◽  
Todd E. Gillis ◽  
Jonathan P. Davis ◽  
Svetlana B. Tikunova ◽  
Michael Regnier
Keyword(s):  
Skeletal Muscle ◽  
Binding Affinity ◽  
Thin Filament ◽  
Troponin C ◽  
Rabbit Skeletal Muscle ◽  
Filament Activation

scholarly journals Dynamics of Thin-Filament Activation in Rabbit Skeletal Muscle Fibers Examined by Time-Resolved X-Ray Diffraction

2009 ◽  
Vol 96 (3) ◽  
pp. 1045-1055 ◽  
Author(s):  
Takumi Tamura ◽  
Jun'ichi Wakayama ◽  
Katsuaki Inoue ◽  
Naoto Yagi ◽  
Hiroyuki Iwamoto
Keyword(s):  
Skeletal Muscle ◽  
Thin Filament ◽  
Muscle Fibers ◽  
Rabbit Skeletal Muscle ◽  
X Ray Diffraction ◽  
Time Resolved ◽  
X Ray ◽  
Skeletal Muscle Fibers ◽  
Filament Activation

scholarly journals Ca2+ Regulation of Rabbit Skeletal Muscle Thin Filament Sliding: Role of Cross-Bridge Number

2003 ◽  
Vol 85 (3) ◽  
pp. 1775-1786 ◽  
Author(s):  
Bo Liang ◽  
Ying Chen ◽  
Chien-Kao Wang ◽  
Zhaoxiong Luo ◽  
Michael Regnier ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Thin Filament ◽  
Rabbit Skeletal Muscle ◽  
Cross Bridge ◽  
Muscle Thin Filament ◽  
Bridge Number

scholarly journals The effect of altered temperature on Ca2(+)-sensitive force in permeabilized myocardium and skeletal muscle. Evidence for force dependence of thin filament activation.

1990 ◽  
Vol 96 (6) ◽  
pp. 1221-1245 ◽  
Author(s):  
N K Sweitzer ◽  
R L Moss
Keyword(s):  
Skeletal Muscle ◽  
Cardiac Muscle ◽  
Thin Filament ◽  
Calcium Sensitivity ◽  
Differential Sensitivity ◽  
Fiber Types ◽  
Tension Development ◽  
Maximum Tension ◽  
Filament Activation ◽  
Muscle Types

The effect of changes in temperature on the calcium sensitivity of tension development was examined in permeabilized cellular preparations of rat ventricle and rabbit psoas muscle. Maximum force and Ca2+ sensitivity of force development increased with temperature in both muscle types. Cardiac muscle was more sensitive to changes in temperature than skeletal muscle in the range 10-15 degrees C. It was postulated that the level of thin filament activation may be decreased by cooling. To investigate this possibility, troponin C (TnC) was partially extracted from both muscle types, thus decreasing the level of thin filament activation independent of temperature and, at least in skeletal muscle fibers, decreasing cooperative activation of the thin filament as well. TnC extraction from cardiac muscle reduced the calcium sensitivity of tension less than did extraction of TnC from skeletal muscle. In skeletal muscle the midpoint shift of the tension-pCa curve with altered temperature was greater after TnC extraction than in control fibers. Calcium sensitivity of tension development was proportional to the maximum tension generated in cardiac or skeletal muscle under all conditions studied. Based on these results, we conclude that (a) maximum tension-generating capability and calcium sensitivity of tension development are related, perhaps causally, in fast skeletal and cardiac muscles, and (b) thin filament activation is less cooperative in cardiac muscle than in skeletal muscle, which explains the differential sensitivity of the two fiber types to temperature and TnC extraction. Reducing thin filament cooperativity in skeletal muscle by TnC extraction results in a response to temperature similar to that of control cardiac cells. This study provides evidence that force levels in striated muscle influence the calcium binding affinity of TnC.

scholarly journals Isolation of Nebulin from Rabbit Skeletal Muscle and Its Interaction with Actin

2010 ◽  
Vol 2010 ◽  
pp. 1-8 ◽  
Author(s):  
Ryo Chitose ◽  
Atsushi Watanabe ◽  
Masato Asano ◽  
Akira Hanashima ◽  
Kouhei Sasano ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Column Chromatography ◽  
Salt Solution ◽  
Actin Filaments ◽  
Thin Filament ◽  
Full Length ◽  
Rabbit Skeletal Muscle ◽  
Native Form ◽  
20 Nm ◽  
Vertebrate Skeletal Muscle

Nebulin is about 800 kDa filamentous protein that binds the entire thin filament of vertebrate skeletal muscle sarcomeres. Nebulin cannot be isolated from muscle except in a completely denatured form by direct solubilization of myofibrils with SDS because nebulin is hardly soluble under salt conditions. In the present study, nebulin was solubilized by a salt solution containing 1 M urea and purified by DEAE-Toyopearl column chromatography via 4 M urea elution. Rotary-shadowed images of nebulin showed entangled knit-like particles, about 20 nm in diameter. The purified nebulin bound to actin filaments to form loose bundles. Nebulin was confirmed to bind actin,α-actinin,β-actinin, and tropomodulin, but not troponin or tropomyosin. The data shows that full-length nebulin can be also obtained in a functional and presumably native form, verified by data from experiments using recombinant subfragments.

scholarly journals Thin-filament regulation of force redevelopment kinetics in rabbit skeletal muscle fibres

2007 ◽  
Vol 579 (2) ◽  
pp. 313-326 ◽  
Author(s):  
Alicia Moreno-Gonzalez ◽  
Todd E. Gillis ◽  
Anthony J. Rivera ◽  
P. Bryant Chase ◽  
Donald A. Martyn ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Thin Filament ◽  
Rabbit Skeletal Muscle ◽  
Muscle Fibres ◽  
Thin Filament Regulation ◽  
Skeletal Muscle Fibres
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