Binding of heavy meromyosin and subfragment-1 to thin filaments in myofibrils and single muscle fibers

Biochemistry ◽  
1980 ◽  
Vol 19 (21) ◽  
pp. 4913-4921 ◽  
Author(s):  
Julian Borejdo ◽  
Olga Assulin
Keyword(s):  
Muscle Fibers ◽  
Single Muscle ◽  
Heavy Meromyosin ◽  
Thin Filaments

scholarly journals Evidence for actin involvement in cardiac Z-lines and Z-line analogues.

1983 ◽  
Vol 96 (2) ◽  
pp. 435-442 ◽  
Author(s):  
M Yamaguchi ◽  
R M Robson ◽  
M H Stromer
Keyword(s):  
Electron Microscopy ◽  
Actin Filaments ◽  
Muscle Fibers ◽  
Opposite Polarity ◽  
Dense Material ◽  
Heavy Meromyosin ◽  
Thin Filaments ◽  
Electron Dense Material ◽  
Before And After

Canine and feline cardiac Z-lines and Z-rods were examined by electron microscopy before and after digestion of muscle fibers with Ca2+-activated protease (CAF). Removal by CAF of electron-dense material which covers Z-lines and Z-rods exposed interdigitating longitudinal filaments (6-7 nm in diameter) apparently continuous with thin filaments of the respective I-bands. The newly exposed longitudinal filaments of CAF-treated Z-lines and of CAF-treated Z-rods bound heavy meromyosin and therefore are actin. The width of Z-lines and length of Z-rods are determined by the amount of overlap of actin filaments of opposite polarity. The oblique filaments in Z-lines and Z-rods are responsible for the perpendicular periodicity of Z-lines and Z-rods, and are attributed to alpha-actinin.

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 DISSECTION AND ELECTROPHORETIC PROTEIN ANALYSIS OF SINGLE MUSCLE FIBERS FROM HISTOLOGICALLY IDENTIFIED FREEZE-DRIED SECTIONS: APPLICATION TO MUSCLE FIBERS WITH RIMMED VACUOLES

1983 ◽  
Vol 4 (5) ◽  
pp. 459-466 ◽  
Author(s):  
ITARU TOYOSHIMA ◽  
KEIKO TANAKA ◽  
NOBUYOSHI FUKUHARA ◽  
TOSHIHIDE KUMAMOTO ◽  
TADASHI MIYATAKE
Keyword(s):  
Muscle Fibers ◽  
Protein Analysis ◽  
Single Muscle ◽  
Freeze Dried

Contraction-induced injury to single muscle fibers: velocity of stretch does not influence the force deficit

1998 ◽  
Vol 275 (6) ◽  
pp. C1548-C1554 ◽  
Author(s):  
Gordon S. Lynch ◽  
John A. Faulkner
Keyword(s):  
Null Hypothesis ◽  
Muscle Injury ◽  
Isometric Force ◽  
Muscle Fibers ◽  
Single Muscle ◽  
Control Value ◽  
Severity Of Injury ◽  
Before And After ◽  
The Difference ◽  
Permeabilized Fibers

We tested the null hypothesis that the severity of injury to single muscle fibers following a single pliometric (lengthening) contraction is not dependent on the velocity of stretch. Each single permeabilized fiber obtained from extensor digitorum longus muscles of rats was maximally activated and then exposed to a single stretch of either 5, 10, or 20% strain [% of fiber length ( L f)] at a velocity of 0.5, 1.0, or 2.0 L f /s. The force deficit, the difference between maximum tetanic isometric force (Po) before and after the stretch expressed as a percentage of the control value for Po before the stretch, provided an estimate of the magnitude of muscle injury. Despite a fourfold range from the lowest to the highest velocities, force deficits were not different among stretches of the same strain. At stretches of 20% strain, even an eightfold range of velocities produced no difference in the force deficit, although 40% of the fibers were torn apart at a velocity of 4 L f /s. We conclude that, within the range of velocities tolerated by single permeabilized fibers, the severity of contraction-induced injury is not related to the velocity of stretch.

MHC and sarcoplasmic reticulum protein isoforms in functionally overloaded cat plantaris muscle fibers

1996 ◽  
Vol 80 (4) ◽  
pp. 1296-1303 ◽  
Author(s):  
R. J. Talmadge ◽  
R. R. Roy ◽  
G. R. Chalmers ◽  
V. R. Edgerton
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Heavy Chain ◽  
Muscle Fibers ◽  
Protein Isoforms ◽  
Type I ◽  
Single Muscle ◽  
Plantaris Muscle ◽  
Plasmic Reticulum ◽  
Deep Region ◽  
Isoform Expression

To determine whether the adaptations in myosin heavy chain (MHC) isoform expression after functional overload (FO) are accompanied by commensurate adaptations in protein isoforms responsible for relaxation [sarco(endo)plasmic reticulum (SR) Ca(2+)-adenosinetriphosphatase (SERCA) and phospholamban (PHL)] in single muscle fibers, the isoforms of MHC and SERCA and the presence or absence of PHL were determined for cat plantaris fibers 3 mo after FO. In control plantaris the relative MHC isoform composition was 23% type I, 21% type IIa, and 56% type IIb. FO resulted in a shift toward slower isoforms (33% type I, 44% type IIa, and 23% type IIb). In the deep region of the plantaris the proportions of type I MHC and hybrid MHC fibers (containing type I and II MHCs) were 40 and 200% greater in FO cats, respectively. FO resulted in a 47% increase in the proportion of fibers containing only the slow SERCA isoform (SERCA2) and a 41% increase in the proportion of fibers containing PHL. The proportions of fibers containing type I MHC, SERCA2, and PHL in control and FO plantaris were linearly correlated. These data show that adaptations in MHC isoform expression are accompanied by commensurate adaptations in sarcoplasmic reticulum protein isoforms in single muscle fibers after FO.

The mutations m.5628T>C and m.8348A>G in single muscle fibers of a patient with chronic progressive external ophthalmoplegia

2012 ◽  
Vol 320 (1-2) ◽  
pp. 131-135 ◽  
Author(s):  
Juliana Gamba ◽  
Beatriz Hitomi Kiyomoto ◽  
Acary Souza Bulle de Oliveira ◽  
Alberto Alain Gabbai ◽  
Beny Schmidt ◽  
...  
Keyword(s):  
Muscle Fibers ◽  
Progressive External Ophthalmoplegia ◽  
Chronic Progressive External Ophthalmoplegia ◽  
Single Muscle

Size changes in single muscle fibers during fixation and embedding

1975 ◽  
Vol 7 (2) ◽  
pp. 383-387 ◽  
Author(s):  
Brenda R. Eisenberg ◽  
Bert A. Mobley
Keyword(s):  
Muscle Fibers ◽  
Single Muscle

Determinants of relaxation rate in skinned frog skeletal muscle fibers

1998 ◽  
Vol 274 (6) ◽  
pp. C1608-C1615 ◽  
Author(s):  
Philip A. Wahr ◽  
J. David Johnson ◽  
Jack. A. Rall
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fibers ◽  
Slow Phase ◽  
Frog Skeletal Muscle ◽  
Force Of Contraction ◽  
Thin Filaments ◽  
Fast Phase ◽  
Skeletal Muscle Fibers ◽  
Kinetics Of ◽  
Overall Kinetics

The influences of sarcomere uniformity and Ca2+ concentration on the kinetics of relaxation were examined in skinned frog skeletal muscle fibers induced to relax by rapid sequestration of Ca2+ by the photolysis of the Ca2+ chelator, diazo-2, at 10°C. Compared with an intact fiber, diazo-2-induced relaxation exhibited a faster and shorter initial slow phase and a fast phase with a longer tail. Stabilization of the sarcomeres by repeated releases and restretches during force development increased the duration of the slow phase and slowed its kinetics. When force of contraction was decreased by lowering the Ca2+concentration, the overall kinetics of relaxation was accelerated, with the slow phase being the most sensitive to Ca2+ concentration. Twitchlike contractions were induced by photorelease of Ca2+ from a caged Ca2+ (DM-Nitrophen), with subsequent Ca2+ sequestration by intact sarcoplasmic reticulum or Ca2+ rebinding to caged Ca2+. These twitchlike responses exhibited relaxation kinetics that were about twofold slower than those observed in intact fibers. Results suggest that the slow phase of relaxation is influenced by the degree of sarcomere homogeneity and rate of Ca2+ dissociation from thin filaments. The fast phase of relaxation is in part determined by the level of Ca2+ activation.

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