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
1983 ◽  
Vol 96 (2) ◽  
pp. 435-442 ◽  
Author(s):  
M Yamaguchi ◽  
R M Robson ◽  
M H Stromer

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.


1998 ◽  
Vol 78 (2) ◽  
pp. 359-391 ◽  
Author(s):  
BARRY M. MILLMAN

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.


1983 ◽  
Vol 4 (5) ◽  
pp. 459-466 ◽  
Author(s):  
ITARU TOYOSHIMA ◽  
KEIKO TANAKA ◽  
NOBUYOSHI FUKUHARA ◽  
TOSHIHIDE KUMAMOTO ◽  
TADASHI MIYATAKE

1998 ◽  
Vol 275 (6) ◽  
pp. C1548-C1554 ◽  
Author(s):  
Gordon S. Lynch ◽  
John A. Faulkner

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.


1996 ◽  
Vol 80 (4) ◽  
pp. 1296-1303 ◽  
Author(s):  
R. J. Talmadge ◽  
R. R. Roy ◽  
G. R. Chalmers ◽  
V. R. Edgerton

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.


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 ◽  
...  

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

1998 ◽  
Vol 274 (6) ◽  
pp. C1608-C1615 ◽  
Author(s):  
Philip A. Wahr ◽  
J. David Johnson ◽  
Jack. A. Rall

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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