Fiber splitting in tonic and phasic skeletal muscles following denervation, chloroquine and Triton WR-1339 treatments

1982 ◽  
Vol 39 (1) ◽  
pp. 111-123 ◽  
Author(s):  
Jerome J. Trout ◽  
William T. Stauber ◽  
Byron A. Schottelius
Keyword(s):  
Skeletal Muscles ◽  
Fiber Splitting ◽  
Triton Wr 1339

Dystrophy of the Diaphragmatic Muscles in Adult Meuse-Rhine-Yssel Cattle: Electromyographical and Histological Findings

1983 ◽  
Vol 20 (1) ◽  
pp. 32-48 ◽  
Author(s):  
S.A. Goedegebuure ◽  
W. Hartman ◽  
H.P. Hoebe
Keyword(s):  
Action Potentials ◽  
Skeletal Muscles ◽  
Duration Of Action ◽  
Progressive Muscular Dystrophy ◽  
Fiber Splitting ◽  
Fiber Size ◽  
Central Nervous Systems ◽  
Cardiac Muscles ◽  
Muscle Disorder ◽  
Electromyographic Investigation

Electromyographic investigation of diaphragmatic muscles of Meuse-Rhine-Yssel cattle revealed a significant decreased duration of action potentials, while the number of polyphasic potentials was increased in four of seven cows. Histologically, the diaphragmatic muscles in all cows were affected severely, as characterized by variation in size of individual fibers, abundant vacuolar and hyaline degeneration with occasional fragmentation and phagocytosis, fiber splitting, apparent increase in internal nuclei, vesicular nuclei, chains of central nuclei, absence of regeneration, and proliferation of endomysial and perimysial connective tissue. Core-like structures seemed to be a hallmark of the disease. The intercostal muscles in all cows had core-like structures and some variation in fiber size; degenerative lesions did occur, but were less severe than in diaphragmatic muscles. In other skeletal muscles and cardiac muscles, core-like structures were present predominantly, indicating a generalized muscle disorder. No lesions were detected in the peripheral or central nervous systems. The muscular alterations were classified as a progressive muscular dystrophy, with a suspicion of hereditary transmission. This dystrophy may be an important animal model.

scholarly journals Histological aspects of skeletal muscle fibers splitting of C57BL/6NCrl mice

2020 ◽  
pp. 291-296 ◽  
Author(s):  
P. Makovický ◽  
P. Makovický
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fiber ◽  
Skeletal Muscles ◽  
Muscle Fibers ◽  
Rectus Femoris ◽  
Skeletal Muscle Fiber ◽  
Fiber Splitting ◽  
Muscular Fiber ◽  
Skeletal Muscle Fibers ◽  
Muscle Fiber Regeneration

The objective of the current study is to present data on the splitting of skeletal muscle fibers in C57BL/6NCrl mice. Skeletal muscles (m. rectus femoris (m. quadriceps femoris)) from 500 (250 ♀ and 250 ♂) C57BL/6NCrl mice in the 16th week of life were sampled during autopsy and afterwards standardly histologically processed. Results show spontaneous skeletal muscle fiber splitting which is followed by skeletal muscle fiber regeneration. One solitary skeletal muscle fiber is split, or is in contact with few localized splitting skeletal muscle fibers. Part of the split skeletal muscular fiber is phagocytosed, but the remaining skeletal muscular fiber splits are merged into one regenerating skeletal muscle fiber. Nuclei move from the periphery to the regenerating skeletal muscle fiber center during this process. No differences were observed between female and male mice and the morphometry results document <1 % skeletal muscle fiber splitting. If skeletal muscular fibers splitting occurs 5 %> of all skeletal muscular fibers, it is suggested to describe and calculate this in the final histopathological report.

Distribution of c-protein isoforms in sarcomeres of developing chick skeletal muscle

1988 ◽  
Vol 46 ◽  
pp. 226-227
Author(s):  
D. A. Fischman ◽  
J. E. Dennis ◽  
T. Obinata ◽  
H. Takano-Ohmuro
Keyword(s):  
Skeletal Muscles ◽  
Thick Filament ◽  
Protein Isoforms ◽  
Actin Binding ◽  
Striated Muscles ◽  
C Protein ◽  
Sarcomeric Protein ◽  
Thick Filaments ◽  
Cross Bridges ◽  
Bridge Bearing

C-protein is a 150 kDa protein found within the A bands of all vertebrate cross-striated muscles. By immunoelectron microscopy, it has been demonstrated that C-protein is distributed along a series of 7-9 transverse stripes in the medial, cross-bridge bearing zone of each A band. This zone is now termed the C-zone of the sarcomere. Interest in this protein has been sparked by its striking distribution in the sarcomere: the transverse repeat between C-protein stripes is 43 nm, almost exactly 3 times the 14.3 nm axial repeat of myosin cross-bridges along the thick filaments. The precise packing of C-protein in the thick filament is still unknown. It is the only sarcomeric protein which binds to both myosin and actin, and the actin-binding is Ca-sensitive. In cardiac and slow, but not fast, skeletal muscles C-protein is phosphorylated. Amino acid composition suggests a protein of little or no αhelical content. Variant forms (isoforms) of C-protein have been identified in cardiac, slow and embryonic muscles.

The effect of ionophore A23178 on the α-actinin crosslinks in the z-band of frog skeletal muscle: An EM study

1986 ◽  
Vol 44 ◽  
pp. 154-155
Author(s):  
F.T. Llados ◽  
V. Krlho ◽  
G.D. Pappas
Keyword(s):  
Muscle Damage ◽  
Transmitter Release ◽  
Skeletal Muscles ◽  
Calcium Uptake ◽  
Muscle Membrane ◽  
Frog Skeletal Muscle ◽  
Ach Release ◽  
Sustained Action ◽  
Calcium Deposits ◽  
Intense Stimulation

It Is known that Ca++ enters the muscle fiber at the junctional area during the action of the neurotransmitter, acetylcholine (ACh). Pappas and Rose demonstrated that following Intense stimulation, calcium deposits are found In the postsynaptic muscle membrane, Indicating the existence of calcium uptake In the postsynaptic area following ACh release. In addition to this calcium uptake, when mammal Ian skeletal muscles are exposed to a sustained action of the neurotransmitter, muscle damage develops. These same effects, l.e., Increased transmitter release, calcium uptake and finally muscle damage, can be obtained by Incubating the muscle with lonophore A23178.

Comparative Morphology of Skeletal Muscles in Man and Macaque

1993 ◽  
Vol 5 (2) ◽  
pp. 137-146
Author(s):  
Seiichiro INOKUCHI ◽  
Tadanao KIMURA ◽  
Masataka SUZUKI ◽  
Junji ITO ◽  
Hiroo KUMAKURA
Keyword(s):  
Skeletal Muscles ◽  
Comparative Morphology

2482-PUB: Circadian Clock Regulates Fuel Metabolism in Skeletal Muscles

Diabetes ◽  
2019 ◽  
Vol 68 (Supplement 1) ◽  
pp. 2482-PUB
Author(s):  
JIDONG LIU ◽  
ZHENG SUN
Keyword(s):  
Circadian Clock ◽  
Skeletal Muscles ◽  
Fuel Metabolism

Diabetes decreases Na+-K+ pump concentration in skeletal muscles, heart ventricular muscle, and peripheral nerves of rat

Diabetes ◽  
1987 ◽  
Vol 36 (7) ◽  
pp. 842-848 ◽  
Author(s):  
K. Kjeldsen ◽  
H. Braendgaard ◽  
P. Sidenius ◽  
J. S. Larsen ◽  
A. Norgaard
Keyword(s):  
Peripheral Nerves ◽  
Skeletal Muscles ◽  
Ventricular Muscle
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