scholarly journals THE FINE STRUCTURE OF STRIATED MUSCLE

1956 ◽  
Vol 2 (4) ◽  
pp. 131-142 ◽  
Author(s):  
A. J. Hodge
Keyword(s):  
Skeletal Muscle ◽  
Phase Contrast ◽  
Striated Muscle ◽  
General Structure ◽  
Electron Microscopic ◽  
Strong Contraction ◽  
Other Substances ◽  
Microscopic Studies ◽  
Insect Skeletal Muscle ◽  
Band Material

The available evidence from phase contrast, polarization optical, and electron microscopic studies on vertebrate skeletal muscle, insect skeletal muscle, and dipteran flight muscle is interpreted as favoring the following general structure of striated muscle. A continuous array of filaments (actin) runs through all bands of the sarcomere. These are linked by an axially periodic system of transverse filamentous bridges. Myosin (and probably other substances) are localized in the A bands. The system of transverse bridges compensates the birefringence of actin and is thus responsible for the isotropy of the I band. Myosin is responsible for the birefringence of the A bands. On strong contraction, A band material migrates to the Z bands to form contraction bands. It is not yet certain whether this migration involves myosin or another A band component.

A HISTOCHEMICAL AND ELECTRON MICROSCOPIC STUDY OF SKELETAL MUSCLE IN A CASE OF POMPE'S DISEASE (GLYCOGENOSIS II)

PEDIATRICS ◽  
1966 ◽  
Vol 37 (2) ◽  
pp. 249-259
Author(s):  
Robert Darrell Cardiff
Keyword(s):  
Skeletal Muscle ◽  
Microscopic Study ◽  
Electron Microscopic Study ◽  
Striated Muscle ◽  
Electron Microscopic ◽  
Pompe’S Disease ◽  
Pompe's Disease ◽  
Microscopic Studies ◽  
Alpha Glucosidase ◽  
Glycogenosis Ii

1. A case of Pompe's disease (glycogenosis II) without biochemically or histochemically demonstrable alpha-glucosidase activity is described. 2. Histochemical studies of skeletal muscle suggested that the glycogen is frequently stored as an acid mucopolysaccharide. 3. Electron microscopic studies revealed that the major glycogen deposits in most tissue were within membrane-limited sacs. Striated muscle was an exception because major deposits were frequently extrasaccular. 4. The findings in this case are discussed in relation to current concepts of Pompe's disease. In view of the extrasaccular glycogen deposits in skeletal muscle, it is suggested that an extralysosomal factor plays a significant role in the pathogenesis of Pompe's disease.

scholarly journals Osmotic Fragility of Human Blood Platelets: Phase Contrast and Electron Microscopic Studies

Blood ◽  
1958 ◽  
Vol 13 (8) ◽  
pp. 773-777 ◽  
Author(s):  
J. GUREVITCH ◽  
D. NELKEN ◽  
D. DANON
Keyword(s):  
Human Blood ◽  
Phase Contrast ◽  
Blood Platelets ◽  
Osmotic Fragility ◽  
Salt Solutions ◽  
Electron Microscopic ◽  
Microscopic Studies ◽  
Human Blood Platelets ◽  
Morphologic Changes

Abstract Phase contrast and electron microscopic studies on the morphologic changes of platelets in various hypotonic salt solutions are presented.

scholarly journals THE RELATIONSHIP BETWEEN MYOFILAMENT PACKING DENSITY AND SARCOMERE LENGTH IN FROG STRIATED MUSCLE

1967 ◽  
Vol 33 (2) ◽  
pp. 255-263 ◽  
Author(s):  
Philip W. Brandt ◽  
Enrique Lopez ◽  
John P. Reuben ◽  
Harry Grundfest
Keyword(s):  
Cross Sections ◽  
Packing Density ◽  
Sarcomere Length ◽  
Striated Muscle ◽  
X Ray Diffraction ◽  
Electron Microscopic ◽  
Semitendinosus Muscle ◽  
Direct Function ◽  
Microscopic Studies

In cross-sections of single fibers from the frog semitendinosus muscle the number of thick myofilaments per unit area (packing density) is a direct function of the sarcomere length. Our data, derived from electron microscopic studies, fit well with other data derived from in vivo, low-angle X-ray diffraction studies of whole semitendinosus muscles. The data are consistent with the assumption that the sarcomere of a fibril maintains a constant volume during changes in sarcomere length. The myofilament lattice, therefore, expands as the sarcomere shortens. Since the distance between adjacent myofilaments is an inverse square root function of sarcomere length, the interaction of the thick and the thin myofilaments during sarcomere shortening may occur over distances which increase 70 A or more. The "expanding-sarcomere, sliding-filament" model of sarcomere shortening is discussed in terms of the current concepts of muscle architecture and contraction.

Antibody localization studies of the M-line in striated muscle

1975 ◽  
Vol 53 (6) ◽  
pp. 788-799 ◽  
Author(s):  
Esther G. Palmer
Keyword(s):  
Skeletal Muscle ◽  
Striated Muscle ◽  
Fluorescein Isothiocyanate ◽  
Double Diffusion ◽  
Prior Treatment ◽  
M Protein ◽  
Organ Specificity ◽  
Rabbit Serum ◽  
Electron Microscopic ◽  
Sucrose Solutions

An investigation of species and organ specificity of M-protein was conducted with antibodies produced to M-protein extracted from porcine skeletal muscle with solutions containing 0.25 M sucrose. Light microscopic observations with fluorescein isothiocyanate (FITC) labeled antibody and electron microscopic observations with unlabeled antibody revealed that anti-M bound only to the M-line of both fresh and glycerinated porcine skeletal and cardiac muscle. Antibody binding was eliminated by extraction of KCl-washed myofibrils with sucrose solutions. Fluorescent staining with FITC-anti-M was eliminated by prior treatment with unlabeled anti-M serum but was not prevented by prior treatment with nonimmune rabbit serum. M-line-staining antibodies were removed from antiserum by absorption with M-protein but not by absorption with actin, tropomyosin, or α-actinin. Double diffusion of anti-M against M-protein resulted in a strong precipitin reaction, which did not occur with myosin, tropomyosin, α-actinin, actin, or phosphorylase. Antibody induced by porcine M-protein bound strongly to the M-line of mouse, rabbit, and human skeletal muscle and weakly to the M-line of frog skeletal muscle.

Immunogold and freeze etch electron microscopic studies of merosin localization in basal lamina of human skeletal muscle fibers

1997 ◽  
Vol 93 (1) ◽  
pp. 34-42 ◽  
Author(s):  
Y. Wakayama ◽  
Makoto Murahashi ◽  
Takahiro Jimi ◽  
Hiroko Kojima ◽  
Seiji Shibuya ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Basal Lamina ◽  
Human Skeletal Muscle ◽  
Muscle Fibers ◽  
Electron Microscopic ◽  
Skeletal Muscle Fibers ◽  
Microscopic Studies
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