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.

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 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.

The electron microscope as a diagnostic tool for skeletal muscle disease

1986 ◽  
Vol 44 ◽  
pp. 372-373
Author(s):  
J. E. Bilbao ◽  
R. A. Turner ◽  
R. T. King ◽  
J. C. Stinson
Keyword(s):  
Skeletal Muscle ◽  
Electron Microscope ◽  
Diagnostic Tool ◽  
Microscopic Examination ◽  
Striated Muscle ◽  
Electron Microscopic Examination ◽  
Muscle Disease ◽  
Electron Microscopic ◽  
Pathologic Physiology ◽  
Reaction Patterns

Time and experience has proven that striated muscle has only a limited number of reaction patterns. However, the electron microscopic examination has given information about the ultrastructural reaction of muscle fibers and about the pathologic physiology of diseased muscle. Although specific abnormalities are not useful when present individually. When present in a combination they may be diagnostic.

Artifact-free electron microscopic immunocytochemistry on rat brain tissue

1991 ◽  
Vol 49 ◽  
pp. 272-273
Author(s):  
Veronika Burmeister ◽  
N. Ludvig ◽  
P.C. Jobe
Keyword(s):  
Microscopic Examination ◽  
Free Electron ◽  
Electron Microscopic Examination ◽  
Ultrastructural Localization ◽  
Rabbit Serum ◽  
Electron Microscopic ◽  
Electron Microscopic Immunocytochemistry ◽  
Phosphate Buffered Saline ◽  
Rat Brain Tissue ◽  
Immune Rabbit

Electron microscopic immunocytochemistry provides an important tool to determine the ultrastructural distribution of various molecules in both normal and pathologic tissues. However, the specific immunostaining may be obscured by artifactual immunoreaction product, misleading the investigator. Previous observations show that shortening the incubation period with the primary antibody from the generally used 12-24 hours to 1 hour substantially reduces the artifactual immunostaining. We now extend this finding by the demonstration of artifact-free ultrastructural localization of the Ca2/calmodulindependent cyclic nucleotide phosphodiesterase (CaM-dependent PDE) immunoreactivity in brain.Anesthetized rats were perfused transcardially with phosphate-buffered saline followed by a fixative containing paraformaldehyde (4%) and glutaraldehyde (0.25%) in PBS. The brains were removed, and 40μm sections were cut with a vibratome. The sections were processed for immunocytochemistry as described by Ludvig et al. Both non-immune rabbit serum and specific CaM-dependent PDE antibodies were used. In both experiments incubations were at one hour and overnight. The immunostained sections were processed for electron microscopic examination.

scholarly journals Triadin Binding to the C-Terminal Luminal Loop of the Ryanodine Receptor is Important for Skeletal Muscle Excitation–Contraction Coupling

2007 ◽  
Vol 130 (4) ◽  
pp. 365-378 ◽  
Author(s):  
Sanjeewa A. Goonasekera ◽  
Nicole A. Beard ◽  
Linda Groom ◽  
Takashi Kimura ◽  
Alla D. Lyfenko ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Ryanodine Receptor ◽  
Calcium Release ◽  
Striated Muscle ◽  
Single Channel ◽  
Triple Mutant ◽  
Double Mutation ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Functional Studies

Ca2+ release from intracellular stores is controlled by complex interactions between multiple proteins. Triadin is a transmembrane glycoprotein of the junctional sarcoplasmic reticulum of striated muscle that interacts with both calsequestrin and the type 1 ryanodine receptor (RyR1) to communicate changes in luminal Ca2+ to the release machinery. However, the potential impact of the triadin association with RyR1 in skeletal muscle excitation–contraction coupling remains elusive. Here we show that triadin binding to RyR1 is critically important for rapid Ca2+ release during excitation–contraction coupling. To assess the functional impact of the triadin-RyR1 interaction, we expressed RyR1 mutants in which one or more of three negatively charged residues (D4878, D4907, and E4908) in the terminal RyR1 intraluminal loop were mutated to alanines in RyR1-null (dyspedic) myotubes. Coimmunoprecipitation revealed that triadin, but not junctin, binding to RyR1 was abolished in the triple (D4878A/D4907A/E4908A) mutant and one of the double (D4907A/E4908A) mutants, partially reduced in the D4878A/D4907A double mutant, but not affected by either individual (D4878A, D4907A, E4908A) mutations or the D4878A/E4908A double mutation. Functional studies revealed that the rate of voltage- and ligand-gated SR Ca2+ release were reduced in proportion to the degree of interruption in triadin binding. Ryanodine binding, single channel recording, and calcium release experiments conducted on WT and triple mutant channels in the absence of triadin demonstrated that the luminal loop mutations do not directly alter RyR1 function. These findings demonstrate that junctin and triadin bind to different sites on RyR1 and that triadin plays an important role in ensuring rapid Ca2+ release during excitation–contraction coupling in skeletal muscle.

The chicken skeletal muscle alpha-actin promoter is tissue specific in transgenic mice

1989 ◽  
Vol 9 (9) ◽  
pp. 3785-3792
Author(s):  
C J Petropoulos ◽  
M P Rosenberg ◽  
N A Jenkins ◽  
N G Copeland ◽  
S H Hughes
Keyword(s):  
Skeletal Muscle ◽  
Transgenic Mice ◽  
Striated Muscle ◽  
Transcriptional Start Site ◽  
Actin Gene ◽  
Tissue Specific ◽  
Adult Mice ◽  
Transgenic Lines ◽  
Alpha Actin ◽  
Chicken Skeletal Muscle

We have generated transgenic mouse lines that carry the promoter region of the chicken skeletal muscle alpha (alpha sk) actin gene linked to the bacterial chloramphenicol acetyltransferase (CAT) gene. In adult mice, the pattern of transgene expression resembled that of the endogenous alpha sk actin gene. In most of the transgenic lines, high levels of CAT activity were detected in striated muscle (skeletal and cardiac) but not in the other tissues tested. In striated muscle, transcription of the transgene was initiated at the normal transcriptional start site of the chicken alpha sk actin gene. The region from nucleotides -191 to +27 of the chicken alpha sk actin gene was sufficient to direct the expression of CAT in striated muscle of transgenic mice. These observations suggest that the mechanism of tissue-specific actin gene expression is well conserved in higher vertebrate species.

scholarly journals The effects of simulated microgravity on skeletal muscle of Japanese quail: transmission electron microscopic study

2011 ◽  
Vol 80 (1) ◽  
pp. 119-124 ◽  
Author(s):  
Katarína Holovská ◽  
Viera Almášiová ◽  
Viera Cigánková ◽  
Peter Škrobánek
Keyword(s):  
Skeletal Muscle ◽  
Japanese Quail ◽  
Structural Changes ◽  
Simulated Microgravity ◽  
Negative Impact ◽  
Electron Microscopic ◽  
Giant Mitochondria ◽  
Transmission Electron ◽  
Muscle Tissues ◽  
And Control

The aim of the present study was to investigate the effects of simulated microgravity (hypodynamia) on the structure of the skeletal muscle (m. gastrocnemius) in developing Japanese quail by transmission electron microscopy. Samples of muscle tissues from experimental (n = 28) and control (n = 28) birds were collected at day 7, 14, 28, 42 and 56 of age. The structure of m. gastrocnenmius was changed depending on hypodynamia length. The first extensive structural changes were found on day 14 of age. The mitochondria were enlarged and the spaces between the myofibrils were slightly extended compared to control. The sarcomeres were irregular and lipid droplets occurred in the sarcoplasm. Further developmental changes occurred on day 28 of age. Mitochondria fused into the giant mitochondria which frequently exceeded the length of one sarcomere. Moreover, at 42 days of age, beside the above mentioned changes, sarcoplasmic reticulum was dilated and the number of mitochondrial cristae was reduced. However, the structure of m. gastrocnemius on day 56 was less damaged compared to the damage observed on day 42 of age. Presented results indicate that the continuous stay of male Japanese quail under simulated microgravity has a negative impact on the structure of m. gastrocnemius, but also the ability of muscle tissue to cope with these specific conditions.

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