scholarly journals THE FINE STRUCTURE OF THE VENTRAL INTERSEGMENTAL ABDOMINAL MUSCLES OF THE INSECT RHODNIUS PROLIXUS DURING THE MOLTING CYCLE

1968 ◽  
Vol 37 (2) ◽  
pp. 462-481 ◽  
Author(s):  
Paul A. Toselli ◽  
Frank A. Pepe
Keyword(s):  
Skeletal Muscle ◽  
Fine Structure ◽  
Chick Embryo ◽  
Muscle Cell ◽  
Cross Sections ◽  
Rhodnius Prolixus ◽  
Abdominal Muscles ◽  
Constant Ratio ◽  
Molting Cycle ◽  
Line Material

The development of the ventral intersegmental abdominal muscles of Rhodnius prolixus is triggered by feeding. The early muscle (1 day after feeding) contains essentially nonstriated fibrils. However, in cross-sections, areas indicating early I bands, Z lines, and A bands can be recognized. Interdigitating thick and thin myofilaments do not assemble into a precise lattice until sometime between 4 and 5 days after feeding. As development continues, the number of fibrils increases, the region corresponding to the Z line increases in density, and the fibrils contain more recognizable striations. The newly formed fibrils broaden as myofilaments are added peripherally. At all stages throughout development, the ratio of thin to thick myofilaments is always 6:1. The formation of fibrils in the abdominal muscles of Rhodnius is different from that in chick embryo skeletal muscle. The major differences are that at all stages in Rhodnius there are (1) a constant ratio of thin to thick myofilaments, and (2) detectable Z-line material. Other findings in Rhodnius suggest (1) that fusion of mononucleated cells with the multinucleated muscle cell occurs, (2) that microtubules develop in the tendon cell concomitantly with development of myofibrils in the associated muscle cell, and (3) that filaments 55A in diameter aggregate into microtubules.

scholarly journals THE FINE STRUCTURE OF THE VENTRAL INTERSEGMENTAL ABDOMINAL MUSCLES OF THE INSECT RHODNIUS PROLIXUS DURING THE MOLTING CYCLE

1968 ◽  
Vol 37 (2) ◽  
pp. 445-461 ◽  
Author(s):  
Paul A. Toselli ◽  
Frank A. Pepe
Keyword(s):  
Fine Structure ◽  
Insect Flight ◽  
Motor Nerve ◽  
Thick Filament ◽  
Rhodnius Prolixus ◽  
Abdominal Muscles ◽  
Molting Cycle ◽  
Thin Filaments ◽  
Characteristic Structure ◽  
Thick Filaments

Rhodnius prolixus, a South American insect, molts five times in its development to an adult after emerging from the egg. Each molting cycle is triggered with a blood-meal. The ventral intersegmental abdominal muscles of Rhodnius develop during each molting cycle and are functional at molting. The fine structure of these fully developed muscles from fourth stage larval insects is studied. They have the characteristic structure of slow muscles. They have multiple motor nerve endings, and the myofibrils are poorly defined in cross-section. Longitudinal sections show long sarcomeres (8–10 µ), irregular Z-lines, and no apparent H zones. No M line is seen. Transverse sections through the A-band region show that each hexagonally arranged thick filament is surrounded by 12 thin filaments. Two thin filaments are shared by two neighboring thick filaments. The ratio of thin to thick filaments is 6:1. This structure is related to that found in vertebrate skeletal muscle and insect flight muscle.

The Dermal Glands of Rhodnius Prolixus

1969 ◽  
Vol 27 ◽  
pp. 258-259
Author(s):  
J. E. Lai-Fook
Keyword(s):  
Fine Structure ◽  
Secretory Activity ◽  
Rhodnius Prolixus ◽  
Outermost Layer ◽  
Cement Layer ◽  
Dermal Glands

Dermal glands are epidermal derivatives which are reported to secrete either the cement layer, which is the outermost layer of the epicuticle or some component of the moulting fluid which digests the endocuticle. The secretions do not show well-defined staining reactions and therefore they have not been positively identified. This has contributed to another difficulty, namely, that of determining the time of secretory activity. This description of the fine structure of the developing glands in Rhodnius was undertaken to determine the time of activity, with a view to investigating their function.

Skeletal muscle cell transplantation: models and methods

2019 ◽  
Vol 41 (4) ◽  
pp. 297-311 ◽  
Author(s):  
Amber L. Mueller ◽  
Robert J. Bloch
Keyword(s):  
Skeletal Muscle ◽  
Cell Transplantation ◽  
Muscle Cell ◽  
Skeletal Muscle Cell

The KATP channel Kir6.2 subunit content is higher in glycolytic than oxidative skeletal muscle fibers

2011 ◽  
Vol 301 (4) ◽  
pp. R916-R925 ◽  
Author(s):  
Krystyna Banas ◽  
Charlene Clow ◽  
Bernard J. Jasmin ◽  
Jean-Marc Renaud
Keyword(s):  
Skeletal Muscle ◽  
Cross Sections ◽  
Fiber Type ◽  
Energy Levels ◽  
Muscle Fibers ◽  
Metabolic Stress ◽  
Oxidative Capacity ◽  
Fiber Types ◽  
Fiber Damage ◽  
The Individual

It has long been suggested that in skeletal muscle, the ATP-sensitive K+ channel (KATP) channel is important in protecting energy levels and that abolishing its activity causes fiber damage and severely impairs function. The responses to a lack of KATP channel activity vary between muscles and fibers, with the severity of the impairment being the highest in the most glycolytic muscle fibers. Furthermore, glycolytic muscle fibers are also expected to face metabolic stress more often than oxidative ones. The objective of this study was to determine whether the t-tubular KATP channel content differs between muscles and fiber types. KATP channel content was estimated using a semiquantitative immunofluorescence approach by staining cross sections from soleus, extensor digitorum longus (EDL), and flexor digitorum brevis (FDB) muscles with anti-Kir6.2 antibody. Fiber types were determined using serial cross sections stained with specific antimyosin I, IIA, IIB, and IIX antibodies. Changes in Kir6.2 content were compared with changes in CaV1.1 content, as this Ca2+ channel is responsible for triggering Ca2+ release from sarcoplasmic reticulum. The Kir6.2 content was the lowest in the oxidative soleus and the highest in the glycolytic EDL and FDB. At the individual fiber level, the Kir6.2 content within a muscle was in the order of type IIB > IIX > IIA ≥ I. Interestingly, the Kir6.2 content for a given fiber type was significantly different between soleus, EDL, and FDB, and highest in FDB. Correlations of relative fluorescence intensities from the Kir6.2 and CaV1.1 antibodies were significant for all three muscles. However, the variability in content between the three muscles or individual fibers was much greater for Kir6.2 than for CaV1.1. It is suggested that the t-tubular KATP channel content increases as the glycolytic capacity increases and as the oxidative capacity decreases and that the expression of KATP channels may be linked to how often muscles/fibers face metabolic stress.

THE MYOGRAM OF THE ISOLATED SKELETAL MUSCLE CELL

Science ◽  
1930 ◽  
Vol 72 (1853) ◽  
pp. 17-18 ◽  
Author(s):  
D. E. S. Brown ◽  
F. J. M. Sichel
Keyword(s):  
Skeletal Muscle ◽  
Muscle Cell ◽  
Skeletal Muscle Cell

scholarly journals Sorting of a nonmuscle tropomyosin to a novel cytoskeletal compartment in skeletal muscle results in muscular dystrophy

2004 ◽  
Vol 166 (5) ◽  
pp. 685-696 ◽  
Author(s):  
Anthony J. Kee ◽  
Galina Schevzov ◽  
Visalini Nair-Shalliker ◽  
C. Stephen Robinson ◽  
Bernadette Vrhovski ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscular Dystrophy ◽  
Actin Cytoskeleton ◽  
Cross Sections ◽  
Thin Filament ◽  
Distinct Structure ◽  
Adjacent Structure ◽  
Cytoskeletal Network ◽  
Ragged Red Fiber

Tropomyosin (Tm) is a key component of the actin cytoskeleton and >40 isoforms have been described in mammals. In addition to the isoforms in the sarcomere, we now report the existence of two nonsarcomeric (NS) isoforms in skeletal muscle. These isoforms are excluded from the thin filament of the sarcomere and are localized to a novel Z-line adjacent structure. Immunostained cross sections indicate that one Tm defines a Z-line adjacent structure common to all myofibers, whereas the second Tm defines a spatially distinct structure unique to muscles that undergo chronic or repetitive contractions. When a Tm (Tm3) that is normally absent from muscle was expressed in mice it became associated with the Z-line adjacent structure. These mice display a muscular dystrophy and ragged-red fiber phenotype, suggestive of disruption of the membrane-associated cytoskeletal network. Our findings raise the possibility that mutations in these tropomyosin and these structures may underpin these types of myopathies.

scholarly journals Posttranscriptional control of embryonic rat skeletal muscle protein synthesis. Control at the level of translation by endogenous RNA.

1988 ◽  
Vol 107 (3) ◽  
pp. 1085-1098 ◽  
Author(s):  
C R Vanderburg ◽  
M A Nathanson
Keyword(s):  
Skeletal Muscle ◽  
Cell Differentiation ◽  
Muscle Cell ◽  
Translational Control ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Skeletal Muscle Protein ◽  
Rat Skeletal Muscle ◽  
Total Rna ◽  
Muscle Cell Differentiation

The onset of muscle cell differentiation is associated with increased transcription of muscle-specific mRNA. Studies from this laboratory using 19-d embryonic rat skeletal muscle, suggest that additional, posttranscriptional controls regulate maturation of muscle tissue via a quantitative effect upon translation, and that the regulatory component may reside within the poly A- RNA pool (Nathanson, M.A., E.W. Bush, and C. Vanderburg. 1986. J. Biol. Chem. 261:1477-1486). To further characterize muscle cell translational control, embryonic and adult total RNA were separated into oligo(dT)cellulose-bound (poly A+) and -unbound (poly A-) pools. Unbound material was subjected to agarose gel electrophoresis to resolve constituents of varying molecular size and mechanically cut into five fractions. Material of each fraction was electroeluted and recovered by precipitation. Equivalent loads of total RNA from 19-20-d embryonic rat skeletal muscle exhibited a 40% translational inhibition in comparison to its adult counterpart. Inhibition was not due to decreased message abundance because embryonic, as well as adult muscle, contained equivalent proportions of poly A+ mRNA. An inhibition assay, based upon the translatability of adult RNA and its inhibition by embryonic poly A- RNA, confirmed that inhibition was associated with a 160-2,000-nt poly A- fraction. Studies on the chemical composition of this fraction confirmed its RNA composition, the absence of ribonucleoprotein, and that its activity was absent from similarly fractionated adult RNA. Rescue of inhibition could be accomplished by addition of extra lysate or mRNA; however, smaller proportions of lysate were required, suggesting a strong interaction of inhibitor and components of the translational apparatus. Additional studies demonstrated that the inhibitor acted at the level of initiation, in a dose-dependent fashion. The present studies confirm the existence of translational control in skeletal muscle and suggest that it operates at the embryonic to adult transition. A model of muscle cell differentiation, based upon transcriptional control at the myoblast level, followed by translational regulation at the level of the postmitotic myoblast and/or myotube, is proposed.

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