Relationship of membrane systems in muscle to isomyosin content

The structures and functions of the various subdivisions of the membrane systems of muscle are reviewed. Morphometric data have been recalculated using functional definitions of the membranes as identified by their proteins. Thus, the junctional coupling between the sarcoplasmic reticulum and T system is separated from the remaining longitudinal sarcoplasmic reticulum that bears the calcium ATPase protein. In addition, the morphometry of the membrane systems is related to the various muscle fiber types as defined histochemically and by protein isoforms. The relation of isomyosin type and membrane quantities are compared for guinea pig, chicken, frog, and lobster skeletal muscles and rat and rabbit cardiac muscles. Fiber plasticity is considered in terms of the mixing and matching of amounts and kinds of membranes and proteins.

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Quantitation and immunocytochemical localization of ubiquitin conjugates within rat red and white skeletal muscles.

Journal of Histochemistry & Cytochemistry ◽

10.1177/36.6.2835410 ◽

1988 ◽

Vol 36 (6) ◽

pp. 621-632 ◽

Cited By ~ 53

Author(s):

D A Riley ◽

J L Bain ◽

S Ellis ◽

A L Haas

Keyword(s):

Skeletal Muscles ◽

White Muscle ◽

Solid Phase ◽

Immunohistochemical Localization ◽

Immunogold Labeling ◽

Relative Content ◽

Muscle Fiber Types ◽

Fiber Types ◽

Immunocytochemical Localization ◽

Tissue Sections

We employed solid-phase immunochemical methods to probe the dynamics of ubiquitin pools within selected rat skeletal muscles. The total ubiquitin content of red muscles was greater than that of white muscles, even though the fractional conjugation was similar for both types of muscle. The specificity for conjugated ubiquitin in solid-phase applications, previously demonstrated for an affinity-purified antibody against SDS-denatured ubiquitin, was retained when used as a probe for ubiquitin-protein adducts in tissue sections. Immunohistochemical localization revealed that differences in ubiquitin pools derived from the relative content of red (oxidative) vs white (glycolytic) fibers, with the former exhibiting a higher content of ubiquitin conjugates. Subsequent immunogold labeling demonstrated statistically significant enhanced localization of ubiquitin conjugates to the Z-lines in both red and white muscle fiber types.

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ULTRASTRUCTURE AND ADENOSINE TRIPHOSPHATASE ACTIVITY OF RED AND WHITE MUSCLE FIBERS OF THE CAUDAL REGION OF A FISH, SALMO GAIRDNERI

The Journal of Cell Biology ◽

10.1083/jcb.55.1.42 ◽

1972 ◽

Vol 55 (1) ◽

pp. 42-57 ◽

Cited By ~ 66

Author(s):

Asish C. Nag

Keyword(s):

Electron Microscopy ◽

Sarcoplasmic Reticulum ◽

Adenosine Triphosphatase ◽

White Muscle ◽

Muscle Fibers ◽

Salmo Gairdneri ◽

Fiber Types ◽

Surface Areas ◽

Biochemical Studies ◽

T System

Electron microscopy, together with quantitation using a tracing device linked to a digital computer, reveals that the red and white muscle fibers of Salmo gairdneri differ in diameter, organization of myofibrils, dimensions of myofilaments, volumes and surface areas of T system and sarcoplasmic reticulum, morphology of mitochondria, and content of mitochondria, lipid, and glycogen. Biochemical studies show that the ATPase activity of white fibers is three times that of the red fibers. Actomyosin content of red fibers is higher than that of the white fibers. The functional significance of these differences between two fiber types is discussed.

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Distribution and dimension of the T-system in different muscle fiber types in the Atlantic hagfish (Myxine glutinosa, L.)

Cell and Tissue Research ◽

10.1007/bf00223227 ◽

1975 ◽

Vol 157 (1) ◽

Cited By ~ 10

Author(s):

Helge Korneliussen ◽

K�re Nicolaysen

Keyword(s):

Muscle Fiber ◽

Muscle Fiber Types ◽

Fiber Types ◽

Myxine Glutinosa ◽

T System

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Relationship between Muscle Fiber Types and Fibrillation Potentials. Enzyme-Histochemial and Electrophysiological Studies of Denervated Skeletal Muscles in Rats.

The Japanese Journal of Rehabilitation Medicine ◽

10.2490/jjrm1963.29.47 ◽

1992 ◽

Vol 29 (1) ◽

pp. 47-54 ◽

Cited By ~ 1

Author(s):

Kiyoshi MINEO

Keyword(s):

Muscle Fiber ◽

Skeletal Muscles ◽

Muscle Fiber Types ◽

Fiber Types ◽

Electrophysiological Studies

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Phosphorylase kinase isozymes in normal and electrically stimulated skeletal muscles

AJP Cell Physiology ◽

10.1152/ajpcell.1986.250.1.c84 ◽

1986 ◽

Vol 250 (1) ◽

pp. C84-C89 ◽

Cited By ~ 8

Author(s):

J. C. Lawrence ◽

J. A. Krsek ◽

W. J. Salsgiver ◽

J. F. Hiken ◽

S. Salmons ◽

...

Keyword(s):

Muscle Activity ◽

Skeletal Muscles ◽

Sodium Dodecyl ◽

Muscle Fiber Types ◽

Phosphorylase Kinase ◽

Fiber Types ◽

Chronic Electrical Stimulation ◽

Rabbit Skeletal Muscles ◽

Stimulation Of

Phosphorylase kinase was quantitatively immunoprecipitated from extracts of different rabbit skeletal muscles, subjected to electrophoresis on polyacrylamide gels in the presence of sodium dodecyl sulfate, and stained with silver. Amounts of the two isozymes, enzymes r and w. were determined by the staining intensities of the alpha'- and alpha -subunits, respectively. The kinase in muscles composed primarily of slow oxidative fibers was almost entirely enzyme r, but several times more of this isozyme was found in muscles with a high proportion of fast oxidative-glycolytic fibers. Enzyme w predominated in muscles composed mostly of fast glycolytic fibers. To investigate the possible role of muscle activity in controlling isozyme levels, tibialis anterior muscles were activated by chronic electrical stimulation of the peroneal nerves. After 10 wk of continuous stimulation, the amount of phosphorylase kinase was decreased by approximately 80%, and the ratio of enzyme r to enzyme w was doubled. These results demonstrate that increased muscle activity can decrease levels of phosphorylase kinase and suggest that activity may regulate the expression of the isozymes in different muscle fiber types.

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Length-tension relationship of mammalian diaphragm muscles

Journal of Applied Physiology ◽

10.1152/jappl.1983.54.6.1681 ◽

1983 ◽

Vol 54 (6) ◽

pp. 1681-1686 ◽

Cited By ~ 72

Author(s):

K. K. McCully ◽

J. A. Faulkner

Keyword(s):

Muscle Fiber ◽

Relaxation Times ◽

Isometric Tension ◽

Diaphragm Muscle ◽

Muscle Fiber Types ◽

Fiber Types ◽

Active Tension ◽

Tension Curves ◽

Relationship Of

We tested the hypothesis that the length-tension relationship of diaphragm muscle is different from that of other skeletal muscle. Isometric contractile properties of small bundles of diaphragm muscle from rats, cats, rhesus monkeys, dogs, and pigs were measured in vitro at 37 degrees C. For diaphragm muscles from all species, twitch contraction and relaxation times and histochemical myofibrillar ATPase indicated a mixture of fast and slow muscle fiber types. By use of tetanic stimulations of 400-ms duration, isometric tension was recorded from bundles of diaphragm muscle at lengths between 50 and 130% of the muscle fiber length at which active tension was maximal (Lo). At lengths below 60–70% of Lo, tetanic tension did not reach a plateau within 400 ms. With longer stimulation durations, active tension could be recorded between 30 and 40% of Lo. The length-tension curves for bundles of fibers from the diaphragm muscle were not different among species and were consistent with results reported for intact limb muscles.

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Functional effects of uridine triphosphate on human skinned skeletal muscle fibers

Canadian Journal of Physiology and Pharmacology ◽

10.1139/y98-003 ◽

1998 ◽

Vol 76 (2) ◽

pp. 110-117 ◽

Cited By ~ 2

Author(s):

R Vianna-Jorge ◽

C F Oliveira ◽

Y Mounier ◽

G Suarez-Kurtz

Keyword(s):

Skeletal Muscle ◽

Sarcoplasmic Reticulum ◽

Muscle Fibers ◽

Fiber Types ◽

Release Channel ◽

Uridine Triphosphate ◽

Skinned Muscle ◽

Skeletal Muscle Fibers ◽

Slow Type ◽

Relationship Of

Chemically skinned human skeletal muscle fibers were used to study the effects of uridine triphosphate (UTP) on the tension-pCa relationship and on Ca2+ uptake and release by the sarcoplasmic reticulum (SR). Total replacement (2.5 mM) of adenosine triphosphate (ATP) with UTP (i) displaced the tension-pCa relationship to the left along the abcissae and increased maximum Ca2+-activated tension, both effects being larger in slow- than in fast-type fibers; (ii) markedly reduced Ca2+ uptake by the SR (evaluated by the caffeine-evoked tension) in both fiber types; (iii) had no effect on the rate of depletion of caffeine-sensitive Ca2+ stores during soaking in relaxing solutions; (iv) induced tension in slow- but not in fast-type fibers. The effects on the SR functional properties are consistent with the notion that UTP is a poor substitute for ATP as a substrate for the Ca ATPase pump and as an agonist of the ryanodine-sensitive Ca2+-release channel. The UTP-induced tension in human slow-type fibers is attributed to effect(s) of the nucleotide on the tension-pCa relationship of the contractile machinery. The present data reveal important differences between the effects of UTP on human versus rat muscle fibers.Key words: skinned muscle fiber, UTP-induced tension, tension-pCa relationship, sarcoplasmic reticulum, calcium transport.

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Cytoskeletal Tropomyosin Tm5NM1 Is Required for Normal Excitation–Contraction Coupling in Skeletal Muscle

Molecular Biology of the Cell ◽

10.1091/mbc.e08-06-0616 ◽

2009 ◽

Vol 20 (1) ◽

pp. 400-409 ◽

Cited By ~ 36

Author(s):

Nicole Vlahovich ◽

Anthony J. Kee ◽

Chris Van der Poel ◽

Emma Kettle ◽

Delia Hernandez-Deviez ◽

...

Keyword(s):

Skeletal Muscle ◽

Sarcoplasmic Reticulum ◽

Actin Filaments ◽

Skeletal Muscles ◽

Actin Binding ◽

Membrane Association ◽

Actin Microfilaments ◽

Excitation Contraction Coupling ◽

Contraction Coupling ◽

T System

The functional diversity of the actin microfilaments relies in part on the actin binding protein tropomyosin (Tm). The muscle-specific Tms regulate actin-myosin interactions and hence contraction. However, there is less known about the roles of the numerous cytoskeletal isoforms. We have shown previously that a cytoskeletal Tm, Tm5NM1, defines a Z-line adjacent cytoskeleton in skeletal muscle. Recently, we identified a second cytoskeletal Tm in this region, Tm4. Here we show that Tm4 and Tm5NM1 define separate actin filaments; the former associated with the terminal sarcoplasmic reticulum (SR) and other tubulovesicular structures. In skeletal muscles of Tm5NM1 knockout (KO) mice, Tm4 localization was unchanged, demonstrating the specificity of the membrane association. Tm5NM1 KO muscles exhibit potentiation of T-system depolarization and decreased force rundown with repeated T-tubule depolarizations consistent with altered T-tubule function. These results indicate that a Tm5NM1-defined actin cytoskeleton is required for the normal excitation–contraction coupling in skeletal muscle.

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REGENERATION OF PIGEON FAST AND SLOW MUSCLE FIBER TYPES AFTER PARTIAL EXCISION AND MINCING

The Journal of Cell Biology ◽

10.1083/jcb.61.2.414 ◽

1974 ◽

Vol 61 (2) ◽

pp. 414-426 ◽

Cited By ~ 10

Author(s):

Robert S. Hikida ◽

Joseph A. Lombardo

Keyword(s):

Sarcoplasmic Reticulum ◽

Slow Muscle ◽

Oxidative Enzymes ◽

Muscle Fiber Types ◽

Fiber Types ◽

Slow Slip ◽

Ultrastructural Examination ◽

Cross Sectional ◽

Ultrastructural Studies ◽

The Matrix

The pigeon's metapatagialis muscles, containing fast fibers in two slips and slow fibers in another slip, were excised for a third of their length, minced, and replaced into their previous sites. After regeneration, the pattern of fiber types and their ATPase and oxidative enzymes were examined histochemically. Ultrastructural examination was carried out on the fast fibers. After 4–17 wk the muscles had regenerated into patterns histochemically similar to the controls only within the slip containing fast fibers. The slow slip was much less regenerated, and had a histochemically embryonic composition. Fiber types were characterized and their cross-sectional areas measured, and the degree of atrophy was greatest in the large fast fibers and the slow fibers. Ultrastructural studies revealed a number of alterations of the mitochondria, including dense and light areas in the matrix and an altered pattern of the cristae into parallel tubular or vesicular aggregations. Other changes included dilated sarcoplasmic reticulum, myofibril disorganization, and a compaction of filaments. The slow fibers were thought to be slower in their regeneration rates because of the pattern of multiple innervation's producing a more complex regenerative pattern.

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