Stimulation-induced damage in rabbit fast-twitch skeletal muscles: a quantitative morphological study of the influence of pattern and frequency

1993 ◽  
Vol 273 (2) ◽  
pp. 357-362 ◽  
Author(s):  
Jan Lexell ◽  
Jonathan Jarvis ◽  
David Downham ◽  
Stanley Salmons
Keyword(s):  
Skeletal Muscles ◽  
Morphological Study ◽  
Fast Twitch

Glutamine synthetase induction by glucocorticoids is preserved in skeletal muscle of aged rats

1996 ◽  
Vol 271 (6) ◽  
pp. E1061-E1066 ◽  
Author(s):  
D. Meynial-Denis ◽  
M. Mignon ◽  
A. Miri ◽  
J. Imbert ◽  
E. Aurousseau ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Glutamine Synthetase ◽  
Skeletal Muscles ◽  
Female Rats ◽  
Mrna Levels ◽  
Aged Rats ◽  
Adult Rats ◽  
Adult Age ◽  
Slow Twitch ◽  
Fast Twitch

Glutamine synthetase (GS) is a glucocorticoid-inducible enzyme that has a key role for glutamine synthesis in muscle. We hypothesized that the glucocorticoid induction of GS could be altered in aged rats, because alterations in the responsiveness of some genes to glucocorticoids were reported in aging. We compared the glucocorticoid-induced GS in fast-twitch and slow-twitch skeletal muscles (tibialis anterior and soleus, respectively) and heart from adult (age 6-8 mo) and aged (age 22 mo) female rats. All animals received dexamethasone (Dex) in their drinking water (0.77 +/- 0.10 and 0.80 +/- 0.08 mg/day per adult and aged rat, respectively) for 5 days. Dex caused an increase in both GS activity and GS mRNA in fast-twitch and slow-twitch skeletal muscles from adult and aged rats. In contrast, Dex increased GS activity in heart of adult rats, without any concomitant change in GS mRNA levels. Furthermore, Dex did not affect GS activity in aged heart. Thus the responsiveness of GS to an excess of glucocorticoids is preserved in skeletal muscle but not in heart from aged animals.

Subunit composition of rodent isomyosins and their distribution in hindlimb skeletal muscles

1987 ◽  
Vol 63 (5) ◽  
pp. 2101-2110 ◽  
Author(s):  
R. W. Tsika ◽  
R. E. Herrick ◽  
K. M. Baldwin
Keyword(s):  
Light Chain ◽  
Skeletal Muscles ◽  
Slow Light ◽  
Muscular Activity ◽  
Light Chains ◽  
Fiber Types ◽  
Myosin Isoforms ◽  
Adult Skeletal Muscle ◽  
Physiological Importance ◽  
Fast Twitch

Three adult skeletal muscle sarcomeric myosin heavy chain (MHC) genes have been identified in the rat, suggesting that the expressed native myosin isoforms can be differentiated, in part, on the basis of their MHC composition. This study was undertaken to ascertain whether the five major native isomyosins [3 fast (Fm1, Fm2, Fm3), 1 slow (Sm), and 1 intermediate (Im)], typically expressed in the spectrum of adult rat skeletal muscles comprising the hindlimb, could be further differentiated on the basis of their MHC profiles in addition to their light chain composition. Results show that in muscles comprised exclusively of fast-twitch glycolytic (FG) fibers and consisting of Fm1, Fm2, and Fm3, such as the tensor fasciae latae, only one MHC, designated as fast type IIb, could be resolved. In soleus muscle, comprised of both slow-twitch oxidative and fast-twitch oxidative-glycolytic fibers and expressing Sm and Im, two MHC bands were resolved and designated as slow/cardiac beta-MHC and fast type IIa MHC. In muscles expressing a mixture of all three fiber types and a full complement of isomyosins, as seen in the plantaris, the MHC could be resolved into three bands. Light chain profiles were characterized for each muscle type, as well as for the purified isomyosins. These data suggest that Im (IIa) consists of a mixture of fast and slow light chains, whereas Fm (IIb) and Sm (beta) isoforms consist solely of fast- and slow-type light chains, respectively. Polypeptide mapping of denatured myosin extracted from muscles expressing contrasting isoform phenotypes suggests differences in the MHC primary structure between slow, intermediate, and fast myosin isotypes. These findings demonstrate that 1) Fm, Im, and Sm isoforms are differentiated on the bases of both their heavy and light chain components and 2) each isomyosin is distributed in a characteristic fashion among rat hindlimb skeletal muscles. Furthermore, these data suggest that the ratio of isomyosins in a given muscle or muscle region is of physiological importance to the function of that muscle during muscular activity.

Abundance and subcellular distribution of MCT1 and MCT4 in heart and fast-twitch skeletal muscles

2000 ◽  
Vol 278 (6) ◽  
pp. E1067-E1077 ◽  
Author(s):  
Arend Bonen ◽  
Dragana Miskovic ◽  
Mio Tonouchi ◽  
Kathleen Lemieux ◽  
Marieangela C. Wilson ◽  
...  
Keyword(s):  
Subcellular Distribution ◽  
Tibialis Anterior ◽  
Skeletal Muscles ◽  
Inverse Relationship ◽  
Extensor Digitorum Longus ◽  
Plasma Membranes ◽  
Rat Hearts ◽  
T Tubules ◽  
Fast Twitch ◽  
White Gastrocnemius

The expression of two monocarboxylate transporters (MCTs) was examined in muscle and heart. MCT1 and MCT4 proteins are coexpressed in rat skeletal muscles, but only MCT1 is expressed in rat hearts. Among six rat fast-twitch muscles (red and white gastrocnemius, plantaris, extensor digitorum longus, red and white tibialis anterior) there was an inverse relationship between MCT1 and MCT4 ( r = −0.94). MCT1 protein was correlated with MCT1 mRNA ( r = 0.94). There was no relationship between MCT4 mRNA and MCT4 protein. MCT1 ( r = −0.97) and MCT4 ( r = 0.88) protein contents were correlated with percent fast-twitch glycolytic fiber. When normalized for their mRNAs, MCT1 but not MCT4 was still correlated with the percent fast-twitch glycolytic fiber composition of rat muscles ( r = −0.98). MCT1 and MCT4 were also measured in plasma membranes (PM), triads (TR), T tubules (TT), sarcoplasmic reticulum (SR), and intracellular membranes (IM). There was an intracellular pool of MCT4 but not of MCT1. The MCT1 subcellular distribution was as follows: PM (100%) > TR (31.6%) > SR (15%) = TT (14%) > IM (1.7%). The MCT4 subcellular distribution was considerably different [PM (100%) > TR (66.5%) > TT (36%) = SR (43%) > IM (24%)]. These studies have shown that 1) the mechanisms regulating the expression of MCT1 (transcriptional and posttranscriptional) and MCT4 (posttranscriptional) are different and 2) differences in MCT1 and MCT4 expression among muscles, as well as in their subcellular locations, suggest that they may have different roles in muscle.

Electrolytes in slow and fast muscle fibers of humans at rest and with dynamic exercise

1983 ◽  
Vol 245 (1) ◽  
pp. R25-R31 ◽  
Author(s):  
G. Sjogaard
Keyword(s):  
Skeletal Muscles ◽  
Vastus Lateralis ◽  
Fiber Types ◽  
Triceps Brachii ◽  
Sodium Potassium ◽  
Mean Values ◽  
Fiber Composition ◽  
Slow Twitch ◽  
Fast Twitch ◽  
Muscle Fiber Membrane

Sodium, potassium, and magnesium were analyzed in human slow-twitch (ST) and fast-twitch (FT) skeletal muscles. In contrast to other species, no relation was found between fiber composition and electrolyte distribution. In soleus (S), vastus lateralis (VL), and triceps brachii (TB) the overall mean values for 6 men and 6 women were 44 mmol K/100 g dry wt and 11 mmol Na/100 g dry wt; the intracellular concentrations were 161 mmol K/l and 26 mmol Na/l with no differences between the muscles. Analysis of fragments of single ST and FT fibers from each of the muscles also showed no difference between the fiber types in Na and K content. Small differences were seen between the muscles with regard to Mg, but these were not related to fiber composition compared with other species. During exercise to exhaustion (3 bouts of bicycling for 3 min at 325-395 W, 6 men) the extracellular electrolyte concentrations for Na, K, and Mg increased from 134 to 140, 4.5 to 5.8, and 0.75 to 0.87 mmol/l, respectively (P less than 0.05). In VL Na content increased from 9.8 to 16.5 mmol/100 g dry wt, while intracellular [Na] remained constant. In contrast, intracellular [K] decreased from 161 to 141 mmol/l (P less than 0.05). No such changes occurred in TB. In concert with other studies the present changes in electrolytes in the working muscles indicate that muscle fatigue may be related to changes at the muscle fiber membrane.

scholarly journals Comparative analysis of the transcriptomes of EDL, psoas, and soleus muscles from mice

BMC Genomics ◽  
2020 ◽  
Vol 21 (1) ◽  
Author(s):  
Pabodha Hettige ◽  
Uzma Tahir ◽  
Kiisa C. Nishikawa ◽  
Matthew J. Gage
Keyword(s):  
Skeletal Muscles ◽  
Striated Muscle ◽  
Fiber Type ◽  
Expression Patterns ◽  
Fiber Types ◽  
Muscle Adaptation ◽  
Myosin Heavy Chain Isoform ◽  
Genes Encoding ◽  
Slow Twitch ◽  
Fast Twitch

Abstract Background Individual skeletal muscles have evolved to perform specific tasks based on their molecular composition. In general, muscle fibers are characterized as either fast-twitch or slow-twitch based on their myosin heavy chain isoform profiles. This approach made sense in the early days of muscle studies when SDS-PAGE was the primary tool for mapping fiber type. However, Next Generation Sequencing tools permit analysis of the entire muscle transcriptome in a single sample, which allows for more precise characterization of differences among fiber types, including distinguishing between different isoforms of specific proteins. We demonstrate the power of this approach by comparing the differential gene expression patterns of extensor digitorum longus (EDL), psoas, and soleus from mice using high throughput RNA sequencing. Results EDL and psoas are typically classified as fast-twitch muscles based on their myosin expression pattern, while soleus is considered a slow-twitch muscle. The majority of the transcriptomic variability aligns with the fast-twitch and slow-twitch characterization. However, psoas and EDL exhibit unique expression patterns associated with the genes coding for extracellular matrix, myofibril, transcription, translation, striated muscle adaptation, mitochondrion distribution, and metabolism. Furthermore, significant expression differences between psoas and EDL were observed in genes coding for myosin light chain, troponin, tropomyosin isoforms, and several genes encoding the constituents of the Z-disk. Conclusions The observations highlight the intricate molecular nature of skeletal muscles and demonstrate the importance of utilizing transcriptomic information as a tool for skeletal muscle characterization.

Response of slow and fast muscle to hypothyroidism: maximal shortening velocity and myosin isoforms

1992 ◽  
Vol 263 (1) ◽  
pp. C86-C94 ◽  
Author(s):  
V. J. Caiozzo ◽  
R. E. Herrick ◽  
K. M. Baldwin
Keyword(s):  
Skeletal Muscles ◽  
Relative Content ◽  
Type I ◽  
Myosin Isoforms ◽  
Velocity Data ◽  
Sprague Dawley ◽  
Shortening Velocity ◽  
Sprague Dawley Rats ◽  
Force Velocity ◽  
Fast Twitch

This study examined both the shortening velocity and myosin isoform distribution of slow- (soleus) and fast-twitch (plantaris) skeletal muscles under hypothyroid conditions. Adult female Sprague-Dawley rats were randomly assigned to one of two groups: control (n = 7) or hypothyroid (n = 7). In both muscles, the relative contents of native slow myosin (SM) and type I myosin heavy chain (MHC) increased in response to the hypothyroid treatment. The effects were such that the hypothyroid soleus muscle expressed only the native SM and type I MHC isoforms while repressing native intermediate myosin and type IIA MHC. In the plantaris, the relative content of native SM and type I MHC isoforms increased from 5 to 13% and from 4 to 10% of the total myosin pool, respectively. Maximal shortening velocity of the soleus and plantaris as measured by the slack test decreased by 32 and 19%, respectively, in response to hypothyroidism. In contrast, maximal shortening velocity as estimated by force-velocity data decreased only in the soleus (-19%). No significant change was observed for the plantaris.

Pretranslational regulation of myoglobin gene expression

1987 ◽  
Vol 252 (4) ◽  
pp. C450-C453 ◽  
Author(s):  
L. E. Underwood ◽  
R. S. Williams
Keyword(s):  
Gene Expression ◽  
Tibialis Anterior ◽  
Skeletal Muscles ◽  
Blot Hybridization ◽  
Oxidative Capacity ◽  
Striated Muscles ◽  
Mrna Content ◽  
Slow Twitch ◽  
Rna Probe ◽  
Fast Twitch

We have used blot hybridization techniques and a specific anti-sense RNA probe to determine whether variation in myoglobin gene expression among mammalian striated muscles is attributable to pretranslational regulatory events. We observed that myoglobin mRNA was expressed to approximately 10- and 5-fold greater levels, respectively, in cardiac and soleus (slow-twitch, oxidative, skeletal) muscles of adult rabbits than in tibialis anterior (fast-twitch, glycolytic, skeletal) muscles. Furthermore, when oxidative capacity of tibialis anterior muscles was increased by 21 days of indirect electrical stimulation, a model of exercise conditioning, myoglobin mRNA content increased approximately 15-fold. We conclude that pretranslational mechanisms are important in regulation of myoglobin gene expression in mammalian muscles.

scholarly journals Impacts of prolonged chlorpyrifos exposure on locomotion and slow-and fast- twitch skeletal muscles contractility in rats

2019 ◽  
Vol 6 ◽  
pp. 598-606 ◽  
Author(s):  
Nancy Hallal ◽  
Hiba El Khayat El Sabbouri ◽  
Ali Salami ◽  
Wiam Ramadan ◽  
Hassan Khachfe ◽  
...  
Keyword(s):  
Skeletal Muscles ◽  
Fast Twitch

scholarly journals Obesity-induced discrepancy between contractile and metabolic phenotypes in slow- and fast-twitch skeletal muscles of female obese Zucker rats

2017 ◽  
Vol 123 (1) ◽  
pp. 249-259 ◽  
Author(s):  
Luz M. Acevedo ◽  
Ana I. Raya ◽  
Rafael Ríos ◽  
Escolástico Aguilera-Tejero ◽  
José-Luis L. Rivero
Keyword(s):  
Muscle Mass ◽  
Skeletal Muscles ◽  
Fiber Type ◽  
Succinic Dehydrogenase ◽  
Zucker Rats ◽  
Fiber Types ◽  
Type Composition ◽  
Obese Zucker Rats ◽  
And Function ◽  
Fast Twitch

A clear picture of skeletal muscle adaptations to obesity and related comorbidities remains elusive. This study describes fiber-type characteristics (size, proportions, and oxidative enzyme activity) in two typical hindlimb muscles with opposite structure and function in an animal model of genetic obesity. Lesser fiber diameter, fiber-type composition, and histochemical succinic dehydrogenase activity (an oxidative marker) of muscle fiber types were assessed in slow (soleus)- and fast (tibialis cranialis)-twitch muscles of obese Zucker rats and compared with age (16 wk)- and sex (females)-matched lean Zucker rats ( n = 16/group). Muscle mass and lesser fiber diameter were lower in both muscle types of obese compared with lean animals even though body weights were increased in the obese cohort. A faster fiber-type phenotype also occurred in slow- and fast-twitch muscles of obese rats compared with lean rats. These adaptations were accompanied by a significant increment in histochemical succinic dehydrogenase activity of slow-twitch fibers in the soleus muscle and fast-twitch fiber types in the tibialis cranialis muscle. Obesity significantly increased plasma levels of proinflammatory cytokines but did not significantly affect protein levels of peroxisome proliferator-activated receptors PPARγ or PGC1α in either muscle. These data demonstrate that, in female Zucker rats, obesity induces a reduction of muscle mass in which skeletal muscles show a diminished fiber size and a faster and more oxidative phenotype. It was noteworthy that this discrepancy in muscle's contractile and metabolic features was of comparable nature and extent in muscles with different fiber-type composition and antagonist functions. NEW & NOTEWORTHY This study demonstrates a discrepancy between morphological (reduced muscle mass), contractile (shift toward a faster phenotype), and metabolic (increased mitochondrial oxidative enzyme activity) characteristics in skeletal muscles of female Zucker fatty rats. It is noteworthy that this inconsistency was comparable (in nature and extent) in muscles with different structure and function.

scholarly journals Glucocorticoids regulate mRNA levels for subunits of the 19 S regulatory complex of the 26 S proteasome in fast-twitch skeletal muscles

2004 ◽  
Vol 378 (1) ◽  
pp. 239-246 ◽  
Author(s):  
Lydie COMBARET ◽  
Daniel TAILLANDIER ◽  
Dominique DARDEVET ◽  
Daniel BÉCHET ◽  
Cécile RALLIÈRE ◽  
...  
Keyword(s):  
Hormonal Regulation ◽  
Skeletal Muscles ◽  
Conclusive Evidence ◽  
Mrna Levels ◽  
Glucocorticoid Treatment ◽  
Regulatory Subunits ◽  
Regulatory Complex ◽  
Insulin Dependent ◽  
Fast Twitch

Circulating levels of glucocorticoids are increased in many traumatic and muscle-wasting conditions that include insulin-dependent diabetes, acidosis, infection, and starvation. On the basis of indirect findings, it appeared that these catabolic hormones are required to stimulate Ub (ubiquitin)–proteasome-dependent proteolysis in skeletal muscles in such conditions. The present studies were performed to provide conclusive evidence for an activation of Ub-proteasome-dependent proteolysis after glucocorticoid treatment. In atrophying fast-twitch muscles from rats treated with dexamethasone for 6 days, compared with pair-fed controls, we found (i) increased MG132-inhibitable proteasome-dependent proteolysis, (ii) an enhanced rate of substrate ubiquitination, (iii) increased chymotrypsin-like proteasomal activity of the proteasome, and (iv) a co-ordinate increase in the mRNA expression of several ATPase (S4, S6, S7 and S8) and non-ATPase (S1, S5a and S14) subunits of the 19 S regulatory complex, which regulates the peptidase and the proteolytic activities of the 26 S proteasome. These studies provide conclusive evidence that glucocorticoids activate Ub-proteasome-dependent proteolysis and the first in vivo evidence for a hormonal regulation of the expression of subunits of the 19 S complex. The results suggest that adaptations in gene expression of regulatory subunits of the 19 S complex by glucocorticoids are crucial in the regulation of the 26 S muscle proteasome.

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