Differential modulation of carbonic anhydrase (CA III) in slow- and fast-twitch skeletal muscles of rat following denervation and reinnervation

1991 ◽  
Vol 69 (10-11) ◽  
pp. 702-710 ◽  
Author(s):  
J. Milot ◽  
P. Frémont ◽  
C. Côté ◽  
R. R. Tremblay
Keyword(s):  
Carbonic Anhydrase ◽  
Skeletal Muscles ◽  
Specific Activity ◽  
Fiber Type ◽  
Mrna Levels ◽  
Short Term ◽  
Carbonic Anhydrase Iii ◽  
Mrna Content ◽  
Slow Twitch ◽  
Fast Twitch

Carbonic anhydrase III (CA III) is influenced by neuronal factors in skeletal muscles of the rat. CA III protein and its mRNA levels were assessed in slow- and fast-twitch muscles after short-term denervation by ligature of the sciatic nerve and reinnervation following removal of the sheath tightly fixed around the nerve. Significant elevations in the CA III mRNA content of fast-twitch muscles were recorded after denervation, but they were cancelled following spontaneous muscle reinnervation. No such variations were observed in the slow-twitch soleus muscle. CA III specific activity or cytosolic CA III protein content increased in both types of muscles after denervation, while a decrease was solely observed in the soleus after reinnervation. These results suggest that neuronal mediators may be responsible for up and down variations in CA III gene expression and (or) mRNA stability in slow- and fast-twitch muscles exposed to identical stimuli. Variations of the mRNA and the protein probably reflect, in a time-related manner, the well-programmed changes in fiber type of the muscles in the context of the denervation–reinnervation model.Key words: carbonic anhydrase III, skeletal muscles, denervation, reinnervation, rat.

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.

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.

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 Induction of carbonic anhydrase III mRNA and protein by denervation of rat muscle

1988 ◽  
Vol 256 (1) ◽  
pp. 147-152 ◽  
Author(s):  
N D Carter ◽  
P J Wistrand ◽  
H Isenberg ◽  
H Askmark ◽  
S Jeffery ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Extensor Digitorum Longus ◽  
Mrna Turnover ◽  
Turnover Rates ◽  
Slow Fibre ◽  
Carbonic Anhydrase Iii ◽  
Slow Twitch ◽  
Denervated Muscles ◽  
Fast Twitch ◽  
Anterior Tibialis

Carbonic anhydrase III (CAIII) protein and mRNA amounts in fast- and slow-twitch rat muscles were examined after resection of the sciatic nerve. Striking changes occur in the fast-twitch anterior tibialis (AT) and extensor digitorum longus (EDL) muscles, where CAIII protein and mRNA are increased several-fold 16 days after denervation. The data suggest that these changes are regulated in part by changes in gene transcription and that they perhaps signal a fast-to-slow fibre type transition in these denervated muscles. AT and EDL show some differences in the effects of denervation, which are suggestive of variation in the timing of denervation-induced responses and/or the CAIII protein/mRNA turnover rates in the two muscles.

Regulation of carbonic anhydrase III by thyroid hormone: opposite modulation in slow- and fast-twitch skeletal muscle

1987 ◽  
Vol 65 (9) ◽  
pp. 790-797 ◽  
Author(s):  
Pierre Frémont ◽  
Claude Lazure ◽  
Roland R. Tremblay ◽  
Michel Chrétien ◽  
Peter A. Rogers
Keyword(s):  
Skeletal Muscle ◽  
Thyroid Hormone ◽  
Carbonic Anhydrase ◽  
Soleus Muscle ◽  
Fiber Type ◽  
Type I ◽  
Fiber Type Composition ◽  
Carbonic Anhydrase Iii ◽  
Type Composition ◽  
Slow Twitch

This laboratory previously reported that a major 30 kilodalton (kDa) protein of the soluble cytoplasmic fraction of the rat slow-twitch soleus muscle is modulated by thyroid hormone. This protein has been purified and a portion of the primary structure has been determined. The sequence analysis suggested that the 30-kDa protein is carbonic anhydrase III (CA III; EC 4.2.1.1). The reaction of the protein with a CA III specific antibody and the similar modulation of CA III by thyroid hormone also support this conclusion. Immunochemical quantification of CA III and measurement of CA activity were performed in skeletal muscles of defined fiber-type composition from rats that were rendered hyperthyroid by treatment with 3,3′,5-triiodo-L-thyronine. These experiments revealed that CA activity and CA III content are deinduced in the soleus muscle (primarily type I fibers) and induced in the superficial vastus lateralis muscle (primarily type IIb), whereas no changes were detected in the tibialis anterior muscle (primary type IIa). These results show that the modulation of CA III by thyroid hormone in rat skeletal muscle is not limited to the slow-twitch soleus muscle and that the amplitude and direction of this modulation are directly related to the initial fiber-type composition of the skeletal muscle.

Diurnal rhythms and effects of fasting and refeeding on rat adipose tissue lipoprotein lipase

1996 ◽  
Vol 271 (6) ◽  
pp. E1092-E1097 ◽  
Author(s):  
M. Bergo ◽  
G. Olivecrona ◽  
T. Olivecrona
Keyword(s):  
Adipose Tissue ◽  
Lipoprotein Lipase ◽  
Specific Activity ◽  
Early Morning ◽  
Diurnal Rhythms ◽  
Mrna Levels ◽  
Short Term ◽  
Early Afternoon ◽  
Rat Adipose Tissue ◽  
Adipose Tissue Lipoprotein Lipase

The activity of lipoprotein lipase (LPL) in adipose tissue is modulated by changes in the nutritional status. We have measured LPL activity, mass, and mRNA levels in rat adipose tissue during normal feeding cycles, during short- and long-term fasting, and during refeeding after fasting. LPL activity displayed a diurnal rhythm. The activity was highest during the night and early morning, decreased to a minimum during the early afternoon, and then increased again. These changes corresponded to the feeding pattern. The increases and/or decreases resulted from changes in LPL synthetic rate compounded by posttranslational mechanisms. During short-term fasting, LPL specific activity decreased to < 30% of control. The specific activity was restored within 4 h by refeeding. On longer fasting, LPL mRNA decreased. This became significant from 36 h. On refeeding, it took 12 h to restore the mRNA levels, whereas tissue LPL activity and mass could not be fully restored by 36 h of refeeding. These data show that LPL activity during short-term fasting is regulated posttranscriptionally, which allows for quick upregulation after refeeding. On longer fasting, other mechanisms affecting LPL transcription and synthesis come into play, and upregulation after refeeding is slowed down.

scholarly journals lncRNA-Six1 Is a Target of miR-1611 that Functions as a ceRNA to Regulate Six1 Protein Expression and Fiber Type Switching in Chicken Myogenesis

Cells ◽  
2018 ◽  
Vol 7 (12) ◽  
pp. 243 ◽  
Author(s):  
Manting Ma ◽  
Bolin Cai ◽  
Liang Jiang ◽  
Bahareldin Ali Abdalla ◽  
Zhenhui Li ◽  
...  
Keyword(s):  
Fiber Type ◽  
Muscle Fibers ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Proliferation And Differentiation ◽  
Slow Twitch Muscle ◽  
Fast Twitch Muscle ◽  
Slow Twitch ◽  
Slow Twitch Fibers ◽  
Fast Twitch

Emerging studies indicate important roles for non-coding RNAs (ncRNAs) as essential regulators in myogenesis, but relatively less is known about their function. In our previous study, we found that lncRNA-Six1 can regulate Six1 in cis to participate in myogenesis. Here, we studied a microRNA (miRNA) that is specifically expressed in chickens (miR-1611). Interestingly, miR-1611 was found to contain potential binding sites for both lncRNA-Six1 and Six1, and it can interact with lncRNA-Six1 to regulate Six1 expression. Overexpression of miR-1611 represses the proliferation and differentiation of myoblasts. Moreover, miR-1611 is highly expressed in slow-twitch fibers, and it drives the transformation of fast-twitch muscle fibers to slow-twitch muscle fibers. Together, these data demonstrate that miR-1611 can mediate the regulation of Six1 by lncRNA-Six1, thereby affecting proliferation and differentiation of myoblasts and transformation of muscle fiber types.

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.

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