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.

Elevated growth hormone increases the Ca2+ sensitivity of slow- and fast-twitch skeletal muscle of female rats

1998 ◽  
Vol 274 (4) ◽  
pp. C861-C865 ◽  
Author(s):  
Xiaoping Xu ◽  
Janet Forrer ◽  
Peter J. Bechtel ◽  
Philip M. Best
Keyword(s):  
Skeletal Muscle ◽  
Growth Hormone ◽  
Muscle Fibers ◽  
Isometric Tension ◽  
Female Rats ◽  
Aged Rats ◽  
Skeletal Muscle Function ◽  
Adult Rats ◽  
Peroneus Longus ◽  
Fast Twitch

To determine the effect of plasma growth hormone (GH) on skeletal muscle function, we measured the free Ca2+concentration-tension relationship of slow-twitch (soleus) and fast-twitch (peroneus longus) muscles isolated from rats undergoing acromegaly in response to implanted, GH-secreting tumors. Muscles from adult (9 mo) and aged rats (24 mo) were studied after the tumor-bearing rats weighed over 50% more than their age-matched controls. Ca2+-activated isometric tension was recorded from skinned muscle fibers. For soleus muscles, the free Ca2+ concentration producing 50% of maximal tension ([Ca2+]50) was 2.0 μM for rats with tumors and 3.4–3.6 μM for controls. For peroneus longus fibers, [Ca2+]50shifted from 6.1–6.7 μM in controls to 3.5 μM after tumors were introduced into either adult or aged rats. Soleus muscle fibers from neonatal rats (14 days) were less sensitive to Ca2+ than those isolated from adult rats, having a [Ca2+]50of 7.3 μM. The Ca2+ sensitivity of peroneus longus fibers did not change with age. We conclude that significant increases in myofibrillar Ca2+ sensitivity occur in skeletal muscles undergoing rapid growth induced by GH-secreting tumors.

scholarly journals Strenuous Acute Exercise Induces Slow and Fast Twitch-Dependent NADPH Oxidase Expression in Rat Skeletal Muscle

Antioxidants ◽  
2020 ◽  
Vol 9 (1) ◽  
pp. 57 ◽  
Author(s):  
Juliana Osório Alves ◽  
Leonardo Matta Pereira ◽  
Igor Cabral Coutinho do Rêgo Monteiro ◽  
Luiz Henrique Pontes dos Santos ◽  
Alex Soares Marreiros Ferraz ◽  
...  
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Nadph Oxidase ◽  
Strenuous Exercise ◽  
Exercise Session ◽  
Type I ◽  
Fiber Types ◽  
Mrna Levels ◽  
Slow Twitch ◽  
Fast Twitch

The enzymatic complex Nicotinamide Adenine Dinucleotide Phosphate (NADPH) oxidase (NOx) may be the principal source of reactive oxygen species (ROS). The NOX2 and NOX4 isoforms are tissue-dependent and are differentially expressed in slow-twitch fibers (type I fibers) and fast-twitch fibers (type II fibers) of skeletal muscle, making them different markers of ROS metabolism induced by physical exercise. The aim of this study was to investigate NOx signaling, as a non-adaptive and non-cumulative response, in the predominant fiber types of rat skeletal muscles 24 h after one strenuous treadmill exercise session. The levels of mRNA, reduced glycogen, thiol content, NOx, superoxide dismutase, catalase, glutathione peroxidase activity, and PPARGC1α and SLC2A4 gene expression were measured in the white gastrocnemius (WG) portion, the red gastrocnemius (RG) portion, and the soleus muscle (SOL). NOx activity showed higher values in the SOL muscle compared to the RG and WG portions. The same was true of the NOX2 and NOX4 mRNA levels, antioxidant enzymatic activities, glycogen content. Twenty-four hours after the strenuous exercise session, NOx expression increased in slow-twitch oxidative fibers. The acute strenuous exercise condition showed an attenuation of oxidative stress and an upregulation of antioxidant activity through PPARGC1α gene activity, antioxidant defense adaptations, and differential gene expression according to the predominant fiber type. The most prominent location of detoxification (indicated by NOX4 activation) in the slow-twitch oxidative SOL muscle was the mitochondria, while the fast-twitch oxidative RG portion showed a more cytosolic location. Glycolytic metabolism in the WG portion suggested possible NOX2/NOX4 non-regulation, indicating other possible ROS regulation pathways.

Phorbol esters affect skeletal muscle glucose transport in a fiber type-specific manner

2004 ◽  
Vol 287 (2) ◽  
pp. E305-E309 ◽  
Author(s):  
David C. Wright ◽  
Paige C. Geiger ◽  
Mark J. Rheinheimer ◽  
Dong Ho Han ◽  
John O. Holloszy
Keyword(s):  
Insulin Resistance ◽  
Skeletal Muscle ◽  
Glucose Transport ◽  
Soleus Muscle ◽  
Insulin Signaling ◽  
Skeletal Muscles ◽  
Phorbol Esters ◽  
Serine Phosphorylation ◽  
Slow Twitch ◽  
Fast Twitch

Recent evidence has shown that activation of lipid-sensitive protein kinase C (PKC) isoforms leads to skeletal muscle insulin resistance. However, earlier studies demonstrated that phorbol esters increase glucose transport in skeletal muscle. The purpose of the present study was to try to resolve this discrepancy. Treatment with the phorbol ester 12-deoxyphorbol-13-phenylacetate 20-acetate (dPPA) led to an ∼3.5-fold increase in glucose transport in isolated fast-twitch epitrochlearis and flexor digitorum brevis muscles. Phorbol ester treatment was additive to a maximally effective concentration of insulin in fast-twitch skeletal muscles. Treatment with dPPA did not affect insulin signaling in the epitrochlearis. In contrast, phorbol esters had no effect on basal glucose transport and inhibited maximally insulin-stimulated glucose transport ∼50% in isolated slow-twitch soleus muscle. Furthermore, dPPA treatment inhibited the insulin-stimulated tyrosine phosphorylation of insulin receptor substrate (IRS)-1 and the threonine and serine phosphorylation of PKB by ∼50% in the soleus. dPPA treatment also caused serine phosphorylation of IRS-1 in the slow-twitch soleus muscle. In conclusion, our results show that phorbol esters stimulate glucose transport in fast-twitch skeletal muscles and inhibit insulin signaling in slow-twitch soleus muscle of rats. These findings suggest that mechanisms other than PKC activation mediate lipotoxicity-induced whole body insulin resistance.

Effects of Exercise on Lactate Transport Into Mouse Skeletal Muscles

1994 ◽  
Vol 19 (3) ◽  
pp. 275-285 ◽  
Author(s):  
Arend Bonen ◽  
Karl J. A. McCullagh
Keyword(s):  
Skeletal Muscle ◽  
Key Words ◽  
Muscle Glycogen ◽  
Skeletal Muscles ◽  
Treadmill Exercise ◽  
Lactate Transport ◽  
Muscle Lactate ◽  
Slow Twitch ◽  
Fast Twitch

Skeletal muscle lactate transport was investigated in vitro in isolated fast-twitch (EDL) and slow-twitch soleus (Sol) skeletal muscles from control and exercised mice. Exercise (23 m/min, 8% grade) reduced muscle glycogen by 37% in EDL (p < 0.05) and by 35% in Sol muscles (p < 0.05). Lactate transport measurements (45 sec) were performed after 60 min of exercise in intact EDL and Sol muscles in vitro, at differing pH (6.5 and 7.4) and differing lactate concentrations (4 and 30 mM). Lactate transport was observed to be greater in Sol than in EDL (p < 0.05). In the exercised muscles there was a small but significant increase in lactate transport (p < 0.05). Lactate transport was greater when exogenous lactate concentrations were greater (p < 0.05) and more rapid at the lower pH (p < 0.05). These studies demonstrated that lactate transport was increased with exercise. Key words: soleus, EDL, treadmill exercise

Biochemical properties of overloaded fast-twitch skeletal muscle

1982 ◽  
Vol 52 (2) ◽  
pp. 467-472 ◽  
Author(s):  
K. M. Baldwin ◽  
V. Valdez ◽  
R. E. Herrick ◽  
A. M. MacIntosh ◽  
R. R. Roy
Keyword(s):  
Skeletal Muscle ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Biochemical Properties ◽  
Female Rats ◽  
Surgical Removal ◽  
Fiber Types ◽  
Slow Twitch ◽  
Fast Twitch ◽  
Myofibril Atpase

Previous studies suggest that fast-twitch skeletal muscle overloaded by surgical removal of synergists contains a greater percent of slow-twitch fibers than normal muscle. Therefore we examined subcellular systems known to represent biochemical properties of slow-twitch skeletal muscle by measuring myosin ATPase, Ca2+ regulation of myofibril ATPase, Ca2+ uptake of sarcoplasmic reticulum (SR), and marker enzymes of glycogenolysis in normal soleus (NS) and in normal (NP) and surgically overloaded (OP) plantaris muscles of adult female rats. The OP muscles were 65% larger than NP muscles (P less than 0.001). Specific activity of myosin and myofibril ATPase was approximately 25% lower in OP compared with NP muscle (P less than 0.05). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of myosin revealed the presence of more slow and less fast myosin light-chain components in OP muscles. Although SR of NP muscle took up more Ca2+ than OP muscle during the initial for both groups. Marker regulatory enzymes of glycogenolysis collectively were reduced by 40% in OP compared with NP muscle (P less than 0.001). Collectively the data are consistent with the concept that some muscle fiber types were converted from “fast” to “slow” in the OP muscle.

Temporal responses of oxidative vs. glycolytic skeletal muscles to K+ deprivation: Na+ pumps and cell cations

1999 ◽  
Vol 276 (6) ◽  
pp. C1411-C1419 ◽  
Author(s):  
Curtis B. Thompson ◽  
Cheolsoo Choi ◽  
Jang H. Youn ◽  
Alicia A. McDonough
Keyword(s):  
Skeletal Muscle ◽  
Posttranscriptional Regulation ◽  
Skeletal Muscles ◽  
Extracellular Fluid ◽  
Protein Levels ◽  
Slow Twitch ◽  
Fast Twitch ◽  
Low K ◽  
Muscle Specificity ◽  
White Gastrocnemius

When K+ output exceeds input, skeletal muscle releases intracellular fluid K+ to buffer the fall in extracellular fluid (ECF) K+. To investigate the mechanisms and muscle specificity of the K+ shift, rats were fed K+-deficient chow for 2–10 days, and two muscles at phenotypic extremes were studied: slow-twitch oxidative soleus and fast-twitch glycolytic white gastrocnemius (WG). After 2 days of low-K+ chow, plasma K+ concentration ([K+]) fell from 4.6 to 3.7 mM, and Na+-K+-ATPase α2 (not α1) protein levels in both muscles, measured by immunoblotting, decreased 36%. Cell [K+] decreased from 116 to 106 mM in soleus and insignificantly in WG, indicating that α2 can decrease before cell [K+]. After 5 days, there were further decreases in α2 (70%) and β2 (22%) in WG, not in soleus, whereas cell [K+] decreased and cell [Na+] increased by 10 mM in both muscles. By 10 days, plasma [K+] fell to 2.9 mM, with further decreases in WG α2 (94%) and β2 (70%); cell [K+] fell 19 mM in soleus and 24 mM in WG compared with the control, and cell [Na+] increased 9 mM in soleus and 15 mM in WG; total homogenate Na+-K+-ATPase activity decreased 19% in WG and insignificantly in soleus. Levels of α2, β1, and β2 mRNA were unchanged over 10 days. The ratios of α2 to α1 protein levels in both control muscles were found to be nearly 1 by using the relative changes in α-isoforms vs. β1- (soleus) or β2-isoforms (WG). We conclude that the patterns of regulation of Na+ pump isoforms in oxidative and glycolytic muscles during K+ deprivation mediated by posttranscriptional regulation of α2β1 and α2β2 are distinct and that decreases in α2-isoform pools can occur early enough in both muscles to account for the shift of K+ to the ECF.

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.

Myosin light chain phosphorylation in fast and slow skeletal muscles in situ

1984 ◽  
Vol 247 (5) ◽  
pp. C462-C471 ◽  
Author(s):  
R. L. Moore ◽  
J. T. Stull
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Skeletal Muscles ◽  
Myosin Light Chain ◽  
White Muscle ◽  
Slow Muscle ◽  
Phosphate Content ◽  
Slow Twitch ◽  
Fast Twitch

The physiological properties of contraction-induced phosphate incorporation into the phosphorylatable light chain (P-light chain) of myosin were examined in fast-twitch white, fast-twitch red, and slow-twitch skeletal muscles in situ. Neural stimulation of rat gastrocnemius muscles between 0.5 and 100 Hz produced an increase in the phosphate content of the P-light chain from the white portion of the muscle, and the rate of P-light chain phosphorylation was frequency dependent. The extent of phosphorylation of P-light chain from the fast-twitch red portion of the gastrocnemius muscle was less. In contrast to fast-twitch skeletal muscle, only high-frequency stimulation (30-100 Hz) produced a small increase in the phosphate content of P-light chain from the slow-twitch soleus muscle. Fast white muscle contained 2.2 and 3.5 times more myosin light chain kinase activity than did the fast red and slow muscle, respectively. The rate of P-light chain dephosphorylation was four times faster in slow muscle than in fast white muscle. Thus the greater extent of phosphorylation of P-light chain in fast-twitch white skeletal muscle fibers may be due in part to the presence of more kinase and less phosphatase activities. Isometric twitch tension potentiation was correlated to the extent of phosphorylation of P-light chain from fast white muscle. The physiological consequences of P-light chain phosphorylation are likely to be of greatest importance in fast-twitch white muscle.

Studies of the halothane-cooling contractures of skeletal muscle

1987 ◽  
Vol 65 (4) ◽  
pp. 697-703 ◽  
Author(s):  
Roberto T. Sudo ◽  
Gisele Zapata ◽  
Guilherme Suarez-Kurtz
Keyword(s):  
Skeletal Muscle ◽  
Synergistic Effects ◽  
Rabbit Muscle ◽  
Slow Twitch ◽  
Fast Twitch ◽  
Dose Dependent ◽  
Muscle Biopsies ◽  
Ca Homeostasis ◽  
Potential Use

The characteristics of transient contractures elicited by rapid cooling of frog or mouse muscles perfused in vitro with solutions equilibrated with 0.5–2.0% halothane are reviewed. The data indicate that these halothane-cooling contractures are dose dependent and reproducible, and their amplitude is larger in muscles containing predominantly slow-twitch type fibers, such as the mouse soleus, than in muscles in which fast-twitch fibers predominate, such as the mouse extensor digitorum longus. The halothane-cooling contractures are potentiated in muscles exposed to succinylcholine. The effects of Ca2+-free solutions, of the local anesthetics procaine, procainamide, and lidocaine, and of the muscle relaxant dantrolene on the halothane-cooling contractures are consistent with the proposal that the halothane-cooling contractures result from synergistic effects of halothane and low temperature on Ca sequestration by the sarcoplasmic reticulum. Preliminary results from skinned rabbit muscle fibers support this proposal. The halothane concentrations required for the halothane-cooling contractures of isolated frog or mouse muscles are comparable with those observed in serum of patients during general anesthesia. Accordingly, fascicles dissected from muscle biopsies of patients under halothane anesthesia for programmed surgery develop large contractures when rapidly cooled. The amplitude of these halothane-cooling contractures declined with the time of perfusion of the muscle fascicles in vitro with halothane-free physiological solutions. It is suggested that the halothane-cooling contractures could be used as a simple experimental model for the investigation of the effects of halothane on Ca homeostasis and contractility in skeletal muscle and for study of drugs of potential use in the management of the contractures associated with the halothane-induced malignant hyperthermia syndrome. It is shown that salicylates, but not indomethacin or mefenamic acid, inhibit the halothane-cooling contractures.

scholarly journals The Functional Role of Calcineurin in Hypertrophy, Regeneration, and Disorders of Skeletal Muscle

2010 ◽  
Vol 2010 ◽  
pp. 1-8 ◽  
Author(s):  
Kunihiro Sakuma ◽  
Akihiko Yamaguchi
Keyword(s):  
Skeletal Muscle ◽  
Functional Role ◽  
Muscular Hypertrophy ◽  
Growth And Remodeling ◽  
Muscular Disorders ◽  
Slow Twitch ◽  
Fast Twitch ◽  
Calcineurin Activity ◽  
Muscle Remodeling

Skeletal muscle uses calcium as a second messenger to respond and adapt to environmental stimuli. Elevations in intracellular calcium levels activate calcineurin, a serine/threonine phosphatase, resulting in the expression of a set of genes involved in the maintenance, growth, and remodeling of skeletal muscle. In this review, we discuss the effects of calcineurin activity on hypertrophy, regeneration, and disorders of skeletal muscle. Calcineurin is a potent regulator of muscle remodeling, enhancing the differentiation through upregulation of myogenin or MEF2A and downregulation of the Id1 family and myostatin. Foxo may also be a downstream candidate for a calcineurin signaling molecule during muscle regeneration. The strategy of controlling the amount of calcineurin may be effective for the treatment of muscular disorders such as DMD, UCMD, and LGMD. Activation of calcineurin produces muscular hypertrophy of the slow-twitch soleus muscle but not fast-twitch muscles.

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