Cytochrome c mRNA in skeletal muscles of immobilized limbs

1996 ◽  
Vol 81 (5) ◽  
pp. 1941-1945 ◽  
Author(s):  
Frank W. Booth ◽  
Wei Lou ◽  
Marc T. Hamilton ◽  
Zhen Yan
Keyword(s):  
Skeletal Muscle ◽  
Cytochrome C ◽  
Muscle Atrophy ◽  
Protein Interaction ◽  
Total Protein ◽  
Tibialis Anterior ◽  
Untranslated Region ◽  
Skeletal Muscles ◽  
Muscle Protein ◽  
Muscle Length

Booth, Frank W., Wei Lou, Marc T. Hamilton, and Zhen Yan.Cytochrome c mRNA in skeletal muscles of immobilized limbs. J. Appl. Physiol. 81(5): 1941–1945, 1996.—Even though immobilization of a slow skeletal muscle in a lengthened position prevents muscle atrophy, it is unknown whether this treatment would prevent a decrease in mitochondrial quantity. We found that, regardless of muscle length in immobilized limbs, the mRNA of a marker for mitochondrial quantity, cytochrome c, decreased. Cytochrome c mRNA per milligram of muscle was 62 and 72% less 1 wk after fixation of the soleus muscle in shortened and lengthened positions, respectively, than age-matched controls. Cytochrome cmRNA per milligram wet weight was 36 and 32% less in the tibialis anterior muscle fixed for 1 wk in the shortened and lengthened positions, respectively, compared with age-matched controls. Recently, in the 3′-untranslated region of cytochrome c mRNA a novel RNA-protein interaction that decreases in chronically stimulated rat skeletal muscle was identified.[Z. Yan, S. Salmons, Y. L. Dang, M. T. Hamilton, and F. W. Booth. Am. J. Physiol. 271 ( Cell Physiol. 40): C1157– C1166, 1996]. The RNA-protein interaction in the 3′-untranslated region of cytochrome c mRNA in soleus and tibialis anterior muscles was unaffected by fixation in either shortened or lengthened position. We conclude that, whereas lengthening muscle during limb fixation abates the loss of total muscle protein, the percentage decrease in cytochrome c mRNA is proportionally greater than total protein. This suggests that the design of countermeasures to muscle atrophy should include different exercises to maintain total protein and mitochondria.

Alpha-actin and cytochrome c mRNAs in atrophied adult rat skeletal muscle

1988 ◽  
Vol 254 (5) ◽  
pp. C651-C656 ◽  
Author(s):  
P. Babij ◽  
F. W. Booth
Keyword(s):  
Skeletal Muscle ◽  
Cytochrome C ◽  
Muscle Atrophy ◽  
Weight Bearing ◽  
Skeletal Muscle Atrophy ◽  
Rna Content ◽  
Mrna Content ◽  
Fast Twitch Muscle ◽  
Alpha Actin ◽  
Fast Twitch

Specific complementary DNA (cDNA) hybridization probes were used to estimate the levels of alpha-actin and cytochrome c mRNAs and also 18S rRNA in three models of skeletal muscle atrophy. After 7 days of hindlimb suspension, or immobilization, or denervation, protein content decreased 26-32% in all muscles studied except suspended fast-twitch muscle, which lost only half as much protein. alpha-Actin mRNA content decreased 51-66% and cytochrome c mRNA content decreased 42-61% in slow- and fast-twitch muscles in all three models of atrophy. However, total RNA content did not show similar directional changes; RNA content decreased 27-44% in suspended and immobilized muscle but was unchanged in denervated fast-twitch muscle. The results were interpreted to suggest that loss of weight-bearing function of skeletal muscle is a major factor affecting the levels of alpha-actin and cytochrome c mRNAs during muscle atrophy.

Role of SIRT2 in regulating the dexamethasone-activated autophagy pathway in skeletal muscle atrophy

2021 ◽  
Author(s):  
Ziqiu HAN ◽  
Cen CHANG ◽  
Weiyi ZHU ◽  
Yanlei ZHANG ◽  
Jing ZHENG ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Atrophy ◽  
Skeletal Muscles ◽  
Weight Ratio ◽  
Beclin 1 ◽  
C2c12 Cells ◽  
Skeletal Muscle Atrophy ◽  
Time To Exhaustion ◽  
Endurance Capacity ◽  
Polymerase Chain Reaction Inhibition

The proteolytic autophagy system is involved in a major regulatory pathway in dexamethasone (Dex)-induced muscle atrophy. Sirtuin 2 (SIRT2) is known to participate in modulating autophagy signaling, exerting effects in skeletal muscle atrophy. We aimed to determine the effects of SIRT2 on autophagy in Dex-induced myoatrophy. Mice were randomly divided into the normal, Dex, and sirtinol groups. C2C12 cells were differentiated into myotubes and transfected with short hairpin (sh)-Sirt2-green fluorescent protein (GFP) or Sirt2-GFP lentivirus. To evaluate the mass and function of skeletal muscles, we measured the myofiber cross-sectional area, myotube size, gastrocnemius muscle wet weight/body weight ratio (%), and time-to-exhaustion. The SIRT2, myosin heavy chain (MyHC), LC3, and Beclin-1 expression levels were detected by western blotting and quantitative reverse transcription-polymerase chain reaction. Inhibition of SIRT2 markedly attenuated the muscle mass and endurance capacity. The same phenotype was observed in Sirt2-shRNA-treated myotubes, as evidenced by their decreased size. Conversely, SIRT2 overexpression alleviated Dex-induced myoatrophy in vitro. Moreover, SIRT2 negatively regulated the expression of the LC3b and Beclin-1 in skeletal muscles. These findings suggested that SIRT2 activation protects myotubes against Dex-induced atrophy through the inhibition of the autophagy system; this phenomenon may potentially serve as a target for treating glucocorticoid-induced myopathy.

scholarly journals Influence of muscle length on muscle atrophy in the mouse tibialis anterior and soleus muscles

2009 ◽  
Vol 30 (1) ◽  
pp. 39-45 ◽  
Author(s):  
Naoto Fujita ◽  
Taro Fujimoto ◽  
Hiromitsu Tasaki ◽  
Takamitsu Arakawa ◽  
Takako Matsubara ◽  
...  
Keyword(s):  
Muscle Atrophy ◽  
Tibialis Anterior ◽  
Muscle Length

scholarly journals Hypoxia impairs adaptation of skeletal muscle protein turnover- and AMPK signaling during fasting-induced muscle atrophy

PLoS ONE ◽  
2018 ◽  
Vol 13 (9) ◽  
pp. e0203630 ◽  
Author(s):  
C. C. de Theije ◽  
A. M. W. J. Schols ◽  
W. H. Lamers ◽  
D. Neumann ◽  
S. E. Köhler ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Atrophy ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Skeletal Muscle Protein ◽  
Ampk Signaling ◽  
Muscle Protein Turnover

scholarly journals Two Weeks of Smoking Cessation Reverse Cigarette Smoke-Induced Skeletal Muscle Atrophy and Mitochondrial Dysfunction in Mice

2020 ◽  
Author(s):  
Tom Tanjeko Ajime ◽  
Jef Serré ◽  
Rob C I Wüst ◽  
Guy Anselme Mpaka Messa ◽  
Chiel Poffé ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Smoking Cessation ◽  
Mitochondrial Dysfunction ◽  
Muscle Mass ◽  
Muscle Atrophy ◽  
Skeletal Muscles ◽  
Skeletal Muscle Atrophy ◽  
Limb Muscle ◽  
Male Mice ◽  
And Function

Abstract Introduction Apart from its adverse effects on the respiratory system, cigarette smoking also induces skeletal muscle atrophy and dysfunction. Whether short-term smoking cessation can restore muscle mass and function is unknown. We, therefore, studied the impact of 1- and 2-week smoking cessation on skeletal muscles in a mouse model. Methods Male mice were divided into four groups: Air-exposed (14 weeks); cigarette smoke (CS)-exposed (14 weeks); CS-exposed (13 weeks) followed by 1-week cessation; CS-exposed (12 weeks) followed by 2 weeks cessation to examine exercise capacity, physical activity levels, body composition, muscle function, capillarization, mitochondrial function and protein expression in the soleus, plantaris, and diaphragm muscles. Results CS-induced loss of body and muscle mass was significantly improved within 1 week of cessation due to increased lean and fat mass. Mitochondrial respiration and protein levels of the respiratory complexes in the soleus were lower in CS-exposed mice, but similar to control values after 2 weeks of cessation. Exposing isolated soleus muscles to CS extracts reduced mitochondrial respiration that was reversed after removing the extract. While physical activity was reduced in all groups, exercise capacity, limb muscle force, fatigue resistance, fiber size and capillarization, and diaphragm cytoplasmic HIF-1α were unaltered by CS-exposure. However, CS-induced diaphragm atrophy and increased capillary density were not seen after 2 weeks of smoking cessation. Conclusion In male mice, 2 weeks of smoking cessation reversed smoking-induced mitochondrial dysfunction, limb muscle mass loss, and diaphragm muscle atrophy, highlighting immediate benefits of cessation on skeletal muscles. Implications Our study demonstrates that CS-induced skeletal muscle mitochondrial dysfunction and atrophy are significantly improved by 2 weeks of cessation in male mice. We show for the first time that smoking cessation as short as 1 to 2 weeks is associated with immediate beneficial effects on skeletal muscle structure and function with the diaphragm being particularly sensitive to CS-exposure and cessation. This could help motivate smokers to quit smoking as early as possible. The knowledge that smoking cessation has potential positive extrapulmonary effects is particularly relevant for patients referred to rehabilitation programs and those admitted to hospitals suffering from acute or chronic muscle deterioration yet struggling with smoking cessation.

scholarly journals Z-ajoene from Crushed Garlic Alleviates Cancer-Induced Skeletal Muscle Atrophy

Nutrients ◽  
2019 ◽  
Vol 11 (11) ◽  
pp. 2724 ◽  
Author(s):  
Hyejin Lee ◽  
Ji-Won Heo ◽  
A-Reum Kim ◽  
Minson Kweon ◽  
Sorim Nam ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Muscle Atrophy ◽  
Cancer Cachexia ◽  
Inflammatory Responses ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Janus Kinase ◽  
Skeletal Muscle Atrophy ◽  
E3 Ligases

Skeletal muscle atrophy is one of the major symptoms of cancer cachexia. Garlic (Allium sativum), one of the world’s most commonly used and versatile herbs, has been employed for the prevention and treatment of diverse diseases for centuries. In the present study, we found that ajoene, a sulfur compound found in crushed garlic, exhibits protective effects against muscle atrophy. Using CT26 tumor-bearing BALB/c mice, we demonstrate in vivo that ajoene extract alleviated muscle degradation by decreasing not only myokines secretion but also janus kinase/signal transducer and activator of transcription 3 (JAK/STAT3) and SMADs/forkhead box (FoxO) signaling pathways, thereby suppressing muscle-specific E3 ligases. In mouse skeletal myoblasts, Z-ajoene enhanced myogenesis as evidenced by increased expression of myogenic markers via p38 mitogen-activated protein kinase (MAPK) activation. In mature myotubes, Z-ajoene protected against muscle protein degradation induced by conditioned media from CT26 colon carcinoma cells, by suppressing expression of muscle specific E3 ligases and nuclear transcription factor kappa B (NF-κB) phosphorylation which contribute to muscle atrophy. Moreover, Z-ajoene treatment improved myofiber formation via stimulation of muscle protein synthesis. These findings suggest that ajoene extract and Z-ajoene can attenuate skeletal muscle atrophy induced by cancer cachexia through suppressing inflammatory responses and the muscle wasting as well as by promoting muscle protein synthesis.

ATP depletion stimulates calcium-dependent protein breakdown in chick skeletal muscle

1992 ◽  
Vol 262 (5) ◽  
pp. E637-E643 ◽  
Author(s):  
J. M. Fagan ◽  
E. F. Wajnberg ◽  
L. Culbert ◽  
L. Waxman
Keyword(s):  
Skeletal Muscle ◽  
Total Protein ◽  
Skeletal Muscles ◽  
Cysteine Proteases ◽  
Atp Depletion ◽  
Metabolic Energy ◽  
Myofibrillar Proteins ◽  
Protein Breakdown ◽  
Calcium Dependent ◽  
Intracellular Proteins

The contribution of metabolic energy to the degradation of intracellular proteins in skeletal muscle was investigated. Isolated chick skeletal muscles deprived of oxygen and muscles incubated in buffer under nonphysiological conditions containing inhibitors of glycolysis and mitochondrial respiration had lower concentrations or undetectable levels of ATP and faster rates of proteolysis. Both total protein breakdown and the breakdown of myofibrillar proteins were stimulated 35-124% in ATP-depleted tissues. However, ATP-depleted muscles incubated in buffer to which no Ca2+ was added showed slower rates of total protein breakdown and no significant change in myofibrillar proteolysis compared with control muscles. Trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane (E-64), a compound that inhibits the calpains and the lysosomal cysteine proteases, completely blocked the Ca(2+)-stimulated breakdown of nonmyofibrillar and myofibrillar proteins in ATP-depleted muscles. However, Ca(2+)-stimulated proteolysis was not inhibited in ATP-depleted muscles incubated with weak bases to prevent lysosome function. These data suggest that intracellular proteins can be degraded in skeletal muscle in the absence of metabolic energy and that the calpains play a major role in the enhanced proteolysis in skeletal muscles depleted of ATP.

Atrophy responses to muscle inactivity. I. Cellular markers of protein deficits

2003 ◽  
Vol 95 (2) ◽  
pp. 781-790 ◽  
Author(s):  
F. Haddad ◽  
R. R. Roy ◽  
H. Zhong ◽  
V. R. Edgerton ◽  
K. M. Baldwin
Keyword(s):  
Muscle Atrophy ◽  
Ribosomal Rna ◽  
Total Protein ◽  
Protein Concentration ◽  
Muscle Protein ◽  
Control Level ◽  
Cellular Processes ◽  
Si Model ◽  
Cellular Markers ◽  
Actin Protein

The goal of this study was to use the model of spinal cord isolation (SI), which blocks nearly all neuromuscular activity while leaving the motoneuron muscle-fiber connections intact, to characterize the cellular processes linked to marked muscle atrophy. Rats randomly assigned to normal control and SI groups were studied at 0, 2, 4, 8, and 15 days after SI surgery. The slow soleus muscle atrophied by ∼50%, with the greatest degree of loss occurring during the first 8 days. Throughout the SI duration, muscle protein concentration was maintained at the control level, whereas myofibrillar protein concentration steadily decreased between 4 and 15 days of SI, and this was associated with a 50% decrease in myosin heavy chain (MHC) normalized to total protein. Actin relative to the total protein was maintained at the control level. Marked reductions occurred in total RNA and DNA content and in total MHC and actin mRNA expressed relative to 18S ribosomal RNA. These findings suggest that two key factors contributing to the muscle atrophy in the SI model are 1) a reduction in ribosomal RNA that is consistent with a reduction in protein translational capacity, and 2) insufficient mRNA substrate for translating key sarcomeric proteins comprising the myofibril fraction, such as MHC and actin. In addition, the marked selective depletion of MHC protein in the muscles of SI rats suggests that this protein is more vulnerable to inactivity than actin protein. This selective MHC loss could be a major contributor for the previously reported loss in the functional integrity of SI muscles. Collectively, these data are consistent with the involvement of pretranslational and translational processes in muscle atrophy due to SI.

Increased contractile activity decreases RNA-protein interaction in the 3'-UTR of cytochrome c mRNA

1996 ◽  
Vol 271 (4) ◽  
pp. C1157-C1166 ◽  
Author(s):  
Z. Yan ◽  
S. Salmons ◽  
Y. I. Dang ◽  
M. T. Hamilton ◽  
F. W. Booth
Keyword(s):  
Cytochrome C ◽  
Protein Interaction ◽  
Tibialis Anterior ◽  
Contractile Activity ◽  
Supernatant Fraction ◽  
Enzyme Linked Immunosorbent Assay ◽  
Mobility Shift ◽  
Muscle Extract ◽  
Mobility Shift Assay ◽  
Gel Mobility Shift

This study was designed to gain an insight into mechanisms by which cytochrome c gene expression is enhanced by increased contractile activity in skeletal muscle. When rat tibialis anterior muscles were stimulated (10 Hz, 0.25 ms) for 0, 2, 6, 12, or 24 h or 2, 5, 9, or 13 days (n = 4 for each time point), cytochrome c protein (enzyme-linked immunosorbent assay) and mRNA (Northern blot analysis) concentrations started to increase by 9 days, and this was associated with concurrent decreases in cytochrome c mRNA-protein interaction (RNA gel mobility shift assay). We found that the decreased RNA-protein interaction in the stimulated muscle extract was restored by ultracentrifugation (150,000 g, 1 h) in the supernatant fraction. The 150,000 g pellet fraction of stimulated muscle was capable of inhibiting the RNA-protein interaction in control tibialis anterior muscles. These results provide evidence of an inhibitory factor that is responsible for decreasing RNA-protein interaction in the 3'-untranslated region of cytochrome c mRNA in continuously stimulated muscle.

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