scholarly journals Massage during muscle unloading increases protein turnover in the massaged and non‐massaged, contralateral limb, but does not attenuate muscle atrophy

2020 ◽  
Vol 229 (3) ◽  
Author(s):  
Christopher K. Kargl ◽  
Brian P. Sullivan ◽  
Timothy P. Gavin
Keyword(s):  
Muscle Atrophy ◽  
Protein Turnover ◽  
Contralateral Limb ◽  
Muscle Unloading

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 Modulation of Muscle Atrophy, Fatigue and MLC Phosphorylation by MuRF1 as Indicated by Hindlimb Suspension Studies on MuRF1-KO Mice

2010 ◽  
Vol 2010 ◽  
pp. 1-9 ◽  
Author(s):  
Siegfried Labeit ◽  
Christine H. Kohl ◽  
Christian C. Witt ◽  
Dittmar Labeit ◽  
Jeong Jung ◽  
...  
Keyword(s):  
Muscle Fatigue ◽  
Muscle Atrophy ◽  
Soleus Muscle ◽  
Coiled Coil ◽  
Hindlimb Suspension ◽  
Twitch Potentiation ◽  
Muscle Tissues ◽  
Mlc Phosphorylation ◽  
First Time ◽  
Muscle Unloading

MuRF1 is a member of the TRIM/RBCC superfamily, a gene family that encompasses a large variety of proteins, all sharing the conserved TRIM (TripartiteMotive) sequential array ofRING,B-box, and coiled-coil domains. Within this family, MuRF1(also named TRIM63) is a specialized member that contributes to the development of muscle atrophy and sarcopenia. Here we studied MuRF1's role in muscle atrophy during muscle unloading induced by hindlimb suspension. Consistent with previous studies, we found that MuRF1 inactivation leads to an attenuated muscle atrophy response. The amount of protection was higher as compared to the denervation model, and within the 10 day-suspension period the soleus muscle was spared from atrophy in MuRF1-KO mice. Contractility studies on hindlimb suspended muscle tissues suggested that MuRF1's functions extend beyond muscle trophicity and implicate MuRF1 in muscle fatigue and MLC phosphorylation control: soleus muscle from MuRF1-KO mice fatigued significantly faster and in addition showed a reduced posttetanic twitch potentiation. Thus the present work further established the role of MuRF1 in muscle atrophy and for the first time shows that MuRF1 plays a role in muscle fatigue and twitch potentiation.

scholarly journals Serum extracellular vesicle miR-203a-3p content is associated with skeletal muscle mass and protein turnover during disuse atrophy and regrowth

2020 ◽  
Vol 319 (2) ◽  
pp. C419-C431
Author(s):  
Douglas W. Van Pelt ◽  
Ivan J. Vechetti ◽  
Marcus M. Lawrence ◽  
Kathryn L. Van Pelt ◽  
Parth Patel ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Muscle Mass ◽  
Muscle Atrophy ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Weight Bearing ◽  
Mirna Content ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

Small noncoding microRNAs (miRNAs) are important regulators of skeletal muscle size, and circulating miRNAs within extracellular vesicles (EVs) may contribute to atrophy and its associated systemic effects. The purpose of this study was to understand how muscle atrophy and regrowth alter in vivo serum EV miRNA content. We also associated changes in serum EV miRNA with protein synthesis, protein degradation, and miRNA within muscle, kidney, and liver. We subjected adult (10 mo) F344/BN rats to three conditions: weight bearing (WB), hindlimb suspension (HS) for 7 days to induce muscle atrophy, and HS for 7 days followed by 7 days of reloading (HSR). Microarray analysis of EV miRNA content showed that the overall changes in serum EV miRNA were predicted to target major anabolic, catabolic, and mechanosensitive pathways. MiR-203a-3p was the only miRNA demonstrating substantial differences in HS EVs compared with WB. There was a limited association of EV miRNA content to the corresponding miRNA content within the muscle, kidney, or liver. Stepwise linear regression demonstrated that EV miR-203a-3p was correlated with muscle mass and muscle protein synthesis and degradation across all conditions. Finally, EV miR-203a-3p expression was significantly decreased in human subjects who underwent unilateral lower limb suspension (ULLS) to induce muscle atrophy. Altogether, we show that serum EV miR-203a-3p expression is related to skeletal muscle protein turnover and atrophy. We suggest that serum EV miR-203a-3p content may be a useful biomarker and future work should investigate whether serum EV miR-203a-3p content is mechanistically linked to protein synthesis and degradation.

Hypoxia Induces Muscle Atrophy And Increased Muscle Protein Turnover

2012 ◽  
Author(s):  
Ramon Langen ◽  
Chiel de Theije ◽  
Wout Lamers ◽  
Eleonore Koehler ◽  
Annemie M. Schols
Keyword(s):  
Muscle Atrophy ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Muscle Protein Turnover

scholarly journals Hypoxia‐induced muscle atrophy involves direct and indirect signaling towards protein turnover regulation

2012 ◽  
Vol 26 (S1) ◽  
Author(s):  
Chiel Charles De Theye ◽  
S Eleonore Koehler ◽  
Wouter H lamers ◽  
Annemie M.W.J. Schols ◽  
Ramon J.C. Langen
Keyword(s):  
Muscle Atrophy ◽  
Protein Turnover

scholarly journals Altered protein turnover signaling and myogenesis during impaired recovery of inflammation-induced muscle atrophy in emphysematous mice

2018 ◽  
Author(s):  
Ramon C.J. Langen ◽  
Judith J.M. Ceelen ◽  
Anita E.M. Kneppers ◽  
Chiel C. De Theije ◽  
Stefan J. Van Hoof ◽  
...  
Keyword(s):  
Muscle Atrophy ◽  
Protein Turnover ◽  
Altered Protein

Distinct responses of protein turnover regulatory pathways in hypoxia- and semistarvation-induced muscle atrophy

2013 ◽  
Vol 305 (1) ◽  
pp. L82-L91 ◽  
Author(s):  
Chiel C. de Theije ◽  
Ramon C. J. Langen ◽  
Wouter H. Lamers ◽  
Annemie M. W. J. Schols ◽  
S. Eleonore Köhler
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Food Intake ◽  
Protein Degradation ◽  
Muscle Atrophy ◽  
Protein Turnover ◽  
Chronic Hypoxia ◽  
Muscle Protein ◽  
Specific Component ◽  
Regulatory Pathways

The balance of muscle protein synthesis and degradation determines skeletal muscle mass. We hypothesized that hypoxia-induced muscle atrophy and alterations in the regulation of muscle protein turnover include a hypoxia-specific component, in addition to the observed effects of reduction in food intake in response to hypoxia. Mice were subjected to normoxic, hypoxic (8% oxygen), or pair-fed conditions for 2, 4, and 21 days. Cell-autonomous effects of hypoxia on skeletal muscle were also assessed in differentiated C2C12 myotubes. Hypoxia induced an initial rapid loss of body and muscle weight, which remained decreased during chronic hypoxia and could only in part be explained by the hypoxia-induced reduction of food intake (semistarvation). Regulatory steps of protein synthesis (unfolded protein response and mammal target of rapamycin signaling) remained active in response to acute and sustained hypoxia but not to semistarvation. Activation of regulatory signals for protein degradation, including increased expression of Murf1, Atrogin-1, Bnip3, and Map1lc3b mRNAs, was observed in response to acute hypoxia and to a lesser extent following semistarvation. Conversely, the sustained elevation of Atrogin-1, Bnip3, and Map1lc3b mRNAs and the increased activity of their upstream transcriptional regulator Forkhead box O1 were specific to chronic hypoxia because they were not observed in response to reduced food intake. In conclusion, altered regulation of protein turnover during hypoxia-induced muscle atrophy resulted from an interaction of semistarvation and a hypoxia-specific component. The finding that food restriction but not hypoxia-induced semistarvation inhibited regulatory steps in protein synthesis suggests a hypoxia-specific impairment of the coordination between protein-synthesis signaling and protein-degradation signaling in skeletal muscle.

scholarly journals Oyster Hydrolysates Attenuate Muscle Atrophy via Regulating Protein Turnover and Mitochondria Biogenesis in C2C12 Cell and Immobilized Mice

Nutrients ◽  
2021 ◽  
Vol 13 (12) ◽  
pp. 4385
Author(s):  
So-Hyun Jeon ◽  
Se-Young Choung
Keyword(s):  
Skeletal Muscle ◽  
Muscle Mass ◽  
Muscle Atrophy ◽  
Protein Turnover ◽  
C2c12 Cell ◽  
Sirtuin 1 ◽  
Skeletal Muscle Atrophy ◽  
Natural Material ◽  
Related Protein ◽  
Protein Levels

Sarcopenia, also known as skeletal muscle atrophy, is characterized by significant loss of muscle mass and strength. Oyster (Crassostrea gigas) hydrolysates have anti-cancer, antioxidant, and anti-inflammation properties. However, the anti-sarcopenic effect of oyster hydrolysates remains uninvestigated. Therefore, we prepared two different oyster hydrolysates, namely TGPN and PNY. This study aimed to determine the anti-muscle atrophy efficacy and molecular mechanisms of TGPN and PNY on both C2C12 cell lines and mice. In vitro, the TGPN and PNY recovered the dexamethasone-induced reduction in the myotube diameters. In vivo, TGPN and PNY administration not only improved grip strength and exercise endurance, but also attenuated the loss of muscle mass and muscle fiber cross-sectional area. Mechanistically, TGPN and PNY increased the expression of protein synthesis-related protein levels via phosphoinositide 3-kinase (PI3K)/protein kinase B (Akt)/mammalian target of the rapamycin pathway, and reduced the expression of protein degradation-related protein levels via the PI3K/Akt/forkhead box O pathway. Also, TGPN and PNY stimulated NAD-dependent deacetylase sirtuin-1(SIRT1), peroxisome proliferator-activated receptor gamma coactivator-1 alpha (PGC-1α), nuclear respiratory factor 1,2, mitochondrial transcription factor A, along with mitochondrial DNA content via SIRT1/PGC-1α signaling. These findings suggest oyster hydrolysates could be used as a valuable natural material that inhibits skeletal muscle atrophy via regulating protein turnover and mitochondrial biogenesis.

scholarly journals Altered protein turnover signaling and myogenesis during impaired recovery of inflammation-induced muscle atrophy in emphysematous mice

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Judith J. M. Ceelen ◽  
Annemie M. W. J. Schols ◽  
Anita E. M. Kneppers ◽  
Roger P. H. A. Rosenbrand ◽  
Magda M. Drożdż ◽  
...  
Keyword(s):  
Muscle Atrophy ◽  
Protein Turnover ◽  
Altered Protein
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