scholarly journals Changes in Membrane Ceramide Pools in Rat Soleus Muscle in Response to Short-Term Disuse

2019 ◽  
Vol 20 (19) ◽  
pp. 4860 ◽  
Author(s):  
Alexey M. Petrov ◽  
Maria N. Shalagina ◽  
Vladimir A. Protopopov ◽  
Valeriy G. Sergeev ◽  
Sergey V. Ovechkin ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Soleus Muscle ◽  
Lipid Raft ◽  
Fluorescent Labeling ◽  
Hindlimb Suspension ◽  
Early Event ◽  
Membrane Asymmetry ◽  
Raft Fraction ◽  
Rat Soleus Muscle ◽  
Muscle Unloading

Lipid raft disruption is an early event during skeletal muscle unloading. Ceramide (Cer) serves as a signaling lipid that can contribute to lipid raft disturbance and muscle atrophy. Using biochemical and fluorescent approaches, the distribution of Cer and related molecules in the rat soleus muscle subjected to 12 h of hindlimb suspension (HS) was studied. HS led to upregulation of TNFα receptor 1 (TNFR1), Cer-producing enzymes, and acid and neutral sphingomyelinase (SMase) in detergent-resistant membranes (lipid rafts), which was accompanied by an increase in Cer and a decrease in sphingomyelin in this membrane fraction. Fluorescent labeling indicated increased Cer in the sarcoplasm as well as the junctional (synaptic) and extrajunctional compartments of the suspended muscles. Also, a loss of membrane asymmetry (a hallmark of membrane disturbance) was induced by HS. Pretreatment with clomipramine, a functional inhibitor of acid SMase, counteracted HS-mediated changes in the Cer/sphingomyelin ratio and acid SMase abundance as well as suppressed Cer accumulation in the intracellular membranes of junctional and extrajunctional regions. However, the elevation of plasma membrane Cer and disturbance of the membrane asymmetry were suppressed only in the junctional compartment. We suggest that acute HS leads to TNFR1 and SMase upregulation in the lipid raft fraction and deposition of Cer throughout the sarcolemma and intracellularly. Clomipramine-mediated downregulation of acid SMase can suppress Cer accumulation in all compartments, excluding the extrajunctional plasma membrane.

scholarly journals Early Lipid Raft-Related Changes: Interplay between Unilateral Denervation and Hindlimb Suspension

2021 ◽  
Vol 22 (5) ◽  
pp. 2239
Author(s):  
Irina G. Bryndina ◽  
Maria N. Shalagina ◽  
Vladimir A. Protopopov ◽  
Alexey V. Sekunov ◽  
Andrey L. Zefirov ◽  
...  
Keyword(s):  
Lipid Raft ◽  
Hindlimb Suspension ◽  
Short Term ◽  
Antiapoptotic Protein ◽  
Muscle Disuse ◽  
Proapoptotic Protein ◽  
Raft Fraction ◽  
Rat Soleus Muscle ◽  
Afferent Inputs ◽  
Underlying Mechanisms

Muscle disuse and denervation leads to muscle atrophy, but underlying mechanisms can be different. Previously, we have found ceramide (Cer) accumulation and lipid raft disruption after acute hindlimb suspension (HS), a model of muscle disuse. Herein, using biochemical and fluorescent approaches the influence of unilateral denervation itself and in combination with short-term HS on membrane-related parameters of rat soleus muscle was studied. Denervation increased immunoexpression of sphingomyelinase and Cer in plasmalemmal regions, but decreased Cer content in the raft fraction and enhanced lipid raft integrity. Preliminary denervation suppressed (1) HS-induced Cer accumulation in plasmalemmal regions, shown for both nonraft and raft-fractions; (2) HS-mediated decrease in lipid raft integrity. Similar to denervation, inhibition of the sciatic nerve afferents with capsaicin itself increased Cer plasmalemmal immunoexpression, but attenuated the membrane-related effects of HS. Finally, both denervation and capsaicin treatment increased immunoexpression of proapoptotic protein Bax and inhibited HS-driven increase in antiapoptotic protein Bcl-2. Thus, denervation can increase lipid raft formation and attenuate HS-induced alterations probably due to decrease of Cer levels in the raft fraction. The effects of denervation could be at least partially caused by the loss of afferentation. The study points to the importance of motor and afferent inputs in control of Cer distribution and thereby stability of lipid rafts in the junctional and extrajunctional membranes of the muscle.

Distribution of myosin heavy chain isoforms in non-weight-bearing rat soleus muscle fibers

1996 ◽  
Vol 81 (6) ◽  
pp. 2540-2546 ◽  
Author(s):  
Robert J. Talmadge ◽  
Roland R. Roy ◽  
V. Reggie Edgerton
Keyword(s):  
Myosin Heavy Chain ◽  
Soleus Muscle ◽  
Heavy Chain ◽  
De Novo ◽  
Weight Bearing ◽  
Muscle Fibers ◽  
Myosin Heavy Chain Isoforms ◽  
Hindlimb Suspension ◽  
Type I ◽  
Rat Soleus Muscle

Talmadge, Robert J., Roland R. Roy, and V. Reggie Edgerton.Distribution of myosin heavy chain isoforms in non-weight-bearing rat soleus muscle fibers. J. Appl. Physiol. 81(6): 2540–2546, 1996.—The effects of 14 days of spaceflight (SF) or hindlimb suspension (HS) (Cosmos 2044) on myosin heavy chain (MHC) isoform content of the rat soleus muscle and single muscle fibers were determined. On the basis of electrophoretic analyses, there was a de novo synthesis of type IIx MHC but no change in either type I or IIa MHC isoform proportions after either SF or HS compared with controls. The percentage of fibers containing only type I MHC decreased by 26 and 23%, and the percentage of fibers with multiple MHCs increased from 6% in controls to 32% in HS and 34% in SF rats. Type IIx MHC was always found in combination with another MHC or combination of MHCs; i.e., no fibers contained type IIx MHC exclusively. These data suggest that the expression of the normal complement of MHC isoforms in the adult rat soleus muscle is dependent, in part, on normal weight bearing and that the absence of weight bearing induces a shift toward type IIx MHC protein expression in the preexisting type I and IIa fibers of the soleus.

Lactate dehydrogenase expression at the onset of altered loading in rat soleus muscle

2004 ◽  
Vol 97 (4) ◽  
pp. 1424-1430 ◽  
Author(s):  
Tyrone A. Washington ◽  
James M. Reecy ◽  
Raymond W. Thompson ◽  
Larry L. Lowe ◽  
Joseph M. McClung ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Enzymatic Activity ◽  
Soleus Muscle ◽  
High Energy ◽  
Northern Blotting ◽  
Mrna Abundance ◽  
Hindlimb Suspension ◽  
Sprague Dawley ◽  
Muscle Lactate ◽  
Rat Soleus Muscle

Both functional overload and hindlimb disuse induce significant energy-dependent remodeling of skeletal muscle. Lactate dehydrogenase (LDH), an important enzyme involved in anaerobic glycolysis, catalyzes the interconversion of lactate and pyruvate critical for meeting rapid high-energy demands. The purpose of this study was to determine rat soleus LDH-A and -B isoform expression, mRNA abundance, and enzymatic activity at the onset of increased or decreased loading in the rat soleus muscle. The soleus muscles from male Sprague-Dawley rats were functionally overloaded for up to 3 days by a modified synergist ablation or subjected to disuse by hindlimb suspension for 3 days. LDH mRNA concentration was determined by Northern blotting, LDH protein isoenzyme composition was determined by zymogram analysis, and LDH enzymatic activity was determined spectrophotometrically. LDH-A mRNA abundance increased by 372%, and LDH-B mRNA abundance decreased by 43 and 31% after 24 h and 3 days of functional overload, respectively, compared with that in control rats. LDH protein expression demonstrated a shift by decreasing LDH-B isoforms and increasing LDH-A isoforms. LDH-B activity decreased 80% after 3 days of functional overload. Additionally, LDH-A activity increased by 234% following 3 days of hindlimb suspension. However, neither LDH-A or LDH-B mRNA abundance was affected following 3 days of hindlimb suspension. In summary, the onset of altered loading induced a differential expression of LDH-A and -B in the rat soleus muscle, favoring rapid energy production. Long-term altered loading is associated with myofiber conversion; however, the rapid changes in LDH at the onset of altered loading may be involved in other physiological processes.

Myosin and troponin changes in rat soleus muscle after hindlimb suspension

1993 ◽  
Vol 74 (3) ◽  
pp. 1156-1160 ◽  
Author(s):  
M. Campione ◽  
S. Ausoni ◽  
C. Y. Guezennec ◽  
S. Schiaffino
Keyword(s):  
Soleus Muscle ◽  
Troponin I ◽  
Troponin T ◽  
High Mobility ◽  
Calcium Sensitivity ◽  
Hindlimb Suspension ◽  
Type I ◽  
Maximal Velocity ◽  
Rat Soleus Muscle ◽  
Fast Twitch

We examined the myosin heavy-chain (MHC), troponin T (TnT), and troponin I (TnI) isoform composition in the rat soleus muscle after 21 days of hindlimb suspension using electrophoretic and immunoblotting analysis with specific monoclonal antibodies. The suspended soleus showed a shift in the MHC isoform distribution with a marked increase (from 1.0 to 33%) in the relative amount of type IIa and IIx MHC and a corresponding decrease in type I MHC. However, type IIb MHC, which represents a major component in fast-twitch muscles, was not detected in suspended soleus muscles. TnT and TnI isoform composition was also changed with the appearance of fast-type TnI and TnT bands. However, a high-mobility TnT band, which represents a major component in fast-twitch muscles, was not expressed in suspended soleus. These isoform transitions may be related to the increased maximal velocity of shortening and higher calcium sensitivity previously reported in the rat soleus after hindlimb suspension.

scholarly journals Membrane lipid rafts are disturbed in the response of rat skeletal muscle to short-term disuse

2017 ◽  
Vol 312 (5) ◽  
pp. C627-C637 ◽  
Author(s):  
Alexey M. Petrov ◽  
Violetta V. Kravtsova ◽  
Vladimir V. Matchkov ◽  
Alexander N. Vasiliev ◽  
Andrey L. Zefirov ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Lipid Rafts ◽  
Lipid Raft ◽  
Motor Nerve ◽  
Membrane Lipid ◽  
Hindlimb Suspension ◽  
Cholera Toxin B Subunit ◽  
Plasma Membrane Lipid ◽  
Intracellular Ca

Marked loss of skeletal muscle mass occurs under various conditions of disuse, but the molecular and cellular mechanisms leading to atrophy are not completely understood. We investigate early molecular events that might play a role in skeletal muscle remodeling during mechanical unloading (disuse). The effects of acute (6–12 h) hindlimb suspension on the soleus muscles from adult rats were examined. The integrity of plasma membrane lipid rafts was tested utilizing cholera toxin B subunit or fluorescent sterols. In addition, resting intracellular Ca2+ level was analyzed. Acute disuse disturbed the plasma membrane lipid-ordered phase throughout the sarcolemma and was more pronounced in junctional membrane regions. Ouabain (1 µM), which specifically inhibits the Na-K-ATPase α2 isozyme in rodent skeletal muscles, produced similar lipid raft changes in control muscles but was ineffective in suspended muscles, which showed an initial loss of α2 Na-K-ATPase activity. Lipid rafts were able to recover with cholesterol supplementation, suggesting that disturbance results from cholesterol loss. Repetitive nerve stimulation also restores lipid rafts, specifically in the junctional sarcolemma region. Disuse locally lowered the resting intracellular Ca2+ concentration only near the neuromuscular junction of muscle fibers. Our results provide evidence to suggest that the ordering of lipid rafts strongly depends on motor nerve input and may involve interactions with the α2 Na-K-ATPase. Lipid raft disturbance, accompanied by intracellular Ca2+ dysregulation, is among the earliest remodeling events induced by skeletal muscle disuse.

Proteomic analysis of rat soleus muscle undergoing hindlimb suspension-induced atrophy and reweighting hypertrophy

PROTEOMICS ◽  
2002 ◽  
Vol 2 (5) ◽  
pp. 543-550 ◽  
Author(s):  
Robert J. Isfort ◽  
Feng Wang ◽  
Kenneth D. Greis ◽  
Yiping Sun ◽  
Thomas W. Keough ◽  
...  
Keyword(s):  
Soleus Muscle ◽  
Proteomic Analysis ◽  
Hindlimb Suspension ◽  
Rat Soleus Muscle

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 NONUNIFORM CHANGE IN RAT SOLEUS MUSCLE FIBERS AFTER HINDLIMB SUSPENSION

1995 ◽  
Vol 44 (1) ◽  
pp. 137-146
Author(s):  
TADASHI OKUMOTO ◽  
AYAKO SAITOH ◽  
HAJIME OHMORI ◽  
SHIGERU KATSUTA
Keyword(s):  
Soleus Muscle ◽  
Muscle Fibers ◽  
Hindlimb Suspension ◽  
Rat Soleus Muscle

scholarly journals Key Markers of mTORC1-Dependent and mTORC1-Independent Signaling Pathways Regulating Protein Synthesis in Rat Soleus Muscle During Early Stages of Hindlimb Unloading

2016 ◽  
Vol 39 (3) ◽  
pp. 1011-1020 ◽  
Author(s):  
Timur Mirzoev ◽  
Sergey Tyganov ◽  
Natalia Vilchinskaya ◽  
Yulia Lomonosova ◽  
Boris Shenkman
Keyword(s):  
Protein Synthesis ◽  
Signaling Pathways ◽  
Soleus Muscle ◽  
Ribosome Biogenesis ◽  
Hindlimb Unloading ◽  
Hindlimb Suspension ◽  
28S Rrna ◽  
Early Stages ◽  
Global Rate ◽  
Rat Soleus Muscle

Background/Aims: The purpose of the study was to assess the amount of rRNA and phosphorylation status of the key markers of mTORC1-dependent (70s6k, 4E-BP1) and mTORC1-independent (GSK-3β, AMPK) signaling pathways controlling protein synthesis in rat soleus during early stages of mechanical unloading (hindlimb suspension (HS) for 1-, 3- and 7 days). Methods: The content of the key signaling molecules of various anabolic signaling pathways was determined by Western-blotting. The amount of 28S rRNA was evaluated by RT-PCR. The rate of protein synthesis was assessed using in-vivo SUnSET technique. Results: HS for 3 and 7 days induced a significant (p<0.05) decrease in the rate of global protein synthesis in soleus muscle in comparison with control. HS within 24 hours resulted in a significant (p<0.05) decrease in p-4E-BP1 content, p-AMPK content and increase in p-p70s6k content in rat soleus muscle. Following three days of HS the content of p-AKT was decreased (p<0.05). After 7 days of HS the phosphorylation level of AKT and GSK-3beta was significantly reduced (p<0.05) compared to control. We also observed a significant decrease in the amount of 28S rRNA in rat soleus following 1, 3 and 7 days of HS. Conclusion: Taken together, the results of our study suggest that a decline in the global rate of protein synthesis in rat soleus during early stages of simulated microgravity is associated with impaired ribosome biogenesis as well as reduced activity of mTORC1-independent signaling pathways.

Corrigenda for vol. 69, Pages 504-508

1991 ◽  
Vol 71 (1) ◽  
pp. 392-392
Keyword(s):  
Soleus Muscle ◽  
Hindlimb Suspension ◽  
Muscle Ultrastructure ◽  
Rat Soleus Muscle ◽  
Band Material

Pages 504–508: D.Desplanches, S.R. Kayar, B.Sempore, R.Flandrois, and H.Hoppeler. “Rat soleus muscle ultrastructure after hindlimb suspension.” Page 506: As a result of technical difficulties in distinguishing mitochondria from Z-band material in some samples, this material was reevaluated. Tables 3 and 4 should read as follows:

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