Size and metabolic properties of single muscle fibers in rat soleus after hindlimb suspension

1987 ◽  
Vol 62 (6) ◽  
pp. 2338-2347 ◽  
Author(s):  
E. O. Hauschka ◽  
R. R. Roy ◽  
V. R. Edgerton
Keyword(s):  
Soleus Muscle ◽  
Muscle Fibers ◽  
Collaborative Study ◽  
Myosin Atpase ◽  
Hindlimb Suspension ◽  
Lengthening Contractions ◽  
Glycerophosphate Dehydrogenase ◽  
Rat Soleus Muscle ◽  
Metabolic Properties ◽  
Fast Twitch

The effects of 28 days of hindlimb suspension (HS) and HS plus 10 daily forceful lengthening contractions on rat soleus muscle fibers were studied. Compared with age-matched controls (CON), soleus wet weights of suspended rats were significantly decreased (approximately 49%). In HS rats, the light adenosinetriphosphatase (ATPase) fibers (staining lightly for myosin ATPase, pH = 8.8) atrophied more than the dark ATPase fibers (staining darkly for myosin ATPase, pH = 8.8). Single-fiber alpha-glycerophosphate dehydrogenase (GPD) and succinate dehydrogenase (SDH) activities and the proportion of dark ATPase fibers were higher in HS than CON rats. Daily forceful lengthening contractions did not prevent the suspension-induced changes. These results considered in conjunction with a collaborative study on the mechanical properties of HS rats (Roy et al., accompanying paper) suggest a shift in the contractile potential of the muscle following HS without a deficit in SDH, a metabolic property commonly associated with resistance to fatigue. The results support the view that soleus muscle fibers can change from a slow-twitch oxidative to a fast-twitch oxidative-glycolytic profile, but rarely to a fast-twitch glycolytic one, and that SDH and GPD activity per volume of tissue can be maintained or increased even when there are severe losses of contractile proteins.

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.

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 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

Rat soleus muscle fiber responses to 14 days of spaceflight and hindlimb suspension

1992 ◽  
Vol 73 (2) ◽  
pp. S51-S57 ◽  
Author(s):  
Y. Ohira ◽  
B. Jiang ◽  
R. R. Roy ◽  
V. Oganov ◽  
E. Ilyina-Kakueva ◽  
...  
Keyword(s):  
Hindlimb Suspension ◽  
Protein Profiles ◽  
Sectional Area ◽  
Cross Sectional ◽  
Glycerophosphate Dehydrogenase ◽  
Rat Soleus Muscle ◽  
Slow Twitch ◽  
Fiber Atrophy ◽  
Slow Twitch Fibers ◽  
Fast Twitch

Morphological and enzymatic responses in fibers expressing fast, slow, or both types of myosin heavy chain (MHC) were studied in rats after 14 days of spaceflight (COSMOS 2044) or hindlimb suspension. Although the percentage of slow-twitch fibers was unchanged, a higher percentage of fibers that expressed both slow and fast MHC was observed in flight and suspended rats than in synchronous ground-based controls. The soleus was 25 and 34% smaller than control after 14 days of flight and suspension, with the reduction in fiber cross-sectional area (CSA) being greater in slow- than in fast-twitch fibers in both experimental groups. The activities of succinate dehydrogenase (SDH) and alpha-glycerophosphate dehydrogenase (GPD) were not significantly affected by flight or suspension. The total SDH activity (i.e., SDH activity x CSA) decreased significantly in the slow-twitch fibers of the flight and the fast-twitch fibers of the suspended rats, in large part due to fiber atrophy. A shift in MHC expression in 14 and 9% of the fibers in flight and suspended rats occurred without a change in myosin adenosinetriphosphatase activity. The SDH and GPD activities of the fibers that expressed both slow and fast MHC were slightly higher than the slow-twitch fibers and slightly lower than the fast-twitch fibers. These data indicate that events were initiated within 14 days of spaceflight or suspension that began to reconfigure the protein profiles of 9–14% of the slow-twitch fibers from typical slow-twitch toward those of fast-twitch fibers, while all fibers were dramatically losing total protein.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Isoform-Specific Na,K-ATPase Alterations Precede Disuse-Induced Atrophy of Rat Soleus Muscle

2015 ◽  
Vol 2015 ◽  
pp. 1-11 ◽  
Author(s):  
Violetta V. Kravtsova ◽  
Vladimir V. Matchkov ◽  
Elena V. Bouzinova ◽  
Alexander N. Vasiliev ◽  
Irina A. Razgovorova ◽  
...  
Keyword(s):  
Muscle Atrophy ◽  
Soleus Muscle ◽  
Muscle Fibers ◽  
Hindlimb Suspension ◽  
Resting Membrane Potential ◽  
Membrane Localization ◽  
Specific Effects ◽  
Contractile Parameters ◽  
Mrna Content ◽  
Rat Soleus Muscle

This study examines the isoform-specific effects of short-term hindlimb suspension (HS) on the Na,K-ATPase in rat soleus muscle. Rats were exposed to 24–72 h of HS and we analyzed the consequences on soleus muscle mass and contractile parameters; excitability and the resting membrane potential (RMP) of muscle fibers; the electrogenic activity, protein, and mRNA content of theα1 andα2 Na,K-ATPase; the functional activity and plasma membrane localization of theα2 Na,K-ATPase. Our results indicate that 24–72 h of HS specifically decreases the electrogenic activity of the Na,K-ATPaseα2 isozyme and the RMP of soleus muscle fibers. This decrease occurs prior to muscle atrophy or any change in contractile parameters. Theα2 mRNA and protein content increased after 24 h of HS and returned to initial levels at 72 h; however, even the increased content was not able to restoreα2 enzyme activity in the disused soleus muscle. There was no change in the membrane localization ofα2 Na,K-ATPase. Theα1 Na,K-ATPase electrogenic activity, protein and mRNA content did not change. Our findings suggest that skeletal muscle use is absolutely required forα2 Na,K-ATPase transport activity and provide the first evidence that Na,K-ATPase alterations precede HS-induced muscle atrophy.

Reloading of atrophied rat soleus muscle induces tenascin-C expression around damaged muscle fibers

2003 ◽  
Vol 284 (3) ◽  
pp. R792-R801 ◽  
Author(s):  
Martin Flück ◽  
Matthias Chiquet ◽  
Silvia Schmutz ◽  
Marie-Hélène Mayet-Sornay ◽  
Dominique Desplanches
Keyword(s):  
Basement Membrane ◽  
Mechanical Loading ◽  
Soleus Muscle ◽  
Muscle Fibers ◽  
Hindlimb Suspension ◽  
Tenascin C ◽  
Muscle Loading ◽  
Rat Soleus Muscle ◽  
Membrane Components ◽  
Basement Membrane Components

The hypothesis was tested that mechanical loading, induced by hindlimb suspension and subsequent reloading, affects expression of the basement membrane components tenascin-C and fibronectin in the belly portion of rat soleus muscle. One day of reloading, but not the previous 14 days of hindlimb suspension, led to ectopic accumulation of tenascin-C and an increase of fibronectin in the endomysium of a proportion (8 and 15%) of muscle fibers. Large increases of tenascin-C (40-fold) and fibronectin (7-fold) mRNA within 1 day of reloading indicates the involvement of pretranslational mechanisms in tenascin-C and fibronectin accumulation. The endomysial accumulation of tenascin-C was maintained up to 14 days of reloading and was strongly associated with centrally nucleated fibers. The observations demonstrate that an unaccustomed increase of rat soleus muscle loading causes modification of the basement membrane of damaged muscle fibers through ectopic endomysial expression of tenascin-C.

Role of weight-bearing function on expression of myosin isoforms during regeneration of rat soleus muscles

1996 ◽  
Vol 270 (3) ◽  
pp. C763-C771 ◽  
Author(s):  
X. A. Bigard ◽  
D. Merino ◽  
B. Serrurier ◽  
F. Lienhard ◽  
Y. C. Guezennec ◽  
...  
Keyword(s):  
Soleus Muscle ◽  
Weight Bearing ◽  
Muscle Fibers ◽  
Immunohistochemical Analysis ◽  
Normal Weight ◽  
Hindlimb Suspension ◽  
Myosin Isoforms ◽  
Homogeneous Population ◽  
Postural Load ◽  
Rat Soleus Muscle

The expression of myosin isoforms was studied in regenerated rat soleus muscle during either normal or altered postural activity. Regeneration was induced following injury by venom from the Notechis scutatus scutatus snake. Immunohistochemical analysis showed that, in regenerating soleus muscle after 3 wk of hindlimb suspension, nearly all fibers reacted positively with the myosin heavy chain (MHC) antibody associated with fast-twitch muscle fibers (fast MHC). When 3 wk of recovery with normal weight-bearing activity followed hindlimb suspension, the regeneration soleus muscle exhibited a nearly homogeneous staining with the MHC antibody associated with the slow-twitch muscle fibers (slow MHC). These findings were in accordance with quantitative analysis of the electrophoretic separation of the native myosin isoforms. Immunohistochemical data showed that removal of weight bearing in the 21-day old regenerated soleus muscles resulted in an increase in fast MHC expression. Together, the results of the present study clearly demonstrate that the postural load is an important component in the induction of slow MHC in regenerating muscle and that the control of the expression of MHC in muscle comprising a homogeneous population of fibers deriving from satellite cells appears more homogeneous and more complete than in a nondegenerated one.

Contractile properties of rat soleus muscle after 15 days of hindlimb suspension

1990 ◽  
Vol 68 (1) ◽  
pp. 334-340 ◽  
Author(s):  
L. Stevens ◽  
Y. Mounier ◽  
X. Holy ◽  
M. Falempin
Keyword(s):  
Soleus Muscle ◽  
Direct Access ◽  
Hindlimb Suspension ◽  
Hill Coefficient ◽  
Complete Agreement ◽  
Fast Twitch Muscle ◽  
Rat Soleus Muscle ◽  
Slow Twitch ◽  
Fast Twitch ◽  
The Hill

The properties of the contractile elements interacting to develop force in atrophied rat soleus muscle were studied by using single skinned fibers, which permitted direct access to the contractile apparatus. Muscle atrophy was induced by 15 days of hindlimb suspension. Suspension resulted in a decrease of maximal tension relative to an important decline in fiber diameter. Ca affinity of the contractile proteins was not changed insofar as the tension-pCa relationship was not shifted along the pCa axis. However, after hindlimb suspension 1) the value of the Hill coefficient from the tension-pCa curve was found to be higher, 2) a higher Ca threshold for activation was reported, and 3) a significant increase in contraction kinetics was described. All these results suggested that after suspension the mechanical properties of the slow-twitch soleus appeared to resemble more closely those of a fast-twitch muscle. Our results were in complete agreement with published histochemical data.

Transcriptional reprogramming during reloading of atrophied rat soleus muscle

2005 ◽  
Vol 289 (1) ◽  
pp. R4-R14 ◽  
Author(s):  
Martin Flück ◽  
Silvia Schmutz ◽  
Matthias Wittwer ◽  
Hans Hoppeler ◽  
Dominique Desplanches
Keyword(s):  
Soleus Muscle ◽  
Muscle Fibers ◽  
Mechanical Damage ◽  
Hindlimb Suspension ◽  
Muscle Weight ◽  
Fourfold Increase ◽  
Tenascin C ◽  
Transcriptional Reprogramming ◽  
Slow Type ◽  
Rat Soleus Muscle

The hypothesis was tested that differential, coregulated transcriptional adaptations of various cellular pathways would occur early with increased mechanical loading of atrophied skeletal muscle and relate to concurrent damage of muscle fibers. Atrophy and slow-to-fast fiber transformation of rat soleus muscle was provoked by 14 days of hindlimb suspension (HS). Subsequent reloading of hindlimbs caused a fourfold increase in the percentage of muscle fibers, demonstrating endomysial tenascin-C staining. Five days after reloading, when 10% of the fibers were damaged, the normal muscle weight and slow-type fiber percentage were reestablished. Microarray analysis revealed major, biphasic patterns of gene expressional alterations with reloading that distinguish between treatments and gene ontologies. Transcript levels of factors involved in protein synthesis and certain proteasomal mRNAs were increased after 1 day of reloading and correlated to the percentage of fibers surrounded by tenascin-C. By contrast, levels of gene messages for fatty acid transporters, respiratory chain constituents, and voltage-gated cation channels were transiently reduced after 1 day of muscle loading and associated with the number of damaged fibers and the regain in muscle weight. This coregulation points toward important retooling of oxidative metabolism and the T- and SR-tubular systems with rebuilding of slow fibers. The observations demonstrate that early nuclear reprogramming with reloading of atrophic soleus muscle is coordinated and links to the processes involved in mechanical damage and regeneration of muscle fibers.

Hypogravity increases cyclopiazonic acid sensitivity of rat soleus muscle

1996 ◽  
Vol 80 (4) ◽  
pp. 1100-1104 ◽  
Author(s):  
C. Huchet-Cadiou ◽  
V. Bonnet ◽  
W. Meme ◽  
C. Leoty
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Soleus Muscle ◽  
Cyclopiazonic Acid ◽  
Hindlimb Suspension ◽  
Acid Sensitivity ◽  
Functional Changes ◽  
Hindlimb Unweighting ◽  
Rat Soleus Muscle ◽  
Fast Twitch

The functional capacity of skeletal muscle sarcoplasmic reticulum was explored in slow rat soleus muscle after 21 days of hindlimb suspension. The sarcoplasmic reticulum function was assessed in intact and saponin-skinned fibers by using cyclopiazonic acid, a specific Ca(2+)-adenosinetriphosphatase inhibitor. After hindlimb unweighting, the sensitivity to cyclopiazonic acid of intact and skinned soleus fibers becomes similar to that found in fast-twitch muscles. This change could be related to the expression of fast Ca2(+)-adenosinetriphosphatase-pump protein in unloaded soleus muscles and agrees with a transformation of soleus muscle from slow- to fast-twitch type. These results also indicate that specific pharmacological tools, like cyclopiazonic acid, could be used to analyze subcellular functional changes due to hindlimb unweighting.

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