Changes in fiber composition of soleus muscle during rat hindlimb suspension

Templeton, G. H.; Sweeney, H. Lee; Timson, Benjamin F.; Padalino, M.; Dudenhoeffer, Gregory A.

doi:10.1152/jappl.1988.65.3.1191

Cited by 85 publications

(40 citation statements)

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“…This view is supported by three ndings. First, conversion from a type I ber to type II and type II ber to type I has been reported in several animal models (Romanul et al 1967, Booth 1982, Hauschka et al 1987, Templeton et al 1988, Maxwell et al 1992, Jarvis et al 1996, Brunetti et al 1997, Sutherland et al 1998. Furthermore, Meier et al (1997) found transformation of ber type I to type II in multi dus muscle of young patients with idiopathic scoliosis.…”

Section: Discussionmentioning

confidence: 95%

Rabbit supraspinatus tendon detachment: Effects of size and time after tenotomy on morphometric changes in the muscle

Fabiś¹,

Danilewicz²,

Omulecka³

2001

Acta Orthopaedica Scandinavica

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Section: Discussionmentioning

confidence: 95%

Rabbit supraspinatus tendon detachment: Effects of size and time after tenotomy on morphometric changes in the muscle

Fabiś¹,

Danilewicz²,

Omulecka³

2001

Acta Orthopaedica Scandinavica

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“…It was reported that the contraction time and half relaxation time of skeletal muscle decreased following hindlimb suspension (HERBERT et al, 1988). These results reflected the increase of fast-type myosin isozyme composition (TEMPLETON et al, 1988). If fiber-type transformation from slow-twitch to fast-twitch fibers were to occur following hindlimb suspension, the decrease of glycolytic enzyme in fast-twitch fiber is a contradictory finding.…”

Section: Discussionmentioning

confidence: 98%

“…TEMPLETON et al (1988) reported that following a 4-week suspension of rat hindlimbs, the percent distribution of type I fiber was reduced and that of type ha fiber was significantly increased. On the other hand, RoY et al (1987) reported that no significant changes in fiber-type distribution were observed in either the superficial region of the gastrocnemius or the tibialis anterior muscles following a 4-week hindlimb suspension in rats.…”

mentioning

confidence: 99%

Ultrastructural and metabolic profiles on single muscle fibers of different types after hindlimb suspension in rats.

Takekura

Yoshioka

1989

Jpn.J.Physiol

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Abstracts The relationships between ultrastructural and metabolic profiles in different types of single muscle fiber after hindlimb suspension in rats were examined. Glycolytic (lactate dehydrogenase, LDH; phosphofructokinase, PFK) and oxidative (succinate dehydrogenase, SDH; malate dehydrogenase, MDH) enzyme activities in extensor digitorum longus (EDL) and soleus (SOL) muscles were measured. Relative mitochondrial and lipid droplet volumes were also measured in single muscle fiber of different types. Glycolytic enzyme activity in EDL muscle and oxidative enzyme activity in soleus muscle decreased following suspension for 2 weeks. LDH and PFK activities in fast-twitch (FG, fast-twitch glycolytic; FOG, fast-twitch oxidative glycolytic) fibers and oxidative enzymes in FOG and FG fibers decreased following suspension. Relative mitochondrial volume decreased significantly in all types (SO, slow-twitch oxidative; FOG, and FG) of fibers following suspension. The mitochondrial volume in SO fiber of the control group was significantly (p <0.01) higher than that of suspended group; however, SDH and MDH activities were not different between the control and suspended groups. The structural and metabolic changes following hindlimb suspension were influenced by different factors, respectively. Changes in ultrastructural and metabolic profiles in response to the hindlimb suspension differed according to the type of fibers.

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“…The atrophy of the soleus muscle during hindlimb unloading is due to a decrease in fiber size with no change in fiber number (31). The decrease in cross-sectional area of type II (fast) fibers in the unloaded mouse soleus muscle is …”

Section: Atrophy Of Type I Versus Type Ii Fibers In Control and Unloamentioning

confidence: 98%

Disruption of either the Nfkb1 or the Bcl3 gene inhibits skeletal muscle atrophy

Hunter¹,

Kandarian²

2004

J. Clin. Invest.

141

160

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The intracellular signals that mediate skeletal muscle protein loss and functional deficits due to muscular disuse are just beginning to be elucidated. Previously we showed that the activity of an NF-κB-dependent reporter gene was markedly increased in unloaded muscles, and p50 and Bcl-3 proteins were implicated in this induction. In the present study, mice with a knockout of the p105/p50 (Nfkb1) gene are shown to be resistant to the decrease in soleus fiber cross-sectional area that results from 10 days of hindlimb unloading. Furthermore, the marked unloading-induced activation of the NF-κB reporter gene in soleus muscles from WT mice was completely abolished in soleus muscles from Nfkb1 knockout mice. Knockout of the B cell lymphoma 3 (Bcl3) gene also showed an inhibition of fiber atrophy and an abolition of NF-κB reporter activity. With unloading, fast fibers from WT mice atrophied to a greater extent than slow fibers. Resistance to atrophy in both strains of knockout mice was demonstrated clearly in fast fibers, while slow fibers from only the Bcl3 -/-mice showed atrophy inhibition. The slow-to-fast shift in myosin isoform expression due to unloading was also abolished in both Nfkb1 and Bcl3 knockout mice. Like the soleus muscles, plantaris muscles from Nfkb1 -/-and Bcl3 -/-mice also showed inhibition of atrophy with unloading. Thus both the Nfkb1 and the Bcl3 genes are necessary for unloading-induced atrophy and the associated phenotype transition. IntroductionReduced muscular activity due to bed rest, limb immobilization, sedentary lifestyles, or space flight is a widespread phenomenon that leads to significant muscle atrophy, weakness, fatigue, and insulin resistance (reviewed in ref. 1). While it has been known for some time that the loss in muscle protein due to disuse results from decreases in protein synthesis and increases in protein degradation rates (2), we are just beginning to learn about the upstream triggers and signaling pathways that regulate the changes in these target systems that determine protein content. While myostatin (3, 4) and glucocorticoids (5) have been studied for a role in atrophy, and both can induce atrophy in normal muscle, neither is required for disuse atrophy in vivo (5, 6). Recent work suggests that inhibition of the Akt growth pathway in muscle may be involved in the progression of disuse atrophy. Proteins of the Akt cascade of kinases involved in growth control are dephosphorylated with unloading (7-9). This is consistent with the decrease in protein synthesis rate.Work from our laboratory has implicated additional regulatory molecules in unloading-induced muscle atrophy: the NF-κB and inhibitory κB (IκB) family of transcriptional regulators (10). We showed marked transactivation of injected NF-κB reporter plasmids in soleus muscles from non-weight-bearing (i.e., hindlimb-unloaded) rats. Gel-shift and immunoblot data using nuclear extracts of these muscles showed that likely NF-κB/IκB candidates for involvement in disuse atrophy were p50 and Bcl-3, but not p65. The cano...

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Changes in fiber composition of soleus muscle during rat hindlimb suspension

Cited by 85 publications

References 0 publications

Rabbit supraspinatus tendon detachment: Effects of size and time after tenotomy on morphometric changes in the muscle

Rabbit supraspinatus tendon detachment: Effects of size and time after tenotomy on morphometric changes in the muscle

Ultrastructural and metabolic profiles on single muscle fibers of different types after hindlimb suspension in rats.

Disruption of either the Nfkb1 or the Bcl3 gene inhibits skeletal muscle atrophy

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