The distribution of satellite cells and their relationship to specific fiber types in soleus and extensor digitorum longus muscles

1982 ◽  
Vol 202 (3) ◽  
pp. 329-337 ◽  
Author(s):  
Marcia C. Gibson ◽  
Edward Schultz
2020 ◽  
Vol 2020 ◽  
pp. 1-18
Author(s):  
Brian T. Bennett ◽  
Junaith S. Mohamed ◽  
Stephen E. Alway

Beta-hydroxy-beta-methylbutyrate (HMB), a naturally occurring leucine metabolite, has been shown to attenuate plantar flexor muscle loss and increase myogenic stem cell activation during reloading after a period of significant muscle wasting by disuse in old rodents. However, it was less clear if HMB would alter dorsiflexor muscle response to unloading or reloading when there was no significant atrophy that was induced by unloading. In this study, we tested if calcium HMB (Ca-HMB) would improve muscle function and alter apoptotic signaling in the extensor digitorum longus (EDL) of aged animals that were unloaded but did not undergo atrophy. The EDL muscle was unloaded for 14 days by hindlimb suspension (HS) in aged (34-36 mo.) male Fisher 344×Brown Norway rats. The rats were removed from HS and allowed normal cage ambulation for 14 days of reloading (R). Throughout the study, the rats were gavaged daily with 170 mg of Ca-HMB or water 7 days prior to HS, then throughout 14 days of HS and 14 days of recovery after removing HS. The animals’ body weights were significantly reduced by ~18% after 14 days of HS and continued to decline by ~22% during R as compared to control conditions; however, despite unloading, EDL did not atrophy by HS, nor did it increase in mass after R. No changes were observed in EDL twitch contraction time, force production, fatigue resistance, fiber cross-sectional area, or markers of nuclear apoptosis (myonuclei + satellite cells) after HS or R. While HS and R increased the proapoptotic Bax protein abundance, BCL-2 abundance was also increased as was the frequency of TUNEL-positive myonuclei and satellite cells, yet muscle mass and fiber cross-sectional area did not change and Ca-HMB treatment had no effect reducing apoptotic signaling. These data indicate that (i) increased apoptotic signaling preceded muscle atrophy or occurred without significant EDL atrophy and (ii) that Ca-HMB treatment did not improve EDL signaling, muscle mass, or muscle function in aged rats, when HS and R did not impact mass or function.


1998 ◽  
Vol 291 (3) ◽  
pp. 455-468 ◽  
Author(s):  
Catherine Lagord ◽  
Laurent Soulet ◽  
Sylvie Bonavaud ◽  
Yann Bassaglia ◽  
Christiane Rey ◽  
...  

1997 ◽  
Vol 160 (2) ◽  
pp. 88-94 ◽  
Author(s):  
W. Barańska ◽  
W. Baron ◽  
P. Skopiński ◽  
H. Ziemba

2017 ◽  
pp. 845-858
Author(s):  
V. SMERDU ◽  
M. PERŠE

The cancerogen 1,2-dimethylhydrazine (DMH), widely used in the experimental animal model of carcinogenesis, affects various organs, but its effect on muscle fibers is unknown. To evaluate the effect of 15-week DMH treatment on the fiber size and myosin heavy chain (MyHC) isoforms, which substantially determine fiber types and their contractile characteristics, pure and hybrid fiber types were immunohistochemically determined according to the MyHC isoform expression in soleus, extensor digitorum longus, gastrocnemius medialis and lateralis muscles of DMH-treated and control male Wistar rats. Whereas the size of fibers was mostly unaffected, the MyHC isoform expression was partially affected in both gastrocnemius samples, but not in the soleus and extensor digitorum longus of DMH-treated rats. The lower proportions of hybrid fiber types and especially that of type 1/2x in most gastrocnemius samples of DMH-treated rats resulted in a shift towards a single MyHC isoform expression, but the extent and pattern of the MyHC isoform shift varied across the different gastrocnemius samples. Such variable response to DMH treatment across muscles indicates that each muscle possesses its own adaptive range. These findings are essential for an accurate evaluation of skeletal muscle characteristics in DMH animal model.


1982 ◽  
Vol 30 (12) ◽  
pp. 1275-1288 ◽  
Author(s):  
D A Riley ◽  
S Ellis ◽  
J Bain

Carbonic anhydrase (CA) activities were studied in soluble extracts and cryostat sections of skeletal muscles from prepubertal and postpubertal rats. Acetazolamide inhibition was utilized to distinguish between activities of the acetazolamide-sensitive (CA I and II) and acetazolamide-resistant (CA III) forms of the enzyme. The inhibition studies indicated that fast-twitch oxidative-glycolytic muscle fibers contained both the sensitive and resistant forms of CA. Acetazolamide-sensitive activity was localized within muscle fibers, axons, myelin, and capillaries. Axoplasmic staining was restricted to subpopulations of myelinated axons in both the dorsal and ventral roots. Soleus muscles exhibited significantly greater activity of CA III than extensor digitorum longus muscles at all ages examined. CA III was richest in slow-twitch oxidative and intrafusal fibers. During puberty, soleus muscle fibers matured and converted from fast-twitch oxidative-glycolytic to slow-twitch oxidative fibers. There was a shift from the sensitive to the resistant form of CA; CA III activity increased about sevenfold. This activity peaked earlier in the muscles of female rats than male rats. These results demonstrated a complex distribution of CA isozymes in the neuromuscular system and pointed out that isozyme content depends on both the type of muscle and the age and sex of the animal.


1982 ◽  
Vol 53 (5) ◽  
pp. 1144-1151 ◽  
Author(s):  
P. W. Watt ◽  
F. J. Kelly ◽  
D. F. Goldspink ◽  
G. Goldspink

Morphological and biochemical changes have been studied in two forelimb (i.e., brachialis and extensor carpi radialis) and two hindlimb (i.e., soleus and extensor digitorum longus) muscles of rats subjected to short bursts of high-intensity exercise over 2 wk. Regardless of muscle type, all four muscles grew significantly, accumulating protein, RNA, and DNA at faster rates than in the growing control tissues. Of the intrinsic fiber types within the individual muscles all increased their cross-sectional areas, but the fast-oxidative, glycolytic fibers (type IIa) showed marginally more hypertrophy than the slow-oxidative (I) or fast-glycolytic fibers (IIb). Induced changes in protein turnover were consistent with the additional growth of the exercised muscles. However, the precise alterations in the rates of protein synthesis and protein breakdown varied according to the fiber type composition of the muscle. The increased growth rate of the two principally fast-twitch muscles (i.e., brachialis and extensor digitorum longus) correlated solely with an enhancement of protein synthesis (measured in vivo). In contrast, the hypertrophy of the slow-twitch soleus appeared to relate only to a decrease in protein breakdown (a calculated value). In a more intermediate type of muscle (i.e., extensor carpi radialis) a complementary combination of an increase in synthesis and a decrease in breakdown was found.


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