scholarly journals The influence of passive stretch on the growth and protein turnover of the denervated extensor digitorum longus muscle

1978 ◽  
Vol 174 (2) ◽  
pp. 595-602 ◽  
Author(s):  
David F. Goldspink
Keyword(s):  
Protein Synthesis ◽  
Extensor Digitorum Longus ◽  
Similar Rate ◽  
Extensor Digitorum Longus Muscle ◽  
Extensor Digitorum ◽  
Denervated Muscle ◽  
Longus Muscle ◽  
Induced Changes ◽  
Passive Stretch

At 7 days after cutting the sciatic nerve, the extensor digitorum longus muscle was smaller and contained less protein than its innervated control. Correlating with these changes was the finding of elevated rates of protein degradation (measured in vitro) in the denervated tissue. However, at this time, rates of protein synthesis (measured in vitro) and nucleic acid concentrations were also higher in the denervated tissue, changes more usually associated with an active muscle rather than a disused one. These anabolic trends have, at least in part, been explained by the possible greater exposure of the denervated extensor digitorum longus to passive stretch. When immobilized under a maintained influence of stretch the denervated muscle grew to a greater extent. Although this stretch-induced growth appeared to occur predominantly through a stimulation of protein synthesis, it was opposed by smaller increases in degradative rates. Nucleic acids increased at a similar rate to the increase in muscle mass when a continuous influence of stretch was imposed on the denervated tissue. In contrast, immobilization of the denervated extensor digitorum longus in a shortened unstretched state reversed most of the stretch-induced changes; that is, the muscle became even smaller, with protein synthesis decreasing to a greater extent than breakdown after the removal of passive stretch. The present investigation suggests that stretch will promote protein synthesis and hence growth of the extensor digitorum longus even in the absence of an intact nerve supply. However, some factor(s), in addition to passive stretch, must contribute to the anabolic trends in this denervated muscle.

scholarly journals Identification in skeletal muscle of a distinct extracellular pool of amino acids, and its role in protein synthesis

1971 ◽  
Vol 121 (5) ◽  
pp. 817-827 ◽  
Author(s):  
R. C. Hider ◽  
E. B. Fern ◽  
D. R. London
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Incubation Medium ◽  
Extensor Digitorum Longus ◽  
Extensor Digitorum ◽  
Longus Muscle ◽  
Kinetics Of

1. The kinetics of radioactive labelling of extra- and intra-cellular amino acid pools and protein of the extensor digitorum longus muscle were studied after incubations with radioactive amino acids in vitro. 2. The results indicated that an extracellular pool could be defined, the contents of which were different from those of the incubation medium. 3. It was concluded that amino acids from the extracellular pool, as defined in this study, were incorporated directly into protein.

scholarly journals The effect of tendon compliance on in vitro/in vivo estimations of sarcomere length

1995 ◽  
Vol 198 (2) ◽  
pp. 503-506
Author(s):  
R James ◽  
I Young ◽  
J Altringham
Keyword(s):  
Extensor Digitorum Longus ◽  
Sarcomere Length ◽  
Extensor Digitorum Longus Muscle ◽  
Extensor Digitorum ◽  
Worst Case ◽  
Longus Muscle ◽  
Tendon Compliance

The errors likely to result from using excised rigor muscles to determine in vivo sarcomere length ranges were calculated for mouse extensor digitorum longus muscle (EDL). This muscle was chosen because its very long tendon makes it particularly susceptible to errors arising from tendon compliance. By placing dissected limbs into different locomotory stances, and allowing them to go into rigor, the range of sarcomere lengths over which muscles operate in vivo can be determined, but it is subject to errors due to tendon compliance. A tendon compliance of 0.24 GPa and a muscle rigor stress of 35 kPa were determined, and these were used to correct the estimates of in vivo sarcomere length, under worst case conditions. The error introduced was very small: a reduction in sarcomere length of less than 0.5 %.

scholarly journals Differential effects of acute changes in cell Ca2+ concentration on myofibrillar and non-myofibrillar protein breakdown in the rat extensor digitorum longus muscle in vitro. Assessment by production of tyrosine and Nτ-methylhistidine

1987 ◽  
Vol 241 (1) ◽  
pp. 121-127 ◽  
Author(s):  
M N Goodman
Keyword(s):  
Extensor Digitorum Longus ◽  
Extensor Digitorum Longus Muscle ◽  
Extensor Digitorum ◽  
Ionophore A23187 ◽  
Myofibrillar Proteins ◽  
Rat Muscle ◽  
Longus Muscle ◽  
Acute Changes ◽  
Tissue Contents

The influence of Ca2+ on myofibrillar proteolysis was evaluated in the isolated extensor digitorum longus muscle incubated in vitro with agents previously shown to increase the intracellular concentration of Ca2+. Myofibrillar proteolysis was evaluated by measuring the release of N tau-methylhistidine, and total proteolysis was evaluated by measuring tyrosine release by incubated muscles after the inhibition of protein synthesis with cycloheximide. Incubated muscles released measurable quantities of N tau-methylhistidine, and muscle contents of the amino acids remained stable over 2 h of incubation. The release of N tau-methylhistidine by incubated muscles was similar to its release by perfused rat muscle in response to brief starvation, indicating the integrity of the incubated muscles. Ca2+ ionophore A23187, dibucaine, procaine, caffeine and elevated K+ concentration increased lactate release by incubated muscles and decreased tissue contents of ATP and phosphocreatine to varying degrees, indicating the metabolic effectiveness of the agents tested. Only A23187 and dibucaine increased total cell Ca2+, and they increased tyrosine release. Caffeine and elevated [K+] increased neither cell Ca2+ nor tyrosine release; however, only A23187 and dibucaine increased tyrosine release significantly. On the other hand, these agents were without effect on myofibrillar proteolysis as assessed by N tau-methylhistidine release by incubated muscles and changes in tissue contents of the amino acid. In fact, some of the agents tested tended to decrease myofibrillar proteolysis slightly. These results indicate that acute elevation of intracellular Ca2+ is associated with increased breakdown of non-myofibrillar but not myofibrillar proteins. Because of this, the role of elevated Ca2+ in muscle atrophy in certain pathological states is questioned. The data also indicate that the breakdown of myofibrillar and non-myofibrillar proteins in muscle is regulated independently and by different pathways, a conclusion reached in previous studies with perfused rat muscle.

Potentiation of in vitro concentric work in mouse fast muscle

1998 ◽  
Vol 84 (1) ◽  
pp. 236-243 ◽  
Author(s):  
R. W. Grange ◽  
R. Vandenboom ◽  
J. Xeni ◽  
M. E. Houston
Keyword(s):  
Extensor Digitorum Longus ◽  
Conditioning Stimulus ◽  
Muscle Length ◽  
Extensor Digitorum Longus Muscle ◽  
Extensor Digitorum ◽  
Fast Muscle ◽  
Phosphate Content ◽  
Longus Muscle

Grange, R. W., R. Vandenboom, J. Xeni, and M. E. Houston.Potentiation of in vitro concentric work in mouse fast muscle. J. Appl. Physiol. 84(1): 236–243, 1998.—Phosphorylation of myosin regulatory light chain (R-LC) is associated with potentiated work and power during twitch afterloaded contractions in mouse extensor digitorum longus muscle [R. W. Grange, C. R. Cory, R. Vandenboom, and M. E. Houston. Am. J. Physiol. 269 ( Cell Physiol. 38): C713–C724, 1995]. We now describe the association between R-LC phosphorylation and potentiated concentric work when the extensor digitorum longus muscle is rhythmically shortened and lengthened to simulate contractions in vivo. Work output (at 25°C) was characterized at sine frequencies of 3, 5, 7, 10, and 15 Hz at excursions of 0.6, 1.2, and 1.6 mm (∼5, 9, and 13% optimal muscle length) at a low level of R-LC phosphorylation. Muscles stimulated during the sine function with a single twitch at specific times before or after the longest muscle length yielded maximal concentric work near the longest muscle length at a sine frequency of 7 Hz (e.g., excursion ∼9% optimal muscle length = 1.6 J/kg). Power increased linearly between sine frequencies of 3 and 15 Hz at all excursions (maximum ∼29 W). After a 5-Hz 20-s conditioning stimulus and coincident with a 3.7-fold increase in R-LC phosphate content (e.g., from 0.19 to 0.70 mol phosphate/mol R-LC), work at the three excursions and a sine frequency of 7 Hz was potentiated a mean of 25, 44, and 50% ( P < 0.05), respectively. The potentiated work during rhythmic contractions is consistent with enhanced interaction between actin and myosin in the force-generating states. On the basis of observations in skinned skeletal muscle fibers (H. L. Sweeney and J. T. Stull. Proc. Natl. Acad. Sci. USA 87: 414–418, 1990), this enhancement could result from increased phosphate incorporation by the myosin R-LC. Under the assumption that the predominant effect of the conditioning stimulus was to increase R-LC phosphate content, our data suggest that a similar mechanism may be evident in intact muscle.

scholarly journals Relationship between intracellular amino acids and protein synthesis in the extensor digitorum longus muscle of rats

1969 ◽  
Vol 114 (2) ◽  
pp. 171-178 ◽  
Author(s):  
R. C. Hider ◽  
E. B. Fern ◽  
D. R. London
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Free Amino ◽  
Extensor Digitorum Longus ◽  
Extensor Digitorum Longus Muscle ◽  
Extensor Digitorum ◽  
Longus Muscle ◽  
Intracellular Amino Acids ◽  
Free Amino Acid Pools

1. The incorporation into protein, and the accumulation into the free amino acid pools, of radioactive l-leucine and glycine was studied in rat extensor digitorum longus muscle. 2. The tissue was incubated first with 14C-labelled and then with 3H-labelled amino acid. 3. The experimental results were consistent with a model based on the premise that the amino acids in protein were incorporated directly from the extracellular pool.

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