scholarly journals Morphological observations and rates of protein synthesis in rat muscles incubated in vitro

1985 ◽  
Vol 232 (3) ◽  
pp. 927-930 ◽  
Author(s):  
C A Maltin ◽  
C I Harris
Keyword(s):  
Protein Synthesis ◽  
Extensor Digitorum Longus ◽  
Marked Decrease ◽  
Extensor Digitorum ◽  
Central Core ◽  
Phosphorylase Activity ◽  
Glucan Phosphorylase ◽  
Isolated Rat

Isolated soleus and extensor digitorum longus muscles from small (40 or 70 g) rats developed a central and substantial (13-57%) loss of glycogen and alpha-glucan phosphorylase activity after incubation for up to 2 h in vitro. The central ‘core’ of the muscles showed a marked decrease in the rate of protein synthesis. It is suggested that during brief periods of incubation the central core of isolated rat muscles becomes hypoxic, and that consequently the viability of such muscles must be in question.

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 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 The effects of cutting or of stretching skeletal muscle in vitro on the rates of protein synthesis and degradation

1980 ◽  
Vol 188 (1) ◽  
pp. 247-254 ◽  
Author(s):  
M J Seider ◽  
R Kapp ◽  
C P Chen ◽  
F W Booth
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Extensor Digitorum Longus ◽  
High Energy ◽  
Extensor Digitorum ◽  
Muscle Fibres ◽  
High Energy Phosphates ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

Rates of protein synthesis were significantly lower in the cut soleus and extensor digitorum longus muscles than in their uncut counterparts. Rates of protein degradation were significantly higher in cut soleus muscles, but not in cut extensor digitorum longus muscles as compared with their uncut controls. Concentrations of ATP and phosphocreatine were significantly lower in cut soleus and extensor digitorum longus muscles after incubation in vitro in contrast with respective control uncut muscles. These data indicate that cutting of muscle fibres alters rates of protein synthesis and degradation, in addition to altering concentrations of high-energy phosphates. Since these findings stressed the importance of using intact muscles to study protein metabolism, additional studies were made on intact muscles in vitro. Stretched soleus muscles had higher concentrations of high-energy phosphates at the end of an incubation period than did unstretched muscles. However, the length of the soleus, extensor digitorum longus and diaphragm muscles during incubation did not affect rates of protein degradation.

scholarly journals The effects of denervation on protein turnover of rat skeletal muscle

1976 ◽  
Vol 156 (1) ◽  
pp. 71-80 ◽  
Author(s):  
D F Goldspink
Keyword(s):  
Protein Synthesis ◽  
Conformational Changes ◽  
Extensor Digitorum Longus ◽  
Soluble Proteins ◽  
Extensor Digitorum ◽  
Muscle Weight ◽  
Active Involvement ◽  
Two Phases ◽  
Denervated Muscles

The effects of denervation on muscle weight, rates of protein synthesis and breakdown, and RNA concentraitons were studied in the soleus and extensor digitorum longus muscle. Althrough the soleus underwent a true atrophy after section of the sciatic nerve, the extensor digitorum longus continued to grow, albeit at a lower rate than innervated controls. At 24h after nerve section protein breakdown was increased in both muscle types when compared with internal controls, and remained so throughout the 10 days studied. The possibility that this increased catabolism might arise from conformational changes of proteins after denervation was not substantiated, as myofibrillar or soluble proteins of denervated and control tissues were equally susceptible to degradation in vitro by three proteinases. Tyrosine uptake into the denervated extensor digitorum longus was decreased throughout the 10 days studied, whereas two phases of increased transport of the amino acid were found in the soleus. Significant decreases in rates of protein synthesis were found 1 and 2 days after denervation and results are presented that suggest that these changes may result from a decrease in ribosomal involvement in the translation process. These initial decreases were not maintained and the rate of protein synthesis was in fact increased when compared with controls, at 7 and 10 days. The increased synthetic rates of the 7-day denervated tissues were reflected as proportional increases in both myofibrillar and soluble proteins. It is suggested that the increase in synthesis at this time may result from an increase in both the abailability and active involvement of ribosomes, and that these anabolic trends may be caused by spontaneous fibrillation and/or the amount of passive stretching of the denervated muscles.

scholarly journals Regulation of protein metabolism by a physiological concentration of insulin in mouse soleus and extensor digitorum longus muscles. Effects of starvation and scald injury

1979 ◽  
Vol 184 (2) ◽  
pp. 323-330 ◽  
Author(s):  
K N Frayn ◽  
P F Maycock
Keyword(s):  
Protein Synthesis ◽  
Protein Metabolism ◽  
Extensor Digitorum Longus ◽  
Muscle Protein ◽  
Extensor Digitorum ◽  
Total Protein Content ◽  
Skin Thickness ◽  
Physiological Concentration ◽  
Scald Injury

1. Although high concentrations of insulin affect both synthesis and degradation of skeletal-muscle protein, it is not known to what extent these effects occur with physiological concentrations. The effects of a physiological concentration of insulin (100 mu units/ml) on muscle protein synthesis, measured with [3H]tyrosine, and on muscle protein degradation, measured by tyrosine release in the presence of cycloheximide, were studied in mouse soleus and extensor digitorum longus muscles in vitro. 2. Insulin significantly stimualated protein synthesis in both muscles, but an inhibition of degradation was seen only in the extensor digitorum longus. 3. Starvation for 24 h decreased the rate of protein synthesis and increased the rate of breakdown in the extensor digitorum longus. Sensitivity to insulin-stimulation of proteins synthesis in the soleus was increased by starvation. 4.;a 20%-surface-area full-skin-thickness dorsal scald injury produced a fall in total protein content in soleus and extensor digitorum muscles, maximal on the third day after injury. Soleus muscles 2 days after injury showed an impairment of protein synthesis; degradation was unaffected and neither synthesis nor degradation in vitro was significantly affected in the extensor digitorum longus. 5. The advantages and limitations of studies of protein metabolism in vitro are discussed.

Correlation between magnesium and potassium contents in muscle: role of Na(+)-K+ pump

1993 ◽  
Vol 264 (2) ◽  
pp. C457-C463 ◽  
Author(s):  
I. Dorup ◽  
T. Clausen
Keyword(s):  
Extensor Digitorum Longus ◽  
Extensor Digitorum ◽  
Deficient Diet ◽  
Young Rats ◽  
Wide Range ◽  
86Rb Influx

In young rats fed a Mg(2+)-deficient diet for 3 wk, Mg2+ and K+ contents in soleus and extensor digitorum longus muscles were significantly reduced and closely correlated. In isolated soleus muscles, Mg2+ depletion induced an even more pronounced loss of K+, and Mg2+ and K+ contents were correlated over a wide range (r = 0.95, P < 0.001). Extracellular Mg2+ (0-1.2 mM) caused no change in total or ouabain-suppressible 86Rb influx. After long-term incubation in Ca(2+)-Mg(2+)-free buffer with EDTA and EGTA, cellular Mg2+ and K+ contents were reduced by 35 and 15%, respectively, without any reduction in ATP and total or ouabain-suppressible 86Rb influx. In Mg(2+)-depleted muscles 42K efflux was increased by up to 42%, and repletion with Mg2+ produced a graded decrease. We conclude that Mg2+ and K+ contents are closely correlated in muscles Mg2+ depleted in vivo or in vitro and that neither extracellular nor moderate intracellular Mg2+ depletion affects total or Na(+)-K+ pump-mediated K+ influx. The reduced K+ content may rather be related to increased K+ efflux from the muscles.

Differential myogenicity of satellite cells isolated from extensor digitorum longus (EDL) and soleus rat muscles revealed in vitro

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

scholarly journals Purine biosynthesis de novo in rat skeletal muscle

1983 ◽  
Vol 216 (3) ◽  
pp. 605-610 ◽  
Author(s):  
T G Sheehan ◽  
E R Tully
Keyword(s):  
Skeletal Muscle ◽  
Extensor Digitorum Longus ◽  
De Novo ◽  
Adenine Nucleotides ◽  
Extensor Digitorum ◽  
Purine Biosynthesis ◽  
Rat Skeletal Muscle ◽  
Purine Synthesis ◽  
Longus Muscle ◽  
Isolated Rat

Purine biosynthesis by the ‘de novo’ pathway was demonstrated in isolated rat extensor digitorum longus muscle with [1-14C]glycine, [3-14C]serine and sodium [14C]formate as nucleotide precursors. Evidence is presented which suggests that the source of glycine and serine for purine biosynthesis is extracellular rather than intracellular. The relative incorporation rates of the three precursors were formate greater than glycine greater than serine. Over 85% of the label from formate and glycine was recovered in the adenine nucleotides, principally ATP. Azaserine markedly inhibited purine biosynthesis from both formate and glycine. Cycloserine inhibited synthesis from serine, but not from formate. Adenine, hypoxanthine and adenosine markedly inhibited purine synthesis from sodium [14C]formate.

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