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.

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 Effects of insulin in vitro on protein turnover in rat epitrochlearis muscle

1983 ◽  
Vol 210 (2) ◽  
pp. 323-330 ◽  
Author(s):  
W S Stirewalt ◽  
R B Low
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Nitrogen Balance ◽  
Protein Metabolism ◽  
Serum Insulin ◽  
Specific Radioactivity ◽  
Physiological Concentration ◽  
Rat Serum ◽  
The Third

Rates of protein synthesis and degradation were measured in the isolated rat epitrochlearis muscle by radiotracer techniques, by using the specific radioactivity of tRNA-bound amino acid as precursor for protein synthesis. The tissue maintained linear rates of protein synthesis for 3 h of incubation in the presence of amino acids and glucose and in the absence of insulin. Under these conditions, however, the muscles were in negative nitrogen balance, with rates of protein degradation exceeding rates of protein synthesis. Under steady-state conditions of labelling, the specific radioactivities of tRNA-bound leucine, phenylalanine and valine were significantly less than their respective values in the incubation medium, at concentrations in the medium varying from 1 to 10 times those in normal rat serum. Insulin caused a dose- and time-dependent increase in tRNA-based protein synthesis rates, more than doubling rates at 5 and 50 ng of insulin/ml. At the lower, physiological, concentration of insulin, the stimulation of protein synthesis was not observed until the third hour of incubation with the hormone, whereas the rate of protein synthesis at the higher concentration was elevated during the second hour. There were no delays in the stimulation by insulin of glucose conversion into glycogen. The delayed stimulatory effects of insulin on the rate of protein synthesis brought the tissue to a nitrogen balance near zero. The presence of the hormone also prevented the increase in the rate of protein degradation seen in the third hour of incubation in the absence of the hormone. These studies demonstrate the viability of the incubated rat epitrochlearis muscle with respect to protein metabolism and sensitivity to the protein anabolic effects of physiological concentrations of insulin, and indicate that the preparation is a suitable experimental model for the study of the control of protein metabolism in fast-twitch skeletal muscle.

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.

Protein synthesis and degradation in flight muscles of adult crickets (Gryllus bimaculatus)

1995 ◽  
Vol 198 (5) ◽  
pp. 1071-1077 ◽  
Author(s):  
T Gomi ◽  
T Okuda ◽  
S Tanaka
Keyword(s):  
Protein Synthesis ◽  
Protein Content ◽  
Total Protein ◽  
Muscle Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Adult Life ◽  
Total Protein Content ◽  
Gryllus Bimaculatus ◽  
Flight Muscles

The development and degeneration of the flight muscles in adult crickets, Gryllus bimaculatus, were studied (1) by determination of the total protein content, (2) by SDS one-dimensional polyacrylamide gel electrophoresis (SDS­PAGE) of muscle protein and (3) by in vitro culturing of the muscle. The total protein content of the dorso-longitudinal muscle (DLM) and metathoracic dorso-ventral muscle (DVM) increased during the early days of adult life in both sexes. This high protein content was maintained for at least a further 10 days in some individuals, while in others it declined to a low level. Mesothoracic DVMs in males also showed an increase in protein content after adult emergence but did not undergo histolysis, whereas those in females showed no significant temporal change in protein content. Removal of hind wings or artificial de-alation was found to be useful in inducing degeneration of DLMs and metathoracic DVMs. This treatment also stimulated ovarian development in females. An analysis by SDS­PAGE provided no evidence for new protein synthesis prior to or during flight muscle degeneration. A high rate of [3H]- or [35S]methionine incorporation was observed in DLMs taken from newly emerged adults, but, in intact crickets, the rate declined rapidly during the first 3 days of adult life, a pattern consistent with that obtained from the measurement of total protein content. Compared with DLMs removed from intact crickets, DLMs taken from de-alated crickets showed reduced rates of protein synthesis during in vitro culturing. This, together with the onset of protein degradation, appears to cause the rapid decrease in total protein content of the muscle in de-alated crickets.

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 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 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 The action of the β-agonist clenbuterol on protein metabolism in innervated and denervated phasic muscles

1989 ◽  
Vol 261 (3) ◽  
pp. 965-971 ◽  
Author(s):  
C A Maltin ◽  
S M Hay ◽  
M I Delday ◽  
G E Lobley ◽  
P J Reeds
Keyword(s):  
Protein Synthesis ◽  
Protein Metabolism ◽  
Extensor Digitorum Longus ◽  
Extensor Digitorum ◽  
Temporal Response ◽  
Muscle Type ◽  
Fractional Rate ◽  
Denervated Muscles ◽  
Gastrocnemius Muscles

1. Clenbuterol treatment in innervated and denervated phasic extensor digitorum longus, plantaris and gastrocnemius muscles from rats caused a significant increase in RNA and protein contents in all muscles except denervated extensor digitorum longus. 2. All muscles showed an increase in the fractional rate of protein synthesis (Ks) with clenbuterol, but the temporal response varied. 3. The data suggest that the effect of clenbuterol on protein metabolism in innervated muscles is muscle-type specific, and demonstrate the homology of response for denervated muscles.

Response of muscle protein synthesis to fasting in suckling and weaned rats

1991 ◽  
Vol 261 (6) ◽  
pp. R1373-R1380 ◽  
Author(s):  
T. A. Davis ◽  
M. L. Fiorotto ◽  
H. V. Nguyen ◽  
D. G. Burrin ◽  
P. J. Reeds
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Extensor Digitorum Longus ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Age Groups ◽  
Extensor Digitorum ◽  
Suckling Period ◽  
Synthetic Capacity

Protein synthetic efficiency (KRNA) is low in immature skeletal muscle of suckling rats and increases toward the end of the suckling period. To determine whether immature skeletal muscle is able to further reduce KRNA in response to fasting, suckling (5, 10, and 16 days of age) and weaned (28 days of age) rats were fed, fasted for 10 h, or fasted for 18 h and injected with a flooding dose of L-[4-3H]phenylalanine for measurement of muscle protein synthesis in vivo. In fed rats, fractional rates of protein synthesis (KS) and protein synthetic capacity decreased during the suckling period. KRNA increased toward the end of the suckling period. In 5-day-old rats, fasting for 10 h produced a 50% decline in KS of extensor digitorum longus and plantaris muscles, but KS did not change further after 18 h of fasting. In older suckled and weaned rats, 10 h of fasting decreased KS of extensor digitorum longus and plantaris muscles 30%; after 18 h of fasting, values had declined to 50% of those in fed animals. The reductions in KS in soleus muscles with 10 and 18 h of fasting were similar to those in other muscles at 5 and 10 days but were less than those in other muscles at 16 and 28 days. Changes in KRNA were similar to those for KS in all muscles from all age groups fasted for 10 and 18 h. Protein synthetic capacity decreased approximately 12% after 18 h of fasting, but this effect did not differ between age groups or muscle types.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Large increases in adipose triacylglycerol flux in Cushingoid CRH-Tg mice are explained by futile cycling

2013 ◽  
Vol 304 (3) ◽  
pp. E282-E293 ◽  
Author(s):  
Charles Harris ◽  
Donald J. Roohk ◽  
Mark Fitch ◽  
Benjamin M. Boudignon ◽  
Bernard P. Halloran ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Collagen Synthesis ◽  
Muscle Protein ◽  
Subcutaneous Fat ◽  
Skin Thickness ◽  
Breakdown Rate ◽  
Triglyceride Synthesis ◽  
Fat Depots ◽  
Breakdown Rates ◽  
Skin Collagen

Glucocorticoids are extremely effective anti-inflammatory therapies, but their clinical use is limited due to severe side effects, including osteoporosis, muscle wasting, fat redistribution, and skin thinning. Here we use heavy water labeling and mass spectrometry to measure fluxes through metabolic pathways impacted by glucocorticoids. We combine these methods with measurements of body composition in corticotropin-releasing hormone (CRH)-transgenic (Tg)+ mice that have chronically elevated, endogenously produced corticosterone and a phenotype that closely mimics Cushing's disease in humans. CRH-Tg+ mice had increased adipose mass, adipose triglyceride synthesis, and greatly increased triglyceride/fatty acid cycling in subcutaneous and abdominal fat depots and increased de novo lipogenesis in the abdominal depot. In bone, CRH-Tg+ mice had decreased bone mass, absolute collagen synthesis rates, and collagen breakdown rate. In skin, CRH-Tg+ mice had decreased skin thickness and absolute collagen synthesis rates but no decrease in the collagen breakdown rate. In muscle, CRH-Tg+ mice had decreased muscle mass and absolute protein synthesis but no decrease in the protein breakdown rate. We conclude that chronic exposure to endogenous glucocorticoid excess in mice is associated with ongoing decreases in bone collagen, skin collagen, and muscle protein synthesis without compensatory reduction (coupling) of breakdown rates in skin and muscle. Both of these actions contribute to reduced protein pool sizes. We also conclude that increased cycling between triglycerides and free fatty acids occurs in both abdominal and subcutaneous fat depots in CRH-Tg+ mice. CRH-Tg mice have both increased lipolysis and increased triglyceride synthesis in adipose tissue.

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