scholarly journals The effect of insulin and intermittent mechanical stretching on rates of protein synthesis and degradation in isolated rabbit muscle

1985 ◽  
Vol 230 (1) ◽  
pp. 117-123 ◽  
Author(s):  
R M Palmer ◽  
P A Bain ◽  
P J Reeds
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Suppressive Effect ◽  
Rabbit Muscle ◽  
Degradation Rates ◽  
Forelimb Muscles ◽  
Amino Acid Balance ◽  
Mechanical Stretching ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

Tyrosine balance and protein synthesis were studied during the same incubation in isolated rabbit forelimb muscles. From these measurements, protein degradation was calculated. Isolated muscles were usually in a state of negative amino acid balance, principally as a result of the 75% decrease in protein synthesis. Muscles from rabbits starved for 18 h had lower rates of both protein synthesis and degradation compared with muscles from normally fed rabbits. Intermittent mechanical stretching and the addition of insulin at 100 microunits/ml increased rates of both protein synthesis and degradation. Increases in the rate of protein synthesis were proportionately greater in the muscles from starved animals. In muscles from both fed and starved donors, increases in protein-synthesis rates owing to intermittent stretching and insulin were proportionately greater than the increases in degradation rates. For example, insulin increased the rate of protein synthesis in the muscles from starved donors by 111% and the rate of degradation by 31%. Insulin also increased the rate of protein synthesis when added at a higher concentration (100 munits/ml); at this concentration, however, the rate of protein degradation was not increased. The suppressive effect of insulin on high rates of protein degradation in other skeletal-muscle preparations may reflect a non-physiological action of the hormone.

scholarly journals Effect of hypophysectomy on the rates of protein synthesis and degradation in rat liver

1979 ◽  
Vol 178 (3) ◽  
pp. 725-731 ◽  
Author(s):  
R D Conde
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Rat Liver ◽  
Protein Metabolism ◽  
Plasma Proteins ◽  
Degradation Rates ◽  
Hypophysectomized Rats ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

The effect of hypophysectomy on the protein metabolism of the liver in vivo was studied. Fractional rates of protein synthesis and degradation were determined in the livers of normal and hypophysectomized rats. Synthesis was measured after the injection of massive amounts of radioactive leucine. Degradation was estimated either as the balance between synthesis and accumulation of stable liver proteins or from the disappearance of radioactivity from the proteins previously labelled by the injection of NaH14CO3. The results indicate that: (1) hypophysectomy diminishes the capacity of the liver to synthesize proteins in vivo, mainly of those that are exported as plasma proteins; (2) livers of both normal and hypophysectomized rats show identical protein-degradation rates, whereas plasma proteins are degraded slowly after hypophysectomy.

scholarly journals Comparison of protein synthesis and degradation in incubated and perfused muscle

1983 ◽  
Vol 212 (3) ◽  
pp. 649-653 ◽  
Author(s):  
A S Clark ◽  
W E Mitch
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Insulin Treatment ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Muscle Protein Degradation ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

Rates of muscle protein synthesis and degradation measured in the perfused hindquarter were compared with those in incubated epitrochlearis muscles. With fed or starved mature rats, results without insulin treatment were identical. With insulin treatment, protein synthesis in perfused hindquarters was greater, though protein degradation was the same. Thus rates of muscle protein degradation estimated by these two methods in vitro correspond closely.

Effects of glucocorticoid treatment on cardiac protein synthesis and degradation

1986 ◽  
Vol 250 (6) ◽  
pp. C821-C827 ◽  
Author(s):  
A. F. Clark ◽  
G. N. DeMartino ◽  
K. Wildenthal
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Lower Body ◽  
Glucocorticoid Treatment ◽  
Body Weights ◽  
Langendorff Perfusion ◽  
Perfused Hearts ◽  
Fasted Rats ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

We treated rats with dexamethasone (DEX, 1 mg . kg-1 . day-1) and examined the effects of this glucocorticoid on heart protein metabolism using atrial explant and Langendorff perfusion preparations. Fasted rats treated with DEX for 2 days had significantly lower body weights (92% of control, P less than 0.001) and larger hearts (106% of control, P less than 0.005) than fasted control animals. Protein and RNA concentrations remained constant. In atrial explants, DEX treatment produced a 19% increase in protein synthesis (P less than 0.001) and a 13% increase in protein degradation (P less than 0.002). In Langendorff-perfused hearts, DEX treatment caused a 36% increase in protein synthesis (P less than 0.02), while protein degradation was 8% above control (P greater than 0.05). Thus, in contrast to their catabolic effects on skeletal muscle, glucocorticoids are anabolic on the heart. The increased accumulation of total cardiac protein during early glucocorticoid administration is mediated entirely via increased rates of synthesis.

scholarly journals Contribution of whole-body protein synthesis to basal metabolism in layer and broiler chickens

1987 ◽  
Vol 57 (2) ◽  
pp. 269-277 ◽  
Author(s):  
T. Muramatsu ◽  
Y. Aoyagi ◽  
J. Okumura ◽  
I. Tasaki
Keyword(s):  
Protein Synthesis ◽  
Broiler Chickens ◽  
Whole Body ◽  
Synthesis Rate ◽  
Body Protein ◽  
Fractional Synthesis Rate ◽  
Degradation Rates ◽  
Fractional Synthesis ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

1. The effect of starvation on whole-body protein synthesis and on the contribution of protein synthesis to basal metabolic rate was investigated in young chickens (Expt 1). Strain differences between layer and broiler chickens in whole-body protein synthesis and degradation rates were examined when the birds were starved (Expt 2).2. In Expt 1, 15-d-old White Leghorn male chickens were used, while in Expt 2 Hubbard (broiler) and White Leghorn (layer) male chickens at 14 d of age were used. They were starved for 4 d, and heat production was determined by carcass analysis after 2 and 4 d of starvation. Whole-body protein synthesis rates were measured on 0, 2 and 4 d of starvation (Expt 1), and on 0 and 4 d of starvation (Expt 2).3. The results showed that starving reduced whole-body protein synthesis in terms of fractional synthesis rate and the amount synthesized. Whole-body protein degradation was increased by starvation both in terms of fractional synthesis rate and the amount degraded on a per kg body-weight basis.4. Reduced fractional synthesis rate of protein in the whole body was accounted for by reductions in both protein synthesis per unit RNA and RNA:protein ratio.5. In the fed state, whole-body protein synthesis and degradation rates, whether expressed as fractional rates or amounts per unit body-weight, tended to be higher in layer than in broiler chickens. In the starved state, the difference in the rate of protein synthesis between the two strains virtually disappeared, while the degradation rates were higher in layer than in broiler birds.6. Based on the assumed value of 3.56 kJ/g protein synthesized (Waterlow et al. 1978), the heat associated with whole-body protein synthesis in the starved state was calculated to range from 14 to 17% of the basal metabolic rate with no strain difference between layer and broiler chickens.

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.

Extensive changes in collagen synthesis and degradation during compensatory lung growth

1988 ◽  
Vol 255 (6) ◽  
pp. C754-C759 ◽  
Author(s):  
R. J. McAnulty ◽  
L. H. Staple ◽  
D. Guerreiro ◽  
G. J. Laurent
Keyword(s):  
Protein Synthesis ◽  
Collagen Synthesis ◽  
Collagen Degradation ◽  
Lung Growth ◽  
Compensatory Lung Growth ◽  
Fractional Rate ◽  
Degradation Rates ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

Unilateral pneumonectomy in rats causes compensatory growth of the remaining lung. This growth involves rapid production of collagen and noncollagen proteins, but the mechanisms for these changes have not been fully investigated. Rates of collagen metabolism were measured using previously validated in vivo methods. Six days after pneumonectomy, a threefold increase in the fractional rate of collagen synthesis was observed (control 11.8 +/- 0.9%/day, pneumonectomy 30.0 +/- 4.6%/day). Collagen degradation rates also increased but returned to normal more rapidly than the synthesis rates. These changes in synthesis and degradation resulted in a 75% increase in collagen content by 28 days. Although degradation of extracellular collagens was apparently increased, the fraction degraded intracellularly decreased by approximately 30%. Noncollagen protein synthesis and degradation rates both increased by approximately 80% (control 44.3 +/- 3.4%/day, pneumonectomy 80.3 +/- 10.2%/day) with a slightly greater increase in synthesis that led to an 85% increase in noncollagen protein content 28 days after pneumonectomy. The data obtained show dramatic changes in protein synthesis and degradation during compensatory lung growth and indicate extensive remodeling of structural elements in lung tissue. The changes for intracellular collagen degradation provide further evidence that this pathway may have an important role in regulating collagen deposition.

scholarly journals Specificity of the effects of leucine and its metabolites on protein degradation in skeletal muscle

1984 ◽  
Vol 222 (3) ◽  
pp. 579-586 ◽  
Author(s):  
W E Mitch ◽  
A S Clark
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Protein Degradation ◽  
Muscle Protein ◽  
Adult Rats ◽  
Limb Muscles ◽  
Leucine Catabolism ◽  
Muscle Protein Degradation ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

The effects of leucine, its metabolites, and the 2-oxo acids of valine and isoleucine on protein synthesis and degradation in incubated limb muscles of immature and adult rats were tested. Leucine stimulated protein synthesis but did not reduce proteolysis when leucine transamination was inhibited. 4-Methyl-2-oxopentanoate at concentrations as low as 0.25 mM inhibited protein degradation but did not change protein synthesis. The 2-oxo acids of valine and isoleucine did not change protein synthesis or degradation even at concentrations as high as 5 mM. 3-Methylvalerate, the irreversibly decarboxylated product of 4-methyl-2-oxopentanoate, decreased protein degradation at concentrations greater than or equal to 1 mM. This was not due to inhibition of 4-methyl-2-oxopentanoate catabolism, because 0.5 mM-3-methylvalerate did not suppress proteolysis, even though it inhibited leucine decarboxylation by 30%; higher concentrations of 3-methylvalerate decreased proteolysis progressively without inhibiting leucine decarboxylation further. During incubation with [1-14C]- and [U-14C]-leucine, it was found that products of leucine catabolism formed subsequent to the decarboxylation of 4-methyl-2-oxopentanoate accumulated intracellularly. This pattern was not seen during incubation with radiolabelled valine. Thus, the effect of leucine on muscle proteolysis requires transamination to 4-methyl-2-oxopentanoate. The inhibition of muscle protein degradation by leucine is most sensitive to, but not specific for, its 2-oxo acid, 4-methyl-2-oxopentanoate.

Effects of Exercise Training on the Performance, Growth, and Protein Turnover of Rainbow Trout (Salmo gairdneri)

1987 ◽  
Vol 44 (9) ◽  
pp. 1614-1621 ◽  
Author(s):  
D. F. Houlihan ◽  
P. Laurent
Keyword(s):  
Protein Synthesis ◽  
Rainbow Trout ◽  
Control Fish ◽  
Salmo Gairdneri ◽  
Degradation Rates ◽  
The Difference ◽  
Net Protein ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation ◽  
Better Than

Rainbow trout (Salmo gairdneri) that were made to swim continuously at 1 body length/s for 6 wk had double the growth rate of tank-rested control fish. The endurance to fatigue at a range of swimming velocities of these trained animals was significantly better than that of the controls. Measurement of the rate of protein synthesis in the tissues was carried out by the free pool flooding technique. Protein degradation rates were calculated from the difference between synthesis and net protein accretion. In controls and trained animals the fractional rates of protein synthesis and degradation were ranked gills > ventricle > red muscle > white muscle whereas the efficiencies of conversion of protein synthetised into protein retained as growth were in the reverse sequence. Synthesis rates in three of the four tissues of the trained animals were approximately double those of the control animals. Calculated degradation rates of proteins also increased in the trained animals; the increased growth rates resulted from the proportionately greater increase in the rate of synthesis. The rate of synthesis decreased to control levels once the trained animals ceased swimming.

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