Growth Rates, Protein Synthesis, and Protein Degradation Rates in Rainbow Trout: Effects of Body Size

1986 ◽  
Vol 59 (4) ◽  
pp. 482-493 ◽  
Author(s):  
D. F. Houlihan ◽  
D. N. McMillan ◽  
P. Laurent
Keyword(s):  
Protein Synthesis ◽  
Rainbow Trout ◽  
Body Size ◽  
Protein Degradation ◽  
Growth Rates ◽  
Degradation Rates

scholarly journals Chronic social stress alters protein metabolism in juvenile rainbow trout, Oncorhynchus mykiss

2021 ◽  
Author(s):  
Roxanne J. Saulnier ◽  
Carol Best ◽  
Daniel J. Kostyniuk ◽  
Kathleen M. Gilmour ◽  
Simon G. Lamarre
Keyword(s):  
Protein Synthesis ◽  
Rainbow Trout ◽  
Oncorhynchus Mykiss ◽  
Protein Degradation ◽  
Growth Rates ◽  
Protein Metabolism ◽  
Social Stress ◽  
White Muscle ◽  
Muscle Protein ◽  
Chronic Social Stress

AbstractWhen confined in pairs, juvenile rainbow trout (Oncorhynchus mykiss) form dominance hierarchies in which subordinate fish exhibit characteristic physiological changes including reduced growth rates and chronically elevated plasma cortisol concentrations. We hypothesized that alterations in protein metabolism contribute to the reduced growth rate of socially stressed trout, and predicted that subordinate trout would exhibit reduced rates of protein synthesis coupled with increases in protein degradation. Protein metabolism was assessed in dominant and subordinate fish after 4 days of social interaction, and in fish that were separated after 4 days of interaction for a 4 days recovery period, to determine whether effects on protein metabolism recovered when social stress was alleviated. Protein metabolism was assessed in liver and white muscle by measuring the fractional rate of protein synthesis and markers of protein degradation. In the white muscle of subordinate fish, protein synthesis was inhibited and activities of the ubiquitin-proteasome pathway (UPP) and the autophagy lysosomal system (ALS) were elevated. By contrast, the liver of subordinate fish exhibited increased rates of protein synthesis and activation of the ALS. When allowed to recover from chronic social stress for 4 days, differences in protein metabolism observed in white muscle of subordinate fish during the interaction period disappeared. In liver, protein synthesis returned to baseline levels during recovery from social stress, but markers of protein degradation did not. Collectively, these data support the hypothesis that inhibition of muscle protein synthesis coupled with increases in muscle protein breakdown contribute to the reduced growth rates of subordinate rainbow trout.

Effects of insulin-like growth factor-I, insulin, and leucine on protein turnover and ubiquitin ligase expression in rainbow trout primary myocytes

2010 ◽  
Vol 298 (2) ◽  
pp. R341-R350 ◽  
Author(s):  
Beth M. Cleveland ◽  
Gregory M. Weber
Keyword(s):  
Protein Synthesis ◽  
Rainbow Trout ◽  
Growth Factor ◽  
Protein Degradation ◽  
Ubiquitin Ligase ◽  
Protein Turnover ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Igf I ◽  
Growth Factor I

The effects of insulin-like growth factor-I (IGF-I), insulin, and leucine on protein turnover and pathways that regulate proteolytic gene expression and protein polyubiquitination were investigated in primary cultures of 4-day-old rainbow trout myocytes. Supplementing media with 100 nM IGF-I increased protein synthesis by 13% ( P < 0.05) and decreased protein degradation by 14% ( P < 0.05). Treatment with 1 μM insulin increased protein synthesis by 13% ( P < 0.05) and decreased protein degradation by 17% ( P < 0.05). Supplementing media containing 0.6 mM leucine with an additional 2.5 mM leucine did not increase protein synthesis rates but reduced rates of protein degradation by 8% ( P < 0.05). IGF-I (1 nM–100 nM) and insulin (1 nM-1 μM) independently reduced the abundance of ubiquitin ligase mRNA in a dose-dependent manner, with maximal reductions of ∼70% for muscle atrophy F-box (Fbx) 32, 40% for Fbx25, and 25% for muscle RING finger-1 (MuRF1, P < 0.05). IGF-I and insulin stimulated phosphorylation of FOXO1 and FOXO4 ( P < 0.05), which was inhibited by the phosphatidylinositol 3-kinase (PI 3-kinase) inhibitor wortmannin, and decreased the abundance of polyubiquitinated proteins by 10–20% ( P < 0.05). Supplementing media with leucine reduced Fbx32 expression by 25% ( P < 0.05) but did not affect Fbx25 nor MuRF1 transcript abundance. Serum deprivation decreased rates of protein synthesis by 60% ( P < 0.05), increased protein degradation by 40% ( P < 0.05), and increased expression of all ubiquitin ligases. These data suggest that, similar to mammals, the inhibitory effects of IGF-I and insulin on proteolysis occur via P I3-kinase/protein kinase B signaling and are partially responsible for the ability of these compounds to promote protein accretion.

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 Rates of protein turnover in vivo and in vitro in ventricular muscle of hearts from fed and starved rats

1984 ◽  
Vol 222 (2) ◽  
pp. 395-400 ◽  
Author(s):  
V R Preedy ◽  
D M Smith ◽  
N F Kearney ◽  
P H Sugden
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Protein Turnover ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Ventricular Muscle ◽  
Degradation Rates ◽  
Perfused Hearts

Starvation of 300 g rats for 3 days decreased ventricular-muscle total protein content and total RNA content by 15 and 22% respectively. Loss of body weight was about 15%. In glucose-perfused working rat hearts in vitro, 3 days of starvation inhibited rates of protein synthesis in ventricles by about 40-50% compared with fed controls. Although the RNA/protein ratio was decreased by about 10%, the major effect of starvation was to decrease the efficiency of protein synthesis (rate of protein synthesis relative to RNA). Insulin stimulated protein synthesis in ventricles of perfused hearts from fed rats by increasing the efficiency of protein synthesis. In vivo, protein-synthesis rates and efficiencies in ventricles from 3-day-starved rats were decreased by about 40% compared with fed controls. Protein-synthesis rates and efficiencies in ventricles from fed rats in vivo were similar to values in vitro when insulin was present in perfusates. In vivo, starvation increased the rate of protein degradation, but decreased it in the glucose-perfused heart in vitro. This contradiction can be rationalized when the effects of insulin are considered. Rates of protein degradation are similar in hearts of fed animals in vivo and in glucose/insulin-perfused hearts. Degradation rates are similar in hearts of starved animals in vivo and in hearts perfused with glucose alone. We conclude that the rates of protein turnover in the anterogradely perfused rat heart in vitro closely approximate to the rates in vivo in absolute terms, and that the effects of starvation in vivo are mirrored in vitro.

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.

scholarly journals Incompatibility of chemical protein synthesis inhibitors with accurate measurement of extended protein degradation rates

2017 ◽  
Vol 5 (5) ◽  
pp. e00359 ◽  
Author(s):  
Christina Chan ◽  
Philip Martin ◽  
Neill J. Liptrott ◽  
Marco Siccardi ◽  
Lisa Almond ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Protein Synthesis Inhibitors ◽  
Degradation Rates ◽  
Chemical Protein Synthesis

scholarly journals Effect of corticosterone treatment on muscle protein turnover in adrenalectomized rats and diabetic rats maintained on insulin

1982 ◽  
Vol 204 (3) ◽  
pp. 663-672 ◽  
Author(s):  
Bhanu R. Odedra ◽  
David J. Millward
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Protein Turnover ◽  
Muscle Wasting ◽  
Muscle Protein ◽  
Diabetic Rats ◽  
Constant Infusion ◽  
Degradation Rates ◽  
Adrenalectomized Rats

The effect of corticosterone on protein turnover in skeletal muscle was investigated in growing rats. Protein synthesis was measured in vivo by the constant infusion of [14C]tyrosine. The extent to which any effect of corticosterone is modulated by the hyperinsulinaemia induced by steroid treatment was examined by giving the hormone not only to adrenalectomized rats but also to streptozotocin-induced diabetic rats maintained throughout the treatment period on two dosages of insulin by an implanted osmotic minipump. Approximate rates of protein degradation were also estimated in some cases as the difference between synthesis and net change in muscle protein mass. Measurements were also made of free 3-methylhistidine concentration in muscle and plasma. At 10mg of corticosterone/100g body wt. per day, growth stopped and muscle wasting occurred, whereas at 5 mg of corticosterone/100g body wt. per day no net loss of protein occurred. However, this low dose did induce muscle wasting when insulin concentration was regulated by a dose of 1.2 units/day. Protein synthesis was markedly depressed in all treated groups, the depression in the insulin-maintained rats being marginally more than in the hyperinsulinaemic adrenalectomized rats. The oxidative soleus muscle appeared to be less susceptible to the effect of the corticosterone than was the more glycolytic plantaris or gastrocnemius muscle. Any effect of the corticosterone on protein degradation was much less than its effects on protein synthesis. Where increases in the degradation rates appeared to occur in the rats treated with 10mg of corticosterone/100g body wt. per day, the increases were less than 20%. The free intracellular 3-methylhistidine concentrations were doubled in all groups treated with 5 mg of corticosterone/100g body wt. per day and increased 5-fold in the adrenalectomized rats treated with 10mg of corticosterone/100g body wt. per day, with no change in plasma concentration in any of the groups. It is therefore concluded that: (a) the suppression of protein synthesis is the main effect of glucocorticoids in muscle; (b) marked increases in insulin afford only minor protection against this effect; (c) stimulation of protein degradation may occur, but to a much lesser extent.

Growth Rates and Protein Turnover in Atlantic Cod,Gadus morhua

1988 ◽  
Vol 45 (6) ◽  
pp. 951-964 ◽  
Author(s):  
D. F. Houlihan ◽  
S. J. Hall ◽  
C. Gray ◽  
B. S. Noble
Keyword(s):  
Growth Rate ◽  
Weight Loss ◽  
Protein Synthesis ◽  
Growth Rates ◽  
Gadus Morhua ◽  
White Muscle ◽  
Atlantic Cod ◽  
Degradation Rates ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

Atlantic cod, Gadus morhua, were maintained on different ration levels or starved to produce a variety of growth rates. The in vivo rates of protein synthesis and degradation were determined for the whole fish and various tissues. As ration level, and hence growth rates, increased, both whole-animal protein synthesis and degradation rates increased linearly; growth occurred because of the preponderance of synthesis over degradation. On average, a 300-g cod growing at 1.0%∙d−1synthesised 1.25 g of protein with 0.4 g of this protein remaining as growth. The proportion of total protein synthesis which was retained as growth increased with increasing growth rate; at a maximum growth rate of 2%∙d−1, over 40% of the protein synthesised was retained as growth. The ranking of the tissues in terms of fractional rates of protein synthesis was liver > gills > intestine > spleen > ventricle > stomach > gonads > white muscle. The white muscle, gills, liver, stomach, spleen, and ventricle all showed similar patterns of increased protein synthesis with increased growth rate. The white muscle has the highest efficiency of retention of protein and accounts for 40% of the total protein accretion per day. In starving fish there was a constant level of protein synthesis, irrespective of the rate of weight loss. However, degradation rates increased in the whole animal and in white muscle as the rate of weight loss increased.

scholarly journals Universality and non-universality of the growth law

2021 ◽  
Author(s):  
Qirun Wang ◽  
Jie Lin
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Ribosomal Proteins ◽  
Correlation Coefficients ◽  
Growth Conditions ◽  
Proliferating Cells ◽  
Translation Speed ◽  
Nutrient Quality ◽  
Degradation Rates ◽  
Mass Fractions

An approximately linear relationship between the fraction of ribosomal proteins in the proteome (ϕR) and the growth rate (μ) holds in proliferating cells when the nutrient quality changes, often referred to as a growth law. While a simple model assuming a constant translation speed of ribosomes without protein degradation can rationalize this growth law, real protein synthesis processes are more complex. This work proposes a general theoretical framework of protein synthesis, taking account of heterogeneous translation speeds among proteins and finite protein degradation. We introduce ribosome allocations as the fraction of active ribosomes producing certain proteins, with two correlation coefficients respectively quantifying the correlation between translation speeds and ribosome allocations, and between protein degradation rates and mass fractions. We prove that the growth law curve generally follows ϕR = (μ + c1)/(c2μ + c3) where c1, c2, and c3 are constants depending on the above correlation coefficients and the translation speed of ribosomal proteins. Our theoretical predictions of ϕR agree with existing data of Saccharomyces cerevisiae. We demonstrate that when different environments share similar correlation coefficients, the growth law curve is universal and up-bent relative to a linear line in slow-growth conditions, which appears valid for Escherichia coli. However, the growth law curve is non-universal and environmental-specific when the environments have significantly different correlation coefficients. Our theories allow us to estimate the translation speeds of ribosomal and non-ribosomal proteins based on the experimental growth law curves.

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