scholarly journals Studies on the range of tissue protein synthesis in pigs: the effect of thyroid hormones

1982 ◽  
Vol 48 (3) ◽  
pp. 571-582 ◽  
Author(s):  
O. Simon ◽  
H. Bergner ◽  
R. Münchmeyer ◽  
Teresa Zebrowska
Keyword(s):  
Protein Synthesis ◽  
Thyroid Hormones ◽  
Growing Pigs ◽  
Constant Infusion ◽  
Kidney Cortex ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Kidney Medulla ◽  
Tissue Protein ◽  
Tissue Protein Synthesis

1. The effects of thyroid hormones on the range of tissue protein synthesis in growing pigs using the constant infusion technique with [14c]leucine and [14C]lysine were studied.2. During a 6 h infusion, samples were taken from blood and, at the end of the infusion, from liver, pancreas, stomach, small and large intestines, kidney cortex, kidney medulla, muscle and skin.3. Lower relative specific radioactivities of free leucine and lysine in several tissues were observed in the hormone-treated group than in the untreated one.4. The range of protein synthesis rate and the daily amount of protein synthesized in tissues was higher in all tissues after application of thyroid hormones.5. Assuming that the organs analysed represented 70% of the total trichloroacetic acid-precipitable protein of the pig, the estimated range of daily protein synthesis was 251–490 and 312–880 g in untreated and hormone-treated pigs respectively.

scholarly journals Dietary Ornithine Affects the Tissue Protein Synthesis Rate in Young Rats

2012 ◽  
Vol 58 (4) ◽  
pp. 297-302 ◽  
Author(s):  
Kazuyo TUJIOKA ◽  
Takashi YAMADA ◽  
Mami AOKI ◽  
Koji MORISHITA ◽  
Kazutoshi HAYASE ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Tissue Protein ◽  
Young Rats ◽  
Tissue Protein Synthesis

Effect of glutamine supplementation of the diet on tissue protein synthesis rate of glucocorticoid-treated rats

Nutrition ◽  
2001 ◽  
Vol 17 (1) ◽  
pp. 35-40 ◽  
Author(s):  
Julio J Boza ◽  
Marco Turini ◽  
Denis Moënnoz ◽  
Franck Montigon ◽  
Jacques Vuichoud ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Glutamine Supplementation ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Tissue Protein ◽  
Tissue Protein Synthesis

Early change in skeletal muscle protein synthesis after limb immobilization of rats

1979 ◽  
Vol 47 (5) ◽  
pp. 974-977 ◽  
Author(s):  
F. W. Booth ◽  
M. J. Seider
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Control Level ◽  
Constant Infusion ◽  
Initial Time ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Limb Immobilization

The atrophy of skeletal muscle accruing from disuse, or limb immobilization, is caused by a decreased rate of protein synthesis and an increased rate of protein degradation. Currently, little information is available regarding the initial time of the decline in the rate of protein synthesis in skeletal muscle. The purpose of the present study was to determine, as precisely as possible, the time at which the protein synthesis rate first begins to decline in skeletal muscle, utilizing immobilized limbs of rats for a model. A constant-infusion technique employing [14C]tyrosine was used to estimate protein synthesis rates. During the first 6 h of immobilization, a significant decline of 37% in the fractional rate of protein synthesis from the control level of 5.7%/day was observed. These results suggest that very early changes are occurring in molecular events that regulate protein synthesis in disused or immobilized skeletal muscle.

scholarly journals The Effects of Age and Adiposity on Casein Digestibility and Tissue Protein Synthesis in Rats

2021 ◽  
Vol 5 (Supplement_2) ◽  
pp. 1196-1196
Author(s):  
Nathalie Atallah ◽  
Claire Gaudichon ◽  
Audrey Boulier ◽  
Alain Baniel ◽  
Dalila Azzout-Marniche ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Dietary Intervention ◽  
Metabolic Response ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Standard Diet ◽  
Young Rats ◽  
Funding Sources ◽  
Significant Difference ◽  
Tissue Protein Synthesis

Abstract Objectives Age and adiposity can impact the digestibility of dietary proteins and the metabolic response to their ingestion. The objective was to evaluate the effects of age and adiposity on casein digestibility and protein synthesis in tissues and organs. Methods Wistar rats of 1 month (n = 15) and 10 months (n = 15) at their arrival were fed ad libitum with a standard diet or High Fat diet to obtain rats of normal and high adiposity levels. Four groups were constituted (n = 7/8): 2 months/normal adiposity, 2 months/high adiposity, 11 months/normal adiposity and 11 months/high adiposity. At the end of the dietary intervention, they were fed the standard diet for 1 week before the test meal. The rats consumed a 4g meal containing 15N-labeled casein (Prodiet® 85B). Six hours after meal ingestion, the rats were euthanized. Intravenous injection of a massive dose of 13C-valine prior to euthanasia was used to determine protein synthesis rate in liver, kidneys, skin and muscle. Body composition was evaluated and digestive contents were collected to measure casein digestibility. Results No weight difference between rats of the same age was observed. However, a significant difference in adiposity was noted, with a surge in body fat of 3% in young rats and 7% in older rats. Digestibility increased with a higher adiposity level (P = 0.04). In young rats, it was 94.1 ± 1.1% in lean rats and 95.2 ± 1.7% in fat rats. In older rats, it was 94.5 ± 2.2% and 95.8 ± 0.7%, in lean and fat rats respectively. Significant effects of age (P < 0.01) and adiposity (P < 0.01) were observed in the muscle fractional synthesis rate (FSR), with age decreasing it and adiposity increasing it. In young rats, FSR was 10.1 ± 2.1%/day and 12.0 ± 3.0%/day in lean and fat rats, respectively, these values being 6.2 ± 1.5%/day and 10.6 ± 2.0%/day in older rats. In the skin, younger rats exhibited a higher FSR (P < 0.01) as it was 11.1 ± 2.6%/day and 12.6 ± 3.7%/day in lean and fat rats respectively, and 8.3 ± 2.3%/day and 8.2 ± 2.7%/day in older rats. No differences were found for the liver and kidneys. Conclusions Protein synthesis in muscle decreased with age while adiposity increased it. This is consistent with an improvement in ribosomal activity at an intermediate state of obesity. The surge in casein digestibility with higher adiposity, although moderate, could have contributed to the improvement in muscle anabolism response. Funding Sources Ingredia.

Assessment of the mathematical issues involved in measuring the fractional synthesis rate of protein using the flooding dose technique

1993 ◽  
Vol 84 (2) ◽  
pp. 177-183 ◽  
Author(s):  
David L. Chinkes ◽  
Judah Rosenblatt ◽  
Robert R. Wolfe
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Intracellular Concentration ◽  
Upper And Lower Bounds ◽  
Constant Infusion ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Underlying Assumption ◽  
Fractional Synthesis Rate ◽  
Fractional Synthesis

1. The fractional synthesis rate of protein is commonly measured by either the constant infusion method or the flooding dose method. The two methods often give different results. 2. An underlying assumption of the traditional flooding dose formula is that the protein synthesis rate is not stimulated by the flooding dose. A new formula for calculation of the fractional synthesis rate is derived with the alternative assumption that the protein synthesis rate is stimulated by an amount proportional to the change in the intracellular concentration of the infused amino acid. The alternative formula is: where EB and EF are the enrichments of bound and free amino acid, respectively (atom per cent excess), and C=1-(EF/EI), where EI is the enrichment of the infusate. This approach defines the lowest possible value for the fractional synthesis rate. The traditional equation gives a maximal value for the fractional synthesis rate. 3. When data from the literature are considered, the fractional synthesis rate of muscle protein as calculated by the constant infusion technique falls between the values of fractional synthesis rate calculated by the two flooding dose formulae when leucine is the tracer, suggesting that a flooding dose of leucine exerts a stimulatory effect on the rate of protein synthesis, but that the increase is not as great as the increase in the intracellular concentration of leucine. 4. The precision of the formula for the calculation of fractional synthesis rate is limited by the accuracy of the underlying assumptions regarding the effect of the flooding dose on the fractional synthesis rate. At present, the best approach would appear to be the use of both equations to calculate the upper and lower bounds of the true fractional synthesis rate.

Comparison of Constant Infusion and Flooding Dose Techniques to Measure Muscle Protein Synthesis Rate in Dogs

1992 ◽  
Vol 122 (4) ◽  
pp. 878-887 ◽  
Author(s):  
Farook Jahoor ◽  
Xiao-Jun Zhang ◽  
Hidefumi Baba ◽  
Yoichi Sakurai ◽  
Robert R. Wolfe
Keyword(s):  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Constant Infusion ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Muscle Protein Synthesis Rate

scholarly journals The effects of fasting or hypoxia on rates of protein synthesis in vivo in subcellular fractions of rat heart and gastrocnemius muscle

1989 ◽  
Vol 257 (2) ◽  
pp. 519-527 ◽  
Author(s):  
V R Preedy ◽  
P H Sugden
Keyword(s):  
Protein Synthesis ◽  
Subcellular Fractions ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Tissue Protein ◽  
Moderate Hypoxia ◽  
Hypoxic Conditions ◽  
Rate Ratios ◽  
H Protein

We measured rates of protein synthesis in vivo in subcellular fractions (soluble, myofibrillar and stromal fractions) of the heart and the gastrocnemius from rats after fasting or under hypoxic conditions (i.e. atmospheres containing 5% or 10% O2). Such interventions are known to inhibit protein synthesis under some circumstances. The recovery of tissue protein after fractionation was 80-100%. The proportions of protein present in the soluble and stromal fractions were different in the two muscles. The rates of protein synthesis in the myofibrillar and stromal fractions were less than those for total mixed tissue protein, whereas the rate for soluble protein was greater. Both fasting and moderate hypoxia (10% O2 for 24 h) inhibited protein synthesis in the gastrocnemius. In this tissue, the synthesis of the myofibrillar fraction was apparently the most sensitive to inhibition, and this resulted in some significant increases in the soluble-fraction/myofibrillar-fraction protein-synthesis rate ratios. In the heart, fasting inhibited protein synthesis, but moderate hypoxia (10% O2 for 24 h) did not. The rate of protein synthesis in the cardiac myofibrillar fraction was again more sensitive to fasting than were the rates in the other fractions, but it was not as sensitive as that in the gastrocnemius. Under severely hypoxic conditions (5% O2 for 1 or 2 h), protein synthesis was decreased in all fractions in both tissues. These results suggest that the rates of protein synthesis in these relatively crude subcellular fractions vary.

Effects of exercise on protein synthesis and myosin heavy chain gene expression in hypothyroid rats

1994 ◽  
Vol 267 (1) ◽  
pp. E63-E67
Author(s):  
H. L. Katzeff ◽  
K. M. Ojamaa ◽  
I. Klein
Keyword(s):  
Gene Expression ◽  
Protein Synthesis ◽  
Thyroid Hormones ◽  
Cardiac Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscle Growth ◽  
Heart Weight ◽  
Synthesis Rate ◽  
Protein Synthesis Rate

Hypothyroidism suppresses muscle growth and alters myosin heavy chain (MHC) gene expression. To study the role of thyroid hormones in exercise-induced muscle growth and protein synthesis, we measured skeletal and cardiac muscle protein synthesis and MHC gene expression in hypothyroid rats allowed to exercise voluntarily. Female Sprague-Dawley rats (200-210 g) were separated into four groups for 28 days of treatment: control, hypothyroid (TX), hypothyroid plus running-wheel exercise (TX+Ex), and hypothyroid plus 25% overfed (TX+OF). Fractional protein synthesis rates (% incorporation/day) were measured using [3H]phenylalanine incorporation 10 min postinjection. The heart weight-to-body weight ratios of the TX and the TX+OF groups showed marked cardiac atrophy over the 28-day period (2.76 +/- 0.12 and 2.50 +/- 0.22 vs. 3.37 +/- 0.18 mg/g, respectively; P < 0.01). However, the TX+Ex group prevented heart, gastrocnemius, and soleus muscle atrophy over the same time period. Heart, gastrocnemius, and soleus muscles had markedly suppressed protein synthesis rates in the TX and TX+OF groups vs. the euthyroid controls (mean fall -72%; P < 0.01, analysis of variance). However, exercise increased protein synthesis rate by 50% (P < 0.05) compared with TX alone in all three muscle groups. Exercise did not modify hypothyroid-induced alterations of cardiac myosin isoform expression. Exercise-mediated effects on skeletal and cardiac muscle growth but not cardiac MHC gene expression appear to be independent of thyroid hormones.

Protein synthesis rates in atrophied gastrocnemius muscles after limb immobilization

1981 ◽  
Vol 51 (1) ◽  
pp. 73-77 ◽  
Author(s):  
K. R. Tucker ◽  
M. J. Seider ◽  
F. W. Booth
Keyword(s):  
Protein Synthesis ◽  
Gastrocnemius Muscle ◽  
Weight Lifting ◽  
Constant Infusion ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Fractional Rate ◽  
Gastrocnemius Muscles ◽  
Infusion Technique ◽  
Limb Immobilization

Fractional rates of protein synthesis in rats were determined by the constant-infusion technique. Rates of protein synthesis in the gastrocnemius muscle were significantly reduced from control values throughout a 7-day period of hindlimb immobilization and 1) significantly increased to control values during the first 6 h following the 7-day period of hindlimb immobilization; 2) remained at control values for the next 2 days; and 3) then significantly increased to about twice control values on the 4th day following immobilization. Exercise of sufficient duration and/or intensity affected a further increase in the protein synthesis rate during recovery from atrophy. For example, running on a motor-driven treadmill 1 h daily for 3 days after ending limb immobilization resulted in a significant increase in the fractional rate of protein synthesis in the gastrocnemius muscle on the 2nd day following immobilization. Also, weight lifting for 200 s on the 2nd day of protein synthesis in the gastrocnemius muscle. Thus increased usage of atrophied muscle was followed by an increased rate of protein synthesis.

scholarly journals Tissue protein synthesis and nucleic acid concentrations in steers treated with somatotropin

1989 ◽  
Vol 62 (3) ◽  
pp. 657-671 ◽  
Author(s):  
J. H. Eisemann ◽  
A. C. Hammond ◽  
T. S. Rumsey
Keyword(s):  
Protein Synthesis ◽  
Small Intestine ◽  
Nucleic Acid ◽  
Specific Radioactivity ◽  
Whole Body ◽  
Tissue Homogenate ◽  
Synthesis Rate ◽  
Body Protein ◽  
Tissue Protein ◽  
Tissue Protein Synthesis

The effect of injection with bovine somatotropin (bST) on the fractional rate of protein synthesis (FSR) in tissues of beef steers was studied using a continuous infusion of [1-14C]leucine. Minimum and maximum FSR were calculated from free leucine specific radioactivity (SRA) in plasma or tissue homogenate respectively. Tissue nucleic acid concentrations were also quantified. Tissue samples were obtained from several muscles, sections of the small intestine and liver. In response to bST, both minimum and maximum FSR increased in muscle but not liver or intestinal tissues. Absolute synthesis rate increased in several muscles and small intestine tissues. Treatment with bST increased the relative SRA of protein-bound leucine in muscles compared with liver; increased the amount of protein synthesis per unit empty body-weight (EBW) in most muscles; and increased weight of small intestine relative to EBW, suggesting a differential response between liver and the other tissues measured. Compositional changes in response to bST occurred only in muscles. DNA concentration increased while protein:DNA decreased in the gastrocnemius muscle and RNA:DNA increased in the longissimus dorsi. The maximum percentage contribution of tissue protein synthesis to whole-body protein synthesis was 12·6, 25·7 and 20·5, and 13·0, 29·4 and 25·8 for liver, muscle, and small intestine in placebo-treated and bST-injected steers respectively.

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