scholarly journals Dietary lysine deficiency greatly affects muscle and liver protein turnover in growing chickens

1996 ◽  
Vol 75 (6) ◽  
pp. 853-865 ◽  
Author(s):  
S. Tesseraud ◽  
R. Peresson ◽  
J. Lopes ◽  
A.M. Chagneau
Keyword(s):  
Protein Synthesis ◽  
Protein Turnover ◽  
Pectoralis Major Muscle ◽  
Pectoralis Major ◽  
Translational Efficiency ◽  
Liver Protein ◽  
Deficient Diet ◽  
Principal Mechanism ◽  
Tissue Protein

We analysed the respective influences of age and lysine deficiency on skeletal muscle and liver protein turnover. Growing male broilers were fed ad libirum on isoenergetic diets containing 2OO g crude protein/kg which varied in their lysine content (7·7 or 10·1 g/kg). Fractional rates of protein synthesis (FSR) were measured in vivo in the liver and the pectoralis major muscle of 2-, 3- and 4-week-old chickens (flooding dose of l-[143H]phenylalanine). Fractional rates of proteolysis (FBR) were estimated for the same tissues as the difference between synthesis and growth. Over the 2-week period liver FSR and FBR were unchanged, whereas muscle FSR decreased with age. This developmental decline was related to the lower capacity for protein synthesis (Cs) without any modifications of the translational efficiency. Whatever the age, lysine deficiency resulted in significant decreases in body weight, tissue protein content and tissue protein deposition, apparently because of reduced amounts of proteins synthesized. We recorded a difference in the response of the two tissues to lysine deficiency, the pectoralis major being more sensitive than the liver. When comparing birds of the same age, liver FSR and FBR were not modified by the diet, where as muscle FSR, Cs and FBR were higher in chicks fed on a lysinc-deficient diet than in the controls. Conversely, when chicks of similar weights were compared, the main effect of the dietary deficiency was an increase in muscle FBR. The results suggest that lysine deficiency not only delayed chick development so that protein turnover was affected, but also induced greater changes in metabolism. Thus, the principal mechanism whereby muscle mass decreased appeared to be a change in FBR.

Regulation of hepatic protein synthesis in chronic inflammation and sepsis

1992 ◽  
Vol 262 (2) ◽  
pp. C445-C452 ◽  
Author(s):  
T. C. Vary ◽  
S. R. Kimball
Keyword(s):  
Protein Synthesis ◽  
Sterile Inflammation ◽  
Chain Elongation ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Translational Efficiency ◽  
Liver Protein ◽  
Ribosomal Subunits ◽  
Hepatic Protein Synthesis

The regulation of protein synthesis was determined in livers from control, sterile inflammatory, and septic animals. Total liver protein was increased in both sterile inflammation and sepsis. The rate of protein synthesis in vivo was measured by the incorporation of [3H]phenylalanine into liver proteins in a chronic (5 day) intra-abdominal abscess model. Both sterile inflammation and sepsis increased total hepatic protein synthesis approximately twofold. Perfused liver studies demonstrated that the increased protein synthesis rate in vivo resulted from a stimulation in the synthesis of both secreted and nonsecreted proteins. The total hepatic RNA content was increased 40% only in sterile inflammation, whereas the translational efficiency was increased twofold only in sepsis. The increase in translational efficiency was accompanied by decreases in the amount of free 40S and 60S ribosomal subunits in sepsis. Rates of peptide-chain elongation in vivo were increased 40% in both sterile inflammation and sepsis. These results demonstrate that sepsis induces changes in the regulation of hepatic protein synthesis that are independent of the general inflammatory response. In sterile inflammation, the increase in protein synthesis occurs by a combination of increased capacity and translational efficiency, while in sepsis, the mechanism responsible for accelerated protein synthesis is an increased translational efficiency.

scholarly journals Altered protein kinetics in vivo after single-limb burn injury

1984 ◽  
Vol 223 (3) ◽  
pp. 747-753 ◽  
Author(s):  
R E Shangraw ◽  
J Turinsky
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Protein Turnover ◽  
Burn Injury ◽  
Whole Body ◽  
Liver Protein ◽  
Protein Kinetics ◽  
Tissue Protein ◽  
Systemic Factors ◽  
Control Protein

Recovery from burn injury is associated with stimulated whole-body protein turnover. Since skeletal muscle and liver are the tissues most likely to influence whole-body measurements, we studied protein kinetics in soleus and plantaris muscles as well as liver 3 days after a 3 s burn on one hindlimb of the rat. Muscles from both the burned and unburned limbs of burned rats were compared with those of uninjured controls to distinguish between local and systemic factors involved. The following measurements were performed: (1) fractional growth rate of the tissue protein pool, determined from tissue protein content on days 2, 3 and 4; (2) fractional protein-synthetic rate, measured by [14C]tyrosine constant infusion on day 3; (3) fractional protein-degradation rate, calculated from the difference between the rates of protein synthesis and growth. Protein growth by soleus and plantaris muscles of control rats and unburned limb of burned rats was not paralleled by those in the burned limb, which showed progressive atrophy between 2 and 4 days post-burn (P less than 0.005). Protein synthesis by soleus but not plantaris muscle in the unburned limb of burned rats was enhanced by 62% (P less than 0.04) above control. Protein synthesis by burned-limb soleus and plantaris muscles was elevated by 114% (P less than 0.001) and 67% (P less than 0.02) respectively above control. Protein degradation by both soleus and plantaris muscles in the unburned limb of burned rats did not differ from control. In contrast, that of soleus and plantaris muscles in the burned limb was stimulated by 230% (P less than 0.001) and 164% (P less than 0.001) respectively compared with controls. Protein turnover of soleus muscles in both control and burned rats was more rapid than in corresponding plantaris muscles. Liver protein mass exhibited steady growth in control rats, but remained unchanged in burned animals between 2 and 4 days post-burn. Liver protein synthesis in burned rats was elevated by 56% (P less than 0.01) and protein breakdown was stimulated by 61% (P less than 0.002) above those of controls. The data indicate that both local and systemic factors influence tissue protein turnover in animals recovering from a single-hindlimb scald.

Protein turnover in skeletal muscle of suckling rats

1989 ◽  
Vol 257 (5) ◽  
pp. R1141-R1146 ◽  
Author(s):  
T. A. Davis ◽  
M. L. Fiorotto ◽  
H. V. Nguyen ◽  
P. J. Reeds
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Protein Turnover ◽  
Weight Bearing ◽  
Translational Efficiency ◽  
Suckling Period ◽  
Synthetic Capacity ◽  
Anterior Tibialis ◽  
Synthetic Efficiency

To determine the normal changes in protein turnover of skeletal muscle in vivo during the suckling period of rats, protein synthesis was measured in soleus, plantaris, anterior tibialis, and extensor digitorum longus (EDL) muscles of 1- to 28-day-old rats using a flooding dose of L-[4-3H]phenylalanine. Protein mass of hind-limb muscles increased nearly 100-fold, and RNA increased approximately 20-fold between 1 and 28 days of age. The total amount of protein synthesized per day increased 34-fold. Fractional protein synthesis rates (Ks) decreased two- to threefold between 1 and 28 days postpartum as a result of a decrease in protein synthetic capacity (RNA/protein). Protein synthetic efficiency (total protein synthesized/RNA) increased during this period. Ks were similar among the four muscles at 1-10 days. At 16 days, Ks increased in soleus and plantaris as a result of increases in protein synthetic efficiency; Ks did not increase in anterior tibialis and EDL. These data suggest that, during the suckling period, protein synthetic capacity in skeletal muscles of rats declines, while protein synthetic efficiency increases. The increase in translational efficiency occurred earlier in weight-bearing muscles (soleus, plantaris) than in non-weight-bearing muscles (anterior tibialis and EDL) and was associated with the appearance of mobility.

scholarly journals An isotopic method for measurement of muscle protein synthesis and degradation in vivo

1987 ◽  
Vol 245 (1) ◽  
pp. 223-228 ◽  
Author(s):  
E J Barrett ◽  
J H Revkin ◽  
L H Young ◽  
B L Zaret ◽  
R Jacob ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Specific Radioactivity ◽  
Molar Ratio ◽  
Tissue Blood Flow ◽  
Tissue Protein ◽  
Venous Plasma

In eight anaesthetized post-absorptive dogs we measured the concentration and specific radioactivity of phenylalanine and leucine in arterial and femoral-venous plasma, together with hindlimb flow during a continuous infusion of L-[ring-2,6-3H]phenylalanine and [1-14C]leucine. The femoral-venous plasma concentration was greater than arterial for both phenylalanine and leucine (P less than 0.05 for each). Despite net amino acid release there was a significant removal of both labelled phenylalanine and labelled leucine. Consequently, a significant dilution of specific radioactivity was observed between artery and vein for both radio-tracers. The uptake of leucine from the arterial circulation by the hindlimb exceeded by 2.6-fold that of phenylalanine; the measured molar ratio of leucine to phenylalanine in hindlimb muscle protein averaged 2.4 +/- 0.1. Since phenylalanine is neither synthesized nor degraded by muscle tissue, the measured removal of tracer and the dilution of tracer specific radioactivity across the hindlimb can be used to estimate rates of phenylalanine incorporation into, and release from, tissue protein. The estimated rate of protein synthesis by hindlimb averaged 644 +/- 250 nmol of phenylalanine/min. This was exceeded by the rate of tissue protein degradation (987 +/- 285 nmol of phenylalanine/min). The present results demonstrate that the dilution of the specific radioactivity of labelled phenylalanine can be readily measured across dog hindlimb. This measurement, coupled with an estimate of tissue blood flow, can provide a readily measured, non-destructive, method for estimation of protein turnover in specific muscle beds in vivo. Measurements can be made repeatedly over time in a single experiment, allowing the study of factors which regulate protein turnover. The method developed here in dogs can be readily extended to clinical studies.

Respiratory energy requirements and rate of protein turnover in vivo determined by the use of an inhibitor of protein synthesis and a probe to assess its effect

1994 ◽  
Vol 92 (4) ◽  
pp. 585-594 ◽  
Author(s):  
T. J. Bouma ◽  
R. De Visser ◽  
J. H. J. A. Janssen ◽  
M. J. De Kock ◽  
P H. Van Leeuwen ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Protein Turnover ◽  
Energy Requirements ◽  
Inhibitor Of Protein Synthesis

scholarly journals Amino acid regulation of synthesis of ribonucleic acid and protein in the liver of rats

1971 ◽  
Vol 124 (2) ◽  
pp. 385-392 ◽  
Author(s):  
R. W. Wannemacher ◽  
C. F. Wannemacher ◽  
M. B. Yatvin
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Free Amino Acids ◽  
Free Amino ◽  
Cellular Protein ◽  
Deficient Diet ◽  
Cellular Protein Content ◽  
Regulate Protein

Weanling (23-day-old) rats were fed on either a low-protein diet (6% casein) or a diet containing an adequate amount of protein (18% casein) for 28 days. Hepatic cells from animals fed on the deficient diet were characterized by markedly lower concentrations of protein and RNA in all cellular fractions as compared with cells from control rats. The bound rRNA fraction was decreased to the greatest degree, whereas the free ribosomal concentrations were only slightly less than in control animals. A good correlation was observed between the rate of hepatic protein synthesis in vivo and the cellular protein content of the liver. Rates of protein synthesis both in vivo and in vitro were directly correlated with the hepatic concentration of individual free amino acids that are essential for protein synthesis. The decreased protein-synthetic ability of the ribosomes from the liver of protein-deprived rats was related to a decrease in the number of active ribosomes and heavy polyribosomes. The lower ribosomal content of the hepatocytes was correlated with the decreased concentration of essential free amino acids. In the protein-deprived rats, the rate of accumulation of newly synthesized cytoplasmic rRNA was markedly decreased compared with control animals. From these results it was concluded that amino acids regulate protein synthesis (1) by affecting the number of ribosomes that actively synthesize protein and (2) by inhibiting the rate of synthesis of new ribosomes. Both of these processes may involve the synthesis of proteins with a rapid rate of turnover.

scholarly journals The effect of protein depletion and repletion on muscle-protein turnover in the chick

1981 ◽  
Vol 194 (3) ◽  
pp. 811-819 ◽  
Author(s):  
M L MacDonald ◽  
R W Swick
Keyword(s):  
Protein Synthesis ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Control Diet ◽  
Breast Muscle ◽  
Synthesis Rate ◽  
Protein Depletion ◽  
Protein Mass ◽  
Fractional Rate

Rates of growth and protein turnover in the breast muscle of young chicks were measured in order to assess the roles of protein synthesis and degradation in the regulation of muscle mass. Rates of protein synthesis were measured in vivo by injecting a massive dose of L-[1-14C]valine, and rates of protein degradation were estimated as the difference between the synthesis rate and the growth rate of muscle protein. In chicks fed on a control diet for up to 7 weeks of age, the fractional rate of synthesis decreased from 1 to 2 weeks of age and then changed insignificantly from 2 to 7 weeks of age, whereas DNA activity was constant for 1 to 7 weeks. When 4-week-old chicks were fed on a protein-free diet for 17 days, the total amount of breast-muscle protein synthesized and degraded per day and the amount of protein synthesized per unit of DNA decreased. Protein was lost owing to a greater decrease in the rate of protein synthesis, as a result of the loss of RNA and a lowered RNA activity. When depleted chicks were re-fed the control diet, rapid growth was achieved by a doubling of the fractional synthesis rate by 2 days. Initially, this was a result of increased RNA activity; by 5 days, the RNA/DNA ratio also increased. There was no evidence of a decrease in the fractional degradation rate during re-feeding. These results indicate that dietary-protein depletion and repletion cause changes in breast-muscle protein mass primarily through changes in the rate of protein synthesis.

Fiber-type composition of nine rat muscles. II. Relationship to protein turnover

1989 ◽  
Vol 257 (6) ◽  
pp. E828-E832 ◽  
Author(s):  
P. J. Garlick ◽  
C. A. Maltin ◽  
A. G. Baillie ◽  
M. I. Delday ◽  
D. A. Grubb
Keyword(s):  
Protein Synthesis ◽  
Regression Analysis ◽  
Protein Turnover ◽  
Fiber Type ◽  
Female Rats ◽  
Protein Breakdown ◽  
Fiber Type Composition ◽  
Type Composition ◽  
Age Regression

Rates of protein synthesis in vivo and fiber-type composition were measured in nine limb muscles of female rats at ages ranging from weaning to 1 yr. In all muscles, there was a decline in protein synthesis with increasing age, mostly as a result of a fall in the RNA content. Rates of protein breakdown and growth were determined in six muscles and these also declined with age. Regression analysis of the data for all ages showed that protein synthesis was correlated with the content of slow oxidative fibers but not with the relative proportions of fast glycolytic to fast oxidative glycolytic fibers.

scholarly journals Key role of l-alanine in the control of hepatic protein synthesis

1987 ◽  
Vol 241 (2) ◽  
pp. 491-498 ◽  
Author(s):  
D Pérez-Sala ◽  
R Parrilla ◽  
M S Ayuso
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Physiological Role ◽  
Chain Elongation ◽  
Liver Protein ◽  
Isolated Liver Cells ◽  
Metabolic Transformation ◽  
Hepatic Protein Synthesis

We investigated the effects of administration of single amino acids to starved rats on the regulation of protein synthesis in the liver. Of all the amino acids tested, only alanine, ornithine and proline promoted statistically significant increases in the extent of hepatic polyribosome aggregation. The most effective of these was alanine, whose effect of promoting polyribosomal aggregation was accompanied by a decrease in the polypeptide-chain elongation time. The following observations indicate that alanine plays an important physiological role in the regulation of hepatic protein synthesis. Alanine was the amino acid showing the largest decrease in hepatic content in the transition from high (fed) to low (starved) rates of protein synthesis. The administration of glucose or pyruvate is also effective in increasing liver protein synthesis in starved rats, and their effects were accompanied by an increased hepatic alanine content. An increase in hepatic ornithine content does not lead to an increased protein synthesis, unless it is accompanied by an increase of alanine. The effect of alanine is observed either in vivo, in rats pretreated with cycloserine to prevent its transamination, or in isolated liver cells under conditions in which its metabolic transformation is fully impeded.

scholarly journals Polyribosomes in isolated liver cells. Preparative procedures, effects of incubation and correlation with protein synthesis

1980 ◽  
Vol 186 (1) ◽  
pp. 35-45 ◽  
Author(s):  
A J Dickson ◽  
C I Pogson
Keyword(s):  
Protein Synthesis ◽  
Rat Liver ◽  
Isolated Hepatocytes ◽  
Liver Cells ◽  
Liver Protein ◽  
Isolated Cells ◽  
Isolated Liver Cells ◽  
Rat Liver Cells ◽  
Isolated Liver

Methods have been derived which permit the isolation of undergraded polyribosomes from isolated rat liver cells. Under the conditions used the polyribosome profile of hepatocytes immediately after isolation was essentially identical with that from intact liver. However, during incubation of cells in complex physiological media there was a progressive dissociation of polyribosomes. The addition of a variety of factors that produce reaggregation of polyribosomes in rat liver in vivo did not prevent dissociation during cell incubations. Although large polyribosomes were lost most rapidly, the albumin-synthesizing capacity of isolated cells was not selectively lost when compared with total protein synthesis. The significance of these results for the use of isolated hepatocytes in the study of liver protein synthesis is discussed.

Sign in / Sign up

Export Citation Format

Share Document