scholarly journals The effects of energy source and tryptophan on the rate of protein synthesis and on hormones of the entero-insular axis in the piglet

1994 ◽  
Vol 71 (5) ◽  
pp. 661-674 ◽  
Author(s):  
A. A. Ponter ◽  
N. O. Cortamira ◽  
B. Seve ◽  
D. N. Salter ◽  
L. M. Morgan
Keyword(s):  
Energy Source ◽  
Protein Synthesis ◽  
Plasma Insulin ◽  
Gastric Inhibitory Polypeptide ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Jejunal Mucosa ◽  
Adequate Diet ◽  
Quadratic Effects

The present experiment was designed to study the influence of dietary energy source (fat or carbohydrate) and tryptophan (TRP) on protein synthesis and plasma insulin concentrations in the piglet. Six dietary regimens, based on either a high-fat (F) or a high-carbohydrate (C) diet with three levels of TRP (deficient, 1; adequate, 2; excess, 3), were used. Fractional protein synthesis rate (ks; % per d) was measured in the liver, Longissimus dorsi (LD), Semitendinosus (ST), skin, femur, brain, pancreas, stomach, mucosa of the duodenum and jejunum, and the whole body, using a‘flooding dose’of 3H-phenylalanine. Mean integrated insulin, gastric inhibitory polypeptide (GIP) and glucose concentrations were higher after the C diets compared with the F diets, TRP supplementation globally augmented ks linearly in the liver, ST, skin and whole body, while it had quadratic effects in the LD (ks highest in the TRP-adequate diet groups) and jejunal mucosa (ks lowest in the TRP-adequate diet groups). Pancreatic ks was increased by TRP addition up to a plateau. ks was highest after the F diets in the digestive tissues while in the skin and LD ks was highest after the C diets. Fasting concentrations of gluconeogenic amino acids were lower (and urea higher) with the F than the C diets, suggesting their use as precursors for glucose synthesis. In conclusion, we have confirmed the depressive effects of TRP deficiency on ks, RNA activity and growth. We could not establish a relationship between plasma insulin and muscle ks. This may be related to the way in which we manipulated plasma insulin concentrations.

scholarly journals Effect of dietary tryptophan on muscle, liver and whole-body protein synthesis in weaned piglets: relationship to plasma insulin

1991 ◽  
Vol 66 (3) ◽  
pp. 423-435 ◽  
Author(s):  
N. O. Cortamira ◽  
B. Seve ◽  
Y. Lebreton ◽  
P. Ganier
Keyword(s):  
Protein Synthesis ◽  
Growth Performance ◽  
Plasma Insulin ◽  
Live Weight ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Liver Protein ◽  
Deficient Diet ◽  
Body Protein

Two experiments were carried out with piglets, 3–5 kg live weight, to evaluate the effects of feeding a tryptophan (TRP)-deficient diet for 2 weeks on protein synthesis rates measured in vivo 2 h after a meal. In the first experiment on twenty piglets fed on 250 g protein/kg diets, TRP deficiency (0.77 g/16 g nitrogen) as compared with adequacy (1.17 g/16 g N) significantly decreased feed intake, growth performance and fractional protein synthesis rates (FSR), without variation of RNA in longissimus dorsi (LD) and with parallel increases in RNA in semitendinosus (ST) muscle and liver. In the second experiment thirty-two piglets were tube-fed deficient and adequate diets at the two feeding levels (LF) previously achieved. Both TRP and LF significantly increased growth performance and FSR, but not RNA, in LD and ST muscle, with a trend to a synergy between the two factors (TRP x LF interaction). In another muscle, trapezius (TR), the same interaction was only apparent in RNA content. Among the three muscles it was in LD that FSR was the most responsive to dietary TRP (significant muscle x TRP interaction). In the liver the TRP x LF interaction on FSR and not RNA was the major significant effect, indicating that higher TRP and higher LF were both required to get the maximum protein synthesis rate. At 30 min after a meal the same significant interaction effect was shown on plasma glucose, whilst the higher LF increased plasma insulin with both diets. After a further 30 min the appearance of a similar significant effect of the TRP x LF interaction on plasma insulin resulted from its abatement when the deficient diet had been fed at high LF. These results suggest that dietary TRP deficiency decreased muscle and liver protein synthesis rates in relation to a decrease in the post-prandial release of insulin following a decreased rate of nutrient absorption.

scholarly journals Glutamine supplementation does not improve protein synthesis rate by the jejunal mucosa of the malnourished rat

2009 ◽  
Vol 29 (8) ◽  
pp. 596-601 ◽  
Author(s):  
Andrea Ferreira S. Tannus ◽  
Dominique Darmaun ◽  
Durval F. Ribas ◽  
José Eduardo D. Oliveira ◽  
Julio Sergio Marchini
Keyword(s):  
Protein Synthesis ◽  
Glutamine Supplementation ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Jejunal Mucosa

scholarly journals Increased intestinal protein synthesis during sepsis and following the administration of tumour necrosis factor α or interleukin-1 α

1992 ◽  
Vol 286 (2) ◽  
pp. 585-589 ◽  
Author(s):  
D von Allmen ◽  
P O Hasselgren ◽  
T Higashiguchi ◽  
J Frederick ◽  
O Zamir ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Interleukin 1 ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Jejunal Mucosa ◽  
Ileal Mucosa ◽  
Intestinal Protein ◽  
Necrosis Factor

The influence of sepsis on intestinal protein synthesis was studied in rats. Sepsis was induced by caecal ligation and puncture (CLP); control rats were sham-operated. Protein synthesis was measured in vivo in the jejunum and ileum following a flooding dose of [14C]leucine. At 8 h after CLP the protein synthesis rate was increased by approx. 15% in jejunal mucosa, and at 16 h after CLP, the protein synthesis rate was increased by 50-60% in the mucosa and seromuscular layer of both jejunum and ileum. In a second series of experiments, rats were treated with recombinant tumour necrosis factor alpha (rTNF alpha) or recombinant interleukin-1 alpha (rIL-1 alpha) administered at a total dose of 300 micrograms/kg body weight over 16 h. Control rats received corresponding volumes of solvent. Treatment with rTNF alpha resulted in an approx. 25% increase in mucosal protein synthesis in jejunum. Following treatment with rIL-1 alpha, protein synthesis increased by 25% in jejunal mucosa and almost doubled in ileal mucosa. The results suggest that sepsis stimulates intestinal protein synthesis and that this response may, at least in part, be mediated by TNF and/or IL-1.

Effect of spaceflight on human protein metabolism

1993 ◽  
Vol 264 (5) ◽  
pp. E824-E828 ◽  
Author(s):  
T. P. Stein ◽  
M. J. Leskiw ◽  
M. D. Schluter
Keyword(s):  
Protein Synthesis ◽  
Nitrogen Balance ◽  
Protein Metabolism ◽  
Space Shuttle ◽  
Single Pulse ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Body Protein ◽  
Space Shuttle Columbia

Nitrogen balance and the whole body protein synthesis rate were measured before, during, and after a 9.5-day spaceflight mission on the space shuttle Columbia. Protein synthesis was measured by the single-pulse [15N]glycine method. Determinations were made 56, 26, and 18 days preflight, on flight days 2 and 8, and on days 0, 6, 14, and 45 postflight. We conclude that nitrogen balance was decreased during spaceflight. The decrease in nitrogen balance was greatest on the 1st day when food intake was reduced and again toward the end of the mission. An approximately 30% increase in protein synthesis above the preflight baseline was found for flight day 8 for all 6 subjects (P < 0.05), indicating that the astronauts showed a stress response to spaceflight.

scholarly journals Increased plasma Gln and Leu Raand inappropriately low muscle protein synthesis rate in AIDS wasting

1998 ◽  
Vol 275 (4) ◽  
pp. E577-E583 ◽  
Author(s):  
Kevin E. Yarasheski ◽  
Jeffrey J. Zachwieja ◽  
Jennifer Gischler ◽  
Jan Crowley ◽  
Mary M. Horgan ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Asymptomatic Group ◽  
Body Protein ◽  
Asymptomatic Subjects ◽  
Muscle Protein Synthesis Rate

Muscle protein wasting occurs in human immunodeficiency virus (HIV)-infected individuals and is often the initial indication of acquired immunodeficiency syndrome (AIDS). Little is known about the alterations in muscle protein metabolism that occur with HIV infection. Nine subjects with AIDS wasting (CD4 < 200/mm3), chronic stable opportunistic infections (OI), and ≥10% weight loss, fourteen HIV-infected men and one woman (CD4 > 200/mm3) without wasting or OI (asymptomatic), and six HIV-seronegative lean men (control) received a constant intravenous infusion of [1-13C]leucine (Leu) and [2-15N]glutamine (Gln). Plasma Leu and Gln rate of appearance (Ra), whole body Leu turnover, disposal and oxidation rates, and [13C]Leu incorporation rate into mixed muscle protein were assessed. Total body muscle mass/fat-free mass was greater in controls (53%) than in AIDS wasting (43%; P = 0.04). Fasting whole body proteolysis and synthesis rates were increased above control in the HIV+ asymptomatic group and in the AIDS-wasting group ( P = 0.009). Whole body Leu oxidation rate was greater in the HIV+ asymptomatic group than in the control and AIDS-wasting groups ( P < 0.05). Fasting mixed muscle protein synthesis rate was increased in the asymptomatic subjects (0.048%/h; P = 0.01) but was similar in AIDS-wasting and control subjects (0.035 vs. 0.037%/h). Plasma Gln Rawas increased in AIDS-wasting subjects but was similar in control and HIV+ asymptomatic subjects ( P < 0.001). These findings suggest that AIDS wasting results from 1) a preferential reduction in muscle protein, 2) a failure to sustain an elevated rate of mixed muscle protein synthesis while whole body protein synthesis is increased, and 3) a significant increase in Gln release into the circulation, probably from muscle. Several interesting explanations for the increased Gln Rain AIDS wasting exist.

Adult Trichostrongylus colubriformis infection did not affect protein synthesis rate in whole-body, intestinal, hepatic and skeletal muscle tissues of lambs fed fresh Lucerne (Medicago sativa)

2007 ◽  
Vol 87 (3) ◽  
pp. 315-325 ◽  
Author(s):  
E. N. Bermingham ◽  
W. C. McNabb ◽  
I. A. Sutherland ◽  
B. R. Sinclair ◽  
B. P. Treloar ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Medicago Sativa ◽  
Parasitic Infection ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Lymphoid Tissues ◽  
Trichostrongylus Colubriformis ◽  
Body Protein

The effects of an established Trichostrongylus colubriformis infection on the whole-body and fractional protein synthesis rates in the small intestine, liver, lymphoid tissues, skeletal muscle and skin were determined in lambs fed fresh Lucerne (Medicago sativa; 800 g DM d-1) on day 48 post-infection. Lambs were dosed with 6000 L3 T. colubriformis larvae for 6 d (n = 5) or kept as parasite-free controls (n = 6). On day 45, the lambs received a bolus injection of deuterated water to measure the size of the whole-body water pool. On day 48, the lambs were continuously infused with [3, 4-3H]-valine into the jugular vein and [1-13C]-valine in the abomasum for 8 h. During the infusion, mesenteric artery blood and terminal tissue samples were collected for measuring the isotopic activity of plasma water, plasma valine, intra cellular valine and protein-bound valine. Intestinal worm numbers on day 48 were higher (P < 0.001) in the infected lambs, however, there was no effect (P > 0.10) of parasitic infection on feed intake, liveweight gain, whole-body protein synthesis and fractional protein synthesis of most tissues. Key words: Parasite infection, protein synthesis, lambs

scholarly journals Modulation of the gut microbiota with antibiotic treatment suppresses whole body urea production in neonatal pigs

2013 ◽  
Vol 304 (3) ◽  
pp. G300-G310 ◽  
Author(s):  
Patrycja Puiman ◽  
Barbara Stoll ◽  
Lars Mølbak ◽  
Adrianus de Bruijn ◽  
Henk Schierbeek ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Gut Microbiota ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Urea Synthesis ◽  
Plasma Urea ◽  
Body Protein ◽  
Neonatal Pigs

We examined whether changes in the gut microbiota induced by clinically relevant interventions would impact the bioavailability of dietary amino acids in neonates. We tested the hypothesis that modulation of the gut microbiota in neonatal pigs receiving no treatment (control), intravenously administered antibiotics, or probiotics affects whole body nitrogen and amino acid turnover. We quantified whole body urea kinetics, threonine fluxes, and threonine disposal into protein, oxidation, and tissue protein synthesis with stable isotope techniques. Compared with controls, antibiotics reduced the number and diversity of bacterial species in the distal small intestine (SI) and colon. Antibiotics decreased plasma urea concentrations via decreased urea synthesis. Antibiotics elevated threonine plasma concentrations and turnover, as well as whole body protein synthesis and proteolysis. Antibiotics decreased protein synthesis rate in the proximal SI and liver but did not affect the distal SI, colon, or muscle. Probiotics induced a bifidogenic microbiota and decreased plasma urea concentrations but did not affect whole body threonine or protein metabolism. Probiotics decreased protein synthesis in the proximal SI but not in other tissues. In conclusion, modulation of the gut microbiota by antibiotics and probiotics reduced hepatic ureagenesis and intestinal protein synthesis, but neither altered whole body net threonine balance. These findings suggest that changes in amino acid and nitrogen metabolism resulting from antibiotic- or probiotic-induced shifts in the microbiota are localized to the gut and liver and have limited impact on whole body growth and anabolism in neonatal piglets.

Effect of growth hormone and resistance exercise on muscle growth in young men

1992 ◽  
Vol 262 (3) ◽  
pp. E261-E267 ◽  
Author(s):  
K. E. Yarasheski ◽  
J. A. Campbell ◽  
K. Smith ◽  
M. J. Rennie ◽  
J. O. Holloszy ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Resistance Training ◽  
Resistance Exercise ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Treated Group ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Body Protein

The purpose of this study was to determine whether growth hormone (GH) administration enhances the muscle anabolism associated with heavy-resistance exercise. Sixteen men (21-34 yr) were assigned randomly to a resistance training plus GH group (n = 7) or to a resistance training plus placebo group (n = 9). For 12 wk, both groups trained all major muscle groups in an identical fashion while receiving 40 micrograms recombinant human GH.kg-1.day-1 or placebo. Fat-free mass (FFM) and total body water increased (P less than 0.05) in both groups but more (P less than 0.01) in the GH recipients. Whole body protein synthesis rate increased more (P less than 0.03), and whole body protein balance was greater (P = 0.01) in the GH-treated group, but quadriceps muscle protein synthesis rate, torso and limb circumferences, and muscle strength did not increase more in the GH-treated group. In the young men studied, resistance exercise with or without GH resulted in similar increments in muscle size, strength, and muscle protein synthesis, indicating that 1) the larger increase in FFM with GH treatment was probably due to an increase in lean tissue other than skeletal muscle and 2) resistance training supplemented with GH did not further enhance muscle anabolism and function.

Albumin and fibrinogen syntheses increase while muscle protein synthesis decreases in head-injured patients

1997 ◽  
Vol 273 (5) ◽  
pp. E898-E902 ◽  
Author(s):  
Odile Mansoor ◽  
Marc Cayol ◽  
Pierre Gachon ◽  
Yves Boirie ◽  
Pierre Schoeffler ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Albumin Synthesis ◽  
Body Protein ◽  
Head Injured ◽  
Injured Patients

The effect of trauma on protein metabolism was investigated in the whole body, muscle, and liver in severely head-injured patients presenting an acute inflammatory response by comparison to fed control subjects receiving a similar diet. Nonoxidative leucine disposal (an index of whole body protein synthesis) and muscle, albumin, and fibrinogen synthesis were determined by means of a primed, continuous infusion ofl-[1-13C]leucine. Nonoxidative leucine disposal increased by 28% in the patients ( P < 0.02). Fractional muscle protein synthesis rate decreased by 50% ( P < 0.01) after injury. Fractional and absolute fribrinogen synthesis rates were multiplied by two and nine, respectively, after injury ( P< 0.001). Albumin levels were lower in patients (25.2 ± 1.2 g/l, means ± SE) than in controls (33.7 ± 1.2 g/l, P < 0.001). However, fractional albumin synthesis rates were increased by 60% in patients (11.4 ± 1.0%/day) compared with controls (7.3 ± 0.4%/day, P < 0.01). Therefore, 1) head trauma induces opposite and large changes of protein synthesis in muscle and acute-phase hepatic proteins, probably mediated by cytokines, glucocorticoids, and other stress hormones, and 2) in these patients, hypoalbuminemia is not due to a depressed albumin synthesis.

scholarly journals Citrulline modulates muscle protein metabolism in old malnourished rats

2006 ◽  
Vol 291 (3) ◽  
pp. E582-E586 ◽  
Author(s):  
S. Osowska ◽  
T. Duchemann ◽  
S. Walrand ◽  
A. Paillard ◽  
Y. Boirie ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Food Intake ◽  
Protein Content ◽  
Muscle Protein ◽  
Protein Energy Malnutrition ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Standard Diet

Protein energy malnutrition is common in the elderly, especially in hospitalized patients. The development of strategies designed to correct such malnutrition is essential. Our working hypothesis was that poor response to nutrition with advancing age might be related to splanchnic sequestration of amino acids, which implies that fewer amino acids reach the systemic circulation. Administration of citrulline, which is not taken up by the liver, can offer a means of increasing whole body nitrogen availability and, hence, improve nutritional status. Thirty old (19 mo) rats were submitted to dietary restriction (50% of food intake) for 12 wk. They were randomized into three groups: 10 rats (R group) were killed and 20 others refed (90% of food intake) for 1 wk with a standard diet (NEAA group) or a citrulline-supplemented diet (Cit group). Before being killed, the rats were injected with [13C]valine, and the absolute protein synthesis rate (ASR) was measured in the tibialis using the flooding-dose method. When the rats were killed, the tibialis was removed for protein content analysis. Blood was sampled for amino acid and insulin analysis. The standard diet did not have any effect on protein synthesis or on the protein content in the muscle. Citrulline supplementation led to higher protein synthesis and protein content in muscle (117 ± 9, 120 ± 14, and 163 ± 4 mg/organ for protein content in R, NEAA, and Cit groups, P < 0.05). The ASR were 0.30 ± 0.04, 0.31 ± 0.04, and 0.56 ± 0.10 mg/h in the three groups, respectively (R and NEAA vs. Cit, P < 0.05). Insulinemia was significantly higher in the Cit group. For the first time, a realistic therapeutic approach is proposed to improve muscle protein content in muscle in frail state related to malnutrition in aging.

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