Somatotropin increases protein balance independent of insulin's effects on protein metabolism in growing pigs

2000 ◽  
Vol 279 (1) ◽  
pp. E1-E10 ◽  
Author(s):  
Rhonda C. Vann ◽  
Hanh V. Nguyen ◽  
Peter J. Reeds ◽  
Norman C. Steele ◽  
Daniel R. Deaver ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protein Metabolism ◽  
Growing Pigs ◽  
Whole Body ◽  
Metabolic Responses ◽  
Glucose Disposal ◽  
Blood Levels ◽  
Protein Balance ◽  
Protein Deposition ◽  
Leucine Oxidation

Somatotropin (ST) administration enhances protein deposition and elicits profound metabolic responses, including hyperinsulinemia. To determine whether the anabolic effect of ST is due to hyperinsulinemia, pair-fed weight-matched growing swine were treated with porcine ST (150 μg · kg body wt−1 · day−1) or diluent for 7 days ( n = 6/group, ∼20 kg). Then pancreatic glucose-amino acid clamps were performed after an overnight fast. The objective was to reproduce the insulin levels of 1) fasted control and ST pigs (basal insulin, 5 μU/ml), 2) fed control pigs (low insulin, 20 μU/ml), and 3) fed ST pigs (high insulin, 50 μU/ml). Amino acid and glucose disposal rates were determined from the infusion rates necessary to maintain preclamp blood levels of these substrates. Whole body nonoxidative leucine disposal (NOLD), leucine appearance (Ra), and leucine oxidation were determined with primed, continuous infusions of [13C]leucine and [14C]bicarbonate. ST treatment was associated with higher NOLD and protein balance and lower leucine oxidation and amino acid and glucose disposals. Insulin lowered Ra and increased leucine oxidation, protein balance, and amino acid and glucose disposals. These effects of insulin were suppressed by ST treatment; however, the protein balance remained higher in ST pigs. The results show that ST treatment inhibits insulin's effects on protein metabolism and indicate that the stimulation of protein deposition by ST treatment is not mediated by insulin. Comparison of the protein metabolic responses to ST treatment during the basal fasting period with those in the fully fed state from a previous study suggests that the mechanism by which ST treatment enhances protein deposition is influenced by feeding status.

Somatotropin-induced protein anabolism in hindquarters and portal-drained viscera of growing pigs

2003 ◽  
Vol 284 (2) ◽  
pp. E302-E312 ◽  
Author(s):  
Jill A. Bush ◽  
Douglas G. Burrin ◽  
Agus Suryawan ◽  
Pamela M. J. O'Connor ◽  
Hanh V. Nguyen ◽  
...  
Keyword(s):  
Blood Flow ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Protein Degradation ◽  
Protein Metabolism ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Growing Pigs ◽  
Whole Body ◽  
Fed State

To differentiate the effect of somatotropin (ST) treatment on protein metabolism in the hindquarter (HQ) and portal-drained viscera (PDV), growing swine ( n = 20) treated with ST (0 or 150 μg · kg−1 · day−1) for 7 days were infused intravenously with NaH13CO3 and [2H5]phenylalanine and enterally with [1-13C]phenylalanine while in the fed state. Arterial, portal venous, and vena cava whole blood samples, breath samples, and blood flow measurements were obtained for determination of tissue and whole body phenylalanine kinetics under steady-state conditions. In the fed state, ST treatment decreased whole body phenylalanine flux, oxidation, and protein degradation without altering protein synthesis, resulting in an improvement in whole body net protein balance. Blood flow to the HQ (+80%), but not to the PDV, was increased with ST treatment. In the HQ and PDV, ST increased phenylalanine uptake (+44 and +23%, respectively) and protein synthesis (+43 and +41%, respectively), with no effect on protein degradation. In ST-treated and control pigs, phenylalanine was oxidized in the PDV (34–43% of enteral and arterial sources) but not the HQ. In both treatment groups, dietary (40%) rather than arterial (10%) extraction of phenylalanine predominated in gut amino acid metabolism, whereas localized blood flow influenced HQ amino acid metabolism. The results indicate that ST increases protein anabolism in young, growing swine by increasing protein synthesis in the HQ and PDV, with no effect on protein degradation. Differing results between the whole body and the HQ and PDV suggest that the effect of ST treatment on protein metabolism is tissue specific.

Somatotropin increases protein balance by lowering body protein degradation in fed, growing pigs

2000 ◽  
Vol 278 (3) ◽  
pp. E477-E483 ◽  
Author(s):  
Rhonda C. Vann ◽  
Hanh V. Nguyen ◽  
Peter J. Reeds ◽  
Douglas G. Burrin ◽  
Marta L. Fiorotto ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Growing Pigs ◽  
Whole Body ◽  
Plasma Urea ◽  
Body Protein ◽  
Fed State ◽  
Protein Deposition ◽  
Leucine Oxidation ◽  
Urea Production

Somatotropin (ST) administration enhances protein deposition in well-nourished, growing animals. To determine whether the anabolic effect is due to an increase in protein synthesis or a decrease in proteolysis, pair-fed, weight-matched (∼20 kg) growing swine were treated with porcine ST (150 μg ⋅ kg− 1 ⋅ day− 1, n = 6) or diluent ( n = 6) for 7 days. Whole body leucine appearance (Ra), nonoxidative leucine disposal (NOLD), urea production, and leucine oxidation, as well as tissue protein synthesis (Ks), were determined in the fed steady state using primed continuous infusions of [13C]leucine, [13C]bicarbonate, and [15N2]urea. ST treatment increased the efficiency with which the diet was used for growth. ST treatment also increased plasma insulin-like growth factor I (+100%) and insulin (+125%) concentrations and decreased plasma urea nitrogen concentrations (−53%). ST-treated pigs had lower leucine Ra (−33%), leucine oxidation (−63%), and urea production (−70%). However, ST treatment altered neither NOLD nor Ks in the longissimus dorsi, semitendinosus, or gastrocnemius muscles, liver, or jejunum. The results suggest that in the fed state, ST treatment of growing swine increases protein deposition primarily through a suppression of protein degradation and amino acid catabolism rather than a stimulation of protein synthesis.

scholarly journals Effects of dietary 20-hydroxyecdysone supplementation on whole-body protein turnover in growing pigs

2020 ◽  
Vol 175 ◽  
pp. 03008
Author(s):  
Olga Obvintseva ◽  
Kenes Erimbetov ◽  
Vitaly Mikhailov
Keyword(s):  
Protein Metabolism ◽  
Protein Turnover ◽  
Live Weight ◽  
Growing Pigs ◽  
The Body ◽  
Biologically Active ◽  
Whole Body ◽  
Body Protein ◽  
Protein Deposition ◽  
Experimental Group

One of the approaches to creating biologically active additives for use in pig breeding can be the use of 20-hydroxyecdysone regulating protein metabolism in piglets. The purpose of the work is to assess the effect of 20-hydroxyecdysone on turnover of protein in piglets. The experiment was carried out on barrows (♂ Danish Yorkshire × ♀ Danish landrace) to achieve a live weight of 53-62 kg. At the age of 60 days, 2 groups of piglets were formed: control and experimental. Piglets of the experimental group were injected with 20-hydroxyecdysone at a dose of 1.6 mg / kg body weight. In piglets of the experimental group, in comparison with the control, a decrease in the excretion of nitrogen in the urine was noted (by 26.8%, P <0.05). Nitrogen deposition was higher in piglets of the experimental group by 19.0% (P <0.001) compared with the control. 20-hydroxyecdysone contributed to increased protein deposition in the body of piglets due to protein synthesizing activity. Thus, the use of 20-hydroxyecdysone in pigs increases the efficiency of using amino acids for the synthesis and deposition of proteins in the body.

scholarly journals Higher Net Protein Balance Following the Ingestion of Free Range Reindeer Compared to Commercial Beef

2020 ◽  
Author(s):  
Melynda S. Coker ◽  
Kaylee R. Ladd ◽  
Scott E. Schutzler ◽  
Sanghee Park ◽  
Rick H. Williams ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Protein Metabolism ◽  
Essential Amino Acid ◽  
Whole Body ◽  
Induced Response ◽  
Protein Balance ◽  
Body Protein ◽  
Wild Game ◽  
Net Protein

Wild game consumption has been associated with health benefits, but the influence on protein metabolism remains unknown. We compared the feeding-induced response to 2 oz of free-range reindeer (FR) versus commercial beef (CB) using stable isotope methodology. Seven male and female participants (age: 38&plusmn;12 years; body mass index: 24&plusmn;3 kg/m2) completed two studies using a randomized, crossover design in which they ingested 2 oz of FR or CB. L-[ring 2H5]phenylalanine &amp; L-[ring 2H2]tyrosine were delivered via primed, continuous intravenous infusion. Blood samples were collected during the basal period and following consumption of FR or CB. Feeding-induced changes in whole body protein synthesis (PS), protein breakdown (PB), and net protein balance (NB) were determined via analysis of plasma samples for phenyalanine and tyrosine enrichment by gas chromatography mass spectrometry; plasma essential amino acid concentrations were determined by liquid chromatography-electrospray ionization-mass spectrometry. Plasma post-prandial essential amino acid (EAA) concentrations were higher with the ingestion of FR compared to CB (P=0.02). The acute feeding-induced response in PS was not different in either trial, but PB was reduced with the ingestion of FR compared to CB (P&lt;0.0001). The difference in PB contributed to a superior level of NB (P&lt;0.0001). When protein kinetics were normalized relative to the amino acids ingested, PB/EAAs and total amino acids ingested were reduced (P&lt;0.01 and 0.001, respectively) in FR compared to CB; contributing to greater NB/total amino acid ingested (P&lt;0.0001) between FR and CB. We conclude that the nutrient profiles of FR may have a more favorable benefit on protein metabolism compared to CB. These data support the potential health benefits of wild game in the preservation of whole-body protein.

Glucose and amino acid metabolism in chronic renal failure: effect of insulin and amino acids

1992 ◽  
Vol 262 (2) ◽  
pp. F168-F176 ◽  
Author(s):  
P. Castellino ◽  
A. Solini ◽  
L. Luzi ◽  
J. G. Barr ◽  
D. J. Smith ◽  
...  
Keyword(s):  
Renal Failure ◽  
Chronic Renal Failure ◽  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Whole Body ◽  
Glucose Disposal ◽  
Amino Acid Infusion ◽  
Leucine Oxidation ◽  
Control Subjects

The effects of hyperinsulinemia and hyperaminoacidemia on glucose and amino acid metabolism were examined in 16 control and 13 chronic renal failure (CRF) patients under two conditions: 1) euglycemic hyperinsulinemia and 2) amino acid infusion. All studies were performed with continuous indirect calorimetry and [1–14C]leucine infusion. In CRF patients insulin-mediated whole body glucose metabolism was reduced by 35% (4.41 +/- 0.50 vs. 6.76 +/- 0.73 mg.kg-1.min-1, P less than 0.01), primarily due to a decrease in nonoxidative glucose disposal (1.70 +/- 0.70 vs. 4.32 +/- 0.60 mg.kg-1.min-1, P less than 0.01); glucose oxidation was similar in both groups. In the postabsorptive state total leucine turnover (1.56 +/- 0.06 vs. 1.75 +/- 0.06), leucine oxidation (0.25 +/- 0.01 vs. 0.30 +/- 0.01), and nonoxidative leucine disposal (1.29 +/- 0.06 vs. 1.40 +/- 0.07 mumol.kg-1.min-1) were reduced in CRF vs. control subjects (all P less than 0.05). In response to hyperinsulinemia, endogenous leucine flux (index of proteolysis), leucine oxidation, nonoxidative leucine disposal (NOLD) (index of protein synthesis), and net leucine flux into protein were similar in CRF and control subjects. In contrast, the ability of hyperaminoacidemia to enhance NOLD (1.54 +/- 0.11 vs. 2.10 +/- 0.10 mumol.kg-1.min-1, P less than 0.01) and net leucine balance (0.27 +/- 0.05 vs. 0.41 +/- 0.05, P less than 0.05) was reduced in CRF patients.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Comprehensive assessment of post-prandial protein handling by the application of intrinsically labelled protein in vivo in human subjects

2021 ◽  
pp. 1-9
Author(s):  
Jorn Trommelen ◽  
Andrew M. Holwerda ◽  
Philippe J. M. Pinckaers ◽  
Luc J. C. van Loon
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Stable Isotope ◽  
Dietary Protein ◽  
Protein Metabolism ◽  
Muscle Protein ◽  
Human Subjects ◽  
Whole Body ◽  
Body Protein

All human tissues are in a constant state of remodelling, regulated by the balance between tissue protein synthesis and breakdown rates. It has been well-established that protein ingestion stimulates skeletal muscle and whole-body protein synthesis. Stable isotope-labelled amino acid methodologies are commonly applied to assess the various aspects of protein metabolism in vivo in human subjects. However, to achieve a more comprehensive assessment of post-prandial protein handling in vivo in human subjects, intravenous stable isotope-labelled amino acid infusions can be combined with the ingestion of intrinsically labelled protein and the collection of blood and muscle tissue samples. The combined application of ingesting intrinsically labelled protein with continuous intravenous stable isotope-labelled amino acid infusion allows the simultaneous assessment of protein digestion and amino acid absorption kinetics (e.g. release of dietary protein-derived amino acids into the circulation), whole-body protein metabolism (whole-body protein synthesis, breakdown and oxidation rates and net protein balance) and skeletal muscle metabolism (muscle protein fractional synthesis rates and dietary protein-derived amino acid incorporation into muscle protein). The purpose of this review is to provide an overview of the various aspects of post-prandial protein handling and metabolism with a focus on insights obtained from studies that have applied intrinsically labelled protein under a variety of conditions in different populations.

Effect of hyperinsulinemia on ovine fetal leucine kinetics during prolonged maternal fasting

1992 ◽  
Vol 263 (4) ◽  
pp. E696-E702 ◽  
Author(s):  
E. A. Liechty ◽  
D. W. Boyle ◽  
H. Moorehead ◽  
Y. M. Liu ◽  
S. C. Denne
Keyword(s):  
Protein Metabolism ◽  
Glucose Utilization ◽  
Whole Body ◽  
Postnatal Life ◽  
Body Protein ◽  
Leucine Oxidation ◽  
Leucine Kinetics ◽  
Ovine Fetus ◽  
Ovine Fetal

The primary effect of insulin on whole body protein metabolism in postnatal life is to reduce proteolysis. To assess the role of insulin in the regulation of protein metabolism in prenatal life, leucine kinetics were determined in the ovine fetus at baseline and in response to hyperinsulinemia. These measurements were made in each fetus in two different maternal states: ad libitum maternal feeding and after a 5-day maternal fast. Maternal fasting resulted in significant increases in baseline fetal leucine rate of appearance (Ra; 51.9 +/- 16.7 vs. 37.3 +/- 3.6 mumol/min, P < 0.05) and leucine oxidation (30.1 +/- 8.9 vs. 8.8 +/- 2.2 mumol/min, P < 0.05). Hyperinsulinemia, which was associated with significant increases in fetal glucose utilization, did not affect total fetal leucine R(a) or leucine release from fetal proteolysis in either maternal state. Under well-fed maternal conditions, hyperinsulinemia produced no changes in the fetal oxidative or nonoxidative disposal of leucine. In contrast, during maternal fasting, hyperinsulinemia reduced fetal leucine oxidation (11.0 +/- 3.7 vs. 31.1 +/- 8.9 mumol/min, P < 0.05) and increased the nonoxidative disposal of leucine (35.4 +/- 4.0 vs. 19.0 +/- 6.1 mumol/min, P < 0.05). This resulted in a change in the fetal leucine accretion rate from negative to positive (-20.9 +/- 7.5 vs. 7.5 +/- 6.7 mumol/min, P < 0.05). These results suggest that, under conditions of restricted maternal substrate intake, fetal hyperinsulinemia and the attendant increase in fetal glucose utilization are associated with increased protein synthesis rather than decreased protein breakdown, thereby improving fetal leucine carcass accretion.

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