scholarly journals Hepatic detoxification of ammonia in the ovine liver: possible consequences for amino acid catabolism

1995 ◽  
Vol 73 (5) ◽  
pp. 667-685 ◽  
Author(s):  
G. E. Lobley ◽  
A. Connell ◽  
M. A. Lomax ◽  
D. S. Brown ◽  
E. Milne ◽  
...  
Keyword(s):  
Amino Acid ◽  
Kinetic Data ◽  
Free Amino ◽  
Liver Blood Flow ◽  
Whole Body ◽  
Acid Oxidation ◽  
Urea Synthesis ◽  
Amino Acid Oxidation ◽  
N Metabolism ◽  
Glutamate Synthesis

The effects of either low (25 μmol/min) or high (235 μmol/min) infusion of NH4Cl into the mesenteric vein for 5 d were determined on O2consumption plus urea and amino acid transfers across the portal-drained viscera (PDV) and liver of young sheep. Kinetic transfers were followed by use of15NH4Cl for 10 h on the fifth day with simultaneous infusion of [1-13C]lleucine to monitor amino acid oxidation. Neither PDV nor liver blood flow were affected by the additional NH3loading, although at the higher rate there was a trend for increased liver O2consumption. NH3-N extraction by the liver accounted for 64–70% of urea-N synthesis and at the lower infusion rate the additional N required could be more than accounted for by hepatic removal of free amino acids. At the higher rate of NH3administration additional sources of N were apparently required to account fully for urea synthesis. Protein synthesis rates in the PDV and liver were unaffected by NH3infusion but both whole-body (P< 0·05) and splanchnic tissue leucine oxidation were elevated at the higher rate of administration. Substantial synthesis of [15N]glutamine occurred across the liver, particularly with the greater NH3supply, and enrichments exceeded considerably those of glutamate. The [15N]urea synthesized was predominantly as the single labelled, i.e. [14N15N], species. These various kinetic data are compatible with the action of ovine hepatic glutamate dehydrogenase (EC1.4.1.2) in periportal hepatocytes in the direction favouring glutamate deamination. Glutamate synthesis and uptake is probably confined to the perivenous cells which do not synthesize urea. The implications of NH3detoxification to the energy and N metabolism of the ruminant are discussed.

Adaptations in protein metabolism during lactation in the rat

1987 ◽  
Vol 58 (3) ◽  
pp. 533-538 ◽  
Author(s):  
Donald J. Naismith ◽  
Siân M. Robinson
Keyword(s):  
Amino Acid ◽  
Protein Metabolism ◽  
Milk Protein ◽  
Acid Oxidation ◽  
Urea Synthesis ◽  
Lean Tissue ◽  
Anabolic Hormone ◽  
Amino Acid Oxidation ◽  
Argininosuccinate Synthase ◽  
Protein Supply

1. The activities of two hepatic enzymes that participate in the regulation of amino acid oxidation and urea synthesis were measured in lactating rats (day 15 of lactation) and virgin controls. The enzymes were alanine aminotransferase (EC 2. 6. 1.2) and argininosuccinate synthase (EC 6. 3. 4.5). Carcasses of the dams were also analysed.2. Changes in the activities of both enzymes in dams fed ad lib. on a diet containing an excess of protein indicated that amino acid oxidation was depressed. In dams restricted in protein to the level of intake of their controls but allowed to satisfy their needs for energy, enzyme activities were significantly reduced. In these animals lean tissue catabolism supplemented the dietary protein supply.3. This adjustment in protein metabolism which effectively spares protein for milk-protein synthesis could be explained either by a reduction in the availability of substrate in the liver, or by the intervention of an anabolic hormone secreted in lactation.

scholarly journals Protein Intake to Maximize Whole-Body Anabolism during Postexercise Recovery in Resistance-Trained Men with High Habitual Intakes is Severalfold Greater than the Current Recommended Dietary Allowance

2019 ◽  
Author(s):  
Michael Mazzulla ◽  
Sidney Abou Sawan ◽  
Eric Williamson ◽  
Sarkis J Hannaian ◽  
Kimberly A Volterman ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Steady State ◽  
Amino Acid ◽  
Resistance Exercise ◽  
Protein Intake ◽  
Whole Body ◽  
Total Amino Acid ◽  
Acid Oxidation ◽  
Amino Acid Oxidation ◽  
Habitual Protein Intake

ABSTRACT Background Dietary protein supports resistance exercise–induced anabolism primarily via the stimulation of protein synthesis rates. The indicator amino acid oxidation (IAAO) technique provides a noninvasive estimate of the protein intake that maximizes whole-body protein synthesis rates and net protein balance. Objective We utilized IAAO to determine the maximal anabolic response to postexercise protein ingestion in resistance-trained men. Methods Seven resistance-trained men (mean ± SD age 24 ± 3 y; weight 80 ± 9 kg; 11 ± 5% body fat; habitual protein intake 2.3 ± 0.6 g·kg−1·d−1) performed a bout of whole-body resistance exercise prior to ingesting hourly mixed meals, which provided a variable amount of protein (0.20–3.00 g·kg−1·d−1) as crystalline amino acids modeled after egg protein. Steady-state protein kinetics were modeled with oral l-[1-13C]-phenylalanine. Breath and urine samples were taken at isotopic steady state to determine phenylalanine flux (PheRa), phenylalanine excretion (F13CO2; reciprocal of protein synthesis), and net balance (protein synthesis − PheRa). Total amino acid oxidation was estimated from the ratio of urinary urea and creatinine. Results Mixed model biphasic linear regression revealed a plateau in F13CO2 (mean: 2.00; 95% CI: 1.62, 2.38 g protein·kg−1·d−1) (r2 = 0.64; P ˂ 0.01) and in net balance (mean: 2.01; 95% CI: 1.44, 2.57 g protein·kg−1·d−1) (r2 = 0.63; P ˂ 0.01). Ratios of urinary urea and creatinine concentrations increased linearly (r = 0.84; P ˂ 0.01) across the range of protein intakes. Conclusions A breakpoint protein intake of ∼2.0 g·kg−1·d−1, which maximized whole-body anabolism in resistance-trained men after exercise, is greater than previous IAAO-derived estimates for nonexercising men and is at the upper range of current general protein recommendations for athletes. The capacity to enhance whole-body net balance may be greater than previously suggested to maximize muscle protein synthesis in resistance-trained athletes accustomed to a high habitual protein intake. This trial was registered at clinicaltrials.gov as NCT03696264.

scholarly journals Intraoperative protein sparing with glucose

2005 ◽  
Vol 99 (3) ◽  
pp. 898-901 ◽  
Author(s):  
Thomas Schricker ◽  
Ralph Lattermann ◽  
Franco Carli
Keyword(s):  
Amino Acid ◽  
Colorectal Surgery ◽  
Normal Saline ◽  
Whole Body ◽  
Control Group ◽  
Acid Oxidation ◽  
Intravenous Glucose ◽  
Amino Acid Oxidation ◽  
Leucine Oxidation ◽  
Glucose Group

We examined the hypothesis that glucose infusion inhibits amino acid oxidation during colorectal surgery. We randomly allocated 14 patients to receive intravenous glucose at 2 mg·kg−1·min−1 (glucose group) starting with the surgical incision or an equivalent amount of normal saline 0.9% (control group). The primary endpoint was whole body leucine oxidation; secondary endpoints were leucine rate of appearance and nonoxidative leucine disposal as determined by a stable isotope tracer technique (l-[1-13C]leucine). Circulating concentrations of glucose, lactate, insulin, glucagon, and cortisol were measured before and after 2 h of surgery. Leucine rate of appearance, an estimate of protein breakdown, and nonoxidative leucine disposal, an estimate of protein synthesis, decreased in both groups during surgery ( P < 0.05). Leucine oxidation intraoperatively decreased from 13 ± 3 to 4 ± 3 μmol·kg−1·h−1 in the glucose group ( P < 0.05 vs. control group) whereas it remained unchanged in the control group. Hyperglycemia during surgery was more pronounced in patients receiving glucose (9.7 ± 0.5 mmol/l, P < 0.05 vs. control group) than in patients receiving normal saline (7.1 ± 1.0 mmol/l). The administration of glucose caused an increase in the circulating concentration of insulin ( P < 0.05) resulting in a lower glucagon/insulin quotient than in the control group ( P < 0.05). Intraoperative plasma cortisol concentrations increased in both groups ( P < 0.05), whereas plasma concentrations of lactate and glucagon did not change. The provision of small amounts of glucose was associated with a decrease in amino acid oxidation during colorectal surgery.

Ammonium chloride-induced acidosis increases protein breakdown and amino acid oxidation in humans

1992 ◽  
Vol 263 (4) ◽  
pp. E735-E739 ◽  
Author(s):  
D. Reaich ◽  
S. M. Channon ◽  
C. M. Scrimgeour ◽  
T. H. Goodship
Keyword(s):  
Amino Acid ◽  
Ammonium Chloride ◽  
Protein Turnover ◽  
Healthy Subjects ◽  
Whole Body ◽  
Acid Oxidation ◽  
Protein Breakdown ◽  
Body Protein ◽  
Amino Acid Oxidation ◽  
Kinetics Of

The effect of acidosis on whole body protein turnover was determined from the kinetics of infused L-[1-13C]leucine. Seven healthy subjects were studied before (basal) and after (acid) the induction of acidosis with 5 days oral ammonium chloride (basal pH 7.42 +/- 0.01, acid pH 7.35 +/- 0.03). Bicarbonate recovery, measured from the kinetics of infused NaH13CO3, was increased in the acidotic state (basal 72.9 +/- 1.2 vs. acid 77.6 +/- 1.6%; P = 0.06). Leucine appearance from body protein (PD), leucine disappearance into body protein (PS), and leucine oxidation (O) increased significantly (PD: basal 120.5 +/- 5.6 vs. acid 153.9 +/- 6.2, P < 0.01; PS: basal 98.8 +/- 5.6 vs. acid 127.0 +/- 4.7, P < 0.01; O: basal 21.6 +/- 1.1 vs. acid 26.9 +/- 2.3 mumol.kg-1.h-1, P < 0.01). Plasma levels of the amino acids threonine, serine, asparagine, citrulline, valine, leucine, ornithine, lysine, histidine, arginine, and hydroxyproline increased significantly with the induction of acidosis. These results confirm that acidosis in humans is a catabolic factor stimulating protein degradation and amino acid oxidation.

Whole Body Branched-Chain L-Amino Acid Oxidation in Overnight Fasted Human Subjects

1997 ◽  
Vol 33 (1-2) ◽  
pp. 189-196 ◽  
Author(s):  
A. Bodner ◽  
H.-W. Hammen ◽  
W. Renn ◽  
U. Wendel ◽  
P. Schadewaldt
Keyword(s):  
Amino Acid ◽  
Human Subjects ◽  
Whole Body ◽  
Acid Oxidation ◽  
Amino Acid Oxidation ◽  
Branched Chain

scholarly journals PSXI-31 Program Chair Poster Pick: Determination of the threonine requirement in adult and senior Labrador Retrievers using the indicator amino acid oxidation technique

2020 ◽  
Vol 98 (Supplement_4) ◽  
pp. 321-322
Author(s):  
Jordan T Weil ◽  
Jessica L Varney ◽  
Jason W Fowler ◽  
Craig N Coon
Keyword(s):  
Amino Acid ◽  
Control Diet ◽  
Genetic Selection ◽  
Isotope Ratio Mass Spectrometry ◽  
Acid Oxidation ◽  
Amino Acid Oxidation ◽  
Amino Acid Requirements ◽  
Indispensable Amino Acids ◽  
Nutrient Profiles ◽  
Labrador Retrievers

Abstract Although nutrient profiles for canines have been developed in the past, the need to update amino acid (AA) requirements has gained importance as genetic selection changes the recommended nutrients. Correctly feeding AA to canines can have enormous effects, considering a deficiency or excess of such nutrient can lead to weight loss, disease, or in some cases, death. Amino acid requirements can be determined through the nitrogen balance or indicator amino acid oxidation (IAAO) methods. In this experiment, the IAAO technique was used to determine the threonine (Thr) requirement in Labrador retrievers. A total of six dogs (6 adult and 6 senior) were subjected to six diets with varying levels of Thr, ranging from deficient to excess. Diets were formulated to 1.6x NRC values for all indispensable amino acids. The control diet was fed for two days, followed by a day in which the test diet was fed, a tracer AA was supplied, and breath samples were collected. On test day, a priming dose of L-[1-13C]phenylalanine (Cambridge Isotope Laboratories, Inc.) based on the subject’s body weight was first supplied, followed by [1-13C]Phe doses every thirty minutes, spanning a four hour period. A respiration mask was placed on each subject every thirty minutes (Oxymax, Columbus Instruments), 13CO2 was collected, and enrichment was determined by isotope ratio mass spectrometry (IRMS). Results for IRMS were converted to atom percent excess (APE) and analyzed using a piecewise model of best fit (JMP® Pro 15). The segmented line regression showed that the Thr mean and population requirements were determined to be 1.21 ± 0.24 and 0.92 ± 0.17 g/1000kcal (mean ± 2SD) for adult and senior dogs, respectively. As the pet food industry becomes more specialized in diets relating to aging, and diseased canines, updating the amino acid requirements related to such animals is increasingly important.

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