The Excretion of Isotope in Urea and Ammonia for Estimating Protein Turnover in Man with [15N]Glycine

1981 ◽  
Vol 61 (2) ◽  
pp. 217-228 ◽  
Author(s):  
E. B. Fern ◽  
P. J. Garlick ◽  
Margaret A. McNurlan ◽  
J. C. Waterlow
Keyword(s):  
Protein Metabolism ◽  
Protein Turnover ◽  
Mean Value ◽  
Intravenous Dose ◽  
Whole Body ◽  
Body Protein ◽  
End Products ◽  
The Mean ◽  
15N Urea ◽  
Normal Adults

1. Four normal adults were given [15N]-glycine in a single dose either orally or intravenously. Rates of whole-body protein turnover were estimated from the excretion of 15N in ammonia and in urea during the following 9 h. The rate derived from urea took account of the [15N]urea retained in body water. 2. In postabsorptive subjects the rates of protein synthesis given by ammonia were equal to those from urea, when the isotope was given orally, but lower when an intravenous dose was given. 3. In subjects receiving equal portions of food every 2 h rates of synthesis calculated from ammonia were much lower than those from urea whether an oral or intravenous isotope was given. Comparison of rates obtained during the post-absorptive and absorptive periods indicated regulation by food intake primarily of synthesis when measurements were made on urea, but regulation primarily of breakdown when measurements were made on ammonia. 4. These inconsistencies suggest that changes in protein metabolism might be assessed better by correlating results given by different end-products, and it is suggested that the mean value given by urea and ammonia will be useful for this purpose.

A comparison of the estimates of whole-body protein turnover in parenterally fed neonates obtained using three different end products

1989 ◽  
Vol 67 (6) ◽  
pp. 624-628 ◽  
Author(s):  
P. Pencharz ◽  
J. Beesley ◽  
P. Sauer ◽  
J. Van Aerde ◽  
U. Canagarayar ◽  
...  
Keyword(s):  
Nitrogen Metabolism ◽  
Protein Metabolism ◽  
Protein Turnover ◽  
The Other ◽  
Whole Body ◽  
Turnover Rates ◽  
Body Protein ◽  
Future Studies ◽  
Simultaneous Measurements ◽  
End Products

Protein turnover rates in neonates have been calculated largely by measuring urinary [15N]urea enrichment following administration of [15N]glycine. Although ammonia has been increasingly recognized as an end product of nitrogen metabolism, in neonates it yields a different estimate of protein turnover than does urea. Comparisons of ammonia and urea end products in parenterally fed neonates have not previously been reported. A third and independent way of estimating protein turnover, developed for adults, is to use breath 13CO2 as an end product following administration of [1-3C]leucine. We therefore carried out simultaneous measurements of protein turnover in 10 parenterally fed neonates, using the three end products. The infants were clinically stable, weighed 2.6 ± 0.2 kg, and received 3.1 ± 0.2 g∙kg−1∙d−1 of amino acid, 2.2 ± 0.1 g∙kg−1∙d−1 of lipids, and an energy intake of 90 ± 4 kcal∙kg−1∙d−1 (1 kcal = 4.186 kJ). The turnover estimates derived from the 13CO2 and [15N]urea end products were very similar. The [15N]ammonia end product produced values approximately 66% (p < 0.01) of the other two. We conclude that the ammonia and urea end products probably originate in different precursor pools. The similarity of the urea and breath carbon dioxide results helps validate the use of the urea end product in studying the nitrogen metabolism of parenterally fed neonates. Ideally in future studies two or more end products should be used, since they provide information about different aspects of the nenonates' protein metabolism.Key words: neonates, protein metabolism, nitrogen-15, [1-13C]leucine.

Whole Body Protein Metabolism in Human Pulmonary Tuberculosis and Undernutrition: Evidence for Anabolic Block in Tuberculosis

1998 ◽  
Vol 94 (3) ◽  
pp. 321-331 ◽  
Author(s):  
Derek C. MacAllan ◽  
Margaret A. McNurlan ◽  
Anura V. Kurpad ◽  
George De Souza ◽  
Prakash S. Shetty ◽  
...  
Keyword(s):  
Pulmonary Tuberculosis ◽  
Body Mass ◽  
Protein Metabolism ◽  
Protein Turnover ◽  
Nutrition Support ◽  
Whole Body ◽  
Body Protein ◽  
Leucine Kinetics ◽  
Body Energy ◽  
Net Protein

1. Differing patterns of protein metabolism are seen in wasting due to undernutrition and wasting due to chronic infection. 2. We investigated whole body energy and protein metabolism in nine subjects with pulmonary tuberculosis, six undernourished subjects (body mass index < 18.5 kg/m2) and seven control subjects from an Indian population. Fasting subjects were infused with l-[1-13C] leucine (2.3 μmol · h−1 · kg−1) for 8 h, 4 h fasted then 4 h fed. Leucine kinetics were derived from 13C-enrichment of leucine and α-ketoisocaproic acid in plasma and CO2 in breath. 3. Undernourished subjects, but not tuberculosis subjects, had higher rates of whole body protein turnover per unit lean body mass than controls [163.1 ± 9.4 and 148.6 ± 14.6 μmol compared with 142.8 ± 14.7 μmol leucine/h per kg, based on α-ketoisocaproic acid enrichment (P = 0.039)]. 4. In response to feeding, protein oxidation increased in all groups. Tuberculosis subjects had the highest fed rates of oxidation (47.0 ± 10.5 compared with 37.1 ± 5.4 μmol · h−1 · kg−1 in controls), resulting in a less positive net protein balance in the fed phase (controls, 39.7 ± 6.2; undernourished subjects, 29.2 ± 10.6; tuberculosis subjects, 24.5 ± 93; P = 0.010). Thus fed-phase tuberculosis subjects oxidized a greater proportion of leucine flux (33.2%) than either of the other groups (controls, 24.0%; undernourished subjects, 24.0%; P = 0.017). 5. Tuberculosis did not increase fasting whole body protein turnover but impaired the anabolic response to feeding compared with control and undernourished subjects. Such ‘anabolic block’ may contribute to wasting in tuberculosis and may represent the mechanism by which some inflammatory states remain refractory to nutrition support.

Role of ovarian hormones in the regulation of protein metabolism in women: effects of menopausal status and hormone replacement therapy

2006 ◽  
Vol 291 (3) ◽  
pp. E639-E646 ◽  
Author(s):  
Michael J. Toth ◽  
Cynthia K. Sites ◽  
Dwight E. Matthews
Keyword(s):  
Postmenopausal Women ◽  
Protein Metabolism ◽  
Protein Turnover ◽  
Hormone Replacement ◽  
Menopausal Status ◽  
Ovarian Hormones ◽  
Hormone Deficiency ◽  
Whole Body ◽  
Protein Breakdown ◽  
Body Protein

The age-related decline in fat-free mass is accelerated in women after menopause, implying that ovarian hormone deficiency may have catabolic effects on lean tissue. Because fat-free tissue mass is largely determined by its protein content, alterations in ovarian hormones would likely exert regulatory control through effects on protein balance. To address the hypothesis that ovarian hormones regulate protein metabolism, we examined the effect of menopausal status and hormone replacement therapy (HRT) on protein turnover. Whole body protein breakdown, oxidation, and synthesis were measured under postabsorptive conditions using [13C]leucine in healthy premenopausal ( n = 15, 49 ± 1 yr) and postmenopausal ( n = 18, 53 ± 1 yr) women. In postmenopausal women, whole body protein turnover and plasma albumin synthesis rates (assessed using [13C]leucine and [2H]phenylalanine) were also measured following 2 mo of treatment with oral HRT (0.625 mg conjugated estrogens + 2.5 mg medroxyprogesterone acetate, n = 9) or placebo ( n = 9). No differences in whole body protein breakdown, oxidation, or synthesis were found between premenopausal and postmenopausal women. Protein metabolism remained similar between groups after statistical adjustment for differences in adiposity and when subgroups of women matched for percent body fat were compared. In postmenopausal women, no effect of HRT was found on whole body protein breakdown, synthesis, or oxidation. In contrast, our results support a stimulatory effect of HRT on albumin fractional synthesis rate, although this did not translate into alterations in circulating albumin concentrations. In conclusion, our results suggest no detrimental effect of ovarian hormone deficiency coincident with the postmenopausal state, and no salutary effect of hormone repletion with HRT, on rates of whole body protein turnover, although oral HRT regimens may increase the synthesis rates of albumin.

Aspects of protein metabolism after elective surgery in patients receiving constant nutritional support

1990 ◽  
Vol 78 (6) ◽  
pp. 621-628 ◽  
Author(s):  
F. Carli ◽  
J. Webster ◽  
V. Ramachandra ◽  
M. Pearson ◽  
M. Read ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Metabolic Rate ◽  
Protein Metabolism ◽  
Protein Turnover ◽  
Resting Metabolic Rate ◽  
Plasma Concentrations ◽  
Whole Body ◽  
Body Protein ◽  
Urinary Nitrogen

1. The present study was designed in an attempt to resolve conflicting views currently in the literature relating to the effect of surgery on various aspects of protein metabolism. 2. Sequential post-operative (2, 4 and 6 days) changes in whole-body protein turnover, forearm arteriovenous difference of plasma amino acids, glucose, lactate and free fatty acids, muscle concentration of free amino acids, RNA and protein, urinary nitrogen and 3-methylhistidine, plasma concentrations of insulin, cortisol and growth hormone, and resting metabolic rate, were measured in six patients undergoing uncomplicated elective total abdominal hysterectomy. 3. All patients received a constant daily diet, either orally or intravenously, based on 0.1 g of nitrogen/kg and an energy content of 1.1 times the resting metabolic rate for 7 days before and 6 days after surgery. 4. Whole-body protein turnover, synthesis and breakdown increased significantly 2 days after surgery (P <0.05) and returned towards pre-operative levels thereafter. 5. Forearm release of branched-chain amino acids and alanine, and efflux of glucose and lactate, were enhanced 4 days after surgery (P <0.05). Muscle glutamine and alanine concentrations were decreased on the fourth and sixth days after surgery (P <0.05). The RNA/protein ratio (indicating the capacity for protein synthesis) was unaltered. 6. A significant increase in urinary nitrogen and 3-methylhistidine was observed on days 3 and 4 after surgery (P <0.05). Thereafter, these parameters remained elevated, although failing to reach statistical significance. 7. The resting metabolic rate was significantly increased (P <0.05) 2 days after surgery but the respiratory quotient (0.77) was unchanged. 8. These data support the contention that whole-body protein synthesis and breakdown increase after surgery. Differences observed pre- and post-operatively between leucine kinetic estimates and other methods of quantifying protein metabolism indicate that only like methodologies should be compared.

scholarly journals Response of Leucine Metabolism to Hyperinsulinemia in Hypothyroid Patients before and after Thyroxine Replacement1

2000 ◽  
Vol 85 (2) ◽  
pp. 697-706 ◽  
Author(s):  
Cecile Rochon ◽  
Igor Tauveron ◽  
Catherine Dejax ◽  
Patrick Benoit ◽  
Pierre Capitan ◽  
...  
Keyword(s):  
Protein Metabolism ◽  
Protein Turnover ◽  
Whole Body ◽  
Body Protein ◽  
Acid Infusion ◽  
Regular Treatment ◽  
Amino Acid Infusion ◽  
Appearance Rate ◽  
Before And After ◽  
Hypothyroid Patients

We have investigated the effect of hypothyroidism and insulin on protein metabolism in humans. Six hypothyroid patients were studied in a postabsorptive state before and after 5 months of regular treatment for hypothyroidism (153 ± 17 μg/day of l-T4). The effect of insulin was assessed under hyperinsulinemic euglycemic and eukalemic conditions. Insulin was infused for 140 min at 0.0063 ± 0.0002 nmol/kg·min. An amino acid infusion was used to blunt insulin-induced hypoaminoacidemia. Whole body protein turnover was measured using l-[1-13C] leucine. When compared to L-T4-induced subclinical thyrotoxic state, hypothyroidism induced a significant decrease (P &lt; 0.05) in leucine endogenous appearance rate (a reflection of proteolysis; 0.89 ± 0.09 vs. 1.33 ± 0.05 μmol/kg·min), oxidation (0.19 ± 0.02 vs. 0.25 ± 0.03 μmol/kg·min), and nonoxidative disposal (a reflection of protein synthesis; 0.87± 0.11 vs. 1.30 ± 0.05 μmol/kg·min). Insulin lowered proteolysis during both the subclinical thyrotoxic and hypothyroid states. Hypothyroidism impaired the antiproteolytic effects of insulin. Thyroid hormones are, therefore, essential for the normal antiproteolytic action of insulin.

Protein kinetics in stable heart failure patients

2003 ◽  
Vol 94 (1) ◽  
pp. 295-300 ◽  
Author(s):  
Charles W. Cortes ◽  
Paul D. Thompson ◽  
Niall M. Moyna ◽  
Margaret D. Schluter ◽  
Maria J. Leskiw ◽  
...  
Keyword(s):  
Protein Metabolism ◽  
Protein Turnover ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Bed Rest ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Body Protein ◽  
Fractional Synthesis

Heart failure (HF) is a slow progressive syndrome characterized by low cardiac output and peripheral metabolic, biochemical, and histological alterations. Protein loss and reduced protein turnover occur with aging, but the consequences of congestive HF (CHF) superimposed on the normal aging response are unknown. This study has two objectives: 1) to determine whether there was a difference between older age-matched controls and those with stable HF (i.e., ischemic pathology) in whole body protein turnover and 2) to determine whether protein metabolism in liver and skeletal muscle protein turnover is impacted by CHF. We measured the whole body protein synthesis rate with a U-15N-labeled algal protein hydrolysate in 10 patients with CHF and in 10 age-matched controls. Muscle fractional synthesis rate of lateral vastus muscle was determined with [U-13C]alanine on muscle biopsies obtained by a standard percutaneous needle biopsy technique. Fractional synthesis rates of five plasma proteins of hepatic origin (fibrinogen, complement C-3, ceruloplasmin, transferrin, and very low-density lipoprotein apoliprotein B-100) were determined by using2H5-labeled l-phenylalanine as tracer. Results showed that whole body protein synthesis rate was reduced in CHF patients (3.09 ± 0.19 vs. 2.25 ± 0.71 g protein · kg−1 · day−1, P < 0.05) as was muscle fractional synthesis rate (3.02 ± 0.58 vs. 1.33 ± 0.71%/day, P < 0.05) and very low-density lipoprotein apoliprotein B-100 (265 ± 25 vs. 197 ± 16%/day, P < 0.05). CHF patients were hyperinsulinemic (9.6 ± 3.1 vs. 47.0 ± 7.8 μU/ml, P < 0.01). The results were compared with those found with bed rest patients. In conclusion, protein turnover is depressed in CHF patients, and both skeletal muscle and liver are impacted. These results are similar to those found with bed rest, which suggests that inactivity is a factor in depressed protein metabolism.

Rapid measurement of whole body and forearm protein turnover using a [2H5]phenylalanine model

1989 ◽  
Vol 256 (5) ◽  
pp. E631-E639 ◽  
Author(s):  
G. N. Thompson ◽  
P. J. Pacy ◽  
H. Merritt ◽  
G. C. Ford ◽  
M. A. Read ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Rapid Assessment ◽  
Whole Body ◽  
Co2 Production ◽  
Constant Infusion ◽  
Body Protein ◽  
Normal Adults

Whole body protein turnover was measured in six normal adults using a model based on a primed constant infusion of [2H5]phenylalanine and, independently, by an established method of a primed constant infusion of [1-13C]leucine. Isotopic plateau in plasma was achieved within 2 h for [2H5]phenylalanine and, in four of the subjects who received a priming dose of [2H4]tyrosine, for [2H4]tyrosine. In all subjects whole body protein turnover measured with the phenylalanine model (mean protein synthesis, 2.65 +/- (SD) 0.16 g.kg-1.24 h-1; catabolism, 3.58 +/- 0.26 g.kg-1.24 h-1) was similar to that measured using the leucine model (synthesis, 3.09 +/- 0.27 g.kg-1.24 h-1; catabolism, 3.70 +/- 0.35 g.kg-1.24 h-1). Mean forearm fractional muscle protein synthesis calculated by the phenylalanine model was 0.06 +/- 0.03%/h, which compares closely with literature values derived by other methods. The phenylalanine model allows the rapid assessment of whole body and muscle protein turnover from plasma samples alone, obviating the need for measurement of expired air CO2 production or enrichment.

scholarly journals A Whole-Grain Diet Improves Whole-Body Protein Turnover Compared to a Macronutrient-Matched Refined-Grain Diet in Adults with Overweight/Obesity

2020 ◽  
Vol 4 (Supplement_2) ◽  
pp. 1661-1661
Author(s):  
Jacob Mey ◽  
John Kirwan
Keyword(s):  
Protein Synthesis ◽  
Protein Metabolism ◽  
Protein Turnover ◽  
Whole Grains ◽  
Whole Body ◽  
Protein Breakdown ◽  
Whole Grain ◽  
Protein Kinetics ◽  
Body Protein ◽  
Fasted State

Abstract Objectives We investigated the effect of consuming a whole-grain diet on whole-body protein metabolism compared to a macronutrient-matched refined-grain diet in adults with overweight/obesity using labelled amino acids (ClinicalTrials.gov Identifier: NCT01411540). Methods We conducted a randomized, controlled crossover trial in 14 adults with overweight/obesity (age: 40 ± 7 yrs, BMI: 33 ± 5 kg/m2) in which isocaloric, macronutrient-matched whole-grain (WG) and refined-grain (RG) diets were fully provided for two 8-week periods (with a 10-week washout period). Diets differed only in the inclusion of whole grains (50 g/1000 kcal). Body composition was measured via DEXA. Whole-body protein kinetics were assessed before and after each diet in the fasted state (13C-Leucine, primed, constant infusion) and over 24 hours (15N-Glycine, bolus). Protein kinetics were normalized to fat-free mass (FFM). Results Both diets resulted in mild weight loss (WG: −2.0 ± 2.5 kg; RG: −2.9 ± 3.3 kg; both P = 0.01 compared to baseline). Fasted-state leucine kinetics revealed greater protein synthesis (WG: 205 ± 61 µmol/kgFFM/hr; RG: 178 ± 36 µmol/kgFFM/hr; P = 0.04) and protein breakdown (WG: 235 ± 68 µmol/kgFFM/hr; RG: 203 ± 40 µmol/kgFFM/hr, P = 0.03) on a WG vs RG diet. This resulted in a more negative fasted-state net balance on a WG diet (WG: −30 ± 8 µmol/kg/hr; RG: −25 ± 6 µmol/kg/hr, P = 0.02). In contrast, 24-hour whole-body protein turnover measured by the end-product method (15N-Glycine), revealed greater protein synthesis (WG: 316 ± 135 mg protein/kgFFM/hr; RG: 250 ± 94 mg protein/kgFFM/hr) with no difference in protein breakdown, yielding a more positive 24-hr net balance on a WG diet (WG: 31 ± 21 mg protein/kgFFM/hr; RG: 10 ± 34 mg protein/kgFFM/hr). Conclusions A whole-grain diet increases whole-body leucine flux and results in a greater 24-hr net protein balance in adults with overweight/obesity compared to a refined-grain diet. This trial suggests whole-grains have an independent effect on protein metabolism and may benefit adults with overweight/obesity. Funding Sources This research was supported by the NIH (UL1 RR024989, T32DK007319 (JPK); T32AT004094 (JTM – trainee)) and an investigator-initiated grant from Nestle (JPK). Nestle Product Technology Center and Cereal Partners Worldwide provided the study meals and foods.

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.

Comparison of 15N-Labelled Glycine, Aspartate, Valine and Leucine for Measurement of Whole-Body Protein Turnover

1979 ◽  
Vol 57 (3) ◽  
pp. 281-283 ◽  
Author(s):  
M. Taruvinga ◽  
A. A. Jackson ◽  
M. H. N. Golden
Keyword(s):  
Amino Acids ◽  
Protein Turnover ◽  
Ammonia Nitrogen ◽  
Whole Body ◽  
Constant Infusion ◽  
Turnover Rates ◽  
Body Protein ◽  
End Products ◽  
Lower Protein ◽  
Branched Chain

1. Whole-body protein turnover was measured in rats by constant infusion of 15N-labelled glycine, aspartate, valine and leucine and measuring the enrichment of hepatic and renal urea and ammonia nitrogen. 2. The values obtained with [15N]glycine were comparable with values reported with methods based on different assumptions. 3. [15N]Aspartate gave rise to an increased enrichment of urea and ammonia and hence to lower protein-turnover rates. 4. [15N]Valine and [15N]leucine gave low enrichments of nitrogenous end products and hence to high protein-turnover rates. 5. All 15N-labelled amino acids are not equally suitable for measuring whole-body protein turnover by the end-product method. The relative amounts of 15N going to the end products can be predicted from the known individual metabolism of aspartate and the branched-chain amino acids.

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