Diurnal variation in urine [15N]urea content, estimates of whole body protein turnover, and isotope recycling in healthy meal-fed children with cystic fibrosis

1983 ◽  
Vol 61 (1) ◽  
pp. 72-80 ◽  
Author(s):  
H. G. Parsons ◽  
M. M. Wood ◽  
P. B. Pencharz
Keyword(s):  
Cystic Fibrosis ◽  
Diurnal Variation ◽  
Amino Nitrogen ◽  
Whole Body ◽  
Diurnal Changes ◽  
Nitrogen Flux ◽  
Body Protein ◽  
Urea Excretion ◽  
Breakdown Rates ◽  
Wide Range

The pattern of urinary urea excretion and labelling with 15N was examined in eight meal-fed 6 to 9 year old children, over a 3-day period using a simulated constant infusion of the label. The children had cystic fibrosis but were healthy and in a good nutritional status at the time of the study. Reciprocal diurnal patterns of urea excretion and [15N]urea enrichment were noted and found to be suitable for mathematical description. Urea excretion was maximal in the evening at approximately 2000 and minimal at 0800, whereas the [15N]urea enrichment was maximal at about 0800 and minimal at 2000. In addition to the diurnal variation the [15N]urea enrichment increased exponentially to a plateau or isotopic steady state. The diurnal variation in [15N]urea enrichment resulted in large diurnal changes in the calculated rates of whole body amino nitrogen flux, synthesis, and breakdown. Flux rates were approximately 44% higher in the evening than in the morning. Synthesis rates were 19% higher in the evening, whereas breakdown rates were 27% greater in the morning. Mean amino nitrogen flux rates were 1.28 (SD 0.13) g N∙kg−1∙day−1. Isotope recycling was estimated from the slope of the [15N]urea enrichment curve between 30 and 54 h from the start of the study. There was a wide range in recycling, 2.9–19.4% (mean 11.4, SD 5.4). Some of the biological and pharmacological importance of the diurnal variation in the protein metabolism is discussed.

Combined ingestion of protein and free leucine with carbohydrate increases postexercise muscle protein synthesis in vivo in male subjects

2005 ◽  
Vol 288 (4) ◽  
pp. E645-E653 ◽  
Author(s):  
René Koopman ◽  
Anton J. M. Wagenmakers ◽  
Ralph J. F. Manders ◽  
Antoine H. G. Zorenc ◽  
Joan M. G. Senden ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Whole Body ◽  
Vastus Lateralis Muscle ◽  
Protein Balance ◽  
Body Protein ◽  
Breakdown Rates ◽  
Postexercise Recovery ◽  
Male Subjects

The present study was designed to determine postexercise muscle protein synthesis and whole body protein balance following the combined ingestion of carbohydrate with or without protein and/or free leucine. Eight male subjects were randomly assigned to three trials in which they consumed drinks containing either carbohydrate (CHO), carbohydrate and protein (CHO+PRO), or carbohydrate, protein, and free leucine (CHO+PRO+Leu) following 45 min of resistance exercise. A primed, continuous infusion of l-[ ring-13C6]phenylalanine was applied, with blood samples and muscle biopsies collected to assess fractional synthetic rate (FSR) in the vastus lateralis muscle as well as whole body protein turnover during 6 h of postexercise recovery. Plasma insulin response was higher in the CHO+PRO+Leu compared with the CHO and CHO+PRO trials (+240 ± 19% and +77 ± 11%, respectively, P < 0.05). Whole body protein breakdown rates were lower, and whole body protein synthesis rates were higher, in the CHO+PRO and CHO+PRO+Leu trials compared with the CHO trial ( P < 0.05). Addition of leucine in the CHO+PRO+Leu trial resulted in a lower protein oxidation rate compared with the CHO+PRO trial. Protein balance was negative during recovery in the CHO trial but positive in the CHO+PRO and CHO+PRO+Leu trials. In the CHO+PRO+Leu trial, whole body net protein balance was significantly greater compared with values observed in the CHO+PRO and CHO trials ( P < 0.05). Mixed muscle FSR, measured over a 6-h period of postexercise recovery, was significantly greater in the CHO+PRO+Leu trial compared with the CHO trial (0.095 ± 0.006 vs. 0.061 ± 0.008%/h, respectively, P < 0.05), with intermediate values observed in the CHO+PRO trial (0.0820 ± 0.0104%/h). We conclude that coingestion of protein and leucine stimulates muscle protein synthesis and optimizes whole body protein balance compared with the intake of carbohydrate only.

Enhancement of tumor proteolysis by TNF-alpha: correlation of in vivo isotope estimates with growth

1991 ◽  
Vol 261 (1) ◽  
pp. R106-R116
Author(s):  
N. W. Istfan ◽  
P. R. Ling ◽  
G. L. Blackburn ◽  
B. R. Bistrian
Keyword(s):  
Protein Synthesis ◽  
Protein Metabolism ◽  
Whole Body ◽  
Independent Effect ◽  
Yoshida Sarcoma ◽  
Protein Breakdown ◽  
Body Protein ◽  
Breakdown Rates ◽  
Made In

To evaluate the accuracy of in vivo estimates of protein synthesis and breakdown, measurements of plasma and tissue leucine kinetics were made in rat tumor tissues at different conditions of growth by use of constant intravenous infusion of [14C]leucine. These measurements were made in Yoshida sarcoma tumors on days 10 and 13 after implantation, with and without tumor necrosis factor (TNF) infusion and on day 10 in Walker-256 carcinosarcoma. Expressed as micromoles of leucine per gram tissue, tumor protein breakdown increased (P less than 0.01) from 0.32 +/- 0.02 to 0.52 +/- 0.09 (SE) mumol/h, with progress of the Yoshida sarcoma tumor between days 10 and 13 after implantation. Similarly, TNF increased tumor proteolysis on day 10 (0.43 +/- 0.03 mumol.h-1.g-1, P less than 0.05 vs. day 10 control) but not on day 13 after implantation of the Yoshida tumor. Estimates of growth derived from the difference between protein synthesis and breakdown rates were not statistically different from those based on actual tumor volume changes in both tumor models. However, estimates of “whole body” protein metabolism (plasma leucine flux) were not affected either by tumor aging or by treatment with TNF. This study shows that in vivo estimates of tissue protein metabolism based on our [14C]leucine constant infusion model closely reflect the growth characteristic of that tissue. A cytotoxic perfusion-independent effect for intravenous TNF on growing tumor tissue is demonstrable as increased protein breakdown. Furthermore, the commonly used concept of whole body protein metabolism, derived solely from tracer dilution in plasma, is an oversimplification.

Plasma insulin concentrations and amino acid turnover in Merino sheep with high or low fleece weight

2004 ◽  
Vol 55 (8) ◽  
pp. 833 ◽  
Author(s):  
N. R. Adams ◽  
S. M. Liu ◽  
J. R. Briegel ◽  
M. J. Thompson
Keyword(s):  
Amino Acids ◽  
Plasma Insulin ◽  
Plasma Concentrations ◽  
Amino Nitrogen ◽  
Whole Body ◽  
Metabolic Demand ◽  
Body Protein ◽  
Wool Growth ◽  
Staple Strength ◽  
Fleece Weight

Although sheep with a relatively high fleece weight have reduced fat deposition and a lower reproductive rate, research has failed to identify any specific metabolic demand that growing a fleece places on the physiology of the sheep. This paper reports two experiments in which the effect of fleece weight was examined in ewes infused intravenously with amino acids. The first experiment was carried out when the ewes were 107 days pregnant, and the second 2 years later in non-pregnant ewes from the same flock. The ewes were derived initially from groups that differed in staple strength, but there was no effect of staple strength group on the characteristics measured in either experiment. In Expt 2, ewes were also infused with a bolus of l-[ring-d5] phenylalanine, and the enrichment in plasma determined by GC/mass spectrometry over the next 24 h. In both experiments, fasting plasma insulin concentrations were lower (P < 0.05) in ewes with a high fleece weight, and this difference continued during infusion in Expt 2 (P < 0.05). In Expt 1, infusion of ewes with amino acids resulted in higher (P < 0.05) plasma concentrations of α-amino nitrogen (indicating amino acids) in the ewes with a higher fleece weight, and in Expt 2, ewes with a high fleece weight had a 19% higher rate of appearance of endogenous phenylalanine (P < 0.05). We conclude that sheep with high wool growth rates have higher whole-body protein turnover rate, which may be achieved in part by lower insulin concentrations. Lower insulin in turn provides a mechanism through which wool growth rate may influence energy availability to other tissues.

The effect of a weight-reducing diet on the nitrogen metabolism of obese adolescents

1988 ◽  
Vol 66 (11) ◽  
pp. 1469-1474 ◽  
Author(s):  
P. B. Pencharz ◽  
R. Clarke ◽  
E. H. Archibald ◽  
N. Vaisman
Keyword(s):  
Nitrogen Metabolism ◽  
Control Diet ◽  
Amino Nitrogen ◽  
Ideal Body Weight ◽  
Ammonia Nitrogen ◽  
Whole Body ◽  
Nitrogen Flux ◽  
Obese Adolescents ◽  
Ideal Body ◽  
Cumulative Excretion

Rates of whole body amino nitrogen flux were measured in 16 obese adolescents undergoing weight reduction with a high protein low energy diet. The subjects received approximately 2.5 g of animal protein per day per kilogram ideal body weight and maintained nitrogen balance throughout the 18 days on the diet. Flux rates were calculated separately from the cumulative excretion of 15N in urinary ammonia and urea following the administration of a single dose of [15N]glycine. The pattern of 15N label appearance in urinary ammonia and urea nitrogen was followed for 72 h after the administration of [15N]glycine. Significant amounts of label continued to be excreted in both urinary ammonia and nitrogen for 36–48 h after label administration. The weight-reducing diet accelerated 15N cumulative excretion in urinary urea, but not in ammonia nitrogen compared with the control diet. Whole body nitrogen flux rates increased rapidly and significantly on the diet. Using the urea end product, this increase was evident on the 4th diet day, but not by the 7th or subsequent days. On the other hand, using the ammonia end product, flux rate increased markedly (p < 0.0001) and remained elevated throughout the whole study. Our results demonstrate adaptive changes in whole body amino-nitrogen metabolism in response to the reducing diet. Different patterns of change are seen depending upon whether an ammonia or a urea end product is used. Our data thus add to the evidence for compartmentation of the body's amino-nitrogen pools.

Whole-Body Protein Turnover before and after Resection of Colorectal Tumours

1983 ◽  
Vol 64 (1) ◽  
pp. 101-108 ◽  
Author(s):  
R. E. Glass ◽  
E. B. Fern ◽  
P. J. Garlick
Keyword(s):  
Protein Synthesis ◽  
Primary Tumour ◽  
Experimental Period ◽  
Whole Body ◽  
Tumour Resection ◽  
Surgical Removal ◽  
Protein Breakdown ◽  
Nitrogen Flux ◽  
Body Protein ◽  
Before And After

1. The rate of whole-body nitrogen flux; protein synthesis and protein breakdown were measured in patients with colorectal cancer (Dukes A—C) just before and 12 weeks after surgical removal of the tumour. The rates were determined from the urinary excretion of 15N in ammonia and in urea over a 9 h period after an oral dose of [15N]glycine. 2. The food intake during the 2 study days was identical for individual patients. The amount each received was determined from measurement of their intake of food ad libitum on the day preceding the pre-operative study and was consumed in six equal portions every 2 h during the experimental period. 3. No significant differences in the rates of nitrogen flux, protein synthesis and protein breakdown were found before and after tumour resection, whether calculated from the excretion of 15N in ammonia or in urea. Some changes in flux, both increases and decreases, were observed in individual patients after tumour removal but these could not be related to classification of the tumour, or to the presence of pre-operative anorexia or weight loss. 4. The results suggest that the primary tumour itself does not alter the overall rate of protein metabolism in the whole body.

scholarly journals Effect of glucose supplement timing on protein metabolism after resistance training

1997 ◽  
Vol 82 (6) ◽  
pp. 1882-1888 ◽  
Author(s):  
B. D. Roy ◽  
M. A. Tarnopolsky ◽  
J. D. Macdougall ◽  
J. Fowles ◽  
K. E. Yarasheski
Keyword(s):  
Resistance Training ◽  
Resistance Exercise ◽  
Protein Metabolism ◽  
Muscle Protein ◽  
Vastus Lateralis ◽  
Myofibrillar Protein ◽  
Whole Body ◽  
Body Protein ◽  
Urea Excretion ◽  
Effect Of Glucose

Roy, B. D., M. A. Tarnopolsky, J. D. MacDougall, J. Fowles, and K. E. Yarasheski. Effect of glucose supplement timing on protein metabolism after resistance training. J. Appl. Physiol. 82(6): 1882–1888, 1997.—We determined the effect of the timing of glucose supplementation on fractional muscle protein synthetic rate (FSR), urinary urea excretion, and whole body and myofibrillar protein degradation after resistance exercise. Eight healthy men performed unilateral knee extensor exercise (8 sets/∼10 repetitions/∼85% of 1 single maximal repetition). They received a carbohydrate (CHO) supplement (1 g/kg) or placebo (Pl) immediately ( t = 0 h) and 1 h ( t = +1 h) postexercise. FSR was determined for exercised (Ex) and control (Con) limbs by incrementall-[1-13C]leucine enrichment into the vastus lateralis over ∼10 h postexercise. Insulin was greater ( P < 0.01) at 0.5, 0.75, 1.25, 1.5, 1.75, and 2 h, and glucose was greater ( P < 0.05) at 0.5 and 0.75 h for CHO compared with Pl condition. FSR was 36.1% greater in the CHO/Ex leg than in the CHO/Con leg ( P = not significant) and 6.3% greater in the Pl/Ex leg than in the Pl/Con leg ( P = not significant). 3-Methylhistidine excretion was lower in the CHO (110.43 ± 3.62 μmol/g creatinine) than Pl condition (120.14 ± 5.82, P < 0.05) as was urinary urea nitrogen (8.60 ± 0.66 vs. 12.28 ± 1.84 g/g creatinine, P < 0.05). This suggests that CHO supplementation (1 g/kg) immediately and 1 h after resistance exercise can decrease myofibrillar protein breakdown and urinary urea excretion, resulting in a more positive body protein balance.

Protein Metabolism in Human Neonates: Nitrogen-Balance Studies, Estimated Obligatory Losses of Nitrogen and Whole-Body Turnover of Nitrogen

1977 ◽  
Vol 52 (5) ◽  
pp. 485-498 ◽  
Author(s):  
P. B. Pencharz ◽  
W. P. Steffee ◽  
W. Cochran ◽  
N. S. Scrimshaw ◽  
W. M. Rand ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Nitrogen Balance ◽  
Growth And Development ◽  
Term Infant ◽  
Nitrogen Losses ◽  
Whole Body ◽  
Nitrogen Flux ◽  
Body Protein ◽  
Mean Values ◽  
The Mean

1. Aspects of nitrogen metabolism in the human neonate were assessed in one full-term infant and six premature infants by means of nitrogen-balance measurements, estimates of obligatory nitrogen losses and determinations of whole-body nitrogen turnover. 2. Our data indicate that the mean protein requirement for maintenance is 1·1 g of protein day−1 kg−1 and that 3·8 g of protein day−1 kg−1 should be sufficient for adequate growth in healthy premature babies. 3. The mean obligatory urinary, faecal and total nitrogen losses were estimated to be 24, 106 and 145 mg day−1 kg−1 respectively. These figures are compared with published values for older infants, and the possible metabolic basis for changes in nitrogen losses during growth and development is discussed. 4. Mean values for whole-body protein synthesis and breakdown were 26·3 ± 7·0 and 23·8 ± 7·4 g of protein day−1 kg−1 respectively. Dietary nitrogen intake accounted for 6–18% of the nitrogen flux through the metabolic pool; urea excretion accounted for 2% of the nitrogen flux. 5. The net protein gain, estimated from nitrogen-balance data, accounted for 9·6% of total daily protein synthesis. 6. These results are discussed in relation to published estimates of whole-body protein synthesis and breakdown at various ages. Their possible significance in the assessment of a ‘maintenance’ requirement for protein and amino acids during the period of rapid growth and development is also considered.

scholarly journals Assessing the whole-body protein synthetic response to feeding in vivo in human subjects

2021 ◽  
pp. 1-9
Author(s):  
Jorn Trommelen ◽  
Luc J. C. van Loon
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Protein Intake ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Human Subjects ◽  
Whole Body ◽  
Body Protein ◽  
Breakdown Rates

All tissues are in a constant state of turnover, with a tightly controlled regulation of protein synthesis and breakdown rates. Due to the relative ease of sampling skeletal muscle tissue, basal muscle protein synthesis rates and the protein synthetic responses to various anabolic stimuli have been well defined in human subjects. In contrast, only limited data are available on tissue protein synthesis rates in other organs. Several organs such as the brain, liver and pancreas, show substantially higher (basal) protein synthesis rates when compared to skeletal muscle tissue. Such data suggest that these tissues may also possess a high level of plasticity. It remains to be determined whether protein synthesis rates in these tissues can be modulated by external stimuli. Whole-body protein synthesis rates are highly responsive to protein intake. As the contribution of muscle protein synthesis rates to whole-body protein synthesis rates is relatively small considering the large amount of muscle mass, this suggests that other organ tissues may also be responsive to (protein) feeding. Whole-body protein synthesis rates in the fasted or fed state can be quantified by measuring plasma amino acid kinetics, although this requires the production of intrinsically labelled protein. Protein intake requirements to maximise whole-body protein synthesis may also be determined by the indicator amino acid oxidation technique, but the technique does not allow the assessment of actual protein synthesis and breakdown rates. Both approaches have several other methodological and inferential limitations that will be discussed in detail in this paper.

Protein coingestion stimulates muscle protein synthesis during resistance-type exercise

2008 ◽  
Vol 295 (1) ◽  
pp. E70-E77 ◽  
Author(s):  
Milou Beelen ◽  
René Koopman ◽  
Annemie P. Gijsen ◽  
Hanne Vandereyt ◽  
Arie K. Kies ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Muscle Protein ◽  
Protein Hydrolysate ◽  
Muscle Protein Synthesis ◽  
Nutritional Intervention ◽  
Whole Body ◽  
Exercise Session ◽  
Body Protein ◽  
Fed State ◽  
Breakdown Rates

In contrast to the effect of nutritional intervention on postexercise muscle protein synthesis, little is known about the potential to modulate protein synthesis during exercise. This study investigates the effect of protein coingestion with carbohydrate on muscle protein synthesis during resistance-type exercise. Ten healthy males were studied in the evening after they consumed a standardized diet throughout the day. Subjects participated in two experiments in which they ingested either carbohydrate or carbohydrate with protein during a 2-h resistance exercise session. Subjects received a bolus of test drink before and every 15 min during exercise, providing 0.15 g·kg−1·h−1 carbohydrate with (CHO + PRO) or without (CHO) 0.15 g·kg−1·h−1 protein hydrolysate. Continuous intravenous infusions with l-[ ring-13C6]phenylalanine and l-[ ring-2H2]tyrosine were applied, and blood and muscle biopsies were collected to assess whole body and muscle protein synthesis rates during exercise. Protein coingestion lowered whole body protein breakdown rates by 8.4 ± 3.6% ( P = 0.066), compared with the ingestion of carbohydrate only, and augmented protein oxidation and synthesis rates by 77 ± 17 and 33 ± 3%, respectively ( P < 0.01). As a consequence, whole body net protein balance was negative in CHO, whereas a positive net balance was achieved after the CHO + PRO treatment (−4.4 ± 0.3 vs. 16.3 ± 0.4 μmol phenylalanine·kg−1·h−1, respectively; P < 0.01). In accordance, mixed muscle protein fractional synthetic rate was 49 ± 22% higher after protein coingestion (0.088 ± 0.012 and 0.060 ± 0.004%/h in CHO + PRO vs. CHO treatment, respectively; P < 0.05). We conclude that, even in a fed state, protein coingestion stimulates whole body and muscle protein synthesis rates during resistance-type exercise.

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