Splanchnic and whole body L-[1-13C,15N]leucine kinetics in relation to enteral and parenteral amino acid supply

1992 ◽  
Vol 262 (5) ◽  
pp. E687-E694 ◽  
Author(s):  
Y. M. Yu ◽  
J. F. Burke ◽  
J. A. Vogt ◽  
L. Chambers ◽  
V. R. Young
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Jugular Vein ◽  
Whole Body ◽  
Protein Breakdown ◽  
Metabolic Fate ◽  
Amino Acid Solution ◽  
Leucine Kinetics ◽  
Body Parameters ◽  
Acid Administration

The effect of the route of administration of a complete amino acid solution (0.24 g.kg-1.h-1) on leucine (Leu) and alpha-ketoisocaproate (KIC) metabolism in the splanchnic region (Sp) was assessed in nine chronically catherized mongrel dogs receiving, for 6 h, amino acids by jugular vein (PN feeding). Results were compared with those obtained previously [Y. M. Yu, D. A. Wagner, E. E. Tredget, J.A. Waleszewski, J. F. Burke, and V. R. Young. Am. J. Physiol. 259 (Endocrinol. Metab. 22): E36-E51, 1990] in eight dogs similarly studied but given amino acids by constant enteral feeding (EN). We used primed continuous intravenous infusions of L-[1-13C,15N]Leu and measurements of arteriovenous isotope and Leu balance across the gut, liver, and Sp to estimate parameters of whole body and organ Leu metabolism [Leu-N and Leu-C flux, Leu----KIC; KIC----Leu, Leu oxidation and rates of Leu appearance (B) from and disappearance (S) into proteins]. Whole body Leu kinetics were the same for both routes of amino acid administration. With PN, KIC----Leu, Leu----KIC, and total metabolic processing were lower than for EN in Sp, and overall Leu balance (S - B) was higher in Sp for EN. Leu appearance from protein breakdown in gut was higher with PN. The rate of KIC----Leu was higher in liver for EN. These findings reveal that route of amino acid (Leu) administration, under these acute feeding conditions, alters the processing and metabolic fate of Leu in Sp but that whole body parameters of Leu metabolism are stable. The implications of these metabolic findings in relation to the maintenance of intestinal function and integrity are discussed.

Amino acids suppress proteolysis independent of insulin throughout the neonatal period

1997 ◽  
Vol 272 (4) ◽  
pp. E592-E599 ◽  
Author(s):  
B. B. Poindexter ◽  
C. A. Karn ◽  
J. A. Ahlrichs ◽  
J. Wang ◽  
C. A. Leitch ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Neonatal Period ◽  
Essential Amino Acids ◽  
Whole Body ◽  
Amino Acid Availability ◽  
Dose Dependent Fashion ◽  
Term Newborns ◽  
Dose Dependent ◽  
Acid Administration

To determine how increased amino acid availability alters rates of whole body proteolysis and the irreversible catabolism of the essential amino acids leucine and phenylalanine throughout the neonatal period, leucine and phenylalanine kinetics were measured under basal conditions and in response to intravenous amino acids in two separate groups of healthy, full-term newborns (at 3 days and 3 wk of age). The endogenous rates of appearance of leucine and phenylalanine (reflecting proteolysis) were suppressed equally in both groups and in a dose-dependent fashion (by approximately 10% with 1.2 g x kg(-1) x day(-1) and by approximately 20% with 2.4 g x kg(-1) x day(-1)) in response to intravenous amino acid delivery. Insulin concentrations remained unchanged from basal values during amino acid administration. The irreversible catabolism of leucine and phenylalanine increased in a stepwise fashion in response to intravenous amino acids; again, no differences were observed between the two groups. This study clearly demonstrates that the capacity to acutely increase rates of leucine oxidation and phenylalanine hydroxylation is fully present early in the neonatal period in normal newborns. Furthermore, these data suggest that amino acid availability is a primary regulator of proteolysis in normal newborns throughout the neonatal period.

Whole body protein kinetics in women: effect of pregnancy and IDDM during anabolic stimulation

2000 ◽  
Vol 279 (5) ◽  
pp. E978-E988 ◽  
Author(s):  
Paul G. Whittaker ◽  
Choy H. Lee ◽  
Roy Taylor
Keyword(s):  
Amino Acids ◽  
Type 1 Diabetes ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Protein Metabolism ◽  
Whole Body ◽  
Protein Breakdown ◽  
Body Protein ◽  
In Pregnancy

The effects of pregnancy and type 1 diabetes [insulin-dependent diabetes mellitus (IDDM)] on protein metabolism are still uncertain. Therefore, six normal and five IDDM women were studied during and after pregnancy, using [13C]leucine and [2H5]phenylalanine with a hyperinsulinemic-euglycemic clamp and amino acid infusion. Fasting total plasma amino acids were lower in pregnancy in normal but not IDDM women (2,631 ± 427 vs. 2,057 ± 471 and 2,523 ± 430 vs. 2,500 ± 440 μmol/l, respectively). Whole body protein breakdown (leucine) increased in pregnancy [change in normal (ΔN) and IDDM women (ΔD) 0.59 ± 0.40 and 0.48 ± 0.26 g · kg−1 · day−1, both P < 0.001], whereas reductions in protein breakdown due to insulin/amino acids (ΔN −0.57 ± 0.19, ΔD −0.58 ± 0.20 g · kg−1 · day−1, both P < 0.001) were unaffected by pregnancy. Protein breakdown in IDDM women was not higher than normal, and neither pregnancy nor type 1 diabetes altered the insulin sensitivity of amino acid turnover. Nonoxidized leucine disposal (protein synthesis) increased in pregnancy (ΔN 0.67 ± 0.45, ΔD 0.64 ± 0.34 g · kg−1 · day−1, both P < 0.001). Pregnancy reduced the response of phenylalanine hydroxylation to insulin/amino acids in both groups (ΔN −1.14 ± 0.74, ΔD −1.12 ± 0.77 g · kg−1 · day−1, both P < 0.05). These alterations may enable amino acid conservation for protein synthesis and accretion in late pregnancy. Well-controlled type 1 diabetes caused no abnormalities in the regulation of basal or stimulated protein metabolism.

Effects of early amino acid administration during total parenteral nutrition on protein metabolism in pre-term infants

1992 ◽  
Vol 82 (2) ◽  
pp. 199-203 ◽  
Author(s):  
R. A. van Lingen ◽  
J. B. van Goudoever ◽  
I. H. T. Luijendijk ◽  
J. L. D. Wattimena ◽  
P. J. J. Sauer
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Birth Weight ◽  
Amino Acid ◽  
Protein Breakdown ◽  
Protein Balance ◽  
15N Enrichment ◽  
Group A ◽  
Group B ◽  
Acid Administration

1. We investigated the effects of starting amino acid administration on post-natal day 2 on protein turnover and nitrogen balance in appropriate-for-gestational-age, very-low-birth-weight infants. Eighteen infants were divided into two groups. Group A received from day 2 onwards an amino acid solution, whereas group B started on this solution after day 4. Both groups were exclusively parenterally fed, 200 kJ day−1 kg−1 on post-natal days 3 and 4. Group A (birth weight 1.5 ± 0.3 kg) received 4.6 g of glucose, 1.9 g of fat and 2.3 g of amino acids day−1 kg−1 body weight. Group B (birth weight 1.4 ± 0.2 kg) received 7.0 g of glucose and 1.9 g of fat day−1 kg−1 body weight. 2. At post-natal day 3, a primed constant infusion of 3 mg of [15N]glycine day−1 kg−1 was given. Protein flux, protein synthesis and protein breakdown were calculated from the 15N enrichment in urinary ammonia. In five out of nine infants in group B no plateau of 15N enrichment in urinary urea could be detected, whereas in group A two out of nine infants did not reach a plateau. For this reason we did not use the end product urea for our calculations. 3. The administration of the amino acids resulted in a higher protein flux (6.9 ± 1.5 g day−1 kg−1 versus 5.2 ± 0.9 g day−1 kg−1) and a higher protein synthesis rate (6.0 ± 1.4 g day−1 kg−1 versus 4.6 ± 0.8 g day−1 kg−1) in group A. There was no statistically significant difference in protein breakdown. The administration of amino acids reversed a negative protein balance (−0.6 ± 0.2 g day−1 kg−1) into a positive one (1.4 ± 0.2 g day−1 kg−1. No adverse effects of the amino acid infusion were seen. 4. We conclude that the early introduction of amino acids has, even at this relatively low energy intake of 200 kJ day−1 kg−1, a positive effect on protein balance by increasing protein synthesis.

Aspects of organ protein, amino acid and glucose metabolism in a porcine model of hypermetabolic sepsis

2003 ◽  
Vol 104 (2) ◽  
pp. 127-141 ◽  
Author(s):  
Maaike J. BRUINS ◽  
Nicolaas E.P. DEUTZ ◽  
Peter B. SOETERS
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Glucose Metabolism ◽  
Protein Metabolism ◽  
Porcine Model ◽  
Whole Body ◽  
Liver Protein ◽  
Protein Breakdown ◽  
Body Protein ◽  
Hyperdynamic Sepsis

Although glucose and protein metabolism have been investigated extensively in experimental models of hypodynamic sepsis, relatively little information is available regarding the compensated stage of sepsis. We investigated interorgan amino acid and glucose metabolism in a porcine model of compensated hyperdynamic sepsis. Fasting catheterized pigs received endotoxin (Escherichia coli lipopolysaccharide; 3µg·h-1·kg-1; intravenous) or saline (controls) and volume resuscitation over 24h to reproduce hyperdynamic sepsis. Primed-constant infusions of p-aminohippurate and 3H-labelled isotopes were used to measure glucose, amino acid and protein metabolism across the portal-drained viscera, liver and hindquarters (to represent muscle) at 0 and 24h of endotoxaemia. Whole-body protein and glucose flux were increased during hyperdynamic compensated sepsis. In endotoxaemic pigs, visceral protein was conserved, and hindquarter protein breakdown exceeded the increase in liver protein synthesis, resulting in net whole-body protein loss. Endotoxaemia increased hindquarter and visceral glycolysis and branched-chain amino acid transamination. The rate of efflux of glutamine and alanine from the hindquarters was higher than anticipated from protein breakdown, indicating de novo synthesis of these amino acids during endotoxaemia. In addition to the hindquarters, the portal-drained viscera provided substantial gluconeogenic amino acids and lactate to the liver. Although increased liver glutamate release constitutes an important nitrogen-sparing mechanism and carbon skeletons are effectively being cycled in glucose, net body protein is lost through increased ureagenesis during the hyperdynamic stage of sepsis. Specific amino acid requirements may develop in compensated hyperdynamic sepsis that is characterized by maintained organ perfusion and increased substrate utilization at the expense of body protein.

Measurement of protein turnover in the small intestine of lambs. 2. Effects of feed intake

1997 ◽  
Vol 128 (2) ◽  
pp. 233-246 ◽  
Author(s):  
S. A. NEUTZE ◽  
J. M. GOODEN ◽  
V. H. ODDY
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Small Intestine ◽  
Experimental Model ◽  
Feed Intake ◽  
Protein Turnover ◽  
Jugular Vein ◽  
Specific Radioactivity ◽  
Whole Body ◽  
Body Protein

This study used an experimental model, described in a companion paper, to examine the effects of feed intake on protein turnover in the small intestine of lambs. Ten male castrate lambs (∼ 10 months old) were offered, via continuous feeders, either 400 (n = 5) or 1200 (n = 5) g/day lucerne chaff, and mean experimental liveweights were 28 and 33 kg respectively. All lambs were prepared with catheters in the cranial mesenteric vein (CMV), femoral artery (FA), jugular vein and abomasum, and a blood flow probe around the CMV. Cr-EDTA (0·139 mg Cr/ml, ∼ 0·2 ml/min) was infused abomasally for 24 h and L-[2,6-3H]phenylalanine (Phe) (420±9·35 μCi into the abomasum) and L-[U-14C]phenylalanine (49·6±3·59 μCi into the jugular vein) were also infused during the last 8 h. Blood from the CMV and FA was sampled during the isotope infusions. At the end of infusions, lambs were killed and tissue (n = 4) and digesta (n = 2) samples removed from the small intestine (SI) of each animal. Transfers of labelled and unlabelled Phe were measured between SI tissue, its lumen and blood, enabling both fractional and absolute rates of protein synthesis and gain to be estimated.Total SI mass increased significantly with feed intake (P < 0·05), although not on a liveweight basis. Fractional rates of protein gain in the SI tended to increase (P = 0·12) with feed intake; these rates were −16·2 (±13·7) and 23·3 (±15·2) % per day in lambs offered 400 and 1200 g/day respectively. Mean protein synthesis and fractional synthesis rates (FSR), calculated from the mean retention of 14C and 3H in SI tissue, were both positively affected by feed intake (0·01 < P < 0·05). The choice of free Phe pool for estimating precursor specific radioactivity (SRA) for protein synthesis had a major effect on FSR. Assuming that tissue free Phe SRA represented precursor SRA, mean FSR were 81 (±15) and 145 (±24) % per day in lambs offered 400 and 1200 g/day respectively. Corresponding estimates for free Phe SRA in the FA and CMV were 28 (±2·9) and 42 (±3·5) % per day on 400 g/day, and 61 (±2·9) and 94 (±6·0) on 1200 g/day. The correct value for protein synthesis was therefore in doubt, although indirect evidence suggested that blood SRA (either FA or CMV) may be closest to true precursor SRA. This evidence included (i) comparison with flooding dose estimates of FSR, (ii) comparison of 3H[ratio ]14C Phe SRA in free Phe pools with this ratio in SI protein, and (iii) the proportion of SI energy use associated with protein synthesis.Using the experimental model, the proportion of small intestinal protein synthesis exported was estimated as 0·13–0·27 (depending on the choice of precursor) and was unaffected by feed intake. The contribution of the small intestine to whole body protein synthesis tended to be higher in lambs offered 1200 g/day (0·21) than in those offered 400 g/day (0·13). The data obtained in this study suggested a role for the small intestine in modulating amino acid supply with changes in feed intake. At high intake (1200 g/day), the small intestine increases in mass and CMV uptake of amino acids is less than absorption from the lumen, while at low intake (400 g/day), this organ loses mass and CMV uptake of amino acids exceeds that absorbed. The implications of these findings are discussed.

scholarly journals Quantitative Analysis of the Whole-Body Metabolic Fate of Branched-Chain Amino Acids

2019 ◽  
Vol 29 (2) ◽  
pp. 417-429.e4 ◽  
Author(s):  
Michael D. Neinast ◽  
Cholsoon Jang ◽  
Sheng Hui ◽  
Danielle S. Murashige ◽  
Qingwei Chu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Quantitative Analysis ◽  
Branched Chain Amino Acids ◽  
Whole Body ◽  
Metabolic Fate ◽  
Branched Chain

scholarly journals Nonessential amino acid usage for protein replenishment in humans: a method of estimation

2019 ◽  
Vol 110 (2) ◽  
pp. 255-264 ◽  
Author(s):  
Paolo Tessari
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Quality ◽  
Essential Amino Acids ◽  
World Health ◽  
Whole Body ◽  
Published Data ◽  
Total Proteins ◽  
Body Protein ◽  
Amino Acid Turnover

ABSTRACT Background Essential amino acids (EAAs) are key factors in determining dietary protein quality. Their RDAs have been estimated. However, although nonessential amino acids (NEAAs) are utilized for protein synthesis too, no estimates of their usage for body protein replenishment have been proposed so far. Objective The aim of this study was to provide minimum, approximate estimates of NEAA usage for body protein replenishment/conservation in humans. Methods A correlation between the pattern of both EAAs and NEAAs in body proteins, and their usage, was assumed. In order to reconstruct an “average” amino acid pattern/composition of total body proteins (as grams of amino acid per gram of protein), published data of relevant human organs/tissues (skeletal muscle, liver, kidney, gut, and collagen, making up ∼74% of total proteins) were retrieved. The (unknown) amino acid composition of residual proteins (∼26% of total proteins) was assumed to be the same as for the sum of the aforementioned organs excluding collagen. Using international EAA RDA values, an average ratio of EAA RDA to the calculated whole-body EAA composition was derived. This ratio was then used to back-calculate NEAA usage for protein replenishment. The data were calculated also using estimated organ/tissue amino acid turnover. Results The individual ratios of World Health Organization/Food and Agriculture Organization/United Nations University RDA to EAA content ranged between 1.35 (phenylalanine + tyrosine) and 3.68 (leucine), with a mean ± SD value of 2.72 ± 0.81. In a reference 70-kg subject, calculated NEAA usage for body protein replenishment ranged from 0.73 g/d for asparagine to 3.61 g/d for proline. Use of amino acid turnover data yielded similar results. Total NEAA usage for body protein replenishment was ∼19 g/d (45% of total NEAA intake), whereas ∼24 g/d was used for other routes. Conclusion This method may provide indirect minimum estimates of the usage of NEAAs for body protein replacement in humans.

The amino acid requirements of pigs for maintenance and for growth

1987 ◽  
Vol 1987 ◽  
pp. 60-60 ◽  
Author(s):  
M.F. Fuller ◽  
R. McWilliam ◽  
T.C. Wang
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Whole Body ◽  
Optimal Balance ◽  
Growing Pig ◽  
Amino Acid Requirements ◽  
Direct Experiment ◽  
Better Than

The optimal balance of amino acids in the diet of the growing pig was estimated by ARC (1981) on the basis of a number of disparate studies augmented by data on the amino acid composition of the whole body on the premise that the amino acids incorporated into accreted body proteins are the major determinant of requirements and that this pattern is not distorted by inequalities in the utilisation of individual amino acids. In an accompanying paper (Wang & Fuller, paper no. 91) an optimal pattern was derived by direct experiment which was shown to be utilised better than that described by ARC (1981). That pattern, however, which related to one particular rate of nitrogen input and the particular rate of protein accretion which that input supported, includes two components, a requirement for maintenance and a requirement for protein accretion. There is clear evidence from studies with rats and chicks that the optimal pattern of amino acids for maintenance and growth are quite different and so the optimal pattern for any particular rate of growth will depend on the relative contributions of the two components. The purpose of this experiment was to estimate both.

scholarly journals In vivo Determination of Amino Acid Bioavailability in Humans and Model Animals

2005 ◽  
Vol 88 (3) ◽  
pp. 923-934 ◽  
Author(s):  
Malcolm F Fuller ◽  
Daniel Tomé
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
The Body ◽  
Whole Body ◽  
Intestinal Lumen ◽  
Stable Isotope Labelling ◽  
Ileal Digestibility ◽  
Hydrolyzed Protein ◽  
Protein Free Diet

Abstract Because the digestion of many dietary proteins is incomplete, and because there is a continuous (but variable) entry into the intestinal lumen of endogenous protein and amino acid nitrogen that is also subject to digestion, the fluxes of nitrogen, amino acids, and protein in the gut exhibit a rather complicated pattern. Methods to distinguish and quantitate the endogenous and dietary components of nitrogen and amino acids in ileal chyme or feces include the use of a protein-free diet, the enzyme-hydrolyzed protein method, different levels of protein intake, multiple regression methods, and stable-isotope labelling of endogenous or exogenous amino acids. Assessment of bioavailability can be made, with varying degrees of difficulty, in man directly but, for routine evaluation of foods, the use of model animals is attractive for several reasons, the main ones being cost and time. Various animals and birds have been proposed as models for man but, in determining their suitability as a model, their physiological, enzymological, and microbiological differences must be considered. Fecal or ileal digestibility measurements, as well as apparent and true nitrogen and amino acid digestibility measurements, have very different nutritional significance and can, thus, be used for different objectives. Measurements at the ileal level are critical for determining amino acid losses of both dietary and endogenous origin, whereas measurements at the fecal level are critical in assessing whole-body nitrogen losses. A complementary and still unresolved aspect is to take into account the recycling of intestinal nitrogen and bacterial amino acids to the body.

scholarly journals Changes in Whole-Body Amino Acid Metabolism in Response to 2 Weeks of the Very-Low Calorie Diet Are Not Affected by Gender

2020 ◽  
Vol 4 (Supplement_2) ◽  
pp. 1700-1700
Author(s):  
Agata Wierzchowska-McNew ◽  
Mariëlle Engelen ◽  
Kristopher Knoop ◽  
Gabriella Ten Have ◽  
John Thaden
Keyword(s):  
Weight Loss ◽  
Amino Acid ◽  
Acid Metabolism ◽  
Whole Body ◽  
Protein Breakdown ◽  
Restricted Diet ◽  
Very Low Calorie Diet ◽  
Low Calorie ◽  
Low Calorie Diet ◽  
Calorie Diet

Abstract Objectives Very Low-Calorie Diet (VLCD) is an approved method to safely achieve substantial short-term weight loss in obese patients. We previously reported that two weeks of the VLCD maintains whole-body protein and amino acid turnover despite a large reduction in lean body mass. Since the observed effects on body weight (BW) and composition differed between men and women, we hypothesized that the changes in amino acid metabolism in a response to the calorie-restricted diet is gender-specific. Methods 34 morbidly obese adults (BMI: 42 ± 0.9 kg/m2, 10 males and 24 females) underwent a VLCD for 2 weeks consisting of 820 kcal/day and 105-grams protein/day. Before the start of the VLCD (baseline), the whole-body production (WBP) rates of multiple amino acids involved in protein metabolism (e.g., glycine (GLY), glutamine (GLN), phenylalanine (PHE), tyrosine (TYR), and arginine (ARG)) were measured after IV pulse administration of their stable isotopes. Weight loss and body composition by dual-energy X-ray absorptiometry were assessed after 2 weeks of the VLCD. Baseline plasma enrichments were measured by LC-MS/MS. Data are presented as mean ± SE. Statistics are performed by Pearson correlation tests. Results The magnitude of the BW loss after 2 weeks of the VLCD differed between males and females (7.0 ± 0.7 kg vs. 4.1 ± 0.2 kg, P &lt; 0.0001, respectively) with a higher reduction in lean body mass observed in men than women (4.3 ± 0.8 kg vs. 2.7 ± 0.4 kg, P &lt; 0.05). Although, females had significantly reduced baseline WBP of ARG (7.3% vs. 2%, P = 0.0027), GLY (22.8% vs. 3.6%, P &lt; 0.001), and PHE (4.8% vs. 3.1%, P = 0.018) in comparison to men, two weeks of the VLCD had a comparable effect on multiple amino acid WBP in both genders. Suppressed contractile myofibrillar protein breakdown rate was observed in both groups (13% vs. baseline, P = 0.02) with no gender difference in net protein breakdown (PHE to TYR conversion rate). Hence, increased catabolism in men cannot be explained by a different response to the 2 weeks of a calorie-restricted diet. Conclusions Despite gender differences in body weight loss and changes in composition in response to a Very Low-Calorie Diet, changes in whole-body amino acid kinetics are not differently affected in men and women. Funding Sources CTRAL Internal Funds.

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