scholarly journals Lysine requirements and whole-body protein turnover in growing pigs

1990 ◽  
Vol 63 (3) ◽  
pp. 503-513 ◽  
Author(s):  
D. N. Salter ◽  
A. I. Montgomery ◽  
Anna Hudson ◽  
D. B. Quelch ◽  
Rosemary J. Elliott
Keyword(s):  
Protein Synthesis ◽  
Protein Turnover ◽  
Protein Quality ◽  
Growing Pigs ◽  
Whole Body ◽  
Separate Experiment ◽  
Deficient Diet ◽  
Total N ◽  
Body Protein ◽  
Biological Value

The influence on protein accretion and whole-body protein turnover of changing dietary protein quality while maintaining constant energy intake was studied by varying the degree of lysine supplementation of a lysine-deficient barley-based diet given to growing pigs. Measurements of nitrogen metabolism and whole-body protein turnover, using both classical and 15N end-product methods following a single dose of lsqb;15N]glycine, were made in 49-kg male pigs given diets containing 109 g lysine-deficient protein/kg supplemented to make them (1) 'deficient', (2) 'adequate' and (3) 'in excess' with respect to lysine. The 15N dose and protein intake values used to calculate amino N flux from the cumulative urinary excretion of 15N in urea and ammonia were corrected respectively for apparent digestibilities of [15N]glycine and total N determined in a separate experiment in pigs fitted with simple ileal cannulas. N retention and biological value were significantly increased by lysine supplementation of the deficient diet to the 'adequate' level, but were not further increased by the higher level of supplementation. Rates of growth paralleled these changes. The poorer biological value of the unsupplemented diet 1 was shown also in a significantly higher excretion of urea N compared with diets 2 and 3. N digestibility was not markedly influenced by the level of lysine supplementation. Both whole-body protein synthesis and degradation increased markedly on 'adequate' supplementation of the diet with lysine, but did not increase further with an excess of lysine. It is concluded that the increase in protein accretion rate observed on supplementation of the diet with lysine was due to a greater increase in the rate of protein synthesis than of degradation, rather than a decrease in degradation rate.

scholarly journals Effects of the amount and quality of dietary protein on nitrogen metabolism and protein turnover of pigs

1987 ◽  
Vol 58 (2) ◽  
pp. 287-300 ◽  
Author(s):  
M. F. Fuller ◽  
P. J. Reeds ◽  
A. Cadenhead ◽  
B. Seve ◽  
T. Preston
Keyword(s):  
Dietary Protein ◽  
Protein Turnover ◽  
Growing Pigs ◽  
Whole Body ◽  
Urea Synthesis ◽  
Total N ◽  
Plasma Urea ◽  
Body Protein ◽  
N Retention

1. The interrelations between protein accretion and whole-body protein turnover were studied by varying the quantity and quality of protein given to growing pigs.2. Diets with 150 or 290g lysine-deficient protein/kg were given in hourly meals, with or without lysine supplementation, to female pigs (mean weight 47 kg).3. After the animals were adapted to the diets, a constant infusion of [14C]urea was given intra-arterially for 30 h, during the last 6 h of which an infusion of [4,5-3H] leucine was also infused at a constant rate. At the same time, yeast-protein labelled with15N was given in the diet for 50 h.4. The rate of urea synthesis was estimated from the specific radioactivity (SR) of plasma urea. The rate of leucine flux was estimated from the SR of plasma leucine. The irrevocable breakdown of leucine was estimated from the3H-labelling of body water. Total N flux was estimated from the16N-labelling of urinary urea.5. Addition of lysine to the low-protein diet significantly increased N retention, with a substantial reduction in leucine breakdown, but there was no significant change in the flux of leucine or of total N.6. Increasing the quantity of the unsupplemented protein also increased N retention significantly, with concomitant increases in leucine breakdown and in the fluxes of leucine and of total N.7. It is concluded that a doubling of protein accretion brought about by the improvement of dietary protein quality is not necessarily associated with an increased rate of whole-body protein turnover.

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 Muscle Protein Synthesis and Whole-Body Protein Turnover Responses to Ingesting Essential Amino Acids, Intact Protein, and Protein-Containing Mixed Meals with Considerations for Energy Deficit

Nutrients ◽  
2020 ◽  
Vol 12 (8) ◽  
pp. 2457 ◽  
Author(s):  
Jess A. Gwin ◽  
David D. Church ◽  
Robert R. Wolfe ◽  
Arny A. Ferrando ◽  
Stefan M. Pasiakos
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Energy Deficit ◽  
Whole Body ◽  
Intact Protein ◽  
Body Protein ◽  
Protein Feeding

Protein intake recommendations to optimally stimulate muscle protein synthesis (MPS) are derived from dose-response studies examining the stimulatory effects of isolated intact proteins (e.g., whey, egg) on MPS in healthy individuals during energy balance. Those recommendations may not be adequate during periods of physiological stress, specifically the catabolic stress induced by energy deficit. Providing supplemental intact protein (20–25 g whey protein, 0.25–0.3 g protein/kg per meal) during strenuous military operations that elicit severe energy deficit does not stimulate MPS-associated anabolic signaling or attenuate lean mass loss. This occurs likely because a greater proportion of the dietary amino acids consumed are targeted for energy-yielding pathways, whole-body protein synthesis, and other whole-body essential amino acid (EAA)-requiring processes than the proportion targeted for MPS. Protein feeding formats that provide sufficient energy to offset whole-body energy and protein-requiring demands during energy deficit and leverage EAA content, digestion, and absorption kinetics may optimize MPS under these conditions. Understanding the effects of protein feeding format-driven alterations in EAA availability and subsequent changes in MPS and whole-body protein turnover is required to design feeding strategies that mitigate the catabolic effects of energy deficit. In this manuscript, we review the effects, advantages, disadvantages, and knowledge gaps pertaining to supplemental free-form EAA, intact protein, and protein-containing mixed meal ingestion on MPS. We discuss the fundamental role of whole-body protein balance and highlight the importance of comprehensively assessing whole-body and muscle protein kinetics when evaluating the anabolic potential of varying protein feeding formats during energy deficit.

scholarly journals The influence of rumen volatile fatty acids on protein metabolism in growing lambs

1989 ◽  
Vol 62 (2) ◽  
pp. 297-310 ◽  
Author(s):  
H. A. Abdul–Razzaq ◽  
R. Bickerstaffe
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Protein Turnover ◽  
Turnover Rate ◽  
Volatile Fatty Acids ◽  
Acid Group ◽  
High Plasma ◽  
Whole Body ◽  
Body Protein ◽  
Tyrosine Oxidation

The effect of acetic or propionic acid rumen fermentation patterns on whole-body protein turnover, tissue protein synthetic rates and body composition was investigated in growing lambs. Protein turnover was assessed using a continuous intravenous infusion of [2,3-3H]tyrosine and tissue protein fractional synthetic rates (FSR) from the specific activities of plasma free, intracellular free and tissue bound tyrosine. Only the FSR of muscle tissue approached significance. The high FSR in the propionic group was attributed to the high plasma insulin concentration. Values for whole-body protein synthesis, corrected for tyrosine oxidation, were similar to those obtained by summating protein synthesis in individual tissues, confirming that tyrosine oxidation should be measured accurately if reliable whole-body protein synthesis values are required. Tyrosine oxidation and flux were high in the acetic acid group, suggesting that amino acids are used for gluconeogenesis. The high protein turnover rate probably ensures an adequate supply of gluconeogenic amino acids and that the penalty of mobilizing body proteins for gluconeogenic amino acids is minimal. In the propionic acid group, high plasma glucose and insulin concentrations were associated with a low protein turnover rate, high ratio of deposited: synthesized protein and a high body fat content. It is concluded that changing the proportion of ruminal volatile fatty acids influences protein turnover, protein synthesis and the efficiency of protein retention. Such factors probably contribute, indirectly, to the observed differences in body composition.

scholarly journals The end-product method of measuring whole-body protein turnover: a review of published results and a comparison with those obtained by leucine infusion

2005 ◽  
Vol 94 (2) ◽  
pp. 141-153 ◽  
Author(s):  
S. L. Duggleby ◽  
J. C. Waterlow
Keyword(s):  
Protein Synthesis ◽  
Gold Standard ◽  
Protein Turnover ◽  
Population Studies ◽  
Whole Body ◽  
Precursor Method ◽  
Body Protein ◽  
Short Account ◽  
Product Method ◽  
Pros And Cons

The present review summarizes the results of all published papers on whole-body protein turnover in man measured by [15N]glycine and the end-product method using both urea and ammonia. It begins with a short account of the underlying assumptions and the justification for the use of [15N]glycine. The results are then compared with those of a large sample of measurements by the ‘gold standard’ precursor method with continuous infusion of [13C]leucine. The pros and cons of the two methods are compared and it is suggested that there is a place for further work by the less invasive end-product method, particularly for population studies of the genetic, environmental and functional determinants of whole-body rates of protein synthesis.

Advances in stable isotope tracer methodology part 2: new thoughts about an “old” method—measurement of whole body protein synthesis and breakdown in the fed state

2019 ◽  
Vol 68 (1) ◽  
pp. 11-15 ◽  
Author(s):  
Robert R Wolfe ◽  
Sanghee Park ◽  
Il-Young Kim ◽  
Paul J Moughan ◽  
Arny A Ferrando
Keyword(s):  
Protein Synthesis ◽  
Dietary Protein ◽  
Protein Turnover ◽  
Peripheral Circulation ◽  
Whole Body ◽  
Balance Model ◽  
Body Protein ◽  
Fed State ◽  
Isotope Tracer ◽  
Tracer Dilution

Whole-body protein turnover (protein synthesis, breakdown, and net balance) model enables quantification of the response to a variety of circumstances, including the response to meal feeding. In the fed state, the whole-body protein turnover model requires taking account of the contribution of absorbed tracee to the observed total appearance of tracee in the peripheral blood (exogenous appearance, RaEXO). There are different approaches to estimating RaEXO. The use of an intrinsically labeled dietary protein is based on the overriding assumption that the appearance in the peripheral circulation of a tracer amino acid incorporated into a dietary protein is exactly proportional to the appearance of absorbed tracee. The bioavailability approach is based on the true ileal digestibility of the dietary protein and the irreversible loss of the tracee in the splanchnic bed via hydroxylation of the tracee (phenylalanine). Finally, RaEXO can be estimated as the increase above the basal rate of appearance of the tracee using traditional tracer dilution methodology. In this paper, we discuss the pros and cons of each approach and conclude that the bioavailability method is the least likely to introduce systematic errors and is therefore the preferable approach.

Effect of dietary protein and energy intakes on whole-body protein turnover and its contribution to heat production in chicks

1993 ◽  
Vol 69 (3) ◽  
pp. 681-688 ◽  
Author(s):  
K. Kita ◽  
T. Muramatsu ◽  
J. Okumura
Keyword(s):  
Protein Synthesis ◽  
Heat Production ◽  
Protein Turnover ◽  
Crude Protein ◽  
Total Heat ◽  
Interactive Effects ◽  
Whole Body ◽  
Small Range ◽  
Body Protein ◽  
Fractional Rate

A factorial 3 × 3 experiment was conducted with chicks to investigate the effect of manipulating crude protein (N × 6.25) intake (CPI) and metabolizable energyintake (MEI) simultaneously, in the range low to high (including adequate) levels with regard to the respective requirements, on whole-body protein turnover and its contribution to total heat production. The fractional rate of whole-body protein synthesis was increased curvilinearly by increasing MEI or CPI from low to high levels. In terms of absolute rates whole-body protein synthesis was enhanced by increasing MEI from low to adequate levels, the effect being greater at adequate and high CPI than at low CPI. The effect of varying CPI and MEI on whole-body protein degradation was similar, but less sensitive, to that on whole-body protein synthesis. Increasing MEI from low to high levels elevated totalheat production at all CPI levels. There were no interactive effects of varying CPI andMEI on the contribution of whole-body protein synthesis to total heat production, and in general the contribution increased with increasing CPI and decreased with increasing MEI.The contribution of whole-body protein synthesis to total heat production fell within a small range from 11.2 to 16.5%.

Chloroquine reduces whole body proteolysis in humans

1994 ◽  
Vol 267 (1) ◽  
pp. E183-E186 ◽  
Author(s):  
P. De Feo ◽  
E. Volpi ◽  
P. Lucidi ◽  
G. Cruciani ◽  
F. Santeusanio ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Protein Turnover ◽  
Plasma Concentrations ◽  
Whole Body ◽  
Body Protein ◽  
Leucine Kinetics ◽  
Lysosomal Proteolysis ◽  
Therapeutic Doses

The antimalaric drug chloroquine is a well known inhibitor of lysosomal proteolysis in vitro. The present study tests the hypothesis that therapeutic doses of the drug decrease proteolysis also in vivo in humans. Leucine kinetics were determined in 20 healthy volunteers given 12 and 1.5 h before the studies 250 and 500 mg, respectively, of chloroquine phosphate (n = 10) or similar tablets of placebo (n = 10). Chloroquine reduced the rates of leucine appearance, a measure of whole body proteolysis, from 2.45 +/- 0.08 to 2.19 +/- 0.08 mumol.kg-1.min-1 (P = 0.038) and those of nonoxidative leucine disposal, an estimate of whole body protein synthesis, from 2.16 +/- 0.08 to 1.95 +/- 0.06 mumol.kg-1.min-1 (P = 0.050). The drug resulted also in a marginally significant (P = 0.051) decrement in the plasma concentrations of glucose. The effects of chloroquine on protein turnover might be potentially useful in counteracting protein wasting complicating several catabolic diseases, whereas those on glucose metabolism can explain the sporadic occurrence of severe hypoglycemic episodes in malaria patients chronically treated with this drug.

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.

Whole body protein synthesis: studies with different amino acids in the rat

1989 ◽  
Vol 257 (5) ◽  
pp. E639-E646 ◽  
Author(s):  
C. Obled ◽  
F. Barre ◽  
D. J. Millward ◽  
M. Arnal
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Protein Turnover ◽  
Specific Radioactivity ◽  
Whole Body ◽  
Body Protein ◽  
Tissue Specific ◽  
Dose Method ◽  
Infusion Method

These studies were undertaken to determine to what extent constant infusion measurements and plasma sampling could provide sensible answers for rates of whole body protein turnover and also which amino acid would be the most representative probe of whole body protein turnover. Whole body protein synthesis rates were estimated in 70-g rats with L-[U-14C]threonine, L-[U-14C]lysine, L-[U-14C]tyrosine, L-[U-14C]phenylalanine, and L-[1-14C]leucine by either simultaneous tracer infusion of four amino acids or by injections of large quantities of 14C-labeled amino acids. In the infusion experiment, indirect estimates of whole body protein turnover based on free amino acid specific radioactivity and stochastic modeling were compared with direct measurement of the incorporation of the tracer into proteins. These two methods of analysis provided similar results for each amino acid, although in each case fractional synthesis rates were lower (by between 26 and 63%) when calculations were based on plasma rather than tissue specific radioactivity. With the flooding-dose method, whole body fractional protein synthesis rates were 41.4, 25.6, 31.1, and 31.4% with threonine, lysine, phenylalanine, and leucine, respectively. These values were similar to those obtained by the continuous infusion method using tissue specific radioactivity for threonine and lysine. For leucine, however, the flooding-dose method provided an intermediate value between the two estimates derived either from the plasma or the tissue specific radioactivity in the infusion method.(ABSTRACT TRUNCATED AT 250 WORDS)

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