scholarly journals Lysine and Threonine Restriction Reproduced the Lower Synthesis but Not the Higher Catabolism of Liver and Muscle Protein of Severely Protein Restricted Growing Rats

2021 ◽  
Vol 5 (Supplement_2) ◽  
pp. 519-519
Author(s):  
Gaëtan Roisné-Hamelin ◽  
Joanna Moro ◽  
Nicolas Delahaye ◽  
Juliane Calvez ◽  
Catherine Chaumontet ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Portal Vein ◽  
Lean Body Mass ◽  
Body Mass ◽  
Protein Turnover ◽  
Vena Cava ◽  
Synthesis Rate ◽  
Severe Restriction ◽  
Growing Rats

Abstract Objectives The availability of indispensable amino acids (IAA) modulates protein turnover. More particularly AAI deficiency reduces protein synthesis while the consequence on proteolysis remains unclear. The present study aims to evaluate the specific response of both protein synthesis and proteolysis to a diet restricted on one strictly indispensable IAA, either lysine or threonine Methods Sixty-four growing rats were divided into 8 groups (n = 8/group). They were fed for 3 weeks isocaloric diets composed with different levels of lysine or threonine (L or T), 15, 25, 40, 60, 75, 100 or 170% of the theoretical lysine/threonine requirements. At the end of the experiment, rats were injected with valine13C and tissues and biological fluids were collected for gene expression measurement and blood amino acids (AA). Protein synthesis rate (Fractional and Absolute rate synthesis, ie FSR, ASR) were determined in liver and muscle. Statistical analysis was done by 1- or 2-factor ANOVA, when data were repeated. Results Severe (L/T15, L/T25) and moderate (T40) lysine or threonine deficiency resulted in a decrease in body weight gain due to a decrease in lean body mass. Severe restriction (L15, T15, T25) decreased the muscle FSR whereas no effect was observed in the liver. When the rate of protein synthesis was expressed per tissue, the ASR was decreased by severe restriction of lysine and threonine in liver and muscle and by moderate threonine deficiency (T40, T60, T75) in muscle. In liver, no effect of lysine and threonine on proteolysis was observed. In muscle, only severe lysine (L15) deficiency increased proteolysis. Dietary lysine deficiency induced a decrease in lysine concentration in the portal vein and in the vena cava whereas for threonine deficiency, all AAIs except threonine were decreased in the portal vein and vena cava. Conclusions These results indicate that the decreased protein synthesis is the primary mechanism involved in decreased lean body mass in response to the severe deficiency in a single AAI. Deficiency of a single AAI reproduce the effect of the low protein diet on protein synthesis. Lysine and threonine deficiency differently affect for a part protein turnover probably in relation with the tissue where they are metabolized. Funding Sources This study was funded by the doctoral school ABIES and AlimH-INRAE department.

Myofibrillar protein synthesis in young and old men

1993 ◽  
Vol 264 (5) ◽  
pp. E693-E698 ◽  
Author(s):  
S. Welle ◽  
C. Thornton ◽  
R. Jozefowicz ◽  
M. Statt
Keyword(s):  
Protein Synthesis ◽  
Lean Body Mass ◽  
Body Mass ◽  
Myofibrillar Protein ◽  
Whole Body ◽  
Synthesis Rate ◽  
Body Protein ◽  
Creatinine Excretion ◽  
Significant Difference ◽  
Myofibrillar Protein Synthesis

We tested the hypothesis that healthy older men (> 60 yr old) have a slower rate of myofibrillar protein synthesis than young men (< 35 yr old). Myofibrillar protein synthesis was determined by the in vivo incorporation of L-[1-13C]leucine into myofibrillar proteins obtained by muscle biopsy. Subjects were eight young (21-31 yr) and eight older (62-81 yr) men, all healthy and moderately active. There was no significant difference in the mean height and weight of the two age groups, but the older group had 12% less lean body mass (determined by 40K counting) and 21% less muscle mass (estimated by urinary creatinine excretion). Upper leg strength was approximately one-third lower in the older subjects according to isokinetic dynamometry. The fractional rate of myofibrillar protein synthesis was 28% slower in the older group (0.039 +/- 0.009 vs. 0.054 +/- 0.010 %/h, mean +/- SD, P < 0.01). Total myofibrillar protein synthesis, estimated as total myofibrillar mass (from creatinine excretion) times the fractional synthesis rate, was 44% slower in the older group (1.4 vs. 2.5 g/h, P < 0.001). Whole body protein synthesis, assessed as the difference between leucine disappearance rate and leucine oxidation, was marginally slower (8%, P = 0.10) in the older group, but not when the data were adjusted for lean body mass. Myofibrillar protein synthesis was a smaller fraction of whole body protein synthesis in the older group (12 vs. 19%). Reduced myofibrillar protein synthesis may be an important mechanism of the muscle atrophy associated with aging.

scholarly journals Impact of prolonged leucine supplementation on protein synthesis and lean growth in neonatal pigs

2015 ◽  
Vol 309 (6) ◽  
pp. E601-E610 ◽  
Author(s):  
Daniel A. Columbus ◽  
Julia Steinhoff-Wagner ◽  
Agus Suryawan ◽  
Hanh V. Nguyen ◽  
Adriana Hernandez-Garcia ◽  
...  
Keyword(s):  
Body Weight ◽  
Protein Synthesis ◽  
Lean Body Mass ◽  
Body Mass ◽  
Mtor Signaling ◽  
Synthesis Rate ◽  
Longissimus Dorsi ◽  
Leucine Supplementation ◽  
Neonatal Pigs ◽  
Lean Growth

Most low-birth weight infants experience extrauterine growth failure due to reduced nutrient intake as a result of feeding intolerance. The objective of this study was to determine whether prolonged enteral leucine supplementation improves lean growth in neonatal pigs fed a restricted protein diet. Neonatal pigs ( n = 14–16/diet, 5 days old, 1.8 ± 0.3 kg) were fed by gastric catheter a whey-based milk replacement diet with either a high protein (HP) or restricted protein (RP) content or RP supplemented with leucine to the same level as in the HP diet (RPL). Pigs were fed 40 ml·kg body wt−1·meal−1 every 4 h for 21 days. Feeding the HP diet resulted in greater total body weight and lean body mass compared with RP-fed pigs ( P < 0.05). Masses of the longissimus dorsi muscle, heart, and kidneys were greater in the HP- than RP-fed pigs ( P < 0.05). Body weight, lean body mass, and masses of the longissimus dorsi, heart, and kidneys in pigs fed the RPL diet were intermediate to RP- and HP-fed pigs. Protein synthesis and mTOR signaling were increased in all muscles with feeding ( P < 0.05); leucine supplementation increased mTOR signaling and protein synthesis rate in the longissimus dorsi ( P < 0.05). There was no effect of diet on indices of protein degradation signaling in any tissue ( P > 0.05). Thus, when protein intake is chronically restricted, the capacity for leucine supplementation to enhance muscle protein accretion in neonatal pigs that are meal-fed milk protein-based diets is limited.

scholarly journals Comparable Organ Protein Fractional Synthesis Rate of High and Low-Active Mice

2020 ◽  
Vol 4 (Supplement_2) ◽  
pp. 1750-1750
Author(s):  
Kristina Cross ◽  
Jorge Granados ◽  
Gabriella Ten Have ◽  
John Thaden ◽  
J Timothy Lightfoot ◽  
...  
Keyword(s):  
Physical Activity ◽  
Lean Body Mass ◽  
Body Mass ◽  
Physical Activity Level ◽  
Protein Turnover ◽  
Activity Level ◽  
Synthesis Rate ◽  
Activity Regulation ◽  
Fractional Synthesis Rate ◽  
Fractional Synthesis

Abstract Objectives With the rise in physical inactivity and its related diseases, it is necessary to understand the mechanisms involved in physical activity regulation. Scientists have explored physical activity regulation by investigating various physiological mechanisms involving hormones, neurotransmitters, and genetics; however, little is known about the role of metabolism on physical activity level. We hypothesize that protein turnover in specific organs like the muscle is higher in mice previously exhibiting high physical activity levels, as a mechanism to adapt to the increased demand. Therefore, we studied protein fractional synthesis rate (FSR) in tissues of inherently high and low active mice. Methods In order to study protein FSR of various organs, we assessed 12-week-old male inherently low-active (LA) mice (n = 23, lean body mass: 21.0 ± 1.1 g, C3H/HeJ strain) and high active (HA) mice (n = 20, lean body mass: 22.5 ± 1.3, C57L/J strain). One day before tissue collection, a D2O bolus was administered via intraperitoneal injection, and mice were provided D2O enriched drinking water to enrich the total body water to about 5% D2O. Eleven tissues (kidney, heart, lung, muscle, fat, jejunum, ileum, liver, brain, skin, and bone) were collected and analyzed for enrichment of alanine in the intracellular and protein-bound pool (LC-MS/MS). FSR was calculated as -ln(1-enrichment) as fraction per day. Data are mean ± SE (unpaired t-test: GraphPad Prism 8.2). Results We did not find significant differences between protein FSR of HA and LA mice in any measured organ. Example: Protein FSR (fraction/day): muscle (LA: 0.0326±-0.0026, HA: 0.0331 ± 0.0018, P = 0.8673), liver (0.3568 ± 0.0219, 0.3499 ± 0.0217, P = 0.8263), brain (0.0981 ± 0.0056, 0.1041 ± 0.0063, P = 0.4758). Conclusions The observed lack of significant differences in high and low-active mice suggests that differences in specific organ tissue protein turnover may not be a mechanism regulating inherent physical activity level. Since protein turnover is representative of the ability to adapt through upregulation and downregulation of metabolic processes, these results show that high-active mice are inherently no more equipped for metabolic regulation than the low active mice. Funding Sources Sydney and J.L. Huffines Institute for Sports Medicine, Human Performance Student Research Grant and CTRAL Grant.

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 The effect of protein depletion and repletion on muscle-protein turnover in the chick

1981 ◽  
Vol 194 (3) ◽  
pp. 811-819 ◽  
Author(s):  
M L MacDonald ◽  
R W Swick
Keyword(s):  
Protein Synthesis ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Control Diet ◽  
Breast Muscle ◽  
Synthesis Rate ◽  
Protein Depletion ◽  
Protein Mass ◽  
Fractional Rate

Rates of growth and protein turnover in the breast muscle of young chicks were measured in order to assess the roles of protein synthesis and degradation in the regulation of muscle mass. Rates of protein synthesis were measured in vivo by injecting a massive dose of L-[1-14C]valine, and rates of protein degradation were estimated as the difference between the synthesis rate and the growth rate of muscle protein. In chicks fed on a control diet for up to 7 weeks of age, the fractional rate of synthesis decreased from 1 to 2 weeks of age and then changed insignificantly from 2 to 7 weeks of age, whereas DNA activity was constant for 1 to 7 weeks. When 4-week-old chicks were fed on a protein-free diet for 17 days, the total amount of breast-muscle protein synthesized and degraded per day and the amount of protein synthesized per unit of DNA decreased. Protein was lost owing to a greater decrease in the rate of protein synthesis, as a result of the loss of RNA and a lowered RNA activity. When depleted chicks were re-fed the control diet, rapid growth was achieved by a doubling of the fractional synthesis rate by 2 days. Initially, this was a result of increased RNA activity; by 5 days, the RNA/DNA ratio also increased. There was no evidence of a decrease in the fractional degradation rate during re-feeding. These results indicate that dietary-protein depletion and repletion cause changes in breast-muscle protein mass primarily through changes in the rate of protein synthesis.

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.

AMINO ACID UTILIZATION AND PROTEIN SYNTHESIS IN THE OVINE FETUS IN UTERO

1984 ◽  
Vol 64 (5) ◽  
pp. 287-288 ◽  
Author(s):  
D. D. KITTS ◽  
A. L. SCHAEFER ◽  
C. R. KRISHNAMURTI
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Key Words ◽  
Protein Turnover ◽  
In Utero ◽  
Intermediary Metabolites ◽  
Tissue Protein ◽  
Amino Acid Utilization ◽  
Ovine Fetus

The utilization of amino acids in chronically catheterized ovine fetuses was measured by isotopic and nonisotopic procedures. Extensive incorporation of amino acid carbon into tissue protein was accompanied by high protein turnover and recycling rates of amino acid carbon. Alternative utilization of amino acids included oxidation and conversion into intermediary metabolites. Key words: Amino acids, utilization, fetus

scholarly journals Amino Acid Supplementation Increases Lean Body Mass, Basal Muscle Protein Synthesis, and Insulin-Like Growth Factor-I Expression in Older Women

2009 ◽  
Vol 94 (5) ◽  
pp. 1630-1637 ◽  
Author(s):  
Edgar L. Dillon ◽  
Melinda Sheffield-Moore ◽  
Douglas Paddon-Jones ◽  
Charles Gilkison ◽  
Arthur P. Sanford ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Growth Factor ◽  
Older Women ◽  
Lean Body Mass ◽  
Body Mass ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Amino Acid Supplementation ◽  
Factor I

Enteral glutamine stimulates protein synthesis and decreases ubiquitin mRNA level in human gut mucosa

2003 ◽  
Vol 285 (2) ◽  
pp. G266-G273 ◽  
Author(s):  
Moïse Coëffier ◽  
Sophie Claeyssens ◽  
Bernadette Hecketsweiler ◽  
Alain Lavoinne ◽  
Philippe Ducrotté ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Cathepsin D ◽  
Mrna Level ◽  
Mass Spectrometry Analysis ◽  
Whole Body ◽  
Synthesis Rate ◽  
Mrna Levels ◽  
Human Gut ◽  
Mucosal Protein

Effects of glutamine on whole body and intestinal protein synthesis and on intestinal proteolysis were assessed in humans. Two groups of healthy volunteers received in a random order enteral glutamine (0.8 mmol·kg body wt-1·h-1) compared either to saline or isonitrogenous amino acids. Intravenous [2H5]phenylalanine and [13C]leucine were simultaneously infused. After gas chromatography-mass spectrometry analysis, whole body protein turnover was estimated from traced plasma amino acid fluxes and the fractional synthesis rate (FSR) of gut mucosal protein was calculated from protein and intracellular phenylalanine and leucine enrichments in duodenal biopsies. mRNA levels for ubiquitin, cathepsin D, and m-calpain were analyzed in biopsies by RT-PCR. Glutamine significantly increased mucosal protein FSR compared with saline. Glutamine and amino acids had similar effects on FSR. The mRNA level for ubiquitin was significantly decreased after glutamine infusion compared with saline and amino acids, whereas cathepsin D and m-calpain mRNA levels were not affected. Enteral glutamine stimulates mucosal protein synthesis and may attenuate ubiquitin-dependent proteolysis and thus improve protein balance in human gut.

The single-biopsy approach in determining protein synthesis in human slow-turning-over tissue: use of flood-primed, continuous infusion of amino acid tracers

2014 ◽  
Vol 306 (11) ◽  
pp. E1330-E1339 ◽  
Author(s):  
Lars Holm ◽  
Søren Reitelseder ◽  
Kasper Dideriksen ◽  
Rie H. Nielsen ◽  
Jacob Bülow ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Continuous Infusion ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Tissue Biopsy ◽  
Infusion Protocol

Muscle protein synthesis (MPS) rate is determined conventionally by obtaining two or more tissue biopsies during a primed, continuous infusion of a stable isotopically labeled amino acid. The purpose of the present study was to test whether tracer priming given as a flooding dose, thereby securing an instantaneous labeling of the tissue pools of free tracee amino acids, followed by a continuous infusion of the same tracer to maintain tracer isotopic steady state, could be used to determine the MPS rate over a prolonged period of time by obtaining only a single tissue biopsy. We showed that the tracer from the flood prime appeared immediately in the muscle free pool of amino acids and that this abundance could be kept constant by a subsequent continuous infusion of the tracer. When using phenylalanine as tracer, the flood-primed, continuous infusion protocol does not stimulate the MPS rate per se. In conclusion, the flood-primed, continuous infusion protocol using phenylalanine as tracer can validly be used to measure the protein synthesis rate in human in vivo experiments by obtaining only a single tissue biopsy after a prolonged infusion period.

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