Effects of a leucine-rich diet on body composition during nutritional recovery in rats (original) (raw)
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Nutrition (Burbank, Los Angeles County, Calif.), 2006
Acute administration of leucine has been shown to stimulate certain protein synthesis related anabolic processes. However, the effect of chronic leucine administration in a catabolic situation caused by food restriction (FR) has not been established. We therefore evaluated the effect of chronic leucine supplementation on the body composition and some indicators of protein nutritional status of rats submitted to FR. Adult male Wistar rats were submitted to 50% FR for 6 weeks. The control group received the AIN-93M diet and the leucine group received the same diet supplemented with 5.91 g L-leucine/kg ration. We then determined carcass chemical composition, serum leptin, albumin and total protein concentrations, and protein, DNA and RNA concentrations in gastrocnemius muscle and liver. No difference in final body weight was observed between groups. However, the leucine group presented a lower amount of body fat (P < 0.05). Leptin concentration showed a directly proportional correla...
Nutrition & Metabolism, 2016
Background: Many people believe in favourable effects of branched-chain amino acids (BCAAs; valine, leucine, and isoleucine), especially leucine, on muscle protein balance and consume BCAAs for many years. We determined the effects of the chronic intake of a BCAA-or leucine-enriched diet on protein and amino acid metabolism in fed and postabsorptive states. Methods: Rats were fed a standard diet, a diet with a high content of valine, leucine, and isoleucine (HVLID), or a high content of leucine (HLD) for 2 months. Half of the animals in each group were sacrificed in the fed state on the last day, and the other half were sacrificed after overnight fast. Protein synthesis was assessed using the flooding dose method (L-[3,4,5-3 H]phenylalanine), proteolysis on the basis of chymotrypsin-like activity (CHTLA) of proteasome and cathepsin B and L activities. Results: Chronic intake of HVLID or HLD enhanced plasma levels of urea, alanine and glutamine. HVLID also increased levels of all three BCAA and branched-chain keto acids (BCKA), HLD increased leucine, ketoisocaproate and alanine aminotransferase and decreased valine, ketovaline, isoleucine, ketoisoleucine, and LDL cholesterol. Tissue weight and protein content were lower in extensor digitorum longus muscles in the HLD group and higher in kidneys in the HVLID and HLD groups. Muscle protein synthesis in postprandial state was higher in the HVLID group, and CHTLA was lower in muscles of the HVLID and HLD groups compared to controls. Overnight starvation enhanced alanine aminotransferase activity in muscles, and decreased protein synthesis in gastrocnemius (in HVLID group) and extensor digitorum longus (in HLD group) muscles more than in controls. Effect of HVLID and HLD on CHTLA in muscles in postabsorptive state was insignificant. Conclusions: The results failed to demonstrate positive effects of the chronic consumption of a BCAA-enriched diet on protein balance in skeletal muscle and indicate rather negative effects from a leucine-enriched diet. The primary effects of both diets are an activated catabolism of BCAAs, which leads to an enhanced production of BCKA, alanine and glutamine and their utilization in visceral tissues and an impaired protein synthesis in postabsorptive state, particularly in fast-twitch (white) muscles.
Life Sciences, 2007
Although many studies have shown that amino acid ingestion acutely stimulates protein anabolism, only few studies have investigated whether long-term supplementation promotes changes in body composition. We therefore tested the hypothesis that l-leucine (LEU) and l-phenylalanine (PHE) supplementation might have a positive impact on the body composition of rats submitted to intermittent periods of food restriction and refeeding (weight cycling or WC). The WC protocol comprised three cycles, each consisting of 1 week of 50% food restriction followed by 2 weeks of ad libitum ingestion. The groups submitted to WC ingested the control diet (WC-CON) or the diet supplemented with LEU + PHE (WC-AA). A pair-fed group receiving the control diet (PF-CON) was used as a reference for the effects of WC. Although food intake was the same in all groups, higher body weight and energy efficiency were observed in the WC-AA group compared to the PF-CON and WC-CON groups although not significantly in relation to the latter. These results were the consequence of a significant increase of lean body mass and body protein content in the WC-AA group compared to the PF-CON and WC-CON groups. The WC-CON and WC-AA groups presented 36.1% and 18.9% more body fat, respectively, than the PF-CON group but this difference was not significant. Neither fasting insulin nor glucose concentration nor postprandial insulin secretion was significantly affected by the supplemented diet. In conclusion, supplementation with LEU + PHE improved the body composition profile of rats submitted to WC, mainly by increasing lean body mass and body protein content.
The Journal of nutrition, 2003
Acute leucine supplementation of the diet has been shown to blunt defects in postprandial muscle protein metabolism in old rats. This study was undertaken to determine whether the effect of leucine persists in a 10-d experiment. For this purpose, adult (9 mo) and old (21 mo) rats were fed a semiliquid 18.2 g/100 g protein standard diet during the 8-h dark period for 1 mo. Then, each group was given either a leucine-supplemented meal or an alanine-supplemented meal (as the control meal) for 1 h and the standard diet the rest of the feeding period. On d 10, rats were fed either no food (postabsorptive group) or the supplemented meal for 1 h. Muscle protein synthesis was assessed in vivo 90-120 min after meal distribution using the flooding dose method (1-(13)C phenylalanine). Leucinemia was similar in rats of both ages in the postabsorptive state. Postprandial plasma leucine concentrations were one- to twofold greater after the leucine meal than after the control meal. In the postabso...
Protein v. enzymic protein hydrolysates. Nitrogen utilization in starved rats
British Journal of Nutrition, 1995
The present study was carried out to compare the effects of four isoenergetic and isonitrogenous diets on the N utilization, total serum protein concentration and serum amino acid profile in starved rats at weaning. These diets differed only in the molecular form of two milk proteins (whey protein and casein), which were either native or partly hydrolysed. Male Wistar rats at weaning were fasted for 3 d and then refed with one of the four diets for 48 h. No differences were observed in the body weight gain, protein digestibility and total serum protein concentration between groups after the refeeding period and all the N balances were positive. N retention was higher in the two groups of rats given the protein-hydrolysate-based diets compared with those given the intact-protein-based diets. This was associated with a lower urinary N excretion in rats, given the whey-protein-hydrolysate and the casein-hydrolysate diets. Despite this fact, the serum amino acid pattern of rats given th...
The Journal of …, 2010
Protein synthesis and eukaryotic initiation factor (eIF) activation are increased in skeletal muscle of neonatal pigs parenterally infused with amino acids. Leucine appears to be the most effective single amino acid to trigger these effects. To examine the response to enteral leucine supplementation, overnight food-deprived 5-d-old pigs were gavage fed at 0 and 60 min a: 1) low-protein diet (LP); 2) LP supplemented with leucine (LP+L) to equal leucine in the high-protein diet (HP); or 3) HP diet. Diets were isocaloric and equal in lactose. Fractional protein synthesis rates and translation initiation control mechanisms were examined in skeletal muscles and visceral tissues 90 min after feeding. Protein synthesis rates in longissimus dorsi, gastrocnemius, and masseter muscles, heart, jejunum, kidney, and pancreas, but not liver, were greater in the LP+L group compared with the LP group and did not differ from the HP group. Feeding LP+L and HP diets compared with the LP diet increased phosphorylation of mammalian target of rapamycin (mTOR), 4E-binding protein 1, ribosomal protein S6 kinase-1, and eIF4G and formation of the active eIF4E×eIF4G complex in longissimus dorsi muscle. In all tissues except liver, activation of mTOR effectors increased in pigs fed LP+L and HP vs. LP diets. Our results suggest that leucine supplementation of a low-protein meal stimulates protein synthesis in muscle and most visceral tissues to a rate similar to that achieved by feeding a high-protein meal and this stimulation involves activation of mTOR downstream effectors.
The Journal of nutrition, 2017
Protein quantity and quality at a meal affect muscle protein synthesis (MPS); however, long-term effects of protein distribution at individual meals on adult muscle mass remain unknown. We used a precise feeding protocol in adult rats to determine if optimizing postmeal MPS response by modifying the meal distribution of protein, and the amino acid leucine (Leu), would affect muscle mass. Two studies were conducted with the use of male Sprague-Dawley rats (∼300 g) trained to consume 3 meals/d, then assigned to diet treatments with identical macronutrient contents (16% of energy from protein, 54% from carbohydrates, and 30% from fat) but differing in protein quality or meal distribution. Study 1 provided 16% protein at each meal with the use of whey, egg white, soy, or wheat gluten, with Leu concentrations of 10.9%, 8.8%, 7.7%, and 6.8% (wt:wt), respectively. Study 2 used whey protein with 16% protein at each meal [balanced distribution (BD)] or meals with 8%, 8%, and 27% protein [unb...
Engineering, 2017
Low protein intake causes a decrease in protein deposition in most animal tissues. The purpose of this study was to investigate whether leucine supplementation would increase the synthesis rate of protein and muscle weight in adult rats, which chronically consume only 58.8% of their protein requirements. Thirty-six male Sprague-Dawley rats were assigned to one of three dietary treatments including a 20% casein diet (CON), a 10% casein + 0.44% alanine diet (R), and a 10% casein + 0.87% leucine diet (RL). After a 10 d dietary treatment, plasma amino acid levels were measured after feeding, the gastrocnemius muscles and soleus muscles were harvested and weighed, and the fractional synthesis rate (FSR) and mammalian target of rapamycin (mTOR) signaling proteins in skeletal muscle were measured. Regarding the plasma amino acid level, the RL group had the highest concentration of leucine (P < 0.05) and the lowest concentration of isoleucine (P < 0.05) among the three groups, and the CON group had a lower concentration of valine (P < 0.05) than the R and RL groups. Compared with the R and RL groups, the CON group diet significantly increased (P < 0.05) feed intake, protein synthesis rate, and the phosphorylation of eukaryotic initiation factor 4E binding protein 1 (4E-BP1), and decreased the weight of abdominal adipose. Compared with the R group, the RL group significantly increased in gastrocnemius muscle weight, protein synthesis rate, and phosphorylation of both ribosomal protein S6 kinase 1 (S6K1) and 4E-BP1. In conclusion, when protein is chronically restricted in adult rat diets, leucine supplementation moderately improves body weight gain and increases muscle protein synthesis through mTOR activation.
2001
Aging is characterized by a progressive loss of muscle mass. A decrease of muscle protein synthesis stimulation has been detected in the postprandial state and correlated to a decrease of muscle protein synthesis sensitivity to leucine in vitro. This study was undertaken to examine the effect of a leucine-supplemented meal on postprandial (PP) muscle protein synthesis during aging. Adult (8 mo old) and old (22 mo old) rats were fed a semiliquid 18.2% protein control diet for 1 mo. The day of the experiment, rats received no food (postabsorptive group) or either an alanine or leucine-supplemented meal for 1 h (postprandial groups: PP and PP Leu groups, respectively). Muscle protein synthesis was assessed in vivo 90–120 min after the meal distribution using the flooding dose method (1-C phenylalanine). Plasma leucine concentrations were significantly greater in the PP Leu group compared with the PP group at both ages. Muscle protein synthesis was significantly greater in the adult PP ...