Differential Effects of Cooked Beans and Cooked Lentils on Protein Metabolism in Intestine and Muscle in Growing Rats

Pirman, Tatjana; Combe, Etiennette; Ribeyre, Marie Claude; Prugnaud, J.; Stekar, Jasna; Mirand, Philippe Patureau

doi:10.1159/000090741

Cited by 10 publications

(17 citation statements)

References 52 publications

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“…In our earlier studies with legumes added in the diet, protein metabolism in gastrocnemius muscle was decreased, if there was an effect on body-weight gain (31) and was almost unchanged if there was no difference in the body-weight gain (32,33) , which is in accordance with results of the present study. Gastrocnemius muscle is sensitive to the nature of the nutrients derived from the diet (34) and, as a fast-twitch oxidative glycolytic muscle, is a good indicator of the average response of whole skeletal muscle (35) .…”

Section: Discussionsupporting

confidence: 93%

Differential response of protein metabolism in splanchnic organs and muscle to pectin feeding

et al. 2008

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The aim of the present study was to determine whether the addition of soluble fibre in the diet affected protein metabolism in the intestinal tissues, some visceral organs and in skeletal muscle. A diet supplemented with pectin (80 g/kg) was fed to young growing rats and the effect on organ mass and protein metabolism in liver, spleen, small and large intestines and gastrocnemius muscle was monitored and compared with the control group. Protein synthesis rates were determined by measuring [ 13 C]valine incorporation in tissue protein. In the pectin-fed rats compared with the controls, DM intake and body weight gain were reduced (9 and 20 %, respectively) as well as gastrocnemius muscle, liver and spleen weights (6, 14 and 11 %, respectively), but the intestinal tissues were increased (64 %). In the intestinal tissues all protein metabolism parameters (protein and RNA content, protein synthesis rate and translational efficiency) were increased in the pectin group. In liver the translational efficiency was also increased, whereas its protein and RNA contents were reduced in the pectin group. In gastrocnemius muscle, protein content, fractional and absolute protein synthesis rates and translational efficiency were lower in the pectin group. The stimulation of protein turnover in intestines and liver by soluble fibre such as pectins could be one of the factors that explain the decrease in muscle turnover and whole-body growth rate. Citrus pectin: Protein metabolism: Splanchnic tissues: MuscleDietary fibres are food components that have essential effects in digestion in humans and animals. Fibre affects large-bowel function, causing an increase in stool output, dilution of colonic contents, a faster rate of passage through the gut and changes in the colonic metabolism of minerals, N and bile acids (1) . Soluble dietary fibre, such as pectin, is not digested by endogenous enzymes but fermented in the large intestine. Colonic fermentation leads to the production of SCFA, which are used as an energy source by enterocytes. Both the high fermentation rate and high viscosity induced by soluble dietary fibre supplementation may be responsible for the observed stimulation of intestinal mucosal cell proliferation (2) .Indeed pectin has been reported to have a trophic effect on the pancreas and intestine (3) , to stimulate intestinal cell proliferation and to increase brush-border membrane enzyme activities (4) . It was also demonstrated that pectin supplementation increased the levels of plasma enteroglucagon (peptides derived from proglucagon processing by intestinal L cells) in rats (4) , which is a humoral factor for intestinal mucosal growth (5) . In addition, dietary pectin has been shown to modulate immune function in the intestine (6,7) and spleen (7) , and also the hepatic metabolism of cholesterol (8) and biliary acids (9) . This may have consequences for protein metabolism in these organs, but to our knowledge no data have been published about the effect of pectin on protein synthesis rate in intestinal tissues, exc...

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Section: Discussionsupporting

confidence: 93%

Differential response of protein metabolism in splanchnic organs and muscle to pectin feeding

et al. 2008

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“…Several studies have evaluated the effect of plant-based protein sources, i.e., raw faba beans [ 18 , 19 , 20 , 21 ], raw peas, cooked lentils or cooked beans [ 22 , 23 , 24 , 25 , 26 ], soy proteins [ 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 , 35 ], faba bean proteins [ 36 ], and wheat proteins [ 33 ] when compared with animal-based protein sources on body protein retention and metabolism in young or old rats, pigs, or humans. All have reported a positive effect of animal proteins on protein metabolism in young animals or humans as compared to plant-based protein sources, regardless of their form, e.g., raw or cooked, protein isolate, or protein hydrolysate.…”

Section: Introductionmentioning

confidence: 99%

Anabolic Properties of Mixed Wheat-Legume Pasta Products in Old Rats: Impact on Whole-Body Protein Retention and Skeletal Muscle Protein Synthesis

et al. 2020

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The mechanisms that are responsible for sarcopenia are numerous, but the altered muscle protein anabolic response to food intake that appears with advancing age plays an important role. Dietary protein quality needs to be optimized to counter this phenomenon. Blending different plant proteins is expected to compensate for the lower anabolic capacity of plant-based when compared to animal-based protein sources. The objective of this work was to evaluate the nutritional value of pasta products that were made from a mix of wheat semolina and faba bean, lentil, or split pea flour, and to assess their effect on protein metabolism as compared to dietary milk proteins in old rats. Forty-three old rats have consumed for six weeks isoproteic and isocaloric diets containing wheat pasta enriched with 62% to 79% legume protein (depending on the type) or milk proteins, i.e., casein or soluble milk proteins (SMP). The protein digestibility of casein and SMP was 5% to 14% higher than legume-enriched pasta. The net protein utilization and skeletal muscle protein synthesis rate were equivalent either in rats fed legume-enriched pasta diets or those fed casein diet, but lower than in rats fed SMP diet. After legume-enriched pasta intake, muscle mass, and protein accretion were in the same range as in the casein and SMP groups. Mixed wheat-legume pasta could be a nutritional strategy for enhancing the protein content and improving the protein quality, i.e., amino acid profile, of this staple food that is more adequate for maintaining muscle mass, especially for older individuals.

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“…By contrast, it has been reported that a diet rich in vegetable protein results in a weaker inhibition of postprandial protein degradation in humans, when compared to a diet rich in animal proteins [26]. A specific enhancing effect of lentils or beans protein on small and large intestine masses, protein content and fed state protein synthesis rates has been reported in the literature [27,28]. In humans, a reduction in albumin synthesis and plasma albumin levels occurs when vegetable protein consumption increases [29].…”

Section: Discussionmentioning

confidence: 99%

“…In humans, a reduction in albumin synthesis and plasma albumin levels occurs when vegetable protein consumption increases [29]. Lower muscle mass and protein synthesis rates have also been demonstrated with legume-based diets (lentils, beans or peas) versus casein in animals [28,30-32]. The reasons for these tissue effects are mostly unclear, in particular because the effect of dietary plant protein may be confounded in part by the potential digestive or metabolic effects of a series of associated factors (e.g.…”

Section: Discussionmentioning

confidence: 99%

Rapeseed and milk protein exhibit a similar overall nutritional value but marked difference in postprandial regional nitrogen utilization in rats

et al. 2011

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BackgroundRapeseed is an emerging and promising source of dietary protein for human nutrition and health. We previously found that rapeseed protein displayed atypical nutritional properties in humans, characterized by low bioavailability and a high postprandial biological value. The objective of the present study was to investigate the metabolic fate of rapeseed protein isolate (RPI) and its effect on protein fractional synthesis rates (FSR) in various tissues when compared to a milk protein isolate (MPI).MethodsRats (n = 48) were given a RPI or MPI meal, either for the first time or after 2-week adaptation to a MPI or RPI-based diet. They were divided in two groups for measuring the fed-state tissue FSR 2 h after the meal (using a flooding dose of 13C-valine) and the dietary N postprandial distribution at 5 h (using 15N-labeled meals).ResultsRPI and MPI led to similar FSR and dietary nitrogen (N) losses (ileal and deamination losses of 4% and 12% of the meal, respectively). By contrast, the dietary N incorporation was significantly higher in the intestinal mucosa and liver (+36% and +16%, respectively) and lower in skin (-24%) after RPI than MPI.ConclusionsAlthough RPI and MPI led to the same overall level of postprandial dietary N retention in rats (in line with our findings in humans), this global response conceals marked qualitative differences at the tissue level regarding dietary N accretion. The fact that FSR did not however differed between groups suggest a differential modulation of proteolysis after RPI or MPI ingestion, or other mechanisms that warrant further study.

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Differential Effects of Cooked Beans and Cooked Lentils on Protein Metabolism in Intestine and Muscle in Growing Rats

Cited by 10 publications

References 52 publications

Differential response of protein metabolism in splanchnic organs and muscle to pectin feeding

Differential response of protein metabolism in splanchnic organs and muscle to pectin feeding

Anabolic Properties of Mixed Wheat-Legume Pasta Products in Old Rats: Impact on Whole-Body Protein Retention and Skeletal Muscle Protein Synthesis

Rapeseed and milk protein exhibit a similar overall nutritional value but marked difference in postprandial regional nitrogen utilization in rats

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