Soy proteins have been shown to result in lower postprandial nitrogen retention than milk proteins, but the mechanisms underlying these differences have not been elucidated. To investigate this question, we measured the postprandial kinetics of the appearance of individual (15)N-amino acids in the serum of healthy adults after the ingestion of either (15)N-soy (n = 8) or (15)N-milk proteins (n = 8) in a mixed single meal (46 kJ/kg). The kinetics of total and dietary amino acids (AA) in the peripheral circulation were characterized by an earlier and higher peak after soy protein ingestion. Dietary AA levels peaked at 2.5 h in the soy group vs. 3.9 h in the milk group (P < 0.02). This time interval difference between groups was associated with a faster transfer of dietary N into urea in the soy group (peak at 3 vs. 4.75 h in the milk group, P < 0.005) and a higher level of incorporation into the serum protein pool from 3 to 8 h after the soy meal. The dietary AA pattern in the peripheral blood closely reflected the dietary protein AA pattern. Postprandial glucose, insulin, and glucagon levels and profiles did not differ between groups. Soy AA were digested more rapidly and were directed toward both deamination pathways and liver protein synthesis more than milk AA. We conclude that differences in the metabolic postprandial fates of soy and milk proteins are due mainly to differences in digestion kinetics; however, the AA composition of dietary proteins may also play a role.

l-Glutamate is one of the most abundant amino acids in alimentary proteins, but its concentration in blood is among the lowest. This is largely because l-glutamate is extensively oxidized in small intestine epithelial cells during its transcellular journey from the lumen to the bloodstream and after its uptake from the bloodstream. This oxidative capacity coincides with a high energy demand of the epithelium, which is in rapid renewal and responsible for the nutrient absorption process. l-Glutamate is a precursor for glutathione and N-acetylglutamate in enterocytes. Glutathione is involved in the enterocyte redox state and in the detoxication process. N-acetylglutamate is an activator of carbamoylphosphate synthetase 1, which is implicated in l-citrulline production by enterocytes. Furthermore, l-glutamate is a precursor in enterocytes for several other amino acids, including l-alanine, l-aspartate, l-ornithine, and l-proline. Thus, l-glutamate can serve both locally inside enterocytes and through the production of other amino acids in an interorgan metabolic perspective. Intestinal epithelial cell capacity to oxidize l-glutamine and l-glutamate is already high in piglets at birth and during the suckling period. In colonocytes, l-glutamate also serves as a fuel but is provided from the bloodstream. Alimentary and endogenous proteins that escape digestion enter the large intestine and are broken down by colonic bacterial flora, which then release l-glutamate into the lumen. l-Glutamate can then serve in the colon lumen as a precursor for butyrate and acetate in bacteria. l-Glutamate, in addition to fiber and digestion-resistant starch, can thus serve as a luminally derived fuel precursor for colonocytes.

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Ageing is characterized by a decline in muscle mass that could be explained by a defect in the regulation of postprandial muscle protein metabolism. Indeed, the stimulatory effect of food intake on protein synthesis and its inhibitory effect on proteolysis is blunted in old muscles from both animals and humans. Recently, low grade inflammation has been suspected to be one of the factors responsible for the decreased sensitivity of muscle protein metabolism to food intake. This study was undertaken to examine the effect of long-term prevention of low grade inflammation on muscle protein metabolism during ageing. Old rats (20 months of age) were separated into two groups: a control group and a group (IBU) in which low grade inflammation had been reduced with a non-steroidal anti inflammatory drug (ibuprofen). After 5 months of treatment, inflammatory markers and cytokine levels were significantly improved in treated old rats when compared with the controls: −22.3% fibrinogen, −54.2% α2-macroglobulin, +12.6% albumin, −59.6% IL 6 and −45.9% IL 1β levels. As expected, food intake had no effect on muscle protein synthesis or muscle proteolysis in controls whereas it significantly increased muscle protein synthesis by 24.8% and significantly decreased proteolysis in IBU rats. The restoration of muscle protein anabolism at the postprandial state by controlling the development of low grade inflammation in old rats significantly decreased muscle mass loss between 20 and 25 months of age. In conclusion, the observations made in this study have identified low grade inflammation as an important target for pharmacological, nutritional and lifestyle interventions that aim to limit sarcopenia and muscle weakness in the rapidly growing elderly population in Europe and North America. Abbreviations COX 2 , cyclo-oxygenase 2; CRP, C reactive protein; 4EBP1, 4E binding protein 1; Foxo3a, forkhead box O3a; IL 6 , interleukin-6; IL 1β , interleukin-1β; MCP 1 , monocyte chemo-attractant protein 1; mTOR, mammalian target of rapamycin; NF-κB, nuclear factor-κB; NSAID, non-steroidal anti-inflammatory drug; PA, post-absorptive; PAI-1, plasminogen activator inhibitor-1; PGE2, prostaglandin-E2; PP, postprandial; S6rp, ribosomal protein S6; S6K1, S6 kinase 1; TNF α , tumor necrosis factor α.

Our results confirm the major role of kinetics in dietary nitrogen postprandial utilization and highlight the paradox of MSPI, which, despite its high Protein Digestibility Corrected Amino Acid Score, ensures a rate of amino acid delivery that is too rapid to sustain the anabolic requirement during the postprandial period. Milk proteins had the best nutritional quality, which suggested a synergistic effect between soluble proteins and caseins.

We used a previously developed compartmental model to assess the postprandial distribution and metabolism of dietary nitrogen (N) in the splanchnic and peripheral areas after the ingestion of a single mixed meal containing either (15)N-labeled milk or soy purified protein. Although the lower whole-body retention of dietary N from soy protein was measured experimentally, the splanchnic retention of dietary N was predicted by the model not to be affected by the protein source, and its incorporation into splanchnic proteins was predicted to reach approximately 35% of ingested N at 8 h after both meals. However, dietary N intestinal absorption and its appearance in splanchnic free amino acids were predicted to be more rapid from soy protein and were associated with a higher deamination, concomitant with a higher efficiency of incorporation of dietary N into proteins in the splanchnic bed. In contrast, soy protein was predicted to cause a reduction in peripheral dietary N uptake, as a consequence of both similar splanchnic retention and increased oxidation compared with milk protein. In addition, protein synthesis efficiency was reduced in the peripheral area after soy protein intake, leading to dietary N incorporation in peripheral proteins that fell from 26 to 19% of ingested N 8 h after milk and soy protein ingestion, respectively. Such a model thus enables a description of the processes involved in the differential metabolic utilization of dietary proteins and constitutes a valuable tool for further definition of the notion of protein quality during the period of protein gain.

Rapeseed protein (RP, Brassica napus) is used in only animal feed despite its high nutritional potential for human nutrition. We sought to assess the nutritional quality of rapeseed by measuring its real ileal digestibility (RID) and net postprandial protein utilization (NPPU) in humans fed (15)N-RP. Volunteers equipped with an intestinal tube at the jejunal (n = 5) or ileal level (n = 7) ingested a mixed meal containing 27.3 g (15)N-RP and a total energy content of 700 kcal (2.93 MJ). Dietary N kinetics was quantified in intestinal fluid, urine, and blood sampled at regular intervals during the postprandial period. The RID of RP was 84.0 +/- 8.8%. Dietary N at the ileal level was mostly in the form of undigested protein from both 12S and 2S rapeseed fractions. Aminoacidemia was not significantly increased by meal ingestion. The postprandial distribution of dietary N was 5.4 +/- 1.8% in urinary urea and ammonia, 8.2 +/- 3.4% in body urea, and 7.7 +/- 2.0% in plasma protein 8 h after the meal. The NPPU of RP amounted to 70.5 +/- 9.6% and the postprandial biological value (PBV) was high at 83.8 +/- 4.6%. RP has a low RID in humans compared with other plant proteins but also exhibits a very low deamination rate. Thus, the PBV of RP is excellent in humans, being as high as that of milk protein. We conclude that RP has a high nutritional potential for human nutrition.

The suitability of the pig as an animal model for predicting protein digestibility in man was evaluated. Healthy adult human subjects (mean body weight 67 kg; n 11) and growing pigs (mean body weight 40 kg; n 15) were fed semi-synthetic mixed meals containing, as a sole source of N, casein (C), hydrolysed casein (HC) or rapeseed isolate (R). There was no prior adaptation to the test meal. Ileal digesta were sampled through a naso-ileal tube (human subjects) or a post-valve T-caecum cannula (pigs) after ingestion of a bolus meal. The protein sources were 15 N-labelled. Amino acid (AA) digestibilities were not determined for R. Ileal apparent N digestibility was markedly lower (14-16 %; P, 0·001) in human subjects than in pigs (C, HC, R). Similarly, most apparent ileal AA digestibilities were lower (8 % on average; P,0·05) in human subjects (C, HC). Ileal true N digestibility was slightly lower (3 -5 %; P,0·001) in human subjects than in pigs (C, HC, R) and most true ileal AA digestibilities were similar (P. 0·05) between the species (C, HC). Exceptions were for phenylalanine, tyrosine, lysine, histidine and aspartic acid for which digestibilities were lower (3 % on average; P, 0·001) in human subjects. A similar ranking of the diets was observed for true ileal N digestibility between species. The inter-species correlation for true ileal digestibility was high for N (r 0·98 over 3 £ 2 data; P¼ 0·11) and AA (r 0·87 over 26 £ 2 data; P,0·0001). Overall, this supports the use of the pig as a model for predicting differences among dietary protein digestibility, especially regarding true ileal N digestibility, in man.