Net appearance of amino acids in portal blood during the digestion of casein or rapeseed proteins in the pig

The kinetics of appearance of amino acids (AA) in portal blood following the ingestion of casein or rapeseed protein were compared. Six pigs, fitted with permanent catheters in the portal vein and in the carotid artery, as well as with an electromagnetic flow probe around the portal vein, received three 800 g test meals, one containing 12% rapeseed proteins (RA12) and the others containing 12% and 24% casein (CA12 and CA24), at 1-week intervals and according to a double Latin square design. Portal and arterial blood samples were collected and portal blood flow rate was recorded for 8 h after the test meals. At the end of measurement, an average of 76.1 +/- 5.6% (mean +/- SEM) of total AA from the CA24 diet had appeared in portal blood, compared with 94.3 +/- 10.4% for the CA12 diet and 103.5 +/- 12.6% for the RA12 diet. Similar results were obtained for essential AA. Differences were found in the kinetics of appearance of individual AA. Eight hours after the meal, 79% of lysine, 84% of methionine, and 73% of valine from the CA24 diet had appeared in portal blood compared, respectively, with 100, 89, and 83% from the CA12 diet and 99, 86, and 106% from the RA12 diet. Arginine from rapeseed had a net appearance level lower (82%) than the overall mixture of essential AA. With casein diets, the net appearance of arginine reached 97% (CA12) and 82% (CA24). Following the ingestion of rapeseed proteins, there seemed to be a significant appearance of endogenous AA in portal blood.(ABSTRACT TRUNCATED AT 250 WORDS)     

Proteolysis in homogenates of perfused rat liver: responses to insulin, glucagon and amino acids

The proteolytic release of leucine and isoleucine was assessed in homogenates of rat livers perfused under conditions known to influence protein degradation in the intact liver. Release was increased by perfusion alone and by additions of glucagon and was inhibited by insulin and amino acids. These responses correlated both with rates of proteolysis during perfusion and with physical alterations of the lysosomal system, reported earlier. Homogenate proteolysis appeared to comprise two components: the release of free amino acids from the total particulate fraction and from peptides in the cytosol. Both components are believed to be generated by elements of the lysosomal system.     

Feeding pigs amino acids as protein-bound or in free form influences postprandial concentrations of amino acids,metabolites, and insulin

Dietary proteins need to be digested first while free amino acids (AAs) and small peptides are readily available for absorption and rapidly appear in the blood. The rapid postprandial appearance of dietary AA in the systemic circulation may result in inefficient AA utilisation for protein synthesis of peripheral tissues if other nutrients implicated in AA and protein metabolism are not available at the same time. The objective of this experiment was to compare the postprandial concentrations of plasma AA and other metabolites after the ingestion of a diet that provided AA either as proteins or as free AA and small peptides. Twenty-four male growing pigs (38.8 ± 2.67 kg) fitted with a jugular catheter were assigned to one of three diets that provided AA either in protein form (INT), free AA and small peptides (HYD), or as free AA (FAA). After an overnight fast and initial blood sampling, a small meal was given to each pig followed by serial blood collection for 360 min. Postprandial concentrations of plasma AA, glucose, insulin, and urea were then measured from the collected blood. Non-linear regression was used to summarise the postprandial plasma AA kinetics. Fasting concentrations of urea and some AA were higher (P < 0.05) while postprandial plasma insulin and glucose were lower (P < 0.01) for INT than for HYD and FAA. The area under the curve of plasma concentration after meal distribution was lower for INT for most AAs (P < 0.05), resulting in a flatter curve compared to HYD and FAA. This was the result of the slower appearance of dietary AA in the plasma when proteins are fed instead of free AA and small peptides. The flatter curve may also result from more AAs being metabolised by the intestine and liver when INT was fed. The metabolism of AA of the intestine and liver was higher for HYD than FAA. Providing AA as proteins or as free AA and small peptides affected the postprandial plasma kinetics of AA, urea, insulin, and glucose. Whether the flat kinetics when feeding proteins has a positive or negative effect on AA metabolism still needs to be explored.     

Portal absorption of 15N and amino nitrogen in the growing pig after ingestion of labelled milk, yogurt or heat-treated yogurt.

The aim of this experiment was to study 15N and amino-nitrogen (AN) portal absorption in the growing pig after ingestion of uniformly (0.2509 APE) labelled 15N milk (M), yogurt ingested just after manufacturing (Y0), yogurt stored for 21 d at 4 degrees C (Y21) and heat-treated yogurt (HY). The highest porto-arterial differences (PAD) in 15N and AN were found in the period between 30 min and 90 min after ingestion. The absorption of nitrogen from M and HY mainly occurred during the 0-120 min time period (about 70% for M and 67% for HY). For Y0 and Y21, a larger displayed absorption period over the 0-240 min time period was observed. Y0 and Y21 presented a quite similar portal absorption profile. The 15N absorption rate was close to 80% for each studied milk product, suggesting that under our experimental conditions, dairy products (M, Y0, Y21 and HY) deliver nearly the same amounts of nitrogen to the organism. AN absorption rates were around 78% with a higher variability between the milk products. These results also indicate that most of the proteins were absorbed within the 240 min postprandial period.     

Circulating immunoreactivities of gastrin,glucagon and VIP after jejuno-ileal bypass

Seven Sprague-Dawley rats (404–440 g) underwent a 90% jejuno-ileal bypass (JIB); the functional loop consisted of $\text{1}\text{3}$ ileum and $\text{2}\text{3}$ jejunum with the bypassed loop being anastamosed to the ascending colon. Seven control rats were sham-operated. After 35 days, the rats were fasted 18 hours and venous blood was collected. Immunoreactivity of gastrin, measured with an antibody binding equally to G17 and G34, was higher in the plasma of the JIB (256±55 SEM pg/ml) than control (85±9 pg/ml) rats. This agrees with recent human studies but is in conflict with results in less mature rats. VIP levels were not significantly different. Glucagon-like immunoreactivity measured with antibodies specific for the C- and N-terminal regions of the hormone, respectively, were also higher in the JIB (510±40 and 129±15 pg/ml) rats.     

Differences in portal flow rates of amino acids and liver composition between rats fed casein or lactalbumin

The portal appearance rates and net rates of amino acids' absorption were studied in rats fed semi-synthetic diets containing either casein or lactalbumin (CAS and LA, respectively) as the only protein sources. Rats were pre-adapted to the experimental diets for 5 days prior to the absorption studies. Rats fed the LA diet had higher (p < 0.05) portal vein concentrations of free essential amino acids than those fed the CAS diet at 0, 60, 105 and 150 min after feeding. Portal and arterial concentrations of arginine, leucine, tryptophan, lysine and methionine were higher (p < 0.05) in rats fed LA at most time points tested, while concentrations of tyrosine were higher (p < 0.05) in CAS fed rats. When portal flow rates were compared, values for arginine, threonine, alanine, leucine, tryptophan and lysine were higher (p < 0.05) in LA at most time points tested, while proline, tyrosine and valine were higher (p < 0.05) for CAS fed rats after 60 and 105 min feeding. Portal blood flow varied (p < 0.05) with time in rats fed protein-free or LA diets, and was higher (p < 0.05) than that of CAS at 105 min. Intestinal net rates of absorption of tyrosine, valine, leucine and lysine were higher (p < 0.05) for LA fed rats as compared to those fed CAS at most time points tested, while alanine and proline net rates were higher (p < 0.05) for CAS fed rats at 60, 105 and 150 min. Amounts of protein in stomach contents of rats fed the CAS diet were significantly higher (p < 0.05) than those in LA fed rats at 60, 105 and 150 min after feeding. The relative liver weight of the rats fed the CAS diet was lower (p < 0.05) than that of animals fed the LA diet. Lower (p < 0.05) liver glycogen and lipid contents were determined in rats fed CAS diet respect to LA or protein-free fed rats. Results indicate that dietary and plasma amino acids profile are only partially related, and that under normal feeding conditions amino acids from CAS and LA are absorbed at different rates, which is likely to affect liver composition and metabolism.     

Synthesis of metabolism-resistant substrates for the transport system for cationic amino acids; their stimulation of the release of insulin and glucagon, and of the urinary loss of amino acids related to cystinuria

Several amino acids have been synthesized as model transport substrates building on the piperidine and cyclohexane rings. Only when the distal N atom is part of an unambiguously cationic structure are these compounds transported predominantly by the cationic amino acid system. These amino acids in labeled form are excreted rather slowly in unmodified state, very little ¹⁴CO₂ being released. Those which are unambiguously cationic (including also homoarginine) led to a greatly increased excretion of arginine, lysine, ornithine and citrulline. Those which might be expected to act as lysine analogs had little effect on the excretion of the basic amino acids, although the excretion of citrulline and the sum of glutamine plus asparagine was accelerated. Certain of the analogs intensified the excretion of citrulline in dissociation from effects on resorption of the basic amino acids, also in dissociation from effects on cystine resorption. These results indicate citrulline resorption does not occur principally by the same agency serving for the basic amino acids, nor by the agency serving for cystine, despite the observed interactions for resorption. The injection of either of three transport analogs for arginine into the rat leads to early increases in the circulating levels of immunologically reactive insulin and glucagon.     

Hypochlorite-induced oxidation of amino acids, peptides and proteins

Summary. Activated phagocytes generate the potent oxidant hypochlorite (HOCl) via the release of the enzyme myeloperoxidase and hydrogen peroxide. HOCl is known to react with a number of biological targets including proteins, DNA, lipids and cholesterol. Proteins are likely to be major targets for reaction with HOCl within a cell due to their abundance and high reactivity with HOCl. This review summarizes information on the rate of reaction of HOCl with proteins, the nature of the intermediates formed, the mechanisms involved in protein oxidation and the products of these reactions. The predicted targets for reaction with HOCl from kinetic modeling studies and the consequences of HOCl-induced protein oxidation are also discussed.     

Ileal endogenous losses in pigs feeding a protein-free diet or diets with different contents of casein or crystalline amino acids

The common usage of protein-free diets to estimate unspecific AA losses has been criticised as unphysiological and incorrect. Therefore, in this study different diets were tested for the determination of endogenous losses (EL) of amino acids (AA) and nitrogen (N) assuming a complete absorption in the small intestine. Seven cannulated gilts received a protein-free diet (Diet PF) or diets with 3%, 6% or 10% crude protein (CP) from crystalline AA (Diets CA) or casein (Diets CAS) according to a 7 × 7 Latin square design. After 6 d adaptation to the diet, ileal digesta was collected for 24 h and thereafter analysed for AA, N and the digestibility markers Cr₂O₃ and acid insoluble ash (AIA). Generally, among all AA, the highest amounts of EL were found for Pro, Glu and Gly, and the smallest for Met. Different levels of CP in Diets CA and CAS had no effect on EL. Significant differences between treatments were observed only for the EL of Glu, Ile, Ser (higher in Diets CA and PF), Pro and Tyr (higher in Diet PF) (p < 0.05). There were no differences in determined EL using Cr₂O₃ or AIA as digestibility markers.