scholarly journals Exogenous and endogenous contributions to nitrogen fluxes in the digestive tract of pigs fed a casein diet. II. Ileal and faecal digestibilities and absorption of amino acids

1991 ◽  
Vol 31 (5) ◽  
pp. 561-573 ◽  
Author(s):  
B. Darcy-Vrillon ◽  
WB Souffrant ◽  
JP Laplace ◽  
A. Rérat ◽  
T. Corring ◽  
...  
1993 ◽  
Vol 33 (4) ◽  
pp. 373-382 ◽  
Author(s):  
WB Souffrant ◽  
A. Rérat ◽  
JP Laplace ◽  
B. Darcy-Vrillon ◽  
R. Köhler ◽  
...  

1990 ◽  
Vol 68 (10) ◽  
pp. 3421 ◽  
Author(s):  
G R Khorasani ◽  
W C Sauer ◽  
L Ozimek ◽  
J J Kennelly

1997 ◽  
Vol 272 (2) ◽  
pp. G257-G264 ◽  
Author(s):  
C. Remesy ◽  
C. Moundras ◽  
C. Morand ◽  
C. Demigne

The aim of the present study was to investigate mechanisms of N salvage by the liver when a diet is protein deficient. For this purpose, rats were adapted to a slightly deficient (11% casein) or moderately surfeit (22% casein) dietary protein level. Animals were sampled during the postprandial or the postabsorptive period, and fluxes across the digestive tract and liver were determined. During the postabsorptive period there was a negative balance of glutamine across the digestive tract in both diet groups. During the postprandial period the digestive balance of glutamine was still negative, despite a substantial supply of dietary glutamine and glutamate, suggesting that glutamine utilization is maximal during this period. There was a net production of glutamate and glutamine by the liver in both diet groups, but glutamine release was 73% higher in rats fed the low-protein diet. In these animals, because of the relatively low capacity of ureagenesis, N utilization was shifted toward glutamine synthesis: overall uptake of amino acids by the liver was approximately 5.3 micromol/min, and net release of glutamine + glutamate was approximately 2.9 micromol/min (hence a 55% cycling, on a molar basis). This cycling was only 12% in rats adapted to the 22% casein diet. When liver ammonia uptake was taken into account, N cycling showed parallel changes: 64% or 15% in rats adapted to the 11% or 22% casein diet, respectively. Besides glutamine delivery, glutamate was also released by the liver, representing an N source for extrasplanchnic tissues. With protein-deficient diets, hepatic glutamine delivery mainly serves to fulfill substrate needs for intestinal metabolism, which represents a mechanism for N salvage. This shift of N metabolism from urea toward glutamine production may imply a glutamate transfer from periportal to glutamine-synthesizing perivenous hepatocytes.


1993 ◽  
Vol 264 (6) ◽  
pp. G1057-G1065 ◽  
Author(s):  
C. Moundras ◽  
C. Remesy ◽  
C. Demigne

The aim of the present study was to evaluate the effect of changes in dietary protein level on overall availability of amino acids for tissues. For this purpose, rats were adapted to diets containing various concentrations of casein (7.5, 15, 30, and 60%) and were sampled either during the postprandial or postabsorptive period. In rats fed the protein-deficient diet, glucogenic amino acids (except threonine) tended to accumulate in plasma, liver, and muscles. In rats fed high-protein diets, the hepatic balance of glucogenic amino acids was markedly enhanced and their liver concentrations were consistently depressed. This response was the result of a marked induction of amino acid catabolism (a 45-fold increase of liver threonine-serine dehydratase activity was observed with the 60% casein diet). The muscle concentrations of threonine, serine, and glycine underwent changes parallel to plasma and liver concentrations, and a significant reduction of glutamine was observed. During the postabsorptive period, adaptation to high-protein diets resulted in a sustained catabolism of most glucogenic amino acids, which accentuated the drop in their concentrations (especially threonine) in all the compartments studied. The time course of metabolic adaptation from a 60 to a 15% casein diet has also been investigated. Adaptation of alanine and glutamine metabolism was rapid, whereas that of threonine, serine, and glycine was delayed and required 7-11 days. This was paralleled by a relatively slow decay of liver threonine-serine dehydratase (T-SDH) activity in contrast to the rapid adaptation of pyruvate kinase activity after refeeding a high-carbohydrate diet.(ABSTRACT TRUNCATED AT 250 WORDS)


2021 ◽  
Author(s):  
Peter M. Homyak ◽  
Eric W. Slessarev ◽  
Shannon Hagerty ◽  
Aral C. Greene ◽  
Kenneth Marchus ◽  
...  

1972 ◽  
Vol 27 (1) ◽  
pp. 177-194 ◽  
Author(s):  
J. V. Nolan ◽  
R. A. Leng

1. To obtain a quantitative model for nitrogen pathways in sheep, a study of ammonia and urea metabolism was made by using isotope dilution techniques with [15N]ammonium sulphate and [15N]urea and [14C]urea.2. Single injection and continuous infusion techniques of isotope dilution were used for measuring ammonia and urea entry rates.3. Sheep were given 33 g of chaffed lucerne hay every hour; the mean dietary N intake was 23.4 g/d.4. It was estimated that 59% of the dietary N was digested in the reticulo-rumen; 29% of the digested N was utilized as amino acids by the micro-organisms, and 71% was degraded to ammonia.5. Of the 14.2 g N/d entering the ruminal ammonia pool, 9.9 g N/d left and did not return to the pool, the difference of 4.3 g N/d represented recycling, largely within the rumen itself (through the pathways: ruminal ammonia → microbial protein → amino acids → ammonia).6. Urea was synthesized in the body at a rate of 18.4 g N/d from 2.0 g N/d of ammonia absorbed through the rumen wall and 16.4 g N/d apparently arising from deamination of amino acids and ammonia absorbed from the lower digestive tract.7. In the 24 h after intraruminal injection of [15N]ammonium salt, 40–50% of the N entering the plasma urea pool arose from ruminal ammonia; 26% of the15N injected was excreted in urinary N.8. Although 5.1g N/d as urea was degraded apparently in the digestive tract, only 1.2g N/d appeared in ruminal ammonia; it is suggested that the remainder may have been degraded in the lower digestive tract.9. A large proportion of the urea N entering the digestive tract is apparently degraded and absorbed and the ammonia incorporated in the pools of nitrogenous compounds that turn over only slowly. This may be a mechanism for the continuous supply to the liver of ammonia for these syntheses.10. There was incorporation of15N into bacterial fractions isolated from rumen contents after intraruminal and intravenous administration of [15N]ammonium salts and [15N]urea respectively.11. A model for N pathways in sheep is proposed and, for this diet, many of the pool sizes and turn-over rates have been either deduced or estimated directly.


2001 ◽  
Vol 85 (6) ◽  
pp. 689-698 ◽  
Author(s):  
G. E. Lobley ◽  
D. M. Bremner ◽  
D. S. Brown

Under conditions of chronic supply the liver removes most amino acids (AA) in excess of net anabolic needs. Little information is available, however, on how acute alterations in AA supply (as might occur with once-daily feeding regimens) are controlled by the liver. Are these also extracted completely in a ‘first-pass’ manner or are there limitations to hepatic uptake? Furthermore, is the rate of removal ‘saturable’ (by Michaelis–Menten kinetics) over the range of supply experienced under normal feeding conditions? These questions have been addressed in a study that involved acute (4.5 h) increases in AA supply. Four sheep were prepared with trans-hepatic vascular catheters and were offered a basal diet (equivalent to 1.6×energy maintenance) throughout. On four occasions, at 7 d intervals, they were infused with various amounts of an AA mixture into the mesenteric vein over a 4.5 h period. The mixture contained fourteen AA in the proportions present in rumen microbial protein. The amounts infused were calculated to provide an additional one, two, three and four times that absorbed from the basal diet. Continuous blood collections were removed over 2 h intervals before (basal diet only) and at 0.5–2.5 and 2.5–4.5 h of AA infusion. Transfers of AA, from the digestive tract and to the liver, were calculated for both plasma and total blood. The recovery of the infused AA across the portal-drained viscera (PDV) was quantitative (100%) only for histidine and proline, the remaining AA were recovered at 56–83 %. These losses correlated (P<0.001) with the arterial concentrations and were probably due to removal of AA from the systemic circulation by the tissues of the digestive tract. Despite the wide range of net PDV appearances (i.e. absorbed plus infused), the percentage of most AA removed by the liver remained constant, but the percentage varied with AA (from 34 for proline to 78 for tryptophan for blood transfers). Thus, even when supply was increased 5-fold over baseline there was no indication that the transport into the liver declined, indeed the absolute removals continued to increase. In contrast, the branched-chain AA (isoleucine, leucine and valine) did not exhibit constant percentage extractions. Their percentage extractions were always the lowest (16, 10 and 25 respectively) and tended to decline at the highest infusion rates, indicative of saturation in hepatic transport and/or metabolism. The arterial concentrations of all infused AA increased (P<0.001) with rate of infusion, again indicative that the liver did not extract all the net AA available across the PDV. Absolute amounts removed were similar between plasma and blood, indicating that most of the hepatic transfers occurred from plasma. The fractional rates of transfer from total inflow to the liver (i.e. with re-circulated AA included) were 3- to 4-fold lower than rates based on the amounts absorbed plus infused. The highest percentage extraction for total blood inflows was for serine (27), but most were between 6 and 16, except for the branched-chain AA, which were all <1. Use of percentage extractions based on total inflows are probably more appropriate for development of mathematical models of liver metabolism, and the current data suggest that constant values may be applied. The needs of the liver for specific mechanisms involving phenylalanine and histidine (plasma protein synthesis), glycine (detoxification of xenobiotics) and alanine (gluconeogenesis) probably also require to be included in such models.


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