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Metabolic acidosis occurs frequently in newborns. Net acid excretion (NAE) in 34 preterm and 12 term infants was measured during the first week of life. Twenty preterm infants received breast milk or formula; the remaining infants received total parenteral nutrition (TPN) -- synthetic amino acids or casein hydrolysate solution. NAE for breast milk vs formula fed infants was 5.4 +/- 0.4 and 7.8 +/- 0.6 muEq/min/m2 (mean +/- SEM). The corresponding values for the two TPN solutions in preterm infants were significantly higher at 12.5 +/- 1.4 and 19.4 +/- 3.5 muEq/min/m2. Term infants produced even greater amount of net acid, 20.6 +/- 2.9 and 35 +/- 3.7 muEq/min/m2 respectively for the two TPN solutions. Milk fed infants are less prone to acidosis because of base generated from milk consumption. Due to its inherent acidogenic effect, TPN solutions induce acidosis more readily. Infants receiving TPN are therefore required to generate a higher NAE rate to maintain acid-base homeostasis compared to milk fed infants.
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PMID:Net acid excretion during first week of life. 680 Sep 70

An experimental infant developed to meet the specific nutritional needs of very-low-birth-weight infants was evaluated by 96-hour balance studies in ten preterm infants (birth weight: 1,130 to 1,530 gm). The formula contained 23.2 gm/liter of protein (whey protein/casein ratio, 60:40), 44.1 gm/liter of fat (50% medium-chain triglycerides) and 85.0 gm/liter of carbohydrate (50% lactose, 50% Polycose), and provided relatively higher amounts of calcium, phosphorus, vitamin D, and electrolytes than are in human milk. All infants were fed 150 ml/kg/day (120 calories/kg/day) by intermittent gavage. Balance studies were carried out nine days following establishment of oral intake. The mean (+/- SEM) nutrient retention rates revealed by balance studies in these infants (calcium, 170 +/- 4 mg/kg/day; phosphorus, 78 +/- 3 mg/kg/day; nitrogen, 426 +/- 8 mg/kg/day; sodium, 1.4 +/- 0.1 mEq/kg/day) were comparable to normal fetal accretion rates. The mean (+/- SEM) fat absorption was 92.5 +/- 0.9%. No clinical intolerances or biochemical abnormalities were observed, and adequate postnatal growth was achieved in all infants. The diet proved to be nutritionally advantagaeous and safe for very-low-birth-weight infants.
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PMID:Nutritional balance studies in very-low-birth-weight infants: enhanced nutrient retention rates by an experimental formula. 740 7

To reveal the role of serotonergic neurons in the regulation of feeding, the levels of 5-hydroxyindoleacetic acid (5-HIAA), a metabolite of serotonin, in the striatum and the hypothalamus were continuously monitored by an in vivo microdialysis technique. Intake of 20% casein diet did not induce significant changes in the 5-HIAA level in these regions. When rats were fed on 5% casein diet (83.5% carbohydrate diet) for 2 h, the level of 5-HIAA in the striatum gradually increased and reached a maximum (226 +/- 44% of basal level, M +/- SEM, n = 7) at 4 h after stopping the diet. In the medial hypothalamus, its level also increased to 183 +/- 19% (n = 10) at 2 h after starting the diet. On the other hand, a 60% casein diet increased the level of 5-HIAA in the lateral hypothalamus to 138 +/- 19% (n = 10) at 2 h after starting the diet. The intravenous infusion of each of these nutrients, glucose, amino acid mixture or lipid, produced more rapid elevation of the 5-HIAA level than oral intake of the diets. When rats were infused with glucose, its level in the striatum continued to be elevated. In the medial hypothalamus, glucose infusion increased 5-HIAA to the maximum (189 +/- 38%, n = 7) at 4 h after starting infusion. In contrast, serotonergic neurons in the lateral hypothalamus seemed to respond only to infusion of the amino acid mixture, and the level of 5-HIAA reached 163 +/- 14% (n = 5) of the basal level at 1 h after starting the infusion. These results suggest that rapid elevation of glucose or amino acids may independently stimulate serotonin metabolism in these brain areas, participating in the feedback regulation of nutrient intake.
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PMID:Amino acids and glucose differentially increased extracellular 5-hydroxyindoleacetic acid in the rat brain. 747 77

It was the purpose of this study to define whether trypsin inhibitors impair protein digestibility via enhanced loss of exogenous or endogenous protein by quantifying those losses using the homoarginine technique, recently developed in this laboratory. Pigs fitted with permanent ileal T-cannulas were fed test meals containing homoarginine-labeled protein. The meals contained casein and increasing doses of trypsin inhibitors (Experiment 1) or alternatively either heat-treated or raw ground soybeans (Experiment 2). Following a casein meal (425 mmol nitrogen, no trypsin inhibitors), ileal protein was predominantly of endogenous rather than of exogenous origin (105 vs. 9 mmol nitrogen). Addition of isolated trypsin inhibitors (3000 mg) enhanced appearance of both endogenous and exogenous protein at the ileum (by 73 and 9 mmol nitrogen, respectively). Feeding raw instead of heat-treated soybeans in one single test meal caused a significant increase of endogenous protein from 217 +/- 42 to 263 +/- 47 mmol (mean +/- SEM) and of exogenous protein from 16 +/- 3 to 48 +/- 14 mmol. If fed continuously for 1 wk, a raw soybean diet caused endogenous protein loss to rise significantly from 221 +/- 26 to 432 +/- 85 mmol. We conclude that ingestion of food containing trypsin inhibitor affects nitrogen balance more by losses of amino acids of endogenous secreta than by losses of dietary amino acids.
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PMID:Soybean trypsin inhibitor(s) reduce absorption of exogenous and increase loss of endogenous protein in miniature pigs. 750 18

Chemonucleolysis is a therapeutic procedure whereby a degradative enzyme is injected intradiscally to reduce disc height/width by depolymerisation of extracellular matrix components. This process is considered to diminish disc pressure on inflamed nerve roots, resulting in the alleviation of sciatic pain. In the present study two krill (Euphasia superba) enzyme preparations, a proteinase and an esterase preparation, were evaluated for their potential as chemonucleolytic agents. Initially, their ability to degrade several protein (azocoll, casein, proteoglycans, PGs) and peptide (CBZ-arg-4-nitroanilide, CBZ-lys-thiobenzyl ester) substrates was assessed in vitro. The krill proteinase preparation rapidly converted azocoll, casein and PGs to small peptides. Furthermore, when this degradative enzyme preparation was evaluated in vivo, a relatively low intradiscal dose (0.54 mg/disc) was found to reduce intervertebral disc widths in beagles to 48% +/- 10.5% (mean +/- SEM) of their pre-injection values within 2 weeks of administration. Moreover, the discs injected with this proteinase had reconstituted up to 80% +/- 9% (mean +/- SEM) of their pre-injection widths at the termination of the experiment (32 weeks). These data suggest that the krill protease preparation has potential as a chemonucleolytic agent which would allow disc matrix reconstitution. Conversely, the krill esterase preparation also degraded PGs, but into relatively large fragments. This limited digestion of PGs indicates that the krill esterase would be a less effective chemonucleolytic agent than the corresponding proteinase.
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PMID:Evaluation of digestive proteinases from the Antarctic krill Euphasia superba as potential chemonucleolytic agents. In vitro and in vivo studies. 761 35

Expression of major histocompatibility (MHC) class II molecules by enterocytes is known to be enhanced in coeliac disease and other disorders characterised by intestinal inflammation--an effect thought to be mediated via intestinal lymphocytes. To investigate if food peptides can exert direct effects on class II expression, the influence of gliadins, casein, and beta lactoglobulin on an intestinal epithelial cell line (HT-29) was examined in the absence of immune cells. Class II expression was determined by flow cytometry and immunofluorescence microscopy using antibodies against the beta chain of all products of the gene subregions DR, DQ, and DP. MHC expression was low in HT-29 cells but could be stimulated by interferon gamma. Tryptin digested gliadin had no effect on class II expression. In the presence of interferon gamma, however, it was able to amplify MHC class II expression to mean (SEM) 150 (4)%. Casein exerted a similar effect (160 (14)%), but undigested gliadin, tryptin digested casein, and beta lactoglobulin had no influence. The observations suggest that within the concert of cytokine mediated interactions between enterocytes and lymphocytes, some dietary peptides could upregulate the presentation of food antigens, leading to a more efficient stimulation of lymphocytes, which in the case of coeliac disease might result in damage to the enterocytes.
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PMID:Effect of gliadin and other food peptides on expression of MHC class II molecules by HT-29 cells. 773 62

Ileal and fecal gut endogenous nitrogen and amino acid excretions in adult domestic cats were determined. Ileal digesta were collected (10 cm of terminal ileum) from the cats fed either a protein-free diet or an enzymatically hydrolyzed casein-based diet (free amino acids and peptides < 10,000 Da) for 1 wk. Chromic oxide was included in each diet as an indigestible marker. The relative contribution of the hindgut to total endogenous gut excretion was investigated in a separate study by feeding cats a protein-free diet with or without added antibiotics for 10 d. Endogenous ileal nitrogen and amino acid nitrogen excretions of (mean +/- SEM 2.4 +/- 0.27 and 1.9 +/- 0.13 mg/g food dry matter intake, respectively, were found for the cats fed the protein-free diet, whereas higher excretions of 3.6 +/- 0.73 (P = 0.12) and 3.6 +/- 0.76 (P = 0.03) mg/g food dry matter intake were obtained in cats fed the enzymatically hydrolyzed casein. Significantly (P < 0.05) higher endogenous ileal amino acid excretions, for the enzymatically hydrolyzed casein-fed cats compared with those fed the protein-free diet, were found for methionine, aspartic acid, serine, glutamic acid, proline, valine and isoleucine, with the differences in excretions of glycine, alanine, leucine and histidine being significant at the 6% level. Most of the endogenous fecal amino acid excretions were unaffected by the inclusion of the antibiotics in the protein-free diet, although bacterial numbers were significantly lower (69%). Antibiotics addition led to significantly higher fecal endogenous excretions of nitrogen, taurine, threonine, serine and histidine but significantly lower excretions of methionine and lysine. Cats, like other simple-stomached mammals, excrete higher amounts of endogenous amino acids at the terminal ileum when the diet contains peptides.
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PMID:Gut endogenous nitrogen and amino acid excretions in adult domestic cats fed a protein-free diet or an enzymatically hydrolyzed casein-based diet. 861 99

The intracellular fate of Shigella dysenteriae type 1 strains grown in casamino acid-yeast extract (CYE) broth and nutrient broth (NB) was studied in casein-elicited mouse peritoneal macrophages. Virulent strains 14731 and W30864 cultured in NB and opsonised with normal mouse serum were susceptible to killing by peritoneal macrophages (66 SEM 1.7% killing by 2 h). In contrast, both strains grown in CYE broth and opsonised with normal mouse serum showed resistance to killing by peritoneal macrophages (76 SEM 1.4% survival by 2 h). Electronmicroscopy demonstrated that the bacteria escaped from the phagosome compartment by lysing the phagocytic vacuole and remained within the cytoplasm. Lipopolysaccharide (LPS) stimulated peritoneal macrophages to kill the opsonised strains 14731 and W30864 grown in CYE broth (85.4 SEM 1.6% killing by 2 h). Recombinant murine gamma interferon (rIFN-gamma) also stimulated macrophages to kill CYE-grown bacteria (52.1 SEM 1.3% killing by 2 h). However, an avirulent rough mutant strain W30864-22 grown in either NB or CYE broth showed marked susceptibility to killing by peritoneal macrophages, which was similar to that of NB-grown strain 14731 or W30864. The results of the present study suggest that in-vitro growth conditions may modulate the susceptibility of S. dysenteriae type 1 to killing by phagocytes.
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PMID:Effect of growth condition on in-vitro susceptibility of Shigella dysenteriae type 1 killing by murine peritoneal macrophages. 864 82

The purpose of this study was to establish, using a flooding dose of L-[ring 2, 6-(3)H] phenylalanine, whether feeding pigs diets that induce high endogenous gut nitrogen losses (ENL) also increases protein synthesis rates in (PSR) the visceral organs. Twelve 18-kg Yorkshire barrows with catheters in the right and left jugular veins were fed for 3 wk either casein-cornstarch- (CC) or barley-canola meal- (BCM) based diets formulated to a similar digestible energy /crude protein ratio and designed to induce either low or high ENL, respectively. Pigs were infused with 10 mL/kg body weight of a 150 mmol. L(-1) phenylalanine solution containing 230 MBq. L(-1) labeled phenylalanine for 12 min and killed 20 min later. Plasma phenylalanine specific radioactivity (SRA) rose to a plateau value within 3 min of starting the infusion and did not change (P > 0.10) thereafter. Fractional rates of protein synthesis (K(s), %/d) based on SRA in plasma- or intracellular-free phenylalanine did not differ (P > 0.10) in all tissues except pancreas (P < 0.05). Diet affected K(s )in liver (P < 0.01) and colon (P < 0.05) but not in pancreas, duodenum, jejunum and cecum. Based on plasma-free phenylalanine SRA, liver K(s)were 85.4 +/- 11.0 vs. 60.5 +/- 5.2 (mean +/- SEM) in CC- and BCM-fed pigs, respectively; these values were 82.3 +/- 4.7 vs. 98.2 +/- 5.8 in the colon. The absolute amount of protein synthesis (g.d(-1)) was higher in the liver (P < 0.05) and pancreas (P < 0. 05) of the CC pigs compared to BCM pigs. No dietary effects were observed in all other organs (P > 0.10). The present results suggest that feeding growing pigs a BCM diet that induces high ENL does not affect PSR in the small intestine of growing pigs from which >50% of ENL originates.
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PMID:Endogenous gut nitrogen losses in growing pigs are not caused by increased protein synthesis rates in the small intestine. 1070 86

Heat and alkali treatment of food may increase the concentrations of protein-bound D-amino acids and cross-links such as lysinoalanine (LAL). To examine how protein treatment affects digestibility, purified test meals [total protein 150 g/kg dry matter (DM), 0.44 MJ/(kg BW(0.75). d)] were prepared, containing (g/kg DM) casein, 75; beta-lactoglobulin, 50; or wheat protein, 40. Each was (15)N-labeled. Test proteins were used either in their native form or after treatment for 6 or 24 h at 65 degrees C, pH 10.5-11.5. Each meal was fed to nine adult miniature pigs (twofold complete cross-classification). Chyme was collected continuously over 33 h postprandially via T-fistulas in the terminal ileum, and digestibilities of test proteins and individual L- and D-amino acids were calculated on the basis of recovery of (15)N and the respective amino acids in the chyme. Treatment of casein, beta-lactoglobulin or wheat protein for 24 h increased levels of D-amino acid residues. L-Asparagine and aspartate (L-Asx) were particularly susceptible; 14. 7 +/- 0.4, 11.7 +/- 0.2 and 11.0 +/- 0.9%, respectively, underwent racemization. LAL levels increased in parallel; 11.7 +/- 0.3, 13.6 +/- 0 and 14.8 +/- 0.0%, respectively, of total lysine was converted to LAL. At the same time, prececal protein digestibility was decreased by 13.4 +/- 2.3, 15.3 +/- 1.4 and 17.8 +/- 1.2% units, respectively (P < 0.05; mean +/- SEM, n = 9). Digestibility of individual L-amino acids decreased by 10-15%, but L-amino acids prone to peptic cleavage, such as L-phenylalanine and L-tyrosine, were not affected. Digestibilities of D-amino acids and LAL were approximately 35%. It seems that mainly D-amino acids, and to a lesser extent LAL, were responsible for lower digestibility by interfering with peptic cleavage.
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PMID:Protein-bound D-amino acids, and to a lesser extent lysinoalanine, decrease true ileal protein digestibility in minipigs as determined with (15)N-labeling. 1091 20


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