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P A Finot

Publications and source records attributed to P A Finot.

At least 19 recordsLinked to original sources
PubMed2001

Effect of glutamine supplementation of the diet on tissue protein synthesis rate of glucocorticoid-treated rats.

Although glutamine status in the critically ill patient can be improved by nutritional means, the most effective way of effecting such supplementation has received little attention. We evaluated two different ways of supplementing clinical nutrition products with glutamine, either with free glutamine or by providing a glutamine-rich protein source, in acute glucocorticoid-treated (intraperitoneal dexamethasone, 120 mg/kg) rats. During the recovery period, the animals received isonitrogenous and isoenergetic diets containing either casein, mixed whey proteins with or without glutamine, or carob protein plus essential amino acids. Plasma and tissue amino acids and glutathione as well as tissue protein synthesis were measured. Dexamethasone treatment lowered weight gain, muscle glutamine, and muscle and jejunal protein synthetic rate. Muscle protein synthesis was increased (from 15.9% to 24.2%/d) only when glutamine was included in the diet as a free amino acid. This increase paralleled a rise in plasma glutamine. We speculate that glutamine provided in dietary protein is extensively metabolized by the splanchnic tissues and does not influence peripheral glutamine status to the same extent as glutamine provided in a free amino acid form. However, both forms of glutamine supplementation were equally effective in increasing protein synthesis in the jejunum (by 25%). This is likely the main benefit of glutamine supplementation of enteral nutrition formulas.

Amino Acids↗
PubMed2001

Free and protein-bound glutamine have identical splanchnic extraction in healthy human volunteers.

The objectives of the present study were to determine the splanchnic extraction of glutamine after ingestion of glutamine-rich protein ((15)N-labeled oat proteins) and to compare it with that of free glutamine and to determine de novo glutamine synthesis before and after glutamine consumption. Eight healthy adults were infused intravenously in the postabsorptive state with L-[1-(13)C]glutamine (3 micromol x kg(-1) x h(-1)) and L-[1-(13)C]lysine (1.5 micromol x kg(-1) x h(-1)) for 8 h. Four hours after the beginning of the infusion, subjects consumed (every 20 min) a liquid formula providing either 2.5 g of protein from (15)N-labeled oat proteins or a mixture of free amino acids that mimicked the oat-amino acid profile and contained L-[2,5-(15)N(2)]glutamine and L-[2-(15)N]lysine. Splanchnic extraction of glutamine reached 62.5 +/- 5.0% and 66.7 +/- 3.9% after administration of (15)N-labeled oat proteins and the mixture of free amino acids, respectively. Lysine splanchnic extraction was also not different (40.9 +/- 11.9% and 34.9 +/- 10.6% for (15)N-labeled oat proteins and free amino acids, respectively). The main conclusion of the present study is that glutamine is equally bioavailable when given enterally as a free amino acid and when protein bound. Therefore, and taking into consideration the drawbacks of free glutamine supplementation of ready-to-use formulas for enteral nutrition, protein sources naturally rich in this amino acid are the best option for providing stable glutamine.

Adult↗
PubMed2000

Role of glutamine on the de novo purine nucleotide synthesis in Caco-2 cells.

BACKGROUND: The body's nucleotide pool derives from three potential sources: de novo synthesis, salvage of preformed-nucleosides/bases or the diet. The relative contributions of these pathways of assimilation are poorly understood in vivo. Dietary nucleotides have been suggested to have beneficial effects an the development and repair of the gastrointestinal tract. Tissues with a rapid turnover, such as the gut and the immune system cells, may utilise preformed nucleotides (coming from the diet), in situations in which there is a high demand of nucleotides for nucleic acid synthesis. Therefore, nucleotides could be considered as conditionally essential nutrients. AIM OF THE WORK AND METHODS: Development of a method to measure synthesis de novo of RNA-purine nucleotides in Caco-2 cells, relying an the incorporation of 14C-glycine into the purine ring of the nucleotide. To establish the fractional synthesis rate of RNA purine nucleotides in Caco-2 cells, grown in culture medium containing different concentrations of glutamine, in the presence or absence of added nucleotides. To investigate the degree to which tissue ribonucleosides are derived from the culture medium or from de novo synthesis in the presence of different concentrations of glutamine, using undifferentiated Caco-2 cells, stressed or not by the addition of IL-1 beta to the medium. RESULTS AND CONCLUSIONS: The presence of high levels of glutamine in the culture medium is essential for cell proliferation (estimated by measurement of the fractional synthesis rate of purine nucleotides) and the presence of nucleotides cannot replace the glutamine dependence of Caco-2 cell proliferation. The incorporation of exogenous purine nucleotides into RNA of Caco-2 cells is rather limited, and it becomes important when cells are stressed by glutamine deprivation. Stress by addition of interleukin-1 beta resulted in the maintenance or the increase in de novo synthesised RNA-purine nucleotides, even in the presence of exogenous nucleotides. However, the addition of interleukin-1 beta to the culture medium led to an enhanced salvage of preformed pyrimidine nucleotides for nucleic acid synthesis when glutamine was present in the medium at a concentration of 0.5 mmol/L.

Caco-2 Cells↗
PubMed2000

Neither glutamine nor arginine supplementation of diets increase glutamine body stores in healthy growing rats.

The aim of the work was to resolve whether glutamine and arginine supplemented diets affect plasma and tissue (muscle, liver and intestinal mucosa) glutamine concentrations, as well as glutaminase and glutamine synthetase specific activities. The trial was performed in growing rats fed 10% protein diets for 3 weeks. Protein sources were: whey proteins (W); whey proteins+free glutamine (WG); whey proteins+arginine (WA); and casein+wheat protein hydrolysate+acid whey (39:39:22), as source containing protein-bound glutamine (CGW). Rats fed the control diet (6.4% glutamine) (W) showed comparable glutamine body stores to those of rats fed the WG diet. In fact, glutamine sup- plementation down-regulated the hepatic glutamine synthetic capacity of growing rats (W/WG: 6.8+/-0.3 vs 6.0+/-0.2 nmol/min/mg protein). Arginine supplementation of the diet (up to 9% of the protein content) resulted in a decrease in plasma and tissue glutamine concentrations (W/WA: plasma, 1218+/-51 vs 1031+/-48 micromol/L; liver 7.5+/-0.4 vs 6.5+/-0.2 micromol/g; muscle: 5.7+/-0.2 vs 4.0+/-0.2 micromol/g). These data suggest that glutamine supplementation of the diet does not increase plasma and tissue glutamine concentrations in healthy growing rats, while the addition of arginine to the diet decreases glutamine body stores.

Amino Acids↗
PubMed1994

Effects of diet-induced hyperthreoninemia. II). Tissue and extracellular amino acid levels in the brain.

Growing rats were fed graded levels of threonine (Thr, 0.4, 0.8, and 3.3 g/100 g diet). Free amino acid content was measured in plasma and brain. Extracellular amino acid levels were measured by microdialysis in brain slices. Large quantities of dietary Thr (3.3 g/100 g) raised plasma and brain Thr and glycine (Gly) levels. Brain and spinal cord extracellular levels of Thr were also raised, whereas the other amino acid levels remained unchanged. A moderate level of dietary Thr (0.8 g/100 g) raised plasma Thr and Gly levels and brain Thr but not Gly level. The diet raised cortical Thr extracellular levels but did not modify the levels of the other amino acids, including glutamate (Glu) and aspartate (Asp). These data suggest that brain neurochemical processes involving Gly, Glu, and Asp are safeguarded in rats fed high Thr levels.

Amino Acids↗
PubMed1993

Stearidonic acid, an inhibitor of the 5-lipoxygenase pathway. A comparison with timnodonic and dihomogammalinolenic acid.

Leukotrienes have been shown to play an important role as mediators in various disease processes, including asthma and inflammation; thus, their synthesis is tightly regulated. The major precursor of leukotrienes is arachidonic acid (20:4n-6). Fatty acids which are structurally similar to 20:4n-6, such as eicosatrienoic acid (20:3n-6; dihomogammalinolenic acid) and eicosapentaenoic acid (20:5n-3; timnodonic acid) have been found to inhibit leukotriene biosynthesis. Because of the structural similarity of octadecatetraenoic acid (18:4n-3; stearidonic acid) with 20:4n-6, the present study was undertaken to determine whether stearidonic acid also exerts an inhibitory effect on the 5-lipoxygenase pathway. Human leukocytes were incubated with 18:4n-3 (20 microM or 10 microM), 20:5n-3 (20 microM) or 20:3n-6 (20 microM) and subsequently stimulated with 1 microM ionophore A23187 and 20:4n-6 (20 microM or 10 microM). The 5-lipoxygenase products were then measured by high-performance liquid chromatography. Leukotriene synthesis was reduced by 50% with 20 microM 18:4n-3 and by 35% with 10 microM 18:4n-3. Formation of 5S,12S-di-hydroxy-eicosatetraenoic acid and of 5-hydroxy-eicosatetraenoic acid was decreased by 25% with 20 microM 18:4n-3 and by 3% with 10 microM 18:4n-3. The inhibition observed with 20 microM 18:4n-3 appeared to be of the same order as that observed with 20 microM 20:5n-3; the inhibition observed with 18:4n-3 was shown to be dose-dependent. The inhibition produced by 20 microM 20:3n-6 was greater than that observed with either 20 microM 18:4n-3 or with 20 microM 20:5n-3.(ABSTRACT TRUNCATED AT 250 WORDS)

8,11,14-Eicosatrienoic Acid↗
PubMed1993

Effects of diet-induced hyperthreoninemia. I). Amino acid levels in the central nervous system and peripheral tissues.

Rats were fed four levels of threonine (Thr, 0.4, 0.6, 0.8, and 5.8 g/100 g diet). After two weeks, Thr, serine (Ser), and glycine (Gly) levels were measured in plasma, liver, muscle, and central nervous system. The diet containing 5.8 g/100 g of Thr elevated Thr and Gly concentrations in plasma and nervous tissue in comparison with a standard diet. In muscle and liver, Thr concentrations were also raised but Gly levels did not change. The hepatic Thr dehydratase activity was enhanced. Diets containing moderate Thr quantities (0.6 and 0.8 g/100 g) induced slight elevations of Thr levels in all tissues. Gly concentrations were not modified. The activity of hepatic Thr dehydratase was diminished. Our results show that a high dietary content of Thr (15 times the normal levels) elevates Gly levels in various tissues, including the brain. On the contrary, diets containing 2 to 4 times the normal levels of Thr induce a weak hyperthreoninemia insufficient to modify brain Gly.

Alcohol Oxidoreductases↗
PubMed1992

Effects of 9, 12, 15-octadecatrien-6-ynoic acid on the metabolism of arachidonic acid in platelets and on platelet aggregation.

An acetylenic fatty acid: 9,12,15-octadecatrien-6-ynoic acid (dicranin) was extracted from Dicranum Scoparium and preincubated with platelets which were then stimulated by exogenous arachidonic acid (20:4 n-6). This molecule at 10(-4) M weakly inhibited the cyclooxygenase activity as assessed by measurement of 12-hydroxy-heptadecatrienoic acid (HHT) In contrast, the 12-hydroxy-eicosatetraenoic acid (12-HETE) synthesized by the 12-lipoxygenase was strongly increased by about 650%. The same effects were observed with 10(-5) M and with 10(-6) M of dicranin but to a lesser extent. Platelet hydroxylated dicranin metabolites were also found and the structure of the main compound determined by GC-MS was a 13-hydroxy derivative. Its origin has not yet been elucidated. Platelet aggregation induced by 1 microgram/ml of U46619, a structural PGH2 analogue was completely abolished in the presence of dicranin. Platelet aggregation induced either by thrombin or by arachidonic acid was inhibited by 10(-4) M of dicranin only after preincubation. This observation indicates that the formation of metabolites of dicranin are necessary to effect this inhibition. Dicranin is thus a new inhibitor of platelet aggregation and may prove to be useful for elucidating the effects of 12-HETE in biological systems.

12-Hydroxy-5,8,10,14-eicosatetraenoic Acid↗
PubMed1992

Effects of 9,12,15-octadecatrien-6-ynoic acid on the metabolism of arachidonic acid in platelets and on the platelet aggregation.

An acetylenic fatty acid: 9,12,15-octadecatrien-6-ynoic acid (dicranin), extracted from Dicranum Scoparium was preincubated with platelets stimulated by exogenous arachidonic acid (20:4 n-6). Dicranin (10(-4) M) weakly inhibited the cyclooxygenase activity as assessed by measurement of 12-hydroxy-heptadecatrienoic acid (HHT) In contrast, the 12-hydroxy-eicosatetraenoic acid (12-HETE) synthesized by the 12-lipoxygenase was strongly increased by about 650%. The same effects were observed with 10(-6) M of dicranin but to a lesser extent. The main platelet hydroxylated dicranin metabolite determined by GC-MS was a 13-hydroxy derivative Platelet aggregation induced either by thrombin or by arachidonic acid or by U46619, an structural PGH2 analogue was inhibited by 10(-4) M of dicranin.

12-Hydroxy-5,8,10,14-eicosatetraenoic Acid↗
PubMed1992

Maillard reaction products and lysinoalanine: urinary excretion and the effects on kidney function of preterm infants fed heat-processed milk formula.

Heat processing is essential for the preservation of milk-based infant formulas. Heating, however, induces a number of chemical changes during which lysine in the milk proteins reacts with reducing sugars to form Maillard reaction products (MRPs) and also reacts with the dehydroalanine resulting from cystine degradation to form lysinoalanine (LAL). Both products have been reported to induce histological changes in the straight portion of the proximal tubule in the rat kidney. This pilot study was made to investigate the urinary excretion by healthy preterm babies of MRPs and LAL contained in infant formula and to determine their influence on kidney function. Twelve healthy male preterm babies were first fed for 10 days with pooled human milk and then for 5 days with each of two experimental premature infant formulas in a cross-over design. The infant formulas were sterilized either by ultra-high temperature (UHT) treatment or by a conventional retort process to give products with low and high levels of MRPs and LAL, respectively. In total, some 15.6% of the initial lysine had been modified in the in-can-sterilized product, compared to 6.2% in the UHT product. Urinary excretion of MRP lactulosyllysine ranged from 1.3 to 3.9% of the ingested amount, whereas that of LAL ranged from 6.2 to 9.3%. The higher level of MRPs and LAL in the formulas compared to breast milk had no influence on creatinine clearance or electrolyte excretion. There was no evidence of tubular damage as determined by the urinary excretion of four kidney-derived enzymes. Feeding of formula, however, did result in a general increase in urinary microprotein levels.(ABSTRACT TRUNCATED AT 250 WORDS)

Analysis of Variance↗
PubMed1991

Improvement in the nutritional quality of bread.

To assess whether the dipeptide N-epsilon-(gamma-L-glutamyl)-L-lysine (glutamyl-lysine) can serve as a nutritional source of lysine, we compared the growth of mice fed (a) an amino acid diet in which lysine was replaced by six dietary levels of glutamyl-lysine; (b) wheat gluten diets fortified with lysine; (c) a wheat bread-based diet (10% protein) supplemented before feeding with lysine or glutamyl-lysine (0, 0.75, 1.50, 2.25, and 3% lysine HCl-equivalent in the final diet), not co-baked and (d) bread diets co-baked with these levels of lysine or glutamyl-lysine. With the amino acid diet, the relative growth response to glutamyl-lysine was about half that of lysine. The effect of added lysine on the nutritional improvement of wheat gluten depended on both lysine and gluten concentrations in the diet. With 10 and 15% gluten, 0.37% lysine HCl produced a marked increase in weight gain. Further increase in lysine HCl to 0.75% proved detrimental to weight gain. Lysine HCl addition improved growth at 20 and 25% gluten in the diet and did not prove detrimental at 0.75%. For whole bread, glutamyl-lysine served nearly as well as lysine to improve weight gain. The nutritive value of bread crust fortified or not was markedly less than that of crumb or whole bread. Other data showed that lysine or glutamyl-lysine at the highest level of fortification, 0.3%, improved the protein quality (PER) of crumb over that of either crust or whole bread, indicating a possible greater availability of the second-limiting amino acid, threonine, in crumb. These data and additional metabolic studies with U-14-C glutamyl-lysine suggest that glutamyl-lysine, co-baked or not, is digested in the kidneys and utilized in vivo as a source of lysine; it and related peptides merit further study as a sources of lysine in low-lysine foods.

Amino Acids↗
PubMed1990

Effects of foods rich in polyphenols on nitrogen excretion in rats.

The extent to which tea, cocoa and carob (foods rich in polyphenols) influence fecal nitrogen (N) excretion was investigated in rats. The studies took into account the methylxanthine contents of tea and cocoa as well as the poor digestibility of cocoa nitrogen. Balance measurements indicated that all three food sources significantly increased fecal nitrogen excretion relative to methylxanthine-matched control diets (p less than 0.01). In the case of cocoa, virtually all the increase could be attributed to the poor digestibility of cocoa protein itself (estimated to be only 28-30% of total N in cocoa powder). There appeared to be no other effects. With extracts of tea and carob, however, the increased excretion of N in feces resulted either from a decreased digestibility of other dietary protein, through interaction with their polyphenols, or from a stimulation of the excretion of endogenous (body) nitrogen. With respect to the latter possibility, a preliminary investigation with the stable isotope of nitrogen (15N) showed that tea produced a marked increase in the excretion of endogenous nitrogen. These studies, therefore, indicate that foods rich in polyphenols have varying effects on N excretion in feces and that, in the case of tea at least, the loss of endogenous nitrogen may be a major contributing factor.

Animals↗
PubMed1989

Black currant seed oil feeding and fatty acids in liver lipid classes of guinea pigs.

Guinea pigs were fed one of three diets containing 10% black currant seed oil (a source of gamma-linolenic (18:3 n-6) and stearidonic (18:4 n-3) acids), walnut oil or lard for 40 days. The fatty acid composition of liver triglycerides, free fatty acids, cholesteryl esters, phosphatidylinositol, phosphatidylserine, cardiolipin, phosphatidylcholine and phosphatidylethanolamine were determined. Dietary n-3 fatty acids found esterified in liver lipids had been desaturated and elongated to longer chain analogues, notably docosapentaenoic acid (22:5 n-3) and docosahexaenoic acid (22:6 n-3). When the diet contained low amounts of n-6 fatty acids, proportionately more of the n-3 fatty acids were transformed. Significantly more eicosapentaenoic acid (EPA) (20:5 n-3) was incorporated into triglycerides, cholesteryl esters, phosphatidylcholine and phosphatidylethanolamine of the black currant seed oil group compared with the walnut oil group. Feeding black currant seed oil resulted in significant increases of dihomogamma-linolenic acid (20:3 n-6) in all liver lipid classes examined, whereas the levels of arachidonic acid (20:4 n-6) remained relatively stable. The ratio dihomo-gamma-linolenic acid/arachidonic acid was significantly (2.5-fold in PI to 17-fold in cholesteryl esters) higher in all lipid classes from the black currant seed oil fed group.

Animals↗
PubMed1989

The effect of Maillard reaction products on zinc metabolism in the rat.

The effect of giving Maillard reaction products (MRP) on zinc metabolism was investigated in the rat. In Expt 1, MRP were prepared by incubating casein with either glucose or lactose under controlled reaction conditions, and were quantified as either 'early' or 'advanced' after estimation of lysine loss and lysine destruction respectively. In Expt 2, the effect of the purified early MRP fructose--lysine (FL) on Zn metabolism was studied. The experimental diets containing 20 mg Zn/kg were given to weanling rats for 21 d. Zn balance was assessed over 9-14 d (Expt 1), or 1-14 d (Expt 2). Femur, liver, kidney and serum Zn concentrations were determined at 21 d. The major effect of the MRP in the casein-sugar mixtures was on urinary Zn excretion. The casein-glucose MRP induced up to a 6-fold increase in the quantity of Zn excreted in the urine. The magnitude of the hyperzincuria increased with the extent of the Maillard reaction. Similar dietary levels of casein-lactose MRP increased urinary Zn loss 2-fold. Free FL had no effect on urinary Zn. Faecal Zn, Zn retention, liver, femur and serum Zn were generally not influenced by giving MRP from casein-sugar mixtures or by giving free FL, although kidney Zn was decreased in rats fed on FL. It was concluded that although urinary Zn excretion can be increased by the presence of MRP in the diet, this is only a minor excretory pathway and would have little influence on overall Zn nutrition in individuals fed on a diet adequate in Zn.

Animals↗
PubMed1989

Metabolic transit and toxicity of Maillard reaction products.

The feeding of Maillard reaction products (MRP) has been reported to lead to a variety of effects on metabolism which may be classed as "anti-nutritional" or "anti-physiological", depending on whether they are due to the loss of essential nutrients or to the presence of the MRP per se. This paper describes the sensitivity of essential nutrients in the "early" and "advanced" stages of the Maillard reaction, the metabolic transit of Amadori compounds, premelanoidins, melanoidins, hydroxymethyl-furfural, carboxymethyl-lysine, as well as the effects of MRP on pancreatic amylase and on urinary zinc excretion.

Animals↗