PubMed Health⌕ Search

Biomedical subjects

D Darmaun

Publications and source records attributed to D Darmaun.

At least 19 recordsLinked to original sources
PubMed2003

[Feeding of infants based on age. Practice guidelines].

This paper presents practical guidelines for nutrition and feeding of infants and toddlers including vitamin D, vitamin K and fluoride supplementations and preventive measures at risk for food allergy based on family history.

Breast Feeding↗
PubMed2002

[Nutritional treatment of acute diarrhea in an infant and young child].

This paper written by the Comité de nutrition de la Société française de pédiatrie is specially devoted to the nutritional treatment of infant and child acute diarrhea, i.e. oral rehydration with salts solution and feeding. It complements an article on drug therapy of child acute diarrhea written by the Groupe francophone d'hépatologie, gastroentérologie et nutrition pédiatriques, and published in this same issue of the Archives de pédiatrie.

Acute Disease↗
PubMed2002

A new labeling approach using stable isotopes to study in vivo plasma cholesterol metabolism in humans.

A method to study reverse cholesterol transport in humans was developed using stable isotopes and kinetic analysis. Three normolipidemic subjects received simultaneous intravenous infusions of deuterated leucine and (13)C-acetate for 14 and 8 hours, respectively. Deuterium enrichment was measured in protein-bound leucine in apolipoproteins (apo) B-100 and A-I (using gas chromatography coupled with mass spectrometry [GCMS]) and (13)C-enrichment in unesterified cholesterol and cholesteryl ester (using gas chromatography coupled to isotope ratio mass spectrometry [GC-C-IRMS]) in very-low-density lipoprotein (VLDL), low-density lipoprotein (LDL), and high-density lipoprotein (HDL) during the tracer infusion. Curves were analyzed using multicompartmental analysis. This protocol is suitable to quantify the different processes involved in reverse cholesterol transport (RCT) in humans, including cholesterol esterification, transfer of cholesteryl ester from HDL towards apo B-100-containing lipoproteins, and the contribution of VLDL, LDL, and HDL in the final steps of RCT. In agreement with previous data from kinetic analysis of radiotracer experiments, our results suggest that in fasting normolipidemic subjects the major fraction of cholesteryl ester enters plasma through esterification in HDL (more than 95%). The major fraction of cholesteryl ester disappears through apo B-100-containing lipoproteins (VLDL and LDL) catabolism (mean of 82%) rather than through removal from HDL (mean of 18% with approximately an equal part for apo AI-dependent and independent catabolism, respectively, 7% and 11%). We conclude that this protocol could be applied to study the modulation of these processes by nutrition, diseases, or pharmacologic treatments.

Acetates↗
PubMed2002

Can glutamine and growth hormone promote protein anabolism in children with cystic fibrosis?

To determine whether recombinant human growth hormone (rhGH), glutamine (GLN) or a combination of both agents can enhance protein synthesis in cystic fibrosis (CF) patients, six 9.6 +/- 0.5-year-old prepubertal children (4 M, 2 F) with CF and stable lung disease with undernutrition (weight/height <50th percentile) or delayed growth (height <5th percentile) received stable isotope infusions, in the postabsorptive state and on 4 separate study days: (a) at baseline, and after a 4-week treatment with either, (b) oral GLN (0.7 g/kg/day), (c) rhGH (0.3 mg/kg/week, SC), or (d) both GLN and rhGH. Four-hour infusions of (13)C-leucine were used to assess leucine appearance rate (Ra, an index of protein breakdown), oxidation (Ox), and non-oxidative leucine disposal (NOLD, an index of protein synthesis). Results are expressed as changes (%) from baseline:We conclude that in children with CF: (1) due to high inter-subject variability, oral glutamine does not significantly enhance protein gain; (2) rhGH has significant anabolic effects which are mediated by stimulation of protein synthesis, and (3) glutamine does not enhance the effect of rhGH.

Bicarbonates↗
PubMed2001

Use of L-[(15)N] glutamic acid and homoglutathione to determine both glutathione synthesis and concentration by gas chromatography-mass spectrometry (GCMS).

A method for simultaneous measurement of both glutathione enrichment and concentration in a biological sample using gas chromatography mass spectrometry is described. The method is based on the preparation of N,S-ethoxycarbonylmethyl ester derivatives of glutathione, and the use of homoglutathione (glutamyl-cysteinyl--alanine) as an internal standard. A procedure for determination of glutamate concentration and enrichment is also reported. Both methods have within-day and day-to-day inter-assay coefficients of variation less than 5%, and recoveries of known added amounts of glutathione and glutamate are close to 100%. Taken together, these methods allowed determination of glutathione concentration and fractional synthesis rate in red blood cells using L-[(15)N] glutamic acid infusion. This approach was applied in vivo to investigate the effects of a 72 h fast, compared with a control overnight fast, on erythrocyte glutathione in a single dog. The 72 h fast was associated with a 39% decline in erythrocyte glutathione level, (2.9 +/- 0.4 versus 4.7 +/- 0.5 mmol l(-1), fasting versus control) with no change in glutathione fractional synthesis (67.4 versus 71.3% d(-1), fasting versus control).

Animals↗
PubMed2001

[Infant formulas and soy protein-based formulas: current data].

For many years soy bean-based formulas (SBBF) were the only dietary product used for infants with cow's milk intolerance. At the present time, their place in infant nutrition is reduced as a result of the availability of new dietary products without lactose and/or cow's milk proteins and the recognition of soy bean protein allergy. There is no evidence that SBBF have any efficiency in infant colic. SBBF have no indication in the prevention of allergy, nor in premature infants' nutrition. Their main indication is the feeding of infants of vegetarian parents who do not want to use cow's milk products. Studies have shown that SBBF contain large quantities of phytoestrogens, particularly isoflavone. Because of experimental data suggesting a possible deleterious effect of phytoestrogens on the neuroendocrine maturation, the reduction of their content in SBBF must be considered.

Colic↗
PubMed2001

Effects of dietary protein restriction and amino acids deficiency on protein metabolism in dogs.

Although stable isotope methods have been used to revisit the protein and amino acid requirements of humans in the last two decades, estimates of the minimum protein requirement of the dog have mainly been based on nitrogen balance studies. The aim of this study was: (i) to assess dog protein metabolism using the (13)C-leucine method, and (ii) to test the effects of protein deprivation and amino acid deficiency on protein metabolism. Eight dogs were fed three consecutive diets: (i) a normoprotein regimen [control; 63 g crude protein (CP)/Mcal metabolizable energy (ME)]; (ii) a protein-restricted diet (PR; 32 g CP/Mcal ME); and (iii) a protein-restricted diet that was, in addition, deficient in lysine and tryptophan (D-PR; 31 g CP/Mcal ME). The energy supply was similar for the three diets. The dogs were adapted to each diet for 2 weeks. After a 24 h fasting period, a 3 h infusion of (13)C-bicarbonate was performed, followed by a 3 h continuous infusion of L-[1-(13)C]leucine. Blood and breath samples were collected before and during the last hour of each isotope infusion for determination of plasma (13)C-alpha-ketoisocaproate and breath (13)CO(2) enrichments by mass spectrometry. Rates of protein breakdown, oxidation, and synthesis were calculated from leucine appearance into plasma, oxidation, and non- oxidative disposal, respectively, and expressed in g N/kg body weight (BW)0.75 per day, assuming body protein contains 0.08 g leucine per g protein. Protein breakdown was 3.71 +/- 0.17, 3.29 +/- 0.16 and 2.73 +/- 0.18 (mean +/- SEM) for control, PR, and D-PR, respectively (p < 0.01 D-PR versus control, and p < 0.05 D-PR versus PR). Protein synthesis was 3.08 +/- 0.13, 2.77 +/- 0.13, and 2.15 +/- 0.18 for control, PR and D-PR, respectively (p < 0.001 D-PR versus control, and p < 0.05 D-PR versus PR). Protein oxidation was 0.63 +/- 0.05, 0.53 +/- 0.05 and 0.58 +/- 0.05 for control, PR and D-PR, respectively (p=NS). These data suggest that: (i) the (13)C-leucine method can be used to assess large variations of protein turnover in dogs; (ii) dogs have the capacity to adapt their protein turnover to the level and to the quality of their protein supplies; and (iii) the dog nitrogen requirement for maintenance may be between 0.41 and 0.55 g N/kg BW(0.75) per day.

Adaptation, Physiological↗
PubMed2001

Protein restriction and dexamethasone as a model of protein hypercatabolism in dogs: effect of glutamine on leucine turnover.

To determine (1) whether protein restriction, combined with glucocorticosteroid treatment, can be used as a hypercatabolic model and (2) if so, whether glutamine attenuates protein wasting in this model, the effects of protein restriction, dexamethasone, and glutamine on leucine metabolism were assessed in dogs. A control group (n = 8) received a maintenance diet; another group (n = 8) received a protein-restricted diet either (1) alone; (2) along with a 7-day corticoid treatment; or (3) along with a 7-day corticoid treatment and a 7-hour intravenous (IV) glutamine infusion. The last day of each regimen, dogs underwent an IV isotope infusion in the fasting state, with a 3-hour NaH(13)CO3 infusion to assess CO2 production, and immediately thereafter, a 3-hour (13)C-leucine infusion to assess leucine appearance rate (Ra), oxidation (Ox), and nonoxidative leucine disposal (NOLD), expressed as micromol x kg(-1) x h(-1). Protein restriction was associated with a 24% decline in leucine Ra (223 +/- 16 v 298 +/- 17; P <.01), an index of whole body proteolysis, and a 29% decline in NOLD (180 +/- 15 v 223 +/- 13; P <.01), an index of whole body protein synthesis. In the protein-restricted group, dexamethasone treatment was associated with a 32% increase in Ra, (295 +/- 28 v 223 +/- 16; P <.05), a 186% increase in Ox (120 +/- 14 v 43 +/- 4; P <.001), with no change in NOLD, when compared with the protein-restricted alone. After protein restriction + dexamethasone, glutamine infusion induced a 40% increase in plasma glutamine (1,090 +/- 70 v 780 +/- 29 micromol x L(-1); P <.01), but failed to alter Ra, Ox, or NOLD. These results suggest that (1) in dogs, protein restriction combined with a 7-day course of dexamethasone results in alterations in leucine kinetics similar to those observed in stress-induced protein wasting in humans, and (2) in that model, a 7-hour IV glutamine infusion in the fasting state does not significantly attenuate protein wasting.

Animals↗
PubMed2001

Effects of glutamine deprivation on protein synthesis in a model of human enterocytes in culture.

To assess the effect of glutamine availability on rates of protein synthesis in human enterocytes, Caco-2 cells were grown until differentiation and then submitted to glutamine deprivation produced by exposure to glutamine-free medium or methionine sulfoximine [L-S-[3-amino-3-carboxypropyl]-S-methylsulfoximine (MSO)], a glutamine synthetase inhibitor. Cells were then incubated with (2)H(3)-labeled leucine with or without glutamine, and the fractional synthesis rate (FSR) of total cell protein was determined from (2)H(3)-labeled enrichments in protein-bound and intracellular free leucine measured by gas chromatography-mass spectrometry. Both protein FSR (28 +/- 1.5%/day) and intracellular glutamine concentration (6.1 +/- 0.6 micromol/g protein) remained unaltered when cells were grown in glutamine-free medium. In contrast, MSO treatment resulted in a dramatic reduction in protein synthesis (4.6 +/- 0.6 vs. 20.2 +/- 0.8%/day, P < 0.01). Supplementation with 0.5-2 mM glutamine for 4 h after MSO incubation, but not with glycine nor glutamate, restored protein FSR to control values (24 +/- 1%/day). These results demonstrate that in Caco-2 cells, 1) de novo glutamine synthesis is highly active, since it can maintain intracellular glutamine pool during glutamine deprivation, 2) inhibition of glutamine synthesis is associated with reduced protein synthesis, and 3) when glutamine synthesis is depressed, exogenous glutamine restores normal intestinal FSR. Due to the limitations intrinsic to the use of a cell line as an experimental model, the physiological relevance of these findings for the human intestine in vivo remains to be determined.

Apolipoproteins A↗
PubMed2000

Role of glucose in the regulation of glutamine metabolism in health and in type 1 insulin-dependent diabetes.

To determine the effect of glucose availability on glutamine metabolism, glutamine kinetics were assessed under conditions of hyperglycemia resulting from 1) intravenous infusion of 7.5% dextrose in healthy adults and 2) insulin deficiency in young adults with insulin-dependent diabetes mellitus (IDDM). Eight healthy adults and five young adults with IDDM were studied in the postabsorptive state by use of a primed continuous infusion of D-[U-(14)C]glucose, L-[5,5,5-(2)H(3)]leucine, and L-[3, 4-(13)C]glutamine. Whether resulting from insulin deficiency or dextrose infusion, the rise in plasma glucose was associated with increased glucose turnover (23.5 +/- 0.7 vs. 12.9 +/- 0.3 micromol. kg(-1). min(-1), P < 0.01 and 20.9 +/- 2.5 vs. 12.8 +/- 0.4 micromol. kg(-1). min(-1), P = 0.03, in health and IDDM, respectively). In both cases, high blood glucose failed to alter glutamine appearance rate (R(a)) into plasma [298 +/- 9 vs. 312 +/- 14 micromol. kg(-1). h(-1), not significant (NS) and 309 +/- 23 vs 296 +/- 26 micromol. kg(-1). h(-1), NS, in health and IDDM, respectively] and the estimated fraction of glutamine R(a) arising from de novo synthesis (210 +/- 7 vs. 217 +/- 10 micromol. kg(-1). h(-1), NS and 210 +/- 16 vs. 207 +/- 21 micromol. kg(-1). h(-1), NS, in health and IDDM, respectively). When compared with the euglycemic day, the apparent contribution of glucose to glutamine carbon skeleton increased when high plasma glucose resulted from intravenous dextrose infusion in healthy volunteers (10 +/- 0.8 vs. 4.8 +/- 0.3%, P < 0.01) but failed to do so when hyperglycemia resulted from insulin deficiency in IDDM. We conclude that 1) the contribution of glucose to the estimated rate of glutamine de novo synthesis does not increase when elevation of plasma glucose results from insulin deficiency, and 2) the transfer of carbon from glucose to glutamine may depend on insulin availability.

Adult↗
PubMed2000

Duodenal vs. gastric administration of labeled leucine for the study of splanchnic metabolism in humans.

Low-rate (6 ml/h) intragastric infusion of stable, isotope-labeled amino acids is commonly used to assess the splanchnic handling of amino acids in humans. However, when used in the postabsorptive state, this method yields unreliable plasma isotopic enrichments, with a coefficient of variation >10%. In this metabolic condition, we confirmed in six subjects that an intragastric infusion of L-[(2)H(3)]leucine at 6 ml/h yields an unreliable isotopic steady state in plasma amino acids with a coefficient of variation of 43 +/- 12% (mean +/- SD). In five additional subjects, we assessed the effects of 1) increasing the rate of delivery of a leucine tracer in an isotonic plasmalike solution at 240 ml/h into the gastric site, and 2) changing the site of infusion from gastric to duodenal with this same high rate of delivery. In contrast to the gastric route, and regardless of the rate of delivery, only the intraduodenal route allowed 1) isotopic plasma steady state (i.e., coefficients of variation were <10%: 5 +/- 3%), and 2) reproducible leucine extraction coefficients (22 +/- 5%). We conclude that an infusion site that bypasses the gastric emptying process, i.e., the duodenal route, along with delivery of a plasmalike solution, is necessary to reach isotopic steady state in plasma when labeled leucine is infused into the gastrointestinal tract in the postabsorptive state.

Adult↗
PubMed1999

Is glutamine a 'conditionally essential' amino acid in Duchenne muscular dystrophy?

To determine whether whole body protein kinetics are altered in Duchenne muscular dystrophy (DMD), six 9 +/- 1-year-old children with DMD and five weight and height matched controls, received intravenous infusion of L-[1-(13)C]leucine and L-[2-(15)N]glutamine in the post-absorptive state. Glutamine rate of appearance was approximatly 24% lower in DMD boys than in controls (321 +/- 22 vs 425 +/- 37 micromol kg(-1)h(-1), P< 0.05) resulting from a 32% decrease in glutamine de novo synthesis (230 +/- 21 vs 340 +/- 34 micromol kg(-1)h(-1), P< 0.05). Whereas there was no difference between groups in estimates of protein degradation and synthesis, leucine oxidation rate was 44% higher in DMD boys than in controls (23 +/- 2 vs 16 +/- 2 micromol kg(-1)h(-1), P< 0.05). The data suggest that the dramatic mucle mass loss observed in DMD boys is associated with a) significant protein wasting, since increased leucine oxidation reflects a more negative whole body leucine balance, and b) a significant decrease in glutamine availability in the postabsorptive state. Glutamine might therefore be a 'conditionally essential' amino-acid in DMD.

Adolescent↗