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PubMedDate not supplied

The effects of oral glutamine supplementation on athletes after prolonged, exhaustive exercise.

Athletes undergoing intense, prolonged training or participating in endurance races suffer an increased risk of infection due to apparent immunosuppression. Glutamine is an important fuel for some cells of the immune system and may have specific immunostimulatory effects. The plasma glutamine concentration is lower after prolonged, exhaustive exercise: this may contribute to impairment of the immune system at a time when the athlete may be exposed to opportunistic infections. The effects of feeding glutamine was investigated both at rest in sedentary controls and after exhaustive exercise in middle-distance, marathon and ultra-marathon runners, and elite rowers, in training and competition. Questionnaires established the incidence of infection for 7 d after exercise: infection levels were highest in marathon and ultra-marathon runners, and in elite male rowers after intensive training. Plasma glutamine levels were decreased by approximately 20% 1 h after marathon running. A marked increase in numbers of white blood cells occurred immediately after exhaustive exercise, followed by a decrease in the numbers of lymphocytes. The provision of oral glutamine after exercise appeared to have a beneficial effect on the level of subsequent infections. In addition, the ratio of T-helper/T-suppressor cells appeared to be increased in samples from those who received glutamine, compared with placebo.

Administration, Oral↗
PubMedDate not supplied

Glutamine supplementation in cancer patients receiving chemotherapy: a double-blind randomized study.

The purpose of this study was to evaluate the efficacy of glutamine in preventing doxifluridine-induced diarrhea and the potential impact of glutamine on the tumor growth. We investigated 65 patients with advanced breast cancer receiving doxifluridine in a double-blind randomized fashion: 33 patients took glutamine (30 g/d, divided in 3 doses of 10 g each) for 8 consecutive days (5-12h) during each interval between chemotherapy, which was administered from day 1 to 4. Thirty-two patients took an equal dose of placebo (maltodextrine). The incidence of diarrhea was registered after each cycle of chemotherapy and severity was scored by the National Cancer Institute (NCI), Bethesda, Maryland, classification. The tumor response was evaluated by the World Health Organization (WHO) criteria. A total of 278 and 259 cycles (median 10 cycles), respectively, were delivered in glutamine and placebo groups. There were 34 and 32 episodes of diarrhea in glutamine and placebo groups, with no statistical difference overall, in the severity and duration of tumor growth, there was no difference in the response rate (21% and 28% of complete or partial response, respectively), in median time to response (2 mo), or in median duration of response. In conclusion, glutamine did not prevent the occurrence of the doxifluridine-induced diarrhea and did not have any impact on tumor response to chemotherapy.

Administration, Oral↗
PubMedDate not supplied

Development of an intravenous glutamine supply through dipeptide technology.

Glutamine is considered as semi-essential amino acid during catabolic stress. Due to its chemical instability in aqueous solutions during heat sterilization and long term storage, it could not be added to infusion solutions so far. In contrast, the dipeptide glycl-L-glutamine exhibits all properties needed for use as glutamine derivative in parenteral nutrition. It is freely soluble in water and does not decompose during heat sterilization. The peptide undergoes rapid enzymatic hydrolysis after infusion. This results in perfect utilization. Glycyl-L-glutamine is already produced in large amounts by chemical synthesis techniques. Both chemical and optical purity of the dipeptide can be controlled by modern chromatographic methods. Glamin, a newly developed complete amino acid solution, contains 20 g of glutamine per liter in form of glycyl-L-glutamine. Since no additional free glycine is added, no imbalances are created by the amino-terminal amino acid of the peptide structure.

Dipeptides↗
PubMedDate not supplied

Role of glutamine in immunologic responses.

Glutamine has traditionally been thought of as a nonessential amino acid, but laboratory and clinical data suggests that it may be essential during certain inflammatory conditions, such as infection and injury. Glutamine is a necessary nutrient for cell proliferation, serves as a specific fuel for inflammatory cells and enterocytes, and, when present in appropriate concentrations, enhances cell function. During inflammatory states, glutamine consumption may outstrip endogenous production and a relative glutamine deficiency state may exist. Animal and clinical studies suggest that improved outcome may be possible by providing the appropriate dose of this nutrient by the appropriate route to achieve adequate tissue concentrations. Such an approach prevents patients from being exposed to some of the inadequacies of present day conventional nutrition. The overall benefit of providing an appropriate glutamine-supplemented diet to all metabolically compromised patients arises from the multiple anabolic and host protective effects of this amino acid, of which immunomodulation is only one important facet of glutamine's essential nature.

Animals↗
PubMed1996

Glutamine repeats and inherited neurodegenerative diseases: molecular aspects.

Several dominantly inherited, late onset, neurodegenerative diseases are due to expansion of CAG repeats, leading to expansion of glutamine repeats in the affected proteins. These proteins are of very different sizes and, with one exception, show no sequence homology to known proteins or to each other; their functions are unknown. In some, the glutamine repeat starts near the N-terminus, in another near the middle and in another near the C-terminus, but regardless of these differences, no disease has been observed in individuals with fewer than 37 repeats, and absence of disease has never been found in those with more than 41 repeats. Protein constructs with more than 41 repeats are toxic to E. coli and to CHO cells in culture, and they elicit ataxia in transgenic mice. These observations argue in favour of a distinct change of structure associated with elongation beyond 37-41 glutamine repeats. The review describes experiments designed to find out what these structures might be and how they could influence the properties of the proteins of which they form part. Poly-L-glutamines form pleated sheets of beta-strands held together by hydrogen bonds between their amides. Incorporation of glutamine repeats into a small protein of known structure made it associate irreversibly into oligomers. That association took place during the folding of the protein molecules and led to their becoming firmly interlocked by either strand- or domain-swapping. Thermodynamic considerations suggest that elongation of glutamine repeats beyond a certain length may lead to a phase change from random coils to hydrogen-bonded hairpins. Possible mechanisms of expansion of CAG repeats are discussed in the light of looped DNA model structures.

Genetic Diseases, Inborn↗
PubMed1997

Effect of glutamine or glucagon-insulin enriched total parenteral nutrition on liver and gut in 70% hepatectomized rats with colon stenosis.

BACKGROUND: Malnutrition of enterocytes is believed to facilitate the breakdown of the intestinal mucosal barrier, furthering a translocation of enteric bacteria with subsequent severe infection, which has been described after extensive hepatectomy. Glutamine and glucagon insulin are said to attenuate the malnutrition of enterocytes. To determine whether this was true, the effects on the remnant liver and the gut of total parenteral nutrition supplemented by admixtures of glutamine and/or glucagon insulin were investigated in rats subjected to massive hepatectomy and transient intestinal stasis. STUDY DESIGN: Rats underwent a permanent cannulation of the superior caval vein without restraining their mobility, a 70% hepatectomy, and a 24 hour string-ligation stenosis of the colon. A standard total parenteral nutrition solution was infused without or with 2% glutamine and without or with glucagon-insulin supplementation, respectively. RESULTS: Glutamine and glucagon-insulin supplemented total parenteral nutrition increased ileal mucosal DNA concentrations during and after intestinal stasis. Glutamine or glucagon-insulin alone had less pronounced effects. In the liver, the combined supplementation resulted in reduced adenosine triphosphate concentrations and increased mitochondrial adenosine triphosphate synthesis as well as in an early increase in DNA concentrations. CONCLUSION: Glutamine and glucagon-insulin enriched total parenteral nutrition attenuates malnutrition of enterocytes after massive abdominal stress and promotes liver regeneration after extensive hepatectomy.

Alanine Transaminase↗
PubMed1987

L-glutamine: an amino acid required for maintenance of the tegumental membrane potential of Schistosoma mansoni.

The tegumental membrane potential (-63 +/- 2.9 mV) of adult male Schistosoma mansoni in RPMI-1640 is significantly depolarized (-26 +/- 7.3 mV) when the parasite is incubated in inorganic media (Hank's Balanced Saline or RPMI-1640 without organic constituents). Of 9 amino acids (L-glutamine, D-glutamine, L-arginine, L-proline, L-aspartate, L-glutamate, L-asparagine, L-isoleucine and L-methionine) L-glutamine alone is sufficient to repolarize the membrane potential to a value (-56 +/- 4.5 mV) not significantly different from that found in RPMI-1640. Repolarization by glutamine is dose-dependent, with significant effects obtained as low as 0.10 mM. The concentration of phosphate in the medium also significantly alters the membrane potential. Physiological levels of phosphate (5.6 mM) are necessary in conjunction with L-glutamine to obtain the full repolarization of the membrane potential. In the absence of organic constituents, the membrane potential is strongly dependent on the external medium pH. When L-glutamine is present in the medium, the membrane potential becomes virtually independent of the external pH.

Amino Acids↗
PubMed1977

Glutamine active site of formylglycinamide ribonucleotide amidotransferase. 1. Labeling of the enzyme with iodoacetate.

A two-step method for labeling the glutamine active site of formyglycinamide ribonucleotide (FGAR) amidotransferase from chicken liver has been developed in which reaction of all other reactive groups with unlabeled iodoacetate is followed by specific labeling of the glutamine site with radioactive reagent. A study of the reaction as a function of duration, temperature, and pH of the incubation as well as concentration of iodoacetate has revealed that two nonessential groups of the enzyme react in the presence of glutamine and that this modified enzyme is relatively resistant to further carboxymethylation. When this modified enzyme was incubated with radioactive iodoacetate in the presence of FGAR, ATP, and Mg2+ after removal of glutamine by dialysis, about 1 mol of radioactive iodoacetate was incorporated per mol of enzyme with inactivation. This method permits labeling of the active site for glutamine without the use of glutamine analogues.

Animals↗
PubMedDate not supplied

Chemical decomposition of glutamine in cell culture media: effect of media type, pH, and serum concentration.

The chemical decomposition of glutamine to ammonia and pyrrolidonecarboxylic acid was studied at 37 degrees C in a pH range of 6.8-7.8 in different media preparations containing various amounts of fetal bovine serum. The media type influenced the decomposition rate, and the first-order rate constants increased with increasing pH values. The serum concentration had little or no effect on the decomposition rate. The importance of chemical decomposition of glutamine on the analysis of glutamine and ammonia metabolism was illustrated by an example of batch cultivation of a hybridoma cell line. The difference between the apparent uptake rate of glutamine and the actual uptake rate (which is corrected for the chemical decomposition) is shown to be as high as 200%. Similar discrepancy between the apparent and actual ammonia production rate is observed. Mathematical analysis was carried out to develop the relationship between the apparent and actual glutamine uptake and ammonia production rates. The analysis reveals that there are three important dimensionless parameter ratios that govern the difference between the apparent and actual glutamine uptake and ammonia production rates.

Ammonia↗
PubMedDate not supplied

A recombinant glutamine-binding protein from Escherichia coli: effect of ligand-binding on protein conformational dynamics.

We have investigated the effect of the binding of glutamine on the conformational dynamics of the recombinant glutamine binding protein (GlnBP) from Escherichia coli by steady-state and time-resolved fluorescence techniques. The structural stability of the protein was also studied by far-UV circular dichroism spectroscopy in the range of temperature between 25 and 80 degrees C. The results showed that the interaction of the protein with the ligand resulted in a marked change of the structural and conformational dynamics features of the protein. In particular, the fluorescence and circular dichroism data showed that the presence of glutamine resulted in a dramatic increase of the protein thermal stability of about 10 degrees C. In addition, the fluorescence time-resolved data pointed out that both in the absence and in the presence of glutamine the protein structure was highly rigid with small amplitude of segmental motion up to 65 degrees C and a low accessibility of the protein tryptophan residues to acrylamide. The obtained results on the structural properties of the recombinant glutamine-binding protein in the absence and in the presence of glutamine can contribute to a better understanding of the transport-related functions of the protein and structurally similar periplasmic transport proteins, as well as to the design and development of new biotechnological applications of this class of proteins.

Binding Sites↗
PubMed2000

NMR and MS analysis of decomposition compounds produced from N-acetyl-L-glutamine at low pH.

N-Acetyl-L-glutamine decomposition products glutamine, glutamic acid, pyroglutamic acid, N-acetylglutamic acid, and a novel compound, N-(2,6-dioxo-3-piperidinyl) acetamide, have been identified by NMR and MS techniques. N-Acetylglutamine, a modified amino acid, offers greater chemical stability than glutamine in conditions that are experienced during typical sterilization and shelf storage of liquid nutritionals. However, to support safety and stability studies, potential decomposition products of N-acetyl-L-glutamine needed to be identified. Therefore, atypically harsh conditions were used; an unbuffered (pH <3) 1 mg/mL water solution of N-acetyl-L-glutamine was heated to 100 degrees C for 3 h. One-dimensional proton and proton-decoupled carbon-13 NMR and electrospray LC-MS/MS techniques were employed to identify the molecular structures of the generated N-acetyl-L-glutamine decomposition products. Additionally, DEPT and two-dimensional NMR techniques TOCSY, GMQCOSY, GHSQC, and GHMBC were employed to derive the final structure of the acetamide.

Chromatography, High Pressure Liquid↗
PubMed2001

Glutamate-glutamine cycle and aging in striatum of the awake rat: effects of a glutamate transporter blocker.

This study investigated the effects of aging on the actions of a specific glutamate reuptake blocker, L-trans-pyrrolidine-2, 4-dicarboxylic acid (PDC), in extracellular glutamate and glutamine in striatum of the awake rat. Microdialysis experiments were performed on young (2-3 months), middle-aged (12-14 months), aged (27-32 months) and very aged (37 months) male Wistar rats. Local infusion of PDC (1-4 mM) in striatum increased the dialysate concentration of glutamate and decreased dialysate concentration of glutamine in all the age-groups. In young rats, decreases of dialysate glutamine were correlated with increases of dialysate glutamate. The same profile glutamine/glutamate as in young rats was found in middle-aged, aged and very aged rats, which suggests that the action of glutamate on the glutamate-glutamine cycle in striatum of the awake rat is not modified as a consequence of aging. We also found a significant correlation between the increases of glutamate produced by PDC and the basal dialysate concentration of glutamine, a relationship that did show a significant change with age. Although the significance of this latter finding remains to be elucidated, it may be important to understand the changes in glutamate-glutamine cycle during aging.

ATP-Binding Cassette Transporters↗
PubMed1998

Energetic and morphological plasticity of C6 glioma cells grown on 3-D support; effect of transient glutamine deprivation.

The energetic metabolism of rat C6 glioma cells has been investigated as a function of the proliferative and differentiation states under three-dimensional (3-D) growing conditions on microcarrier beads. First, the transient deprivation of glutamine from the culture medium induced a marked decrease in the growth rate and a differentiation of C6 cells through the oligodendrocytic phenotype. Second, the respiratory capacity of the C6 cells during short-term subcultures with or without glutamine continuously declined as a function of the cell density, in part due to the mitochondrial content decrease. During the transition from the early exponential to the plateau growth phase in glutamine-containing medium, the oxygen consumption rate per single cell decreased concomitantly with a decrease in the glucose consumption and lactate production rates. This phenomenon led to a sixfold decrease in the total ATP production flux, without significantly affecting the cellular ATP/ADP ratio, thus indicating that some ATP-consuming processes were simultaneously suppressed during C6 proliferation. In glutamine-free medium, the cellular ATP/ADP ratio transiently increased due to growth arrest and to a reduced ATP turnover. Moreover, the results indicated that glutamine is not an essential respiratory substrate for rat C6 glioma under short-term glutamine deprivation. Worth noting was the high contribution of the mitochondrial oxidative phosphorylation toward the total ATP synthesis (about 80%), regardless of the proliferation or the differentiation status of the C6 cells.

Animals↗
PubMed1997

Modulation of glutamine synthesis in cultured astrocytes by nitric oxide.

1. Previous results suggest that glutamine synthesis in brain could be modulated by nitric oxide. The aim of this work was to assess this possibility. 2. As glutamine synthetase in brain is located mainly in astrocytes, we used primary cultures of astrocytes to assess the effects of increasing or decreasing nitric oxide levels on glutamine synthesis in intact astrocytes. 3. Nitric oxide levels were decreased by adding nitroarginine, an inhibitor of nitric oxide synthase. To increase nitric oxide we used S-nitroso-N-acetylpenicillamine, a nitric oxide generating agent. 4. It is shown that S-nitroso-N-acetylpenicillamine decreases glutamine synthesis in intact astrocytes by approximately 40-50%. Nitroarginine increases glutamine synthesis slightly in intact astrocytes. 5. These results indicate that brain glutamine synthesis may be modulated in vivo by nitric oxide.

Animals↗
PubMed1990

Glucose deprivation neuronal injury in vitro is modified by withdrawal of extracellular glutamine.

Cultured cortical neurons deprived of glucose in a defined solution containing 2 mM glutamine became acutely swollen and went on to degenerate over the next day; this neuronal loss could be substantially attenuated by an N-methyl-D-aspartate (NMDA) antagonist. Removal of extracellular glutamine produced two effects: an increase in overall neuronal injury and a decrease in the protective effect of an NMDA antagonist. Both effects of glutamine removal were glutamine concentration dependent (EC50 for both approximately 300 microM) and not reversed by substitution of equimolar concentrations of alanine or arginine. These observations suggest that glucose deprivation neuronal injury may be tonically regulated by the presence of extracellular glutamine. We speculate that glutamine may reduce overall injury by serving as an energy substrate in the absence of glucose, but may increase NMDA receptor-mediated injury by serving as a precursor for transmitter excitatory amino acids.

Animals↗
PubMed1975

Renal mitochondrial glutamine metabolism and dietary potassium and protein content.

Renal mitochondrial glutamine metabolism and dietary potassium and protein content. Glutamine distribution, glutamate accumulation, phosphate-dependent glutaminase (PDG) concentrations and intact mitochondrial ammonia production were studied in renal mitochondria from rats fed low, normal and high potassium diets and in mitochondria from rats fed high or low protein diets. The rats given a low potassium diet were potassium-depleted by 10 to 20% but in none of the groups were there any abnormalities of extracellular acid-base status. Glutamine was present in the outer space of mitochondria but could not be depleted in the matrix space in any group. In both the potassium-depleted and the high protein animals, we found increased matrix -14-C-uptake of glutamine (as -14-C-glutamate), increased intact mitochondrial ammonia production and increased concentrations of PDG. In the K+-depleted group there was a decreased matrix -14C-uptake when -14C-gamma-ketoglutarate of -14C-glutamate was present in the medium. Potassium loading produced no change in mitochondrial glutamine metabolism. Protein loading (compared with protein depletion) and potassium depletion induce an increased uptake of glutamine into the renal mitochondrial matrix space which leads to its increased deamidation. This adaption may explain the increased renal ammonia production seen in these situations when compared to their respective controls.

Ammonia↗
PubMed1979

Relationship between lactate and glutamine metabolism in vitro by the kidney: differences between dog and rat and importance of alanine synthesis in the dog.

Interaction between lactate (1 or 5 mM) and glutamine (1 or 5 mM) metabolism was studied with renal cortical slices incubated at a pH of 7.0 and obtained from acidotic (ammonium chloride) dogs and rats. The effect of aminooxyacetate (0.2 mM), dichloroacetate (3 mM), and fluoroacetate (0.05 mM) was also studied. Significant differences were observed between dog and rat. In the dog, lactate had no effect on glutamine uptake and vice versa, but gluconeogenesis increased. Ammonia production, however, decreased by 13 to 21%, whereas a significant increase in alanine production was noted. In the rat, glutamine extraction and ammonia production dropped by 33% with 5 mM lactate. In contrast to the observation in the dog, no production of alanine was noted, but significant accumulation of glutamate took place. Amino-oxyacetate inhibited alanine production in the dog and reestablished ammoniagenesis, and it led to a marked decrement in the uptake of lactate and glucose production in both species. Dichloroacetate in the dog resulted in a reduction in pyruvate, alanine, glucose, and ammonia production while glutamate accumulation was observed. In both species, fluoroacetate stimulated glutamine uptake and ammonia production. With lactate alone, fluoroacetate decreased lactate uptake and glucose production. With both lactate and glutamine in the medium, fluoroacetate prevented any effect of lactate on ammoniagenesis. The present study demonstrates that lactate has a modest depressing effect on renal ammonia production by dog slices through increased synthesis of alanine and redistribution of nitrogen from glutamine. In the rat, the depressing effect of lactate on ammonia production in the alanine amino-transferase deficient kidney occurs through accumulation of glutamate. The data also reveal that oxidation of lactate to carbon dioxide is greater in the dog than it is in the rat, but that gluconeogenesis from lactate is more important in the rat.

Acidosis↗
PubMed1986

Regulation of glutamine metabolism in dog kidney in vivo.

In summary, we propose: that renal ammoniagenesis is regulated both by factors dependent and independent of the acid-base status, the net effect of the ammoniagenic process on the proton balance being directly related to the rate of urinary ammonium excretion; that the renal metabolism of glutamine should not be examined independently of the metabolism of other substrate physiologically taken up by the kidney; that different pathways for glutamine metabolism will change during acid-base disorders of organic or nonorganic origin; that, among the main glutamine utilizing pathways, only the GLDH pathway is influenced directly by the acid-base status; the ammoniagenic transamination pathways is regulated by substrate availability in the kidney; that the lowest ammoniagenic flux in the kidney coincides with the rate of alanine production since alanine appears to derive directly from glutamine. When this pathway is stimulated without concomitant acidosis, most of the ammonia produced is not excreted in urine but released in the renal venous blood: thus, no significant effect on the acid-base balance is produced; that glutamine is metabolized by proximal kidney tubules of acidotic dogs probably through net oxidation; that the quantitative analysis of the metabolic consequence of this process indicates that the rate of ATP turnover at this site may effectively place an upper limit to the rate of glutamine oxidation, and ammonia production by the kidney, and that this limit is nearly reached in chronically acidotic animals.

Acid-Base Equilibrium↗