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PubMedDate not supplied

Induction of the mitochondrial permeability transition in cultured astrocytes by glutamine.

Ammonia is a toxin that has been strongly implicated in the pathogenesis of hepatic encephalopathy (HE), and astrocytes appear to be the principal target of ammonia toxicity. Glutamine, a byproduct of ammonia metabolism, has been implicated in some of the deleterious effects of ammonia on the CNS. We have recently shown that ammonia induces the mitochondrial permeability transition (MPT) in cultured astrocytes, but not in neurons. We therefore determined whether glutamine is also capable of inducing the MPT in cultured astrocytes. Astrocytes were treated with glutamine (4.5 mM) for various time periods and the MPT was assessed by changes in 2-deoxyglucose (2-DG) mitochondrial permeability, calcein fluorescence assay, and by changes in cyclosporin A (CsA)-sensitive inner mitochondrial membrane potential (deltapsi(m)) using the potentiometric dye, JC-1. Astrocytes treated with glutamine significantly increased 2-DG permeability (120%, P<0.01), decreased mitochondrial calcein fluorescence, and concomitantly dissipated the deltapsi(m). All of these effects were blocked by CsA. These data indicate that glutamine induces the MPT in cultured astrocytes. The induction of the MPT by glutamine in astrocytes, and the subsequent development of mitochondrial dysfunction, may partially explain the deleterious affects of glutamine on the CNS in the setting of hyperammonemia.

Astrocytes↗
PubMed2003

Modulating effect of glutamine on IL-1beta-induced cytokine production by human gut.

BACKGROUND & AIMS: Balance between pro-and anti-inflammatory mediators plays a key role in the pathogenesis and treatment of inflammatory bowel disease. Glutamine can modulate cytokine production by intestinal mucosa in healthy subjects, but studies in inflammatory states are still limited. The aim of this work was to evaluate the effects of glutamine on IL-1beta-induced cytokine production by human gut. METHODS: Duodenal biopsies from healthy volunteers were stimulated in vitro by IL-1beta in the presence of increasing glutamine concentrations. Cytokine production was assessed in culture media by ELISA and cytokine mRNA expression in biopsies by RT-PCR. Results, in pg/mg of tissue, (median [range]), were compared by non-parametric paired tests. RESULTS: IL-1beta stimulation increased IL-6 and IL-8, but did not affect IL-4 and IL-10 production. IL-8 and IL-6 production from stimulated biopsies significantly decreased with increasing glutamine concentration from 0.5 to 10mM, (2543 [828-3634] to 1499 [282-2617] for IL-8, 62 [22-117] to 24 [12-99] for IL-6, both P<0.05), whereas IL-10 production was increased (0.7 [0.2-1.6] to 1.2 [2.6-0.5],P<0.05). Glutamine also increased IL-10 mRNA level in biopsies (P<0.05). IL-4 production was not affected by glutamine. CONCLUSIONS: Glutamine was shown in human intestinal mucosa to reduce the production of the pro-inflammatory cytokines IL-6 and IL-8, and enhance the production of the anti-inflammatory cytokine, IL-10.

Adult↗
PubMed1998

Dietary glutamine supplementation reduces plasma nitrate levels in rats.

It was recently shown that L-glutamine inhibits vascular nitric oxide (NO) production in vitro. The present study investigated the effect of glutamine enriched enteral diets on in vivo NO production in the rat. Nitrate, the stable end-product of NO production, was measured in plasma and 24 h urine collections in glutamine supplemented rats (6.25%, 12.5% and 25% w/w) and compared to the effect of isocaloric, nitrogenous control diets. Glutamine supplementation increased plasma levels of glutamine (up to 91%), arginine (up to 17%) and citrulline (up to 54%). After 1 week of glutamine supplementation plasma nitrate levels were significantly reduced by 50% compared to control (P < 0. 0001); irrespective of the amount of supplementation. No further decrease was observed after 2 weeks of feeding. No differences in daily urinary losses were found between the groups. These results point to an in vivo inhibitory effect of glutamine supplemented enteral feeding on NO production.

Animals↗
PubMed2002

Regulation of glutamine metabolism during the development of Bombyx mori larvae.

Waste ammonia is re-assimilated into amino acids via the amide group of glutamine and the amino group of glutamate (i.e. through glutamine synthetase/glutamate synthase pathway) for silk synthesis in the silkworm, Bombyx mori, in the last larval stadium. Glutamine concentration in hemolymph gradually decreased with the progress of the fifth instar and it remained at very low levels during the spinning stage, then followed by a sharp increase at the larval-pupal ecdysis. The changes in glutamine synthetase (GS) activity in silkworm tissues were relatively small through the larval development, while the changes in glutamate synthase (GOGAT) activity, especially in the posterior silk glands, were more drastic. In addition, activities of GOGAT in the tissues were much higher than those of the other enzymes involved in glutamine utilization, suggesting that glutamine pool was regulated mainly by the changes in GOGAT activity. Western blot analysis indicated that the changes in GOGAT protein level correlated with the changes in GOGAT activity. Topical application of a juvenile hormone analogue, methoprene, induced an accumulation of glutamine in the hemolymph of the fifth instar larvae. The levels of GOGAT protein and activity in the tissues of the methoprene treated larvae were much lower than those of the control larvae, whereas the methoprene treatment had no effect on the levels of GS activity. In conclusion, GOGAT expression promoted by reduction of juvenile hormone titer is quite important for enhanced utilization of nitrogen for synthesis of silk protein during the last larval instar.

Animals↗
PubMed2002

Hepatic glutamine metabolism.

Expression of high activities of both glutamine synthetase and glutaminase allows the liver to play a major role in the regulation of glutamine homeostasis. The liver shows net glutamine output in metabolic acidosis, in prolonged starvation and animals bearing tumors, net glutamine uptake in the postabsorptive state, on consuming high protein diets, and in uncontrolled diabetes or sepsis. Liver glutamine synthetase is expressed only in a small population of perivenous cells that allows it to salvage any ammonia not incorporated into urea in periportal cells. Hepatic glutaminase is a unique isozyme found only in periportal liver parenchymal cells where it provides glutamate and ammonia for the urea cycle. Control of hepatic glutamine metabolism occurs almost exclusively through changes in the activity of glutaminase, with no change in glutamine synthetase flux.

Animals↗
PubMedDate not supplied

Effect of epidermal growth factor on glutamine metabolic enzymes in small intestine and skeletal muscle of parenterally fed rats.

Exogenous epidermal growth factor (EGF) markedly increases the in vivo uptake of glutamine by small intestine during total parenteral nutrition (TPN). Since glutamine is the major oxidative fuel for the small intestine and is synthesized mainly in skeletal muscle, we investigated whether EGF would induce changes in the activity of the enzymes that mediate glutamine degradation (glutaminase) and synthesis (glutamine synthetase) in the two tissues. Male Sprague Dawley rats were randomized into three groups: group I (chow) were fed rat chow and water and libitum, group II (TPN) received a standard formula of TPN, and group III (TPN-EGF) received the same TPN as group II and injections of EGF (0.1 microgram/ gm body weight (bw)) subcutaneously twice daily. TPN was given for 2 wk; when EGF was administered along with TPN, the glutaminase activity of intestinal mucosa and the glutamine synthetase activity of skeletal muscle were increased, respectively, by 25% and 24% (P < 0.05, versus TPN group). These data suggest a mechanism whereby EGF enhances the intestinal utilization of glutamine by changing the activities of glutamine metabolic enzymes in the small intestine and skeletal muscle during TPN.

Animals↗
PubMedDate not supplied

Dietary glutamine enhances cytokine production by murine macrophages.

To examine the effects of dietary glutamine on cytokine production by macrophages, mice were fed for 2 wk on a control diet that included 200.0 g casein/kg providing 19.6 g glutamine/kg or a glutamine-enriched diet that provided 54.8 g glutamine/kg partly at the expense of casein. There were no differences in weight gain between animals fed the two diets. The plasma concentrations of a number of amino acids differed according to the diet fed; this variation largely reflected the variation in the levels of the different amino acids in the diets. Plasma glutamine concentration was not significantly affected by dietary glutamine level. The production of three cytokines, tumor necrosis factor-alpha, interleukin-1 beta, and interleukin-6, was greater for lipopolysaccharide-stimulated macrophages from mice fed the glutamine-enriched diet. Thus, increasing the amount of glutamine in the murine diet enhances the ability of macrophages to respond to stimulation, at least in terms of cytokine production. These observations suggest that increasing the availability of glutamine orally could promote immune responses involving macrophage-derived cytokines.

Amino Acids↗
PubMed1993

Imidazole glycerol phosphate synthase: the glutamine amidotransferase in histidine biosynthesis.

Two proteins essential for the biosynthesis of the amino acid histidine in Escherichia coli have been overexpressed and purified to apparent homogeneity. The protein encoded by the hisF gene has an ammonia-dependent activity that results in the conversion of the biosynthetic intermediate N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4- carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (IGP) and 5-aminoimidazole-4-carboxamido-1-beta-D- ribofuranosyl 5'-monophosphate (AICAR). The second protein encoded by the hisH gene exhibits no detectable catalytic properties with biosynthetic intermediate PRFAR, glutamine, or ammonia. In combination, the proteins are capable of a stoichiometric conversion of glutamine and PRFAR to form AICAR, IGP, and glutamate. Neither protein alone is capable of mediating a conversion of the nucleotide substrate to a free metabolic intermediate. The HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the IGP synthase holoenzyme. Steady-state kinetic parameters for the holoenzyme indicate that glutamine is a more efficient substrate relative to ammonium ion by a factor of 10(3). The HisF subunit will support an ammonia-dependent reaction with a turnover number similar to that of the holoenzyme with glutamine. The glutaminase activity for the holoenzyme is 0.8% of that in the presence of the nucleotide substrate PRFAR. There are critical subunit interactions that mediate the catalytic properties for glutamine hydrolysis. The catalytic turnover of glutamine can be increased up to 37-fold by the addition of either the product IGP or the biosynthetic precursor N1-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (5'-ProFAR). The mechanistic significance of this glutaminase activity compared to other trpG type glutamine amidotransferases is discussed.

Anthranilate Synthase↗
PubMed1981

Reconstitution of binding protein dependent active transport of glutamine in spheroplasts of Escherichia coli.

In order to directly prove that the periplasmic glutamine binding protein is an essential component of the osmotic shock sensitive active transport system for glutamine in Escherichia coli, we demonstrated the reconstitution of binding protein dependent glutamine transport in spheroplasts of that organism. It was shown by arsenate inhibition that the reconstituted transport system was energy dependent, and the use of azaserine, an inhibitor of glutamine-utilizing enzymes, indicated that the restoration of transport by binding protein did not require the metabolizing of the transport substrate. Furthermore, the binding protein dependent transport of glutamine was shown to require at least one other macromolecular component, presumably membrane bound, which was absent in a strain containing a deletion of the genes coding for the glutamine transport system but was present in a strain carrying a mutation only in the structural gene for the glutamine binding protein.

Arsenates↗
PubMed1976

Manganese(II) and substrate interaction with unadenylylated glutamine synthetase (Escherichia coli w). I. Temperature and frequency dependent nuclear magnetic resonance studies.

A comprehensive study of solvent interaction with unadenylylated glutamine synthetase (E1.7) has been conducted using the enzyme isolated from Escherichia coli W. The longitudinal, (1/T1p)b, and transverse, (1/T2p)b, proton relaxation rates were measured with various enzyme samples as a function of frequency (6-48 MHZ) and temperature (1-40 degrees C). With Mn(II) bound at the "tight" metal ion site approximately two water molecules are rapidly exchanging with bulk solvent. This number is reduced to approximately one in the presence of glutamine. All data were successfully analyzed according to the Solomon-Bloembergen-Morgan (SBM) scheme for dipolar relaxation of water protons interacting with enzyme-bound Mn(II). The correlation time for this process varies from 1 to 3 X 10(-9) for the complexes described above. Significant contributions to the correlation time arise from both 1/taum, the exchange rate for water molecules bound at the metal site, and from 1/taus, the electron spin relaxation rate for Mn(II) with the latter rate showing a frequency dependence at the magnetic field strengths used in this study. A study of Mn(II) binding to E1.7 at 25 degrees C revealed two classes of metal ion sites, a "tight" set of one per subunit with KD=5.0 X 10(-7) M and a "weak" set of one per subunit with KD=4.5 X10(-5)M. In the presence of glutamine the affinity of the first site for Mn(II) was unchanged but the KD value for the weak site changed to 3 X 10(-6)M. In E1.7 samples with Mn(II) bound at both the tight and weak metal ion sites the data are interpretable with two rapidly exchanging water molecules interacting with each bound Mn(II)ion. With saturating amounts of glutamine or of ADP or of glutamine plus ADP plus arsenate, the proton relaxation rates progressively decreased suggesting that the substrates or inhibitors used were interacting with the bound Mn(II) ions resulting in diminished solvent accessibility to these bound ions. These results are interpretable in terms of ligand substitution into the coordination sphere of the bound Mn(II) ions. Indeed this is probably the case for Mn(II) at the weak metal ion site since Hunt et al. ((1975), Arch. Biochem. Biophys. 166, 102) showed that Mn(II) can bind as the Mn(II)-ADP complex to the second metal ion site. Results of proton relaxation rate data on E1.7 with Mn(II) bound at both the tight and weak metal ion sites led to the conclusion that these metal ion sites are greater than 6 A apart. In comparison with proton relaxation rate data on fully adenylylated glutamine synthetase (E11.8) as studied by Villafranca and Wedler ((1974), Biochemistry 13, 3286), the first "tight" metal ion site in E11.8 has three rapidly exchanging water molecules. Mn(II) has a weaker binding constant to E11.8 (KD approximately 5 X 10(-6)M) at the pH value used in both studies and a suggestion is made that an additional protein ligand is binding to Mn(II) in glutamine synthetase when the subunits are not adenylylated.

Adenine Nucleotides↗
PubMedDate not supplied

Substitution of glutamine by pyruvate to reduce ammonia formation and growth inhibition of mammalian cells.

In mammalian cell culture technology glutamine is required for biomass synthesis and as a major energy source together with glucose. Different pathways for glutamine metabolism are possible, resulting in different energy output and ammonia release. The accumulation of ammonia in the medium can limit cell growth and product formation. Therefore, numerous ideas to reduce ammonia concentration in cultivation broths have been developed. Here we present new aspects on the energy metabolism of mammalian cells. The replacement of glutamine (2 mM) by pyruvate (10 mM) supported cell growth without adaptation for at least 19 passages without reduction in growth rate of different adherent commercial cell lines (MDCK, BHK21, CHO-K1) in serum-containing and serum-free media. The changes in metabolism of MDCK cells due to pyruvate uptake instead of glutamine were investigated in detail (on the amino acid level) for an influenza vaccine production process in large-scale microcarrier culture. In addition, metabolite profiles from variations of this new medium formulation (1-10 mM pyruvate) were compared for MDCK cell growth in roller bottles. Even at very low levels of pyruvate (1 mM) MDCK cells grew to confluency without glutamine and accumulation of ammonia. Also glucose uptake was reduced, which resulted in lower lactate production. However, pyruvate and glutamine were both metabolized when present together. Amino acid profiles from the cell growth phase for pyruvate medium showed a reduced uptake of serine, cysteine, and methionine, an increased uptake of leucine and isoleucine and a higher release of glycine compared to glutamine medium. After virus infection completely different profiles were found for essential and nonessential amino acids.

Ammonia↗
PubMed2004

Glutamine in commercial liquid nutritional products.

Total glutamine concentrations in commercial nutritional products have been determined by enzymatic hydrolysis followed by HPLC quantification of free glutamine and free pyroglutamic acid. Hydrolysis was accomplished by a published three-enzyme (Pronase, leucine aminopeptidase, prolidase), 20-h/37 degrees C digestion. Glutamine was determined as its FMOC derivative by reverse phase HPLC-fluorescence, and pyroglutamic acid was determined directly by organic acid HPLC-UV. Approximately 4.11% of the released glutamine is converted to pyroglutamic acid during the 20-h digestion. Experimental ratios of enzyme hydrolysis glutamine to acid hydrolysis glutamic acid + glutamine + pyroglutamic acid (GLX) indicate that the method recovers >90% of the protein-bound glutamine. The nutritional products with casein dominant intact protein systems typically deliver >9 g of glutamine/100 g of protein, or approximately 40 g of glutamine/100 g of GLX.

Chromatography, High Pressure Liquid↗
PubMed2002

Insulin-like growth factor-I stimulates Na+-dependent glutamine absorption in piglet enterocytes.

Agents that enhance intestinal glutamine transport may be useful under conditions in which intestinal mucosal function is compromised. Here we examined whether oral administration of insulin-like growth factor (IGF-I) stimulates absorption of L-glutamine in piglet intestine. Colostrum-deprived piglets received human recombinant IGF-I (3.5 mg/kg/day) or vehicle orogastrically every 8 hr for four days after birth. Piglets were killed on day 5 and the proximal jejunum was removed. Basal electrical parameters and L-glutamine-stimulated changes in short-circuit current were measured in muscle-stripped tissues, and rates of L-glutamine uptake were measured in everted jejunal sleeves. Oral IGF-I had no effect on jejunal mucosal mass. Short-circuit current responses to mucosal addition of 10 mM L-glutamine were increased by oral IGF-I. Total and carrier-mediated uptakes of L-glutamine per milligram were greater in tissues from IGF-I-treated piglets due to a significantly greater maximal rate of uptake (Jmax). Thus, oral administration of IGF-I stimulates Na+-dependent glutamine absorption in piglet small intestine, an effect that is independent of changes in intestinal mucosal mass.

Administration, Oral↗
PubMed1998

Immunostimulating effect of oral glutamine.

Glutamine represents the principal metabolic substrate for all rapidly proliferating cells. Since part of the glutamine efficacy could be related to immunoregulating properties, we assessed the effects of orally administered glutamine on serum interleukin-2 (IL-2) levels and intestinal T-cell populations in 48 athymic (nude) mice. Twenty-four mice received a standard diet enriched by glutamine (added to drinking water at a 4% concentration), while the other 24 served as the control group and received the same diet without glutamine. In glutamine-fed animals, we observed a marked increase in IL-2 concentrations after 10 days of treatment in comparison with control group and a modest but significant increase in intestinal T-cell counts. These results suggest that oral glutamine is able to exert local and systemic immunostimulating activity that could be of relevance in the prevention of gut integrity and immune defense loss associated, for example, with trauma, surgery, and starvation.

Adjuvants, Immunologic↗
PubMed1981

Ammonia partitioning between glutamine and urea: interorgan participation in metabolic acidosis.

The distribution of precursor nitrogen between urea and glutamine was studied in control and acidotic rats. Acidosis, either acutely induced with hydrochloric acid or chronically induced with ammonium chloride, resulted in a rise in ammonia and a fall in urinary urea excretion; the percent of urinary nitrogen excreted as ammonia rose from 3.5 +/- 0.4 and 4.9 +/- 0.5 in fed and pair-fed controls to 25.9 +/- 3.9 and 37 +/- 5 in acidosis induced by hydrochloric acid and ammonium chloride. Hepatoportal vein urea concentration differences were significantly reduced, whereas glutamine concentration differences were significantly elevated, consistent with a shift of nitrogen from ureagenesis to glutamine; alanine and ammonia concentration differences were significantly decreased and increased respectively in the acidotic animals, suggesting that former supported urea synthesis whereas ammonia may preferentially support glutamine synthesis. Evidence of a feed-forward involvement of the gut in influencing hepatic nitrogen distribution was suggested by an increased ammonia and decreased alanine release in acidotic rats. Bilateral ureteral ligation was performed on control and acidotic rats to determine the fate of the redirected urinary ammonia. Ammonia did not accumulate in the blood, rather it was initially incorporated into glutamine, elevating the plasma level, and then it was subsequently deposited into urea. The shift of nitrogen back into urea in acidotic animals was confirmed by the greater postligation urea production rates supported by hepatic uptake of both alanine and glutamine. These results are discussed in terms of interorgan participation involving the liver, gut, and muscle in the partitioning of nitrogen between glutamine and urea.

Acidosis, Renal Tubular↗
PubMed2005

A double-blind randomized placebo-controlled study of oral glutamine in the prevention of mucositis in children undergoing hematopoietic stem cell transplantation: a pediatric blood and marrow transplant consortium study.

Severe mucositis is a common cause of morbidity in hematopoietic stem cell transplant (HSCT) recipients. Glutamine has been shown to reduce mucositis in children receiving chemotherapy. Patients were randomized in a double-blind manner to receive glutamine or glycine at a dose of 2 g/m(2)/dose (maximum dose 4 g) twice daily until 28 days post transplant or discharge if sooner. Mucositis was graded by use of a modified Walsh scale. A total of 120 children were evaluable: 57 children received glutamine and 63 received glycine. The mean mucositis score was 3.0+/-0.3 vs 3.9+/-0.4 (P=0.07) in the glutamine and glycine groups, respectively. The glutamine group demonstrated a reduction in mean number of days of intravenous narcotics use (12.1+/-1.5 vs 19.3+/-2.8 in the glycine group, P=0.03) and total parenteral nutrition (17.3+/-1.7 vs 27.3+/-3.6 in glycine group, P=0.01). There was no statistically significant difference in toxicity between the two groups. Glutamine appears to be safe and beneficial in reducing the severity of mucositis. Strong consideration should be given to include oral glutamine supplementation as a routine part of supportive care of SCT patients.

Administration, Oral↗
PubMed2003

Oral glutamine in paediatric oncology patients: a dose finding study.

OBJECTIVE: The purpose of this study was to determine the most appropriate dose of oral glutamine to use in a further clinical study in paediatric oncology patients. DESIGN: This was a phase I, pharmokinetic study. SETTING: The study was carried out at The Yorkshire Regional Centre for Paediatric Oncology and Haematology, St James's University Hospital, Leeds, UK. SUBJECTS: Thirteen patients undergoing treatment for paediatric malignancy participated in this study. All 13 completed the study. INTERVENTIONS: The most appropriate dose was determined by patient acceptability and by plasma glutamine and ammonia levels measured at timed intervals after ingestion of a single glutamine dose. RESULTS: Doses of 0.35, 0.5 and 0.65 g/kg were well tolerated with no untoward plasma glutamine and ammonia levels. One patient was recruited to a higher dose of 0.75 g/kg, but the plasma glutamine and ammonia levels peaked at 2601 and 155 micro mol/l, respectively. The ammonia level was greater than the acceptable upper limit. It was difficult to disperse the glutamine adequately at this dose, resulting in the suspension being found to be unpalatable and therefore no further patients were recruited at this dose. CONCLUSION: It was concluded that 0.65 g/kg is a safe dose of glutamine to use in a clinical study in paediatric oncology patients.

Administration, Oral↗
PubMed2006

Persistent arterial hyperammonemia increases the concentration of glutamine and alanine in the brain and correlates with intracranial pressure in patients with fulminant hepatic failure.

In this prospective study of patients with fulminant hepatic failure (FHF), we tested the hypothesis that arterial hyperammonemia results in cerebral accumulation of the osmotic active amino acids glutamine and alanine, processes that were expected to correlate with intracranial pressure (ICP). By using in vivo brain microdialysis technique together with ICP monitoring in 17 FHF patients (10 females/7 males; median age 49 (range 18 to 66) years), we found that arterial ammonia concentration correlated to brain content of glutamine (r=0.47; P<0.05) but not to alanine. A persisting high arterial ammonia concentration (above 200 micromol/L) characterized patients who developed high ICP (n=8) while patients who did not experience surges of increased ICP (n=9) had a decline in the ammonia level (P<0.05). Moreover, brain glutamine and alanine concentrations were higher at baseline and increased further in patients who developed intracranial hypertension compared with patients who experienced no surges of high ICP. Brain glutamine concentration increased 32% from baseline to 6536 (697 to 9712) micromol/L (P<0.05), and alanine 44% from baseline to 104 (81 to 381) micromol/L (P<0.05). Brain concentration of glutamine (r=0.59, P<0.05), but not alanine, correlated to ICP. Also arterial ammonia concentration correlated to ICP (r=0.73, P<0.01). To conclude, this study shows that persistence of arterial hyperammonemia is associated with profound changes in the cerebral concentration of glutamine and alanine. The elevation of brain glutamine concentration correlated to ICP in patients with FHF.

Adolescent↗