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PubMedDate not supplied

Plasma glutamine response to enteral administration of glutamine in human volunteers (free glutamine versus protein-bound glutamine).

The goal of the present work was to compare the plasma glutamine response to exogenous glutamine administration in human volunteers; glutamine was provided as a free amino acid, bound to proteins, or in the form of peptides. Plasma glutamine concentrations were measured in eight human volunteers at 30, 60, 90, 120, and 240 min after receiving a drink containing 30 g of protein from one of the five different proteins tested (sodium caseinate, sodium caseinate + free glutamine, carob germ flour, carob protein concentrate, and carob protein hydrolysate). Peak plasma glutamine concentrations were 42% higher than postabsorptive basal values when exogenous glutamine was administered in the form of free glutamine added to caseinate (925.9 +/- 67.7 versus 651.3 +/- 44.0 micromol/L, respectively). In contrast, when glutamine was offered 100% bound to proteins (carob proteins), peak plasma glutamine concentration increased only between 18% and 23% from basal values, possibly because of the lower digestibility of carob proteins versus that of caseinate + free glutamine, to a different glutamine utilization at the gut level, or to a different response in endogenous glutamine kinetics to enteral administration of glutamine, depending on the molecular form of the glutamine source (free or protein bound).

Adult↗
PubMed2005

Glutamine metabolism in uricotelic species: variation in skeletal muscle glutamine synthetase, glutaminase, glutamine levels and rates of protein synthesis.

High intracellular glutamine levels have been implicated in promoting net protein synthesis and accretion in mammalian skeletal muscle. Little is known regarding glutamine metabolism in uricotelic species but chicken breast muscle exhibits high rates of protein accretion and would be predicted to maintain high glutamine levels. However, chicken breast muscle expresses high glutaminase activity and here we report that chicken breast muscle also expresses low glutamine synthetase activity (0.07+/-0.01 U/g) when compared to leg muscle (0.50+/-0.04 U/g). Free glutamine levels were 1.38+/-0.09 and 9.69+/-0.12 nmol/mg wet weight in breast and leg muscles of fed chickens, respectively. Glutamine levels were also lower in dove breast muscle (4.82+/-0.35 nmol/mg wet weight) when compared to leg muscle (16.2+/-1.0 nmol/mg wet weight) and much lower (1.80+/-0.46 nmol/mg wet weight) in lizard leg muscle. In fed chickens, rates of fractional protein synthesis were higher in leg than in breast muscle, and starvation (48 h) resulted in a decrease in both glutamine content and rate of protein synthesis in leg muscle. Thus, although tissue-specific glutamine metabolism in uricotelic species differs markedly from that in ureotelic animals, differences in rates of skeletal muscle protein synthesis are associated with corresponding differences in intramuscular glutamine content.

Animals↗
PubMed2004

Analysis of glutamine accumulation in rat brain mitochondria in the presence of a glutamine uptake inhibitor, histidine, reveals glutamine pools with a distinct access to deamidation.

Rat cerebral nonsynaptic mitochondria were incubated in medium containing 2 mM glutamine (Gln) or 2 mM glutamate (Glu), in the presence of a Gln uptake inhibitor histidine (His) as well as other basic amino acids, lysine and arginine (Lys, Arg) not inhibiting Gln uptake. Subsequently, the mitochondrial contents of Glu and Gln were determined by HPLC. Incubation in the presence of Glu alone increased the Glu content from approximately 3.5 to 15 nmol/mg protein, without affecting the Gln content. On the other hand, incubation with Gln increased the content of Gln from approximately 1.5 to approximately 12 nmol/mg, and that of Glu to 10 nmol/mg. As expected, addition of His did not alter the Glu and Gln content resulting from incubation with Glu. However, His significantly decreased to almost the preincubation level the content of Glu in mitochondria incubated with Gln, without affecting the content of Gln. No other amino acid had any effect on these parameters. The results point to the existence of distinct Gln pools, one of which is accessible to external Gln via a His-sensitive transporter and is accessible for deamidation in the mitochondria.

Amides↗
PubMed2000

Glutamine supplementation for preventing morbidity in preterm infants.

BACKGROUND: The amino acid glutamine is the preferred respiratory fuel for rapidly proliferating cells under normal conditions. Recent research has suggested a number of roles for glutamine during critical illness. This research has been largely performed in experimental animals and in adults in a variety of disease settings. There is little information on the role of glutamine in children and infants, or whether glutamine supplementation is beneficial in preterm babies. OBJECTIVES: To determine the effects of glutamine supplementation on morbidity and weight gain in preterm babies. SEARCH STRATEGY: Searches were made using Medline and Embase electronic databases and specific handsearching in the English language. The search strategy followed the guidelines of the Neonatal Cochrane Review Group. SELECTION CRITERIA: Randomised controlled trials comparing glutamine supplementation to no glutamine supplementation in preterm babies at any time from birth to discharge from hospital. DATA COLLECTION AND ANALYSIS: Data regarding clinical outcomes including duration of parenteral nutrition, time to full enteral nutrition, rate of weight gain, rate of positive blood cultures and duration of hospital stay were extracted by both reviewers. Analysis was performed by the primary reviewer (TRJT) in accordance with the standards of the Cochrane Neonatal Review Group. MAIN RESULTS: Three trials met the selection criteria. Data on proportion of babies having one or more of positive blood cultures were available from all three studies. Meta-analysis showed no significant difference between glutamine-supplemented and non-supplemented babies; RR = 0.73 (95% CI 0.44, 1.23), RD = -8.8% (95% CI -23.2, 5.5). Data for other outcome variables were pooled from two studies. There were no significant differences between glutamine-supplemented and non-supplemented babies for days to full enteral nutrition (WMD 0.42, 95% CI -3.0, 3.8), rate of weight gain (WMD 0.6 g/kg/d, 95% CI -1.6, 2.8) or days of hospital stay (WMD -2.4, 95% CI -14.9, 10.2). REVIEWER'S CONCLUSIONS: There is no evidence to support the routine use of parenteral or enteral glutamine supplementation in preterm babies. A large randomised controlled trial should be performed to determine whether or not glutamine supplementation enhances gut integrity and reduces sepsis rate.

Dietary Supplements↗
PubMed2000

Response of glutamine metabolism to glutamine-supplemented parenteral nutrition.

BACKGROUND: Increasing evidence suggests that glutamine is important for the function of many organ systems and supports the use of glutamine-enriched total parenteral nutrition (TPN) during severe illness. However, the effect of prolonged glutamine supplementation on glutamine kinetics has not been studied. OBJECTIVE: We investigated the effect of 8-10 d of TPN enriched with glutamine dipeptides on glutamine kinetics. DESIGN: Twenty-three preoperative patients were randomly allocated to receive either TPN enriched with glutamine dipeptides (60 micromol glutamine*kg body wt(-1)*h(-1)) or isonitrogenous, isoenergetic, glutamine-free TPN. A primed, continuous, 6-h intravenous infusion of L-[5-(15)N]glutamine and L-[1-(13)C]leucine was given before (baseline) and 8-10 d after the TPN solutions were administered. Baseline measurements were performed after a 40-h administration of a standard solution of glucose and amino acids (no glutamine). RESULTS: Glutamine-enriched TPN increased the total appearance rate of glutamine (P: < 0.05) but did not inhibit or increase the endogenous appearance rate. The standard TPN solution also increased the glutamine appearance rate (P: < 0.05), but the change was much smaller than in the glutamine-supplemented group (P: < 0.01). The plasma glutamine concentration did not rise significantly during either treatment, suggesting increased tissue glutamine utilization, especially in the glutamine-supplemented group. CONCLUSION: In view of the enhanced glutamine requirements in response to trauma and disease by tissues such as those of the gut, the immune system, and the liver, increased glutamine availability during glutamine-enriched TPN may be beneficial preoperatively in patients with gastrointestinal disease.

Aged↗
PubMed1975

Immunochemical evidence for glutamine-mediated degradation of glutamine synthetase in cultured Chinese hamster cells.

The specific activity of glutamine synthetase in cultured Chinese hamster cells is inversely related to the concentration of glutamine in the surrounding solution. Enzyme specific activity increases 8- to 10-fold when glutamine is removed from serum-free F12 growth media. The induction of glutamine synthetase activity occurs only after glutamine removal and not after the removal of other amino acids (methionine, leucine, or isoleucine). The analysis of the glutamine-mediated decrease in glutamine synthetase activity has been simplified by the finding that depression proceeds in nutrient-free buffered saline solution (141 mM NaCl, 5.4 mM KCl and 30 mM Tricine (pH 7.4). Under these conditions, 0.1 mM cyanide blocks glutamine-mediated depression. The cyanide inhibition is reversed by the addition of 1.0 mM glucose which suggests that ATP is required for depression. Glutamine-mediated depression is temperature-dependent, occurring between 25 and 45 degrees with an optimum rate at 37 degrees. Studies of the time course of induction and depression as a function of glutamine concentration suggest that glutamine regulates the rate at which the enzyme is either modified or degraded. We have employed an antibody prepared against homogeneous Chinese hamster liver glutamine synthetase to measure the amount of glutamine synthetase protein in extracts of cells containing induced or depressed levels of enzyme activity. A highly sensitive immunoprecipitation procedure enables quantitation of nanogram amounts of glutamine synthetase protein. Glutamine synthetase in cell extracts containing induced levels of enzyme activity possesses the same molecular specific activity (ratio of activity to antigenicity) as homogeneous Chinese hamster liver glutamine synthetase. The molecular specific activity of glutamine synthetase is almost the same in extracts of cells with depressed levels of enzyme obtained by growth for short (2 hours) and long (24 hours) times in the presence of glutamine. These data suggest that glutamine-mediated depression of glutamine synthetase results from degradation of enzyme molecules.

Animals↗
PubMed1998

Absence of glutamine isotopic steady state: implications for the assessment of whole-body glutamine production rate.

1. During infusion of [5-15N]glutamine in patients with gastrointestinal cancer we unexpectedly observed a gradual decrease in time of the appearance rate (Ra) of glutamine in plasma. Here we investigate whether the failure to achieve a plateau isotopic enrichment in plasma is, among other factors, due to incomplete equilibration of the glutamine tracer with the large intramuscular free glutamine pool.2. Plasma and intramuscular glutamine enrichment were measured during 6-11 h infusions of L-[5-15N]glutamine and L-[1-13C]glutamine in post-absorptive patients admitted to hospital for elective abdominal surgery. L-[1-13C]Leucine and L-[ring-2H5]phenylalanine were infused to measure the proportion of glutamine appearing in plasma directly due to its release from protein.3. The glutamine tracer entered muscle, but the rise in intramuscular glutamine enrichment was small, presumably as a result of the enormous size of the intramuscular glutamine pool and the limited speed of entry of glutamine into muscle. In each patient the intramuscular glutamine enrichment was lower than that in plasma (P<0.001), and both increased with tracer infusion time (P<0.001), indicating incomplete equilibration of the glutamine tracer.4.A comparison of the results obtained by the two glutamine tracers indicated that recycling of the nitrogen label contributed to about 15% of the decrease in Ra.5. There was a gradual reduction in the glutamine release from proteolysis, which contributed to 16-21% of the decline in Ra.6. We conclude that slow equilibration of the glutamine tracer with the large muscle glutamine pool significantly contributes to the absence of isotopic steady state. Consequently, the appearance rate of glutamine in plasma measured during short tracer infusion periods (hours) considerably overestimates the whole-body glutamine flux.

Aged↗
PubMed2004

Absorption of enterally administered N-acetyl-l-glutamine versus glutamine in pigs.

BACKGROUND AND AIMS: Glutamine instability in liquid media suggests that evaluation of reasonable enteral nutrition sources of glutamine is needed. N-acetyl-l-glutamine offers no instability and no intolerance problems. This research was conducted to study the absorption and apparent digestibility of glutamine versus N-acetyl-l-glutamine. METHODS: Two pig models were used. (1) In a clamped jejunal loop experiment, we measured the concentrations of glutamine and N-acetyl-l-glutamine in the intestinal infused solutions, intestinal mucosa, and portal and peripheral blood. (2) In a feeding experiment, we determined their apparent digestibility. RESULTS: N-acetyl-l-glutamine ( approximately 76%) was slightly less absorbed than glutamine ( approximately 85%) from the intestinal lumen into mucosa, where it was not detected as intact molecule, suggesting almost complete hydrolysis during absorption. Virtually no intact N-acetyl-l-glutamine was observed in the blood compartments; glutamine from lumenal N-acetyl-l-glutamine had the same behavior as that from lumenal-free glutamine in portal and peripheral blood. The apparent ileal digestibility of N-acetyl-l-glutamine was lower than that of free glutamine, as N-acetyl-l-glutamine was probably retained in the intestinal lumen to a greater extent than glutamine. CONCLUSION: N-acetyl-l-glutamine appeared to be a good candidate for glutamine fortification of enteral nutrition formulas.

Animals↗
PubMed2004

Paradoxical changes of muscle glutamine release during hyperinsulinemia euglycemia and hypoglycemia in humans: further evidence for the glucose-glutamine cycle.

Insulin suppresses and counterregulatory hormones increase proteolysis. Therefore, if proteolysis were a major factor determining amino acid fluxes in plasma, one would expect release of glutamine into plasma to be suppressed by insulin under euglycemic conditions and to be stimulated under hypoglycemic conditions. However, release of glutamine into plasma remains unaltered or increases during euglycemic hyperinsulinemia and decreases during insulin-induced hypoglycemia. To investigate the mechanisms for these paradoxical observations and the role of skeletal muscle, we infused overnight fasted volunteers with [U-(14)C] glutamine and measured release of glutamine into plasma, its removal from plasma, and forearm glutamine net balance, fractional extraction, uptake and release during 4-hour euglycemic ( approximately 5.0 mmol/L, n = 7) and hypoglycemic ( approximately 3.1 mmol/L, n = 8) hyperinsulinemic ( approximately 230 pmol/L) clamp experiments. During the euglycemic clamps, plasma glutamine uptake and release (both P <.05) and forearm muscle glutamine fractional extraction (P <.05), uptake (P <.02) and release (P <.01) all increased, whereas forearm glutamine net balance remained unchanged. The increase in muscle glutamine release (from 1.85 +/- 0.26 to 2.18 +/- 0.30 micromol. kg(-1). min(-1)) accounted for approximately 60% of the increase in total glutamine release into plasma (from 5.54 +/- 0.47 to 6.10 +/- 0.64 micromol. kg(-1). min(-1)) and correlated positively with the increase in muscle glucose uptake (r = 0.80, P <.03). During the hypoglycemic clamps, plasma glutamine uptake and release and forearm glutamine release remained unaltered, but forearm glutamine fractional extraction and uptake decreased approximately 25% (both P <.01) so that forearm glutamine net release increased from 0.37 +/- 0.06 to 0.61 +/- 0.09 micromol. kg(-1). min(-1) (P <.03). We conclude that skeletal muscle is largely responsible for the increased release of glutamine into plasma during euglycemic hyperinsulinemia in humans, and that this may be due to increased conversion of glucose to glutamine as part of the glucose-glutamine cycle; during hypoglycemic hyperinsulinemia decreased glutamine uptake by skeletal muscle may be important for providing substrate for increased glutamine gluconeogenesis.

Adult↗
PubMedDate not supplied

Comparison of parenteral nutrition supplemented with L-glutamine or glutamine dipeptides.

Although glutamine is an important fuel used by the intestinal mucosa and other visceral organs, it is not present in any commercially available parenteral amino acid solution. To compare the effects of L-glutamine with glutamine dipeptides, we studied the effects of each in 8 dogs and 60 Wistar rats. In the dog study, three amino acid solutions were compared: standard commercial amino acid solution (control), alanine-glutamine dipeptide-enriched solution (glutamine 3.4%), and glycine-glutamine dipeptide-enriched solution (glutamine 3.6%). Arterial and venous samples were collected to compare the effects of the three solutions on skeletal muscle amino acid exchange. In the rat study, two studies were undertaken: group 1 rats underwent only central venous catheterization; group 2 rats underwent central venous catheterization and a 50% intestinal resection. Within each group, three different solutions were infused: standard amino acid solution (control), glutamine-enriched (1.5% glutamine) solution, or glutamine dipeptide-enriched (1% glutamine) solution. After 7 days of parenteral nutrition, samples of gut, blood, and muscle were collected for determination of mucosal thickness, villus area, serum amino acid profile, liver and renal function tests, and muscle composition. When glutamine or glutamine-dipeptide solutions were administered, the dogs showed increasing serum glutamine concentrations and enhanced glutamine uptake across the hind leg muscle. Similarly, both groups of rats demonstrated significant differences in serum glutamine levels, nitrogen balance, intestinal mucosa thickness, and villus area. We conclude that both glutamine and glutamine-dipeptide infusions increase serum glutamine concentrations and result in regional tissue effects. Both exerted similar metabolic effects with no apparent complications.

Amino Acids↗
PubMed1990

Glutamine-enriched diets support muscle glutamine metabolism without stimulating tumor growth.

Glutamine is a principal fuel utilized by rapidly growing tumors. Advanced malignant disease results in muscle glutamine depletion and weight loss. Concern exists about providing dietary glutamine to the host with cancer since it may stimulate tumor growth. This study examined the effects of oral glutamine on muscle glutamine metabolism and tumor growth. Twenty-four rats with large sarcomas were pair fed a glutamine-enriched or glutamine-free elemental diet. Diets were isonitrogenous and isocaloric. After 6 days of feeding, the animals were anesthetized and arterial glutamine, hindquarter glutamine flux, muscle glutamine content, tumor weight, tumor DNA content, tumor glutaminase activity, and number of metaphase mitoses/high power field (HPF) in the tumor were determined. There was no difference in arterial glutamine between the two groups, but provision of a glutamine-enriched diet increased muscle glutamine content by 60% (2.31 +/- 0.21 mumole/g tissue vs 1.44 +/- 0.22 mumol/g tissue, P less than 0.05), which supported muscle glutamine release. There were no differences among tumor DNA content, tumor glutaminase activity, or tumor weight and there was no difference histologically in the number of metaphase mitoses/HPF. Glutamine-enriched oral diets may replete host glutamine stores and support muscle glutamine metabolism without stimulating tumor growth.

Animals↗
PubMed1978

Effects of glutamine, methionine sulfone and dexamethasone on rates of synthesis of glutamine synthetase in cultured hepatoma cells.

Glutamine synthetase (EC 6.3.1.2) activity of hepatoma tissue culture cells is elevated by corticosteroids and depressed by glutamine (Kulka, R.G., Tomkins, G.M. and Crook, R.B. (1972) J. Cell Biol., 54, 175--179). The transfer of cells from high (1--5 mM) to low (0.2--0.4 mM) concentrations of glutamine causes a marked increase in glutamine synthetase activity. The addition of a glutamine antagonist, methionine sulfone (1 mM) to cells suspended in high (1 mM) concentrations of glutamine also causes an increase of glutamine synthetase activity which is greater than that elicited by the transfer of cells to low concentrations of glutamine. Rates of synthesis of glutamine synthetase have been measured by radioimmunoprecipitation in hepatoma tissue culture cells incubated under various conditions. Incubation of cells with the synthetic corticosteroid hormone, dexamethasone, markedly stimulates the relative rate of glutamine synthetase biosynthesis. Glutamine, or its analogue, methionine sulfone, have no effect on the relative rate of synthesis of the enzyme. However, total protein and RNA synthesis increase markedly with increasing external glutamine concentration in the range 0--1 mM. Methionine sulfone (1 mM) inhibits the degradation of glutamine synthetase in the presence of 1 mM glutamine. The data are consistent with the conclusion that the corticosteroid, dexamethasone, elevates glutamine synthetase activity by stimulating its rate of synthesis, whereas methionine sulfone elevates glutamine synthetase activity by inhibiting the glutamine-stimulated degradation of preformed enzyme.

Animals↗
PubMedDate not supplied

Glutamine synthetase activity and glutamine content in brain: modulation by NMDA receptors and nitric oxide.

Acute intoxication with large doses of ammonia leads to rapid death. The main mechanism for ammonia elimination in brain is its reaction with glutamate to form glutamine. This reaction is catalyzed by glutamine synthetase and consumes ATP. In the course of studies on the molecular mechanism of acute ammonia toxicity, we have found that glutamine synthetase activity and glutamine content in brain are modulated by NMDA receptors and nitric oxide. The main findings can be summarized as follows. Blocking NMDA receptors prevents ammonia-induced depletion of brain ATP and death of rats but not the increase in brain glutamine, indicating that ammonia toxicity is not due to increased activity of glutamine synthetase or formation of glutamine but to excessive activation of NMDA receptors. Blocking NMDA receptors in vivo increases glutamine synthetase activity and glutamine content in brain, indicating that tonic activation of NMDA receptors maintains a tonic inhibition of glutamine synthetase. Blocking NMDA receptors in vivo increases the activity of glutamine synthetase assayed in vitro, indicating that increased activity is due to a covalent modification of the enzyme. Nitric oxide inhibits glutamine synthetase, indicating that the covalent modification that inhibits glutamine synthetase is a nitrosylation or a nitration.Inhibition of nitric oxide synthase increases the activity of glutamine synthetase, indicating that the covalent modification is reversible and it must be an enzyme that denitrosylate or denitrate glutamine synthetase.NMDA mediated activation of nitric oxide synthase is responsible only for part of the tonic inhibition of glutamine synthetase. Other sources of nitric oxide are also contributing to this tonic inhibition. Glutamine synthetase is not working at maximum rate in brain and its activity may be increased pharmacologically by manipulating NMDA receptors or nitric oxide content. This may be useful, for example, to increase ammonia detoxification in brain in hyperammonemic situations.

Adenosine Triphosphate↗
PubMed1993

Effects of glutamine deprivation on glutamine transport and synthesis in primary culture of rat skeletal muscle.

The effects of deprivation and supplementation of exogenous glutamine (0.06 and 2.2 mM in the culture medium, respectively) were studied in mononucleated myoblasts and in multinucleated myotubes. Myoblasts cultured in glutamine-deprived medium showed reductions in plating efficiency and myotube fusion index. Myotubes grown in glutamine-supplemented cultures had higher intracellular glutamine concentrations than those grown in glutamine-deprived medium (67 +/- 4.2 vs. 46 +/- 3.6 nmol/mg cell protein, respectively) and glutamine-supplemented myotubes utilized glutamine, whereas glutamine-deprived myotubes released it. Glutamine deprivation for 12 h caused a significant, cycloheximide-blockable increase in the capacity for glutamine uptake via system Nm in both myoblasts and myotubes (maximum velocity increases of 23 +/- 5.3 and 35 +/- 4.2%, respectively), which was reversed by glutamine replenishment. Depriving myotubes of glutamine did not alter the kinetics of uptake of amino acid transport systems A, ASC, or L. Glutamine deprivation resulted in a threefold increase in glutamine synthetase activity, whereas glutaminase activity remained unchanged. System Nm and glutamine synthetase appear to undergo adaptive upregulation in glutamine-deprived muscle cells to compensate for the reduced exogenous glutamine supply.

Amino Acids↗
PubMed1995

Response of glutamine metabolism to exogenous glutamine in humans.

To determine whether exogenous glutamine affects whole body glutamine metabolism, preliminary experiments were performed to verify that L-[1-13C]-, L-[U-14C]-, and L-[3,4-3H]glutamine given simultaneously by vein provided similar estimates of glutamine appearance rates [Ra; 355 +/- 24, 373 +/- 19, and 393 +/- 24 (SE) mumol.kg-1.h-1, respectively, P = NS] in six healthy men; glutamine oxidation accounted for 32 +/- 3 and 51 +/- 5% (P < 0.01) of glutamine Ra when it was measured using L-[U-14C]- and L-[1-13C]glutamine, respectively. Five subjects received two 5-h intravenous infusions of L-[3,4-3H]glutamine and a simultaneous nasogastric infusion of L-[1-13C]glutamine on 2 separate days in the postabsorptive state, along with saline on 1 day and natural L-glutamine (856 +/- 45 mumol.kg-1.h-1) on another day in a randomized order. Splanchnic glutamine extraction (determined from [13C]glutamine appearance into systemic blood) reached 74 +/- 4 and 53 +/- 5% during the enteral infusion of tracer alone and in combination with a large load of glutamine, respectively. Glutamine infusion was associated with increased plasma glutamine concentration (from 630 +/- 50 to 1,297 +/- 75 microM), Ra (from 258 +/- 20 to 589 +/- 45 mumol.kg-1.h-1), and oxidation (from 179 +/- 20 to 477 +/- 47 mumol.kg-1.h-1, all P < 0.01), no change in glutamine release from proteolysis, and a decline in glutamine de novo synthesis (from 156 +/- 15 to 93 +/- 13 mumol.kg-1.h-1).(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗
PubMed2006

Effect of alanyl-glutamine supplementation on plasma and tissue glutamine concentrations in rats submitted to exhaustive exercise.

OBJECTIVE: We investigated the effect of supplementation with L-glutamine and L-alanyl-L-glutamine (DIP) on the plasma and tissue glutamine concentrations of exercise-trained rats immediately and 3 hours after a single exercise session until exhaustion. METHODS: Thirty-six male rats were divided into six groups, and then subdivided into groups submitted only to the exhaustion test: control (CON-EXA, n = 6), glutamine (GLN-EXA, n = 6) and DIP-EXA (n = 6), or to the exhaustion test followed by a recovery period lasting 3 hours: control (CON-REC, n = 6), glutamine (GLN-REC, n = 6) and DIP-REC (n = 6). The training protocol consisted of bouts of swimming exercise (60 min x day(-1)) for 6 weeks. During the last 21 days, before sacrifice, the glutamine and DIP groups received a daily dose of 1 g x kg(-1) of glutamine and 1.5 g x kg(-1) of DIP, respectively. The GLN-REC and DIP-REC groups were also supplemented immediately after the exhaustion test. Concentrations of glutamine, glutamate, glucose and ammonia in plasma and of glutamine, protein and glycogen in liver and muscle were evaluated. RESULTS: The time to exhaustion did not differ between groups. A higher concentration of glutamine in the gastrocnemius and soleus muscles was observed for the DIP-EXA group compared to the CON-EXA and GLN-EXA groups (P < 0.05). The DIP-REC group presented a higher plasma and liver glutamine concentration than the CON-REC group (P < 0.05). Muscle glutamine and protein concentration was higher in both the GLN-REC and DIP-REC groups compared to the CON-REC group (P < 0.05). CONCLUSIONS: Chronic supplementation with DIP promoted a higher muscle glutamine concentration than chronic supplementation with glutamine immediately after exercise. However, no significant difference in plasma or tissue glutamine concentrations was observed between acute supplementation with glutamine and DIP during the post-exhaustive exercise recovery period.

Animals↗
PubMed1998

Glutamine biosynthesis and the utilization of succinate and glutamine by Rhizobium etli and Sinorhizobium meliloti.

Sinorhizobium meliloti 1021 and Rhizobium etli CE3 turn over nitrogen and carbon from glutamine to ammonium and CO2, respectively. Some of the ammonium released is assimilated back into glutamine, indicating that a glutamine cycle similar to that in Neurospora operates in Rhizobium. In addition, a previously unrecognized metabolic pathway in Rhizobium was discovered--namely, conversion of glutamine-carbon to gamma-hydroxybutyric acid and beta-hydroxybutyric acid. Additionally, some of the 2-oxoglutarate derived from glutamine catabolism in Rhizobium is converted to succinate in glutamine-containing medium. Both S. meliloti 1021 and R. etli CE3 oxidize succinate preferentially over glutamine when provided with both carbon sources. In contrast to Sinorhizobium meliloti 1021 and Rhizobium etli CE3, an S. meliloti double mutant that lacks both glutamine synthetase (GS) I and II preferentially oxidizes glutamine over succinate when supplied with both substrates. GSII activity is induced in wild-type S. meliloti 1021 and R. etli CE3 grown in succinate-glutamine medium, and this enzyme participates in the cycling of glutamine-carbon and -nitrogen. On the other hand, GSII activity is repressed in both micro-organisms when glutamine is the only carbon source. These findings show that, in medium containing both glutamine and succinate, glutamine synthesis helps drive the utilization of succinate. When glutamine is in excess as an energy-providing substrate its synthesis is restricted, allowing for more effective utilization of glutamine as an energy source.

Amino Acids↗
PubMed2000

Dietary glutamine suppresses endogenous glutamine turnover in the rat.

Plasma glutamine turnover was determined using 1-14C-labeled glutamine in rats that consumed crystalline amino acid diets containing the equivalent of 16% protein with 25% of the amino acids as glutamine or a control diet containing no glutamine (or glutamate) for 10 days. Glutamine turnover in glutamine-fed animals was 66% of the rate in the control group. Glutamine feeding caused 20% higher levels of arterial plasma glutamine. Arterial-portal differences across the portal-drained viscera showed net glutamine uptake in control animals but no net uptake or release in the glutamine-fed group. Skeletal muscle glutamine synthetase activity was similar in both groups. The results indicate that long-term consumption of relatively large amounts of dietary glutamine decreases the turnover of plasma glutamine and thus reduces the need for endogenous glutamine synthesis.

Amino Acids↗