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PubMed1984

Regulation of glutamine synthetase and glutaminase activities in cultured skeletal muscle cells.

Glutamine is synthesized in skeletal muscle, released to the circulation, and transported to other tissues, where it may provide important substrate for gluconeogenesis, ammoniagenesis, and energy-yielding pathways. With the ultimate goal of delineating the factors that control glutamine production and release by skeletal muscle, we have studied the regulation of two key enzymes, glutamine synthetase and glutaminase, in the L6 line of rat skeletal muscle cells grown in monolayer culture. The cultured myotubes were found to have glutamine synthetase and phosphate-dependent glutaminase activities. Glutamine synthetase activity was increased following incubation (1) in glutamine-free medium (threefold); (2) in medium containing high glutamic acid concentrations (fourfold); and (3) in medium supplemented with dexamethasone (threefold). In each case the increase in glutamine synthetase activity required several hours to reach a maximum and was prevented by cycloheximide, suggesting that the change occurred through increased enzyme biosynthesis. No substances tested were found to affect glutaminase activity. We conclude that glutamine synthetase in cultured skeletal muscle is responsive to substrate, product, and hormonal regulation.

Animals↗
PubMed1988

Amino acid pools in CHL V79 cells during induction of thermotolerance: reduction in free intracellular glutamine.

The amino acid pools in Chinese hamster lung V79 cells were measured as a function of time during hyperthermic exposure at 40.5 degrees and 45.0 degrees C. Sixteen of the 20 protein amino acids were present in sufficient quantity to measure accurately. The total amino acid pool and all individual amino acids, except glutamine, remained relatively constant for at least 90 min at 40.5 degrees C and for 30 min at 45 degrees C. The glutamine pool decreased rapidly to 20% of its control value within 30 min at 40.5 degrees C with a T1/2 = 15 min. At 45 degrees C, the decrease was 36%. Thermotolerance developed at 40.5 degrees C with a T1/2 = 30 min; thus, glutamine depletion preceeds the development of thermotolerance. The depletion of glutamine is probably due to increased metabolism and oxidation of glutamine through the TCA cycle at hyperthermic temperatures. Glutamine, as is true for other amino acids, was shown to protect proteins from thermal inactivation and V79 cells from hyperthermic killing when added in excess (4-10 mM) to the medium during heat stress. However, the stability of the total amino acid pool during the development of thermotolerance indicates that resistance to heat does not result from the accumulation of amino acids which then protect against thermal damage. The effects of the large decrease in the glutamine pool are unknown, although glutamine depletion may act as a signal for part of the heat shock response.

Amino Acids↗
PubMed2003

Glutamine and the maintenance of meiotic arrest in mouse oocytes: influence of culture medium, glucose, and cumulus cells.

The selection of culture media and supplements therein has a tremendous impact on the regulation of oocyte maturation in vitro. In the present study, we have evaluated how altering the levels of glutamine in the presence or absence of glucose affects meiotic arrest in cumulus cell-enclosed oocytes (CEO) and denuded oocytes (DO) when cultured in either the simple medium M16 or the more complex Eagle's minimum essential medium (MEM). We have also tested the effectiveness of follicle-stimulating hormone (FSH) in triggering germinal vesicle breakdown (GVB) and purine de novo synthesis in differing MEM culture conditions. When DO were cultured 17-18 hr in hypoxanthine (HX)- or dbcAMP-supplemented M16 medium, neither glucose nor glutamine had any effect on oocyte maturation, with dbcAMP the more effective inhibitor. In the absence of glutamine, cumulus cells promoted meiotic resumption, since significantly lower levels of meiotic arrest were maintained in CEO than in DO by either HX or dbcAMP, but addition of the amino acid dose-dependently decreased the maturation percentage in CEO below that observed in DO. In MEM, glutamine and glucose again had little effect on the maturation of DO, although the percentage of maturing DO in HX-supplemented medium was about 20% lower than that in M16 medium. In the absence of glucose, high levels of maturation were observed in CEO in glutamine-free medium that were dose-dependently lowered by the amino acid. However, when glucose was present, CEO were as effectively arrested as DO when glutamine was absent, with no further effect of the amino acid. This inhibitory action of glucose was dependent on the essential amino acids present in MEM. The effects of glutamine were not due to changes in metabolic coupling between the oocyte and cumulus cells. Measurement of purine de novo synthesis indicated that the maintenance of meiotic arrest as well as FSH induction of meiotic resumption were associated with increases in purine synthesis. We conclude that glucose and glutamine act cooperatively to promote the synthesis of new purine compounds within the somatic compartment and that the timing and duration of such synthesis determines whether meiotic resumption will be suppressed or promoted.

Animals↗
PubMed1999

Effect of glutamine on Th1 and Th2 cytokine responses of human peripheral blood mononuclear cells.

Decreased glutamine concentrations are found in patients with catabolic stress and are related to susceptibility to infections. In this study, we evaluated the role of glutamine in Th1/Th2 cytokine responses. Peripheral blood mononuclear cells were stimulated with phytohemagglutinin (PHA), live attenuated bacillus Calmette-Guérin (BCG), or measles virus in the presence of different glutamine concentrations. We found that glutamine at an optimal concentration (0.6 mM) significantly enhanced PHA-stimulated lymphocyte proliferation as well as Th1 [interferon-gamma (IFN-gamma) and interleukin-2 (IL-2)] and Th2 cytokine (IL-4 and IL-10) production. In the absence of glutamine, BCG and measles virus elicited minimal lymphocyte proliferation, whereas BCG enhanced Th1 cytokine response and measles virus promoted Th2 cytokine response. Interestingly, addition of glutamine promoted the BCG-elicited Th1 cytokine response (IFN-gamma), but suppressed the measles-induced Th2 cytokine response (IL-10). These results suggest that appropriate glutamine levels may influence host responses to different antigens and microorganisms. Furthermore, predominately Th1, but not Th2, cytokine responses required the presence of optimal concentrations of glutamine.

BCG Vaccine↗
PubMed2002

Glutamine decreases interleukin-8 and interleukin-6 but not nitric oxide and prostaglandins e(2) production by human gut in-vitro.

BACKGROUND: Glutamine modulates cytokine production in various tissues but its effects on the production of other inflammatory mediators such as eicosanoids and nitric oxide have not been investigated in human gut. AIM: To evaluate the influence of glutamine on interleukin (IL)-8, IL-6, nitric oxide and prostaglandin E(2) production by human gut. METHODS: Ten fasted volunteers received either enteral glutamine or isonitrogenous amino acids over 6 h in a cross-over design. Series of duodenal biopsies were frozen or cultured for 24 h with 0.5 or 5 mM of glutamine or amino acids. IL-6, IL-8 and PGE(2) were measured in culture media by ELISA and nitrites by Griess assay. mRNA levels for IL-6, IL-8, Cyclooxygenase-2 and NO synthase-2 were assessed in biopsies by RT-PCR. Results in percent, (median [range]) were compared by Wilcoxon test. RESULTS: Glutamine decreased IL-8 and IL-6 in-vitro production: 63 [2-173] vs 100 [19-177] and 37 [5-489] vs 100 [33-431], both P<0.05. IL-8 mRNA level also decreased in biopsies cultured with 5 mM glutamine: 26 [13-142] vs 92 [34-215], P<0.05. Nitrites and PGE(2) concentrations were not significantly affected by glutamine. CONCLUSION: Glutamine has a specific inhibitory effect on pro-inflammatory cytokine production in the gut and may contribution to the modulation of intestinal inflammation.

Adult↗
PubMed2001

Glutamine enhances the gut-trophic effect of growth hormone in rat after massive small bowel resection.

Background. Bowel-specific nutrient, glutamine, growth hormone, and modified diet have been reported to jointly improve nutrient absorption in patients with short bowel syndrome. However, controversy exists about the exact treatment factor. In this study we attempted to analyze the individual and combined effect of glutamine supplementation and growth hormone on small bowel adaptation by using tube feeding to control luminal nutrition supply. Materials and methods. Thirty-two adult male Sprague-Dawley rats (278 +/- 8 g) underwent 85% mid-small bowel resection and were randomly assigned to four groups: Control, receiving control liquid diet via a gastrotomy tube; GLN, receiving liquid diet enriched with 20 g. L(-1) glutamine; GH, receiving subcutaneous growth hormone (GH) (0.3 IU, bid); and GLN + GH, receiving both glutamine supplementation and GH treatment. All animals were provided with isocaloric (60 kcal/day) and isonitrogenous (0.686 g/day) nutrition. Absorption tests were performed in the form of oral nutrient tests with (14)C-labeled glucose and (3)H-labeled palmitic acid on the Postoperative Day 12. Results. GH treatment significantly increased the plasma insulin-like growth factor I (IGF-I) level, body weight, jejunal and ileal villous height and mucosal thickness, and peak plasma (14)C and (3)H levels. Glutamine supplementation did not produce a significant difference; however, combined with GH treatment, glutamine supplementation further increased body weight, plasma IGF-I level, jejunal and ileal villous height and mucosal thickness, and peak plasma (14)C and (3)H levels significantly. Conclusions. After massive small bowel resection, enteral glutamine supplementation alone has no remarkable beneficial effect on bowel adaptation. However, glutamine supplementation enhanced the gut-trophic effect of GH.

Absorption↗
PubMed1988

Pyruvate carboxylation in glutamine synthesis from alanine by isolated guinea-pig renal cortical tubules.

Isolated guinea-pig kidney cortex tubules were incubated in Krebs-Henseleit buffer containing NaH14CO3 (25 mM) and L-alanine (5 mM). A high rate of alanine metabolism was found to be accompanied by a high rate of both 14CO2 fixation and glutamine synthesis. The fixation of 14CO2 was virtually abolished in the presence of oxalate, a known inhibitor of pyruvate carboxylase, indicating that, in guinea-pig renal cortex, this enzyme is responsible for the synthesis of oxaloacetate in the conversion of alanine into glutamine. More than 90% of the label fixed was found in carbon 1 mainly of glutamine and to a lesser extent of glutamate. In the presence of alanine + NaH14CO3 + MSO, an inhibitor of glutamine synthetase, most of the 14CO2 fixed by pyruvate carboxylase was subsequently released and carbon 1 of glutamate was the only site of labelling. In the presence of alanine + NaH14CO3, the fact that not all the glutamine found was labelled in carbon 1 could be explained by glutamine synthesis from endogenous substrates as well as by glutamine synthesis from alanine after prior equilibration of [4-14C]-oxaloacetate with fumarate; that such equilibration occurred was demonstrated by the observation that [1-14C]-glutamine and [1-14C]-glutamate were synthesized from [1-14C]-alanine.

Alanine↗
PubMed1996

Alterations in carrier-mediated glutamine transport after a model of canine jejunal autotransplantation.

The effects of small bowel transplantation (SBTx) on absorptive function are unknown. Preliminary experiments showed a decrease in absorption of glutamine. Our aim was to determine mechanisms of decreased ileal transport of glutamine utilizing a model of intestinal autotransplantation. Seven dogs were studied before and after a model of jejunoileal autotransplantation. In vivo absorption experiments were performed before and two and eight weeks postoperatively with an electrolyte solution containing glutamine (20 mM). In vitro glutamine transport was studied using brush-border membrane vesicles (BBMV) prepared from ileal mucosa obtained from six other dogs and compared to a controls. In vivo net absorptive flux of glutamine decreased at two weeks but returned toward baseline by eight weeks (P = 0.06). Transport of glutamine into BBMVs was decreased at two weeks and remained decreased at eight weeks. KmaxNa+, a measure of carrier affinity was unchanged but VmaxNa+, a function of the number of transporter was decreased at two and eight weeks. Glucose transport was unchanged. It is concluded that jejunoileal autotransplantation decreases ileal absorption of glutamine by a decrease in carrier-mediated transport of glutamine.

Alanine↗
PubMed1993

Glucose and glutamine metabolism of a murine B-lymphocyte hybridoma grown in batch culture.

The energy metabolism of a mammalian cell line grown in vitro was analyzed by substrate consumption rates and metabolic flux measurements. The data allowed the determination of the relative importance of the pathways of glucose and glutamine metabolism to the energy requirements of the cell. Changes in the substrate concentrations during culture contributed to the changing catalytic activities of key enzymes, which were determined. 1. A murine B-lymphocyte hybridoma (PQXB1/2) was grown in batch culture to a maximum cell density of 1-2 x 10(6) cells/mL in 3-4 d. The intracellular protein content showed a maximum value during the exponential growth phase of 0.55 mg/10(6) cells. Glutamine was completely depleted, but glucose only partially depleted to 50% of its original concentration when the cells reached a stationary phase following exponential growth. 2. The specific rates of glutamine and glucose utilization varied during culture and showed maximal values at the midexponential phase of 2.4 nmol/min/10(6) cells and 4.3 nmol/min/10(6) cells, respectively. 3. A high proportion of glucose (96%) was metabolized by glycolysis, but only limited amounts by the pentose phosphate pathway (3.3%) and TCA cycle (0.21%). 4. The maximum catalytic activity of hexokinase approximates to the measured flux of glycolysis and is suggested as a rate-limiting step. In the stationary phase, the hexokinase activity reduced to 11% of its original value and may explain the reduced glucose utilization at this stage. 5. The maximal activities of two TCA cycle enzymes were well above the measured metabolic flux and are unlikely to pose regulatory barriers. However, the activity of pyruvate dehydrogenase was undetectable by spectrophotometric assay and explains the low level of flux of glycolytic metabolites into the TCA cycle. 6. A significant proportion of the glutamine (36%) utilized by the cells was completely oxidized to CO2. 7. The measured rate of glutamine transport into the cells approximated to the metabolic flux and is suggested as a rate-limiting step. 8. Glutamine metabolism is likely to occur via glutaminase and amino transaminase, which have significantly higher activities than glutamate dehydrogenase. 9. The calculated potential ATP production suggests that, overall, glutamine is the major contributor of cellular energy. However, at the midexponential phase, the energy contribution from the catabolism of the two substrates was finely balanced--glutamine (55%) and glucose (45%).

Adenosine Triphosphate↗
PubMed2004

Effects on skeletal muscle of intravenous glutamine supplementation to ICU patients.

OBJECTIVE: To evaluate the effect of four doses of intravenous glutamine supplementation on skeletal muscle metabolism. DESIGN: A prospective, blinded, randomized study. SETTING: The general Intensive Care Unit (ICU) of a university hospital. PATIENTS: ICU patients with multiple organ failure (n=40), who were expected to stay in the unit for more than five days. INTERVENTION: Patients received 0, 0.28, 0.57 or 0.86 g of glutamine per kg bodyweight per day intravenously for five days as part of an isocaloric, isonitrogenous and isovolumetric diet. RESULTS: Plasma glutamine concentration responded to glutamine supplementation with normalization of plasma levels in a dose-dependent way, while free muscle glutamine concentration, as well as muscle protein synthesis and muscle protein content, did not change significantly. CONCLUSION: Intravenous glutamine supplementation to ICU patients for a period of five days resulted in normalization of plasma glutamine concentrations in a dose-dependent way whereas muscle glutamine concentrations were unaffected.

Adult↗
PubMed1999

Metabolic responses to different glucose and glutamine levels in baby hamster kidney cell culture.

In this work, a BHK21 clone producing a recombinant antibody/cytokine fusion protein was used to study the dependence of cell metabolism on the glucose and glutamine levels in the culture medium. Results obtained indicate that both glucose and glutamine consumptions show a Michaelis-Menten dependence on glucose and glutamine concentrations respectively. A similar dependence is also observed for lactate and ammonia productions. The estimated value of the Michaelis constant for the dependence of lactate production on glucose (KLacGlc) was 1.4 +/- 0.1 mM and for the dependence of ammonia production on glutamine (KAmmGln) was 0.25 +/- 0.11 mM and 0.10 +/- 0.03 mM, at glucose concentrations of 0.28 mM and 5.6 mM respectively. At very low glucose concentrations, the glucose to lactate yield decreased markedly, showing a metabolic shift towards lower lactate production. This metabolic shift was also confirmed by the significant increase in the specific oxygen consumption rate also observed at low glucose concentrations. Although it was highly dependent on glucose concentration, the oxygen consumption also increased with the increase in glutamine concentration. At very low glutamine concentrations, the glutamine to ammonia yield increased, showing a more efficient glutamine metabolism.

Ammonia↗
PubMed1998

The effects of high-intensity intermittent exercise on the plasma concentrations of glutamine and organic acids.

Glutamine is an essential substrate for the proper functioning of cells of the immune system. Falls in plasma glutamine concentration after exercise may have deleterious consequences for immune cell function and render the individual more susceptible to infection. The purpose of the present study was to examine changes in plasma glutamine concentration (measured using a validated enzymatic spectrophotometric method) following an acute bout of intermittent high-intensity exercise. Eight well-trained male games players took part in the study. Subjects reported to the laboratory following an overnight fast and performed a 1-h cycle exercise task consisting of 20 1-min periods at 100% maximal O2 consumption (VO2max) each separated by 2 min of recovery at 30% VO2max. Venous blood samples were taken before exercise and at 5 min, 1 h, 2.5 h, 5 h and 24 h post-exercise. Glutamine was measured by enzymatic spectrophotometric determination of the ammonia concentration before and after treatment of the plasma with glutaminase (EC 3.5.1.2). Plasma glutamine concentration did not fall in the immediate post-exercise period [pre-exercise 681 (23) microM compared with 663 (46) microM at 5 min post-exercise, mean (SEM)], but fell to 572 (35) microM at 5 h post-exercise (P < 0.05 compared with pre-exercise). Plasma lactate concentration rose to 8.8 (1.0) mM at the end of exercise and fell to 1.8 (0.4) mM at 1 h post-exercise, but plasma concentrations of free fatty acids and beta-hydroxybutyrate both rose substantially in the post-exercise period (to 240% and 400% of pre-exercise levels, respectively). The circulating leucocyte count increased significantly during exercise (P < 0.01), continued to increase in the hours following exercise and peaked at 2.5 h post-exercise (mainly due to a neutrophilia). The fall in the plasma glutamine concentration at 5 h post-exercise could be due to increased renal uptake of glutamine, which generally occurs in conditions of metabolic acidosis or due to a greater removal of glutamine from the plasma resulting from the elevated circulating leucocyte count.

3-Hydroxybutyric Acid↗
PubMed2005

Estrogen (17beta-estradiol) enhances glutamine synthetase activity in C6-glioma cells.

Glutamine synthetase (GS) is the major glutamine-forming enzyme of vertebrates and is accepted to be a marker of astroglial cells. Maturation of astroglial cells is characterized by an increase of GS activity, and the regulation of this enzyme is the topic of many publications. Because of the fundamental role of the GS in controlling brain glutamate and glutamine level, it is essential to understand the mechanism of expression of this enzyme. To our knowledge, the effect of estrogen (17beta-estradiol) on GS activity in glial cells has not been reported. We examined the effect of treatment with estrogen on glutamine synthetase enzyme activity in glial cells. C6-glioma cells in later passage have many astrocytic characteristics and provided a convenient and well-established model system. We adapted a colorimetric method to measure GS-catalyzed gamma-glutamyltransferase (GT) activity in C6-glioma cells. The assay monitors GT activity of glutamine synthetase by following the absorbance of the product gamma-glutamyl hydroxamate at 540 nm. We observed that, the absorbance of gamma-glutamyl hydroxamate significantly increased in estrogen treated cells (0.13 +/- 0.03), as compared to untreated cells (0.058 +/- 0.015). Estrogen also significantly increased concentration of glutamine in C6-glioma cells as measured by fluorometric assay. In addition, western blot analysis showed that estrogen significantly increased the amount of glutamine synthetase compared to control. This estrogen effect could have important physiological implications on cerebral glutamate and glutamine metabolism.

Cell Line, Tumor↗
PubMed1976

Importance of the flux of phosphate across the inner membrane of kidney mitochondria for the activation of glutaminase and the transport of glutamine.

The effect of mersalyl, an inhibitor of phosphate transport across the inner mitochondrial membrane, was investigated on the uncoupled respiration of pig kidney mitochondria in the presence of glutamine as substrate and on the activity of the phosphate-dependent glutaminase in the intact organelles. In addition, the submitochondrial location of the enzyme was reinvestigated. (1) It was found that mersalyl completely inhibits uncoupled respiration of the mitochondria in the presence of glutamine as substrate, whereas respiration with glutamate was not affected. The same amount of mersalyl which inhibits coupled oxidation of glutamine also inhibits coupled oxidation of glutamate and some other substrates. (2) Mersalyl strongly inhibited the activation of glutaminase in intact mitochondria only in the presence of inhibitiors of electron transport or of an uncoupler. The addition of a detergent prevented or fully released the inhibition. The effect of mersalyl was observed even when the mitochondria were pre-incubated with phosphate or incubated in the phosphate-free medium. If mersalyl and carbonyl cyanide m-chlorophenylhydrazone (CCCP) were added 3 min after pre-incubation with phosphate the same intramitochondrial concentration of the anion as in control experiments was found, whereas the activity of glutaminase was severely inhibited. These findings suggest that the activation of the enzyme by phosphate in intact nonenergized mitochondria occurs only if the activator moves across the inner mitochondrial membrane. (3) Mersalyl (plus CCCP) markedly decreased [14C]glutamine- and [32P]-phosphate-permeable mitochondrial spaces. A close correlation between the decrease of phosphate and glutamine permeable spaces and the inhibition of glutaminase activity was found. (4) If the activation energy of the enzyme was determined with frozen mitochondrial preparations, a discontinuity or break in the Arrhenius plot was observed, whereas the presence of a detergent completely abolished the break. Digitonin or ultrasonic treatment of the mitochondria followed by separation of the membrane and the soluble fraction revealed that glutaminase is a membrane-bound enzyme. On the basis of these findings it is concluded that there is an association between the transport on one side and the transport of glutamine and glutaminase activity on the other. It is possible that the movement of phosphate across the membrane activates the enzyme which facilitates diffusion of glutamine down a concentration gradient. However, the existance of a specific glutamine-phosphate carrier is not ruled out.

Animals↗
PubMed1986

Characterization of L-threonine and L-glutamine transport in murine P388 leukemia cells in vitro. Presence of an N-like amino acid transport system.

The transport of L-threonine and L-glutamine into murine P388 leukemia cells has been characterized. Threonine appears to be a specific substrate for a Na+-dependent amino acid transport system similar to system ASC of the HTC hepatoma cell. Threonine transport is uninhibited by 2-aminobicyclo[2,2,1]heptane-2-carboxylic acid and alpha-(methylamino)isobutyric acid, shows a pattern of transport similar to that seen in HTC hepatoma cells over the pH range of 5.5-7.5, and is inhibited by L-serine and L-cysteine. Approximately two-thirds of glutamine transport into P388 cells also appears to enter P388 cells via this ASC-analogous system. However, based upon (a) inhibition studies with threonine (where the K1 of threonine inhibition of glutamine transport was 7-fold the Km of threonine transport), (b) inhibition analysis of glutamine transport with various amino acids and amino acid analogues, and (c) different patterns of transport between threonine and glutamine over the pH range of 5.5-7.5, approximately one-third of glutamine transport can be attributed to a second Na+-dependent amino acid transport system. This system appears to be similar to the system N of rat hepatocytes. Glutamine and threonine do not appear to enter P388 cells via systems A or L to any significant degree. P388 cells do not appear to exhibit 'adaptive regulation' of amino acid transport. Differences in 'adaptive regulation' could therefore not be utilized for comparing threonine and glutamine transport.

Aminoisobutyric Acids↗
PubMed1984

Involvement of protease in L-glutamine control of nucleic acid and polyphosphate metabolism in cells transformed by 9,10-dimethyl-1,2-benzanthracene, SV40 and H-ras oncogene.

Mammalian cells transformed with either 9,10-dimethyl-1,2-benzanthracene, SV40 or H-ras oncogene dramatically changed their ability to synthesize DNA and RNA and metabolize polyphosphate when L-glutamine was withdrawn from the growth medium or when heat shocked (growth at 42 degrees C). Untransformed, DNA and RNA synthesis decreased by 50-80% when glutamine was withdrawn, but polyphosphate accumulated whether or not glutamine was supplied. Heat shock did not alter this response. Transformed isogenic cells responded differently; at 37 degrees C, they decreased their synthesis of DNA and RNA if starved for glutamine, whereas at 42 degrees C, synthesis was optimal without glutamine. Transformed cells accumulated polyphosphate at 37 degrees C when starved for glutamine, but at 42 degrees C, no polyphosphate accumulated. This apparent non-dependence on glutamine by transformed cells when heat shocked was found to be due to the production of glutamine from serum proteins through induction of a protease(s).

9,10-Dimethyl-1,2-benzanthracene↗
PubMed1990

Effects of physiological and pathological levels of glucocorticoids on skeletal muscle glutamine metabolism in the rat.

The effects of physiological and pathological concentrations of glucocorticoids were investigated using the glucocorticoid antagonist RU486 and the synthetic glucocorticoid dexamethasone, respectively. The effects of these treatments on the concentrations of glutamine and other amino acids in skeletal muscle and plasma and on the rates of release of glutamine and alanine from incubated preparations of skeletal muscle of the rat were investigated. Dexamethasone treatment increased the concentration of glutamine and the rate of release of this amino acid from incubated soleus muscle preparations. This treatment decreased the concentration of glutamine in both gastrocnemius and EDL muscles, but was without effect on the rate of glutamine release from EDL muscles. In contrast, administration of the glucocorticoid antagonist RU486 decreased the rate of glutamine release from muscle. It is concluded that glucocorticoids have marked effects on the metabolism of glutamine by skeletal muscle per se and that these hormones may be important in the control of the rate of glutamine release from muscle in both physiological and pathological conditions.

Amino Acids↗
PubMed1989

Glutamine dependency of human skin fibroblasts: modulation by hexoses.

The combined effects of carbohydrates and glutamine were investigated in diploid strains of normal human skin fibroblasts cultured for 21 days under eight different culture conditions: hexose-free medium or medium containing D-glucose, D-galactose, or D-fructose, with or without added glutamine. Cell growth, hexose consumption, lactate production, intracellular glycogen content and extracellular amino acid levels were measured every third to fourth day. In the presence of glutamine, cells reached a higher saturation density in fructose medium than in glucose or galactose medium but per cell consumption of fructose and galactose was much less than that of glucose. Consumption of all three carbohydrates per unit cell growth exhibited three distinct phases: Days 1-3, 3-10, and 10-20, respectively. In the absence of glutamine the rate of cell growth was not altered in glucose or galactose medium, but slowed down considerably in fructose medium. Glutamine deprivation also led to changes in hexose consumption. In hexose-free media the cell growth rate at first was very slow, but rose after 2 or 3 weeks of culture. The levels of extracellular nonessential amino acids varied according to medium and growth phase. One of the most exciting findings was that human fibroblasts are able to maintain a slight excess of glutamine in all media not supplemented with glutamine and, more surprisingly, to synthesize it in a medium containing galactose and glutamine.

Amino Acids↗