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PubMed1989

Regulation of Chlorella nitrate reductase: control of enzyme activity and immunoreactive protein levels by ammonia.

Nitrate reductase catalyzes the initial step in the conversion of nitrate to organic nitrogen and is thought to be repressed by ammonia and induced by nitrate. Induction by nitrate and repression by ammonia were studied by following changes in NADH:nitrate reductase and the associated partial activities NADH:cytochrome c reductase and methylviologenr:nitrate reductase. Immunoreactive protein was assessed by enzyme-linked immunosorbent assay and immunoblotting. Molybdenum cofactor levels were investigated using the nit-1 complementation assay as well as fluorescence of the oxidized cofactor. The results indicate that the NADH:cytochrome c reductase activity is "induced" faster than the nitrate-reducing activity and suggest that incorporation of the molybdo-pterin cofactor may be rate limiting in the expression of activity. Molybdenum cofactor levels are significantly elevated in nitrate-treated cells. Under "repressing" conditions all activities decreased at approximately the same rate. A more rapid conversion of the enzyme to a reversibly inactive form also occurred under these conditions. Changes in immunoreactive protein levels correlated most closely with NADH:cytochrome c reductase activity but appeared to increase faster during induction and decrease slightly slower during repression than the enzyme activities. Removal of exogenous ammonia results in the appearance of nitrate reducing activity, as well as immunoreactive protein (derepression). Studies using protein and RNA synthesis inhibitors indicated that de novo synthesis is required for nitrate reductase induction and were in agreement with the results of the immunoreactive studies.

Ammonia↗
PubMed1983

Ammonia accumulation in acetate-growing yeast.

During growth on acetate, the pH of yeast cultures rises from 5.8 to around 7-8 in the stationary phase. This was found to result from acetic acid uptake and accompanying H+ loss. In addition, acetate-growing yeast were found to accumulate ammonia. The influence of pH on ammonia transport and accumulation was studied with the analogue [14C]methylamine with the following results. (a) Methylamine uptake kinetics from 0.1-50 mM were consistent with a single-component uptake system (NH+4 permease) at pH values more acidic than 6.5, and with a two-component system (NH+4 permease and NH3 diffusion) above pH 7.5. (b) Equilibrium accumulation of methylamine was found to increase with increasing pH. (c) Methylamine efflux from methylamine-loaded cells increased as the external pH decreased. It was concluded from measurements of the internal pH under various culture conditions that the accumulation of ammonia in acetate-growing alkaline cultures resulted from the sum of two processes: (1) an energy-driven NH+4 transport; and (2) NH3 diffusion dependent on the delta pH.

Acetates↗
PubMed1987

The potentiation of ammonia toxicity by sodium benzoate is prevented by L-carnitine.

Sodium benzoate has been recommended and even been used for the treatment of hyperammonemia in humans. More recently, a note of caution was raised since it has been shown that in experimental animals, sodium benzoate potentiates ammonia toxicity and inhibits urea synthesis in vitro. This has been further confirmed in the work presented here and the mechanism by which benzoate increases mortality and the levels of blood ammonia in mice given ammonium acetate have also been studied. In hyperammonemia, urea production and N-acetylglutamate levels were decreased by sodium benzoate. Pretreatment of mice with L-carnitine suppressed mortality following ammonium acetate plus sodium benzoate administration. Under these conditions L-carnitine lowered blood ammonia and increased urea production and N-acetylglutamate levels.

Ammonia↗
PubMed1980

Factors that affect the uptake of ammonia by the brain: the blood-brain pH gradient.

The brain uptake index (BUI) for [13N]ammonia was measured in 7 areas of the rat brain at 8 different pH values ranging from 6.58 to 7.73. When the regional BUI was plotted as a function of the pH of the test bolus, a significant linear correlation was found for each region (P less than 0.001). The highest slope was observed in the thalamus-basal ganglia complex (0.392 +/- 0.018) (S.D.), and the lowest in the ventral pons (0.143 +/- 0.011). These studies indicate that the brain-blood pH gradient plays a major role in determining the forward flux of ammonia from the blood into the brain in the physiological pH range. Regional differences in the slope may be due to metabolic factors. This pH effect may be important in clinical conditions characterized by hyperammonemia such as hepatic encephalopathy, and in the interpretation of [13N]ammonia emission tomographic images of the brain.

Ammonia↗
PubMed1996

Modulation of ligand binding to components of the GABAA receptor complex by ammonia: implications for the pathogenesis of hyperammonemic syndromes.

The effects of 5-2500 microM concentrations of neutral ammonium salts on the binding of ligands to components of the GABAA receptor complex were investigated. [3H]Flunitrazepam binding to the benzodiazepine receptor was enhanced by ammonium (10-500 microM), but not sodium tartrate with EC50 = 98 microM and Emax = 31%. Further increasing ammonium tartrate concentrations (500-2500 microM) decreased [3H]flunitrazepam binding to control levels. The ammonium tartrate-induced increase in [3H]flunitrazepam binding was manifested as a 50% decrease in Kd. Furthermore, GABA increased the potency of ammonium tartrate in enhancing [3H]flunitrazepam binding by 63%. [3H]Ro 15-1788 and [3H]Ro 15-4513 binding to the benzodiazepine receptor was not significantly enhanced by ammonium tartrate (Emax approximately 13%). Ammonium tartrate also increased, then decreased the binding of 500 nM [3H]muscimol to the GABAA receptor (EC50 = 52 microM, Emax = 30%) in a concentration-dependent manner, but had no effect on [3H]SR 95-531 binding (Emax < 16%). The ammonium tartrate-induced alterations in [3H]muscimol binding were demonstrated in saturation assays as the loss of the high affinity binding site and a 27% increase in the Bmax of the low affinity binding site. These results indicate that ammonia biphasically enhances, then returns ligand binding to both the GABA and benzodiazepine receptor components of the GABAA receptor complex to control levels in a barbiturate-like fashion. This suggests that ammonia may enhance GABAergic neurotransmission at concentrations commonly encountered in hepatic failure, an event preceding the suppression of inhibitory neuronal function observed at higher (> 1 mM) ammonia concentrations. This increase in GABAergic neurotransmission is consistent with the clinical picture of lethargy, ataxia and cognitive deficits associated with liver failure and congenital hyperammonemia.

Ammonia↗
PubMed1984

Hepatocyte heterogeneity in ammonia metabolism: impairment of glutamine synthesis in CCl4 induced liver cell necrosis with no effect on urea synthesis.

After induction of a perivenous liver cell necrosis by CCl4 pretreatment of the rat, ammonia uptake by perfused liver is decreased. This was due to an inhibition of glutamine synthesis from added ammonia, whereas urea synthesis was not affected by CCl4 pretreatment. The data confirm recent findings on hepatocyte heterogeneity in ammonia metabolism and are explained by an impairment of perivenous glutamine synthetase, but not of periportal urea synthesis, by the perivenous liver cell necrosis induced by CCl4. Regarding the pathogenesis of hyperammonemia in acute severe liver disease like CCl4 poisoning, the data point to a role of an impaired glutamine synthesis, but not to an impairment of urea synthesis.

Ammonia↗
PubMed1977

Octopamine and ammonia plasma levels in hepatic encephalopathy.

It has been recently proposed that hepatic encephalopathy could be due to the accumulation of octopamine acting as a false neurotransmitter, and the increase of ammonia might reflect this accumulation. The simultaneous determination of octopamine and ammonia was performed in 88 cases with or without encephalopathy. The correlation between the two substances appeared to be good (P less than 0.01; r = 0.5), except in shunted patients. All the cases with low octopamine and high ammonia were patients who had been submitted to surgical portal-systemic anastomosis. This finding does not seem to be coincidental; in this type of patients, the mechanism of hepatic encephalopathy could involve other beta-hydroxyphenylethanolamines in addition to octopamine. The presence of the inhibition of the reaction of transmethylation constantly observed during octopamine plasma assay is in favour of this hypothesis.

Ammonia↗
PubMed1982

Rapid determination of ammonia in whole blood and plasma using flow injection analysis.

A flow injection method for the determination of ammonia in whole blood and plasma is described. The method utilizes diffusion of ammonia into a stream of a pH-sensitive indicator, which is monitored by a photometer. A volume of 90 microliter is needed and the result is obtained within 1 min. Ammonia concentrations increase during storage due to deamination. It is proposed to use plasma samples, which could be stored frozen at - 20 degrees C without significant change.

Ammonia↗
PubMed1984

A simple and rapid microdiffusion method for blood ammonia using a reflectance meter and a reagent plate, and its clinical evaluation for liver diseases.

A simple and rapid procedure using 20 microliters of whole blood is described for estimating blood ammonia by means of a reflectance meter using a reagent plate, which operates by the principle of microdiffusion. The most suitable condition for microdiffusion was at 37 degrees C for 15 min, in which the standard curve was linear, and reproducibility and recovery were sastisfactory. Blood ammonia levels by this method correlate significantly with the values by an ion exchange method in 72 patients with liver disease (r = + 0.970, y = 1.13x - 11). The method has a distinct advantage in sensitivity, simplicity, and rapidity for blood ammonia determination.

Ammonia↗
PubMed1984

Plasma ammonia concentrations in newborns and children.

Many, mostly congenital, hyperammonemic syndromes may occur in the first days of life. For the diagnosis of these disorders plasma ammonia levels physiologically present in neonates and early childhood should be known, preferably by the use of an enzymatic method. Full-term newborns had higher capillary ammonia concentrations on the first day of life (30-144 mumol/l) than on the fifth day (31-104 mumol/l). In the same individuals the arterial (38-89 mumol/l) are lower than the capillary concentrations (69-112 mumol/l). The venous concentrations in school children were not higher than in adults. The scatter of capillary values, however, is great. For diagnostic purposes of disorders of ammonia detoxication sampling of arterial or venous blood is preferable.

Adult↗
PubMed1986

Injected mRNA does not increase protein synthesis in unfertilized, fertilized, or ammonia-activated sea urchin eggs.

We have investigated whether the rate of protein synthesis in unfertilized and fertilization-activated sea urchin eggs is limited by the availability of mRNA by injecting eggs, zygotes, and ammonia-activated eggs with globin mRNA. Message-injected and buffer-injected cells were labeled with radioactive amino acids and the proteins separated on a polyacrylamide gel. The relative amounts of newly synthesized globin and endogenous proteins were obtained by scanning the gel fluorograph. Globin mRNA is translated poorly in Strongylocentrotus droebachiensis eggs and does not significantly increase or decrease endogenous protein synthesis. In zygotes and ammonia-activated eggs, however, globin mRNA is translated well and appears to compete with endogenous mRNAs for the limiting component of the translational machinery as it is released. Our results are consistent with the hypothesis that either ribosomes or recruitment factors are gradually activated after fertilization or ammonia treatment, that such components are the rate-limiting factor, and that they impart the typical sigmoidal increase in protein synthesis rate observed in fertilized eggs before the first cleavage.

Ammonia↗
PubMed1995

Role of luminal ammonia in the development of gastropathy and hypergastrinemia in the rat.

BACKGROUND/AIMS: Chronic infection with Helicobacter pylori causes persistent elevations in gastric juice ammonia levels. Thus, we studied the effects of experimentally induced increases in gastric juice ammonia levels on gastric structure and function and gastrin homeostasis. METHODS: Rats were fed either normal chow or the diet supplemented (20 g/dL) with ammonium or sodium acetate. RESULTS: Long-term dietary ammonium loading for 2 weeks or longer resulted in a 1.5-2-fold increase in the weight and mucosal thickness of the stomach and proximal duodenum with evidence of mild gastritis and enterochromaffinlike cell hyperplasia. The ammonium-containing diet also induced a significant 2-3-fold increase in both circulating gastrin levels of fed rats and an increase in the postprandial gastrin responses over control values. Antral gastrin levels were also markedly elevated by long-term ingestion of the test diet, which was increased 3-4-fold over control values in fasted animals and less so after meal stimulation. Consistent with these findings, gastrin-specific messenger RNA was increased 2.5-3-fold in the antrum of ammonium fed rats, whereas actin-specific messenger RNA was not affected or decreased. Animals fed a diet supplemented with 20 g/dL sodium acetate sustained modest increases in mucosal thickness and serum and antral gastrin concentration, suggesting that nonspecific gastric injury and inflammation is also a factor that influences G-cell function. CONCLUSIONS: Long-term exposure of the antral mucosa to elevated levels of ammonia in the gastric juice in the presence of gastritis, conditions similar to that occurring in subjects infected with H. pylori, seem to be causative factors in the development of G-cell hyperfunction.

Acetates↗
PubMed1985

Porta-caval shunting changes neuronal sensitivity to ammonia.

The relations between an effect of ammonia on postsynaptic inhibition, the amount of ammonium acetate i.v. to obtain this effect, and the tissue concentrations of NH4+ and glutamine were investigated in the cerebral cortex of cats without and with portacaval shunts. Normal cats required 2.43 mmol/kg ammonium acetate to affect postsynaptic inhibition. Cerebral NH4+ and glutamine increased from 0.21 mumol/g to 0.77 mumol/g and from 2.92 mumol/g to 5.54 mumol/g, respectively. In portacaval shunted cats, postsynaptic inhibition was normal in spite of increases of NH4+ and glutamine to 1.37 mumol/g and 14.28 mumol/g, respectively. Only 0.7 mmol/kg of ammonium acetate were sufficient to affect postsynaptic inhibition. This was associated with a statistically insignificant increase of NH4+ to 1.61 mumol/g and no change of glutamine. A chronic portasystemic shunt markedly increases the tolerance of postsynaptic inhibition to NH4+. However, postsynaptic inhibition becomes very sensitive to an acute systemic ammonia load and the associated increase of tissue NH4+ in the cerebral cortex. These observations help to understand the pathogenesis of the encephalopathy precipitated in patients with portasystemic shunts by an acute systemic ammonia load such as resulting from a gastrointestinal hemorrhage.

Acetates↗
PubMed1988

Increase in plasma ammonia and amino acids when rats are fed a 44% casein diet.

Rats were trained to eat a 6% casein basal diet during a 3-hour period per day. They were then fed either the same 6% casein diet or a 44% casein diet for 3 hours. No food intake depression was observed in the rats eating 44% casein diet during the 3-hour period. Plasma ammonia and amino acids and brain amino acids were measured at 0, 4, 12 and 24 hours after presentation of the 6% or 44% casein diets. Plasma ammonia rose to 134 (p less than 0.01) and 110 micromolar (p less than 0.05) in the 44% casein fed rats at 4 and 12 hours, respectively, as compared to 67 and 53 micromolar, respectively, for the 6% casein fed rats. All plasma amino acid concentrations except methionine and glutamate were elevated (p less than 0.05) at 4 hours. In the brain, threonine, glutamine and tyrosine concentrations were elevated (p less than 0.05) at 4 hours after diet presentation. At 24 hours, valine, isoleucine, leucine, phenylalanine, and methionine concentrations were also elevated (p less than 0.05). Because intake of the 44% casein diet decreases the second day of its presentation, as noted in an earlier experiment, the increases in plasma ammonia and its possible entry into the brain as reflected by increased brain glutamine together with changes in amino acid concentrations should be considered collectively among possible metabolic signals affecting intake of high protein diets.

Amino Acids↗
PubMed1989

Effects of ammonia and histamine on lung irritant receptors in the rabbit.

The effects of ammonia and histamine on the responses of rapidly adapting pulmonary stretch receptor (RAR) activity before and after administration of isoprenaline or atropine were studied in spontaneously breathing rabbits. Inhalation of vapor from 15% ammonia solution increased the activity of RARs and this increased activity was not significantly altered by isoprenaline (50 micrograms/kg) or atropine (0.3 mg/kg). The RARs increased their activity following intravenous injections of histamine (20, 40 and 60 micrograms/kg). The excitatory responses to histamine at different doses were blocked by prior treatment with isoprenaline (50 micrograms/kg). In 8 of the tested 11 different RAR preparations on 11 rabbits, atropine (0.3 mg/kg) greatly diminished the increases of RAR activity produced by histamine at different doses. These results suggest that the ammonia-induced RAR stimulation results in a direct action of the endings whereas the activation of RARs by histamine is probably due to the combined influence of both local airway constriction and postganglionic parasympathetic pathway-mediated bronchoconstriction.

Ammonia↗
PubMed1988

Some pitfalls and considerations of plasma ammonia estimation.

Several approaches to the estimation of plasma ammonia have been tested and compared: indophenol, Nessler, iodometric techniques were studied as well as enzymatic spectrophotometric and radiometric methods. Their lower safe limits of estimation were determined and it was found that most of them were not viable for plasma estimations because of its very low ammonia levels. The need for a concentration/purification step and the lack of repetability in this phase at very low concentrations, made very unreliable the utilization of all methods studied except for the enzymatic radiometric method tested that was barely usable for plasma ammonia estimations.

Ammonia↗
PubMed1993

Inactivation of histidine ammonia-lyase from Streptomyces griseus by dicarbonyl reagents.

Histidine ammonia-lyase from Streptomyces griseus was inactivated by methylglyoxal and phenylglyoxal, dicarbonyl reagents known to react specifically with arginyl residues in proteins. The inactivation showed pseudo-first-order kinetics and could be prevented by protection with histidinol phosphate, a competitive inhibitor of histidine ammonia-lyase. Analysis of the amino acid composition of histidine ammonia-lyase after treatment with phenylglyoxal, together with the kinetics of inactivation, suggested that inactivation was a consequence of specific reaction with one or more essential arginyl residues at or near the active site of the enzyme.

Amino Acid Sequence↗
PubMed1986

The role of amino acid catabolism in the formation of the tricarboxylic acid cycle intermediates and ammonia in anoxic rat heart.

Amino acid catabolism, the tricarboxylic acid cycle intermediates and ammonia formation were studied in isolated perfused rat heart under anoxia. The total net anaplerosis due to amino acid degradation in anoxia was equal to that in oxygenation (6.29 and 6.09 mumol/g dry weight per h, respectively) as a result of the increased transamination of glutamic and aspartic acids. During anoxic perfusion, the rate of catabolism of glutamic and aspartic acids was 1.5-times higher than in normoxia, while depletion of branched-chain amino acids, lysine, proline, arginine and methionine, was inhibited. Alanine was the product of excessive degradation of glutamic and aspartic acids. Under anaerobic conditions, in spite of inhibition of amino acid deamination, ammonia formation was increased 2.7-fold as compared to oxygenation. The principal amount of ammonia (96%) was produced at degradation of adenine nucleotides. A 2.5-fold increase in the pool of the tricarboxylic acid cycle intermediates under anoxia was associated mainly with accumulation of succinate. The data suggest that the coupling of alanine- and aspartate amino transferases is a mechanism controlling the tricarboxylic acid cycle pool size in anoxic heart.

Adenine Nucleotides↗