Glucuronic acid conjugates of aspartic and glutamic acids in urine.
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Aspartic Acid↗
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Effects of acromelic acid A on the binding of [3H]glutamic acid and [3H]kainic acid to synaptic membranes and on the depolarization at the frog spinal cord.
Triton treatment of synaptic membranes from the frog spinal cord enhanced the specific binding of [3H]glutamic acid compared with non-treated fresh and frozen ones, but not that of [3H]kainic acid. Acromelic acid A specifically inhibited the binding of [3H]kainic acid, and was approximately 100 times more potent than kainic acid. Acromelic acid A and excitatory amino acids caused a depolarization in the ventral root of the frog spinal cord in a dose-dependent manner, and the effect of acromelic acid A was much superior to that of kainic acid or domoic acid. Acromelic acid A is one of the most potent kainic acid agonist at the frog spinal cord.
Animals↗
Active-site mutations of diphtheria toxin: effects of replacing glutamic acid-148 with aspartic acid, glutamine, or serine.
Glutamic acid-148, an active-site residue of diphtheria toxin identified by photoaffinity labeling with NAD, was replaced with aspartic acid, glutamine, or serine by directed mutagenesis of the F2 fragment of the toxin gene. Wild-type and mutant F2 proteins were synthesized in Escherichia coli, and the corresponding enzymic fragment A moieties (DTA) were derived, purified, and characterized. The Glu----Asp (E148D), Glu----Gln (E148Q), and Glu----Ser (E148S) mutations caused reductions in NAD:EF-2 ADP-ribosyltransferase activity of ca. 100-, 250-, and 300-fold, respectively, while causing only minimal changes in substrate affinity. The effects of the mutations on NAD-glycohydrolase activity were considerably different; only a 10-fold reduction in activity was observed for E148S, and the E148D and E148Q mutants actually exhibited a small but reproducible increase in NAD-glycohydrolytic activity. Photolabeling by nicotinamide-radiolabeled NAD was diminished ca. 8-fold in the E148D mutant and was undetectable in the other mutants. The results confirm that Glu-148 plays a crucial role in the ADP-ribosylation of EF-2 and imply an important function for the side-chain carboxyl group in catalysis. The carboxyl group is also important for photochemical labeling by NAD but not for NAD-glycohydrolase activity. The pH dependence of the catalytic parameters for the ADP-ribosyltransferase reaction revealed a group in DTA-wt that titrates with an apparent pKa of 6.2-6.3 and is in the protonated state in the rate-determining step.(ABSTRACT TRUNCATED AT 250 WORDS)
Adenosine Diphosphate Ribose↗
Effect of glutamic acid on broilers given submarginal crude protein with adequate essential amino acids using feeds high and low in potassium.
Broiler males were examined for their response to feeds containing CP 1 to 2% below levels advocated by NRC (1994) and when supplemented with L-glutamic acid. Crude protein and glutamic acid treatments were imposed in starting, growing, and finishing feeds over 7 wk with K at high and low levels likely to occur in practice (0.80 vs 0.65 to 0.55%). All feeds were formulated to be isocaloric (3.20 kcal ME/g) and satisfy NRC (1994) essential amino acid (EAA) minimum requirements. Improved live weight gain occurred during the first 6 wk with supplementation of glutamic acid to the low CP feed but not when intact protein per se was used to increase CP. A similar advantage in growth was obtained from glutamic acid in response to its addition at equivalence of 1 to 2% CP as well as when dietary adjustments maintained low CP. Response to altered K could not be interpreted because of concurrent differences in glutamic acid and AMEn intakes. High glutamic acid levels did not decrease abdominal fat unless CP increased concurrently, whereas carcass back bruising and drumstick deformations were relieved by supplemental glutamic acid independent of CP. Increased weight gain from glutamic acid was only evident with drumsticks and debris that included the back when carcasses were cone-deboned. Supplemental glutamic acid is believed to improve the rate of connective tissue formation during rapid growth.
Amino Acids, Essential↗
Effect of lithium and other alkali metals on brain chemistry and behavior. I. Glutamic acid and GABA in brain regions.
Glutamic acid and GABA concentrations were measured in brain areas of rats injected with the chloride salts of Li+, Na+, K", Rb+ or Cs+ for 5 days. Regional changes in brain glutamic acid and GABA were found in animals after lithium, rubidium or cesium, but not potassium, compared to sodium treatments. Increased glutamic acid and GABA levels, caused by lithium and rubidium, were found in brain structures (hypothalamus and amygdala) known to be involved in emotional behavior. Whether these changes are associated with the effective use of lithium and, perhaps, of rubidium in affective disorders remains obscure.
Affective Symptoms↗
cDNA and deduced amino acid sequence of mouse matrix gla protein: one of five glutamic acid residues potentially modified to gla is not conserved in the mouse sequence.
A cDNA library was constructed using the mouse osteoblastic cell line MC3T3-E1 treated with 1 alpha,25-dihydroxyvitamin D3, based on the finding that the treatment increased ninefold the expression of 0.7 kb matrix gla protein (MGP) mRNA. cDNA clones encoding mouse MGP were isolated from the library. The nucleotide sequence showed an open reading frame of 312 nucleotides encoding 104 amino acids. Murine MGP shared 84-89% amino acid sequence homology with bovine, rat, and human MGP. However, there are five glutamic acid residues potentially modified to gamma-carboxyglutamic acid (gla) in those species; in murine MGP, lysine replaced glutamic acid 37. Also, an extra tyrosine was added at the carboxyl terminus. The significance of the substitution is discussed in relation to the gamma-carboxylation sites in MGP protein.
Amino Acid Sequence↗
Glutamic acid decarboxylase and gamma-aminobutyric acid in Huntington's disease fibroblasts and other cultured cells, determined by a [3H]muscimol radioreceptor assay.
A sensitive and reproducible [3H]muscimol radioreceptor assay was developed for measuring low levels of both glutamic acid decarboxylase activity and gamma-aminobutyric acid. By using this technique, endogenous gamma-aminobutyric acid and glutamic acid decarboxylase activity were detected in two rat neuroblastomas, B35 and B50, a human medulloblastoma cell line, TE671, and cultured human skin fibroblasts. Glutamic acid decarboxylase activities and gamma-aminobutyric acid levels were compared for human skin fibroblasts obtained from patients with Huntington's disease and their controls in a well-controlled, blind study. However, no significant difference was found to either measure between Huntington and control cells. Glutamic acid decarboxylase activity was relatively low in all cell types examined except for the TE671 cells, which had more than four times the activity found in the other cells. This human medulloblastoma cell line appears to be a good model for studying gamma-aminobutyric acid metabolism and the control of glutamic acid decarboxylase expression.
Carboxy-Lyases↗
Reduction of cerebrospinal fluid glutamic acid in Huntington's chorea and in schizophrenic patients.
Glutamic acid levels were investigated in the cerebrospinal fluid and blood serum of patients with schizophrenia, Huntington's chorea, and sciatic nerve compression by lumbar disc protrusion. In the serum the glutamic acid levels were equal in all three groups; in the cerebrospinal fluid (CSF) of schizophrenic and Hungtington's patients, however, the glutamic acid was decreased to almost half that of the lumbar disc group which served as control. Most of the patients were treated with neuroleptic drugs. However, since in one case (the daughter of a Huntington's patient) the CSF glutamic acid was decreased although this woman had had no neuroleptic treatment, it seems more likely that the glutamic acid decrease is due to the disease rather than to the neuroleptic treatment.
Adult↗
Selective stimulation of neurotransmitter release from chick retina by kainic and glutamic acids.
The excitatory action of kainic and glutamic acids in chick whole retina was demonstrated as an immediate stimulation of the release of labeled gamma-aminobutyric acid (GABA) and glycine in a superfusion system. This stimulatory effect was 3-10 times greater than that produced by a depolarizing K+ concentration; in addition, it was independent of Ca2+ in the medium, but notably inhibited when Na+ was omitted from the medium. Under identical experimental conditions, neither kainic nor glutamic acid had any effect on the release of labeled dopamine or alpha-aminoisobutyric acid, thus indicating that their effect is not unspecific or due to cell damage. Similar although less marked stimulation of labeled GABA and glycine release by kainic acid was obtained in subcellular retinal fractions, particularly in fraction P1, which contained photoreceptor terminals and outer segments. This stimulation was also Ca2+ independent and greatly reduced when Na+ was omitted from the medium. It is suggested that the stimulation of GABA release by kainic and glutamic acids is probably due to a Na+-dependent, carrier-mediated mechanism that responds to the entry of Na+ produced by the interaction of glutamic and kainic acids with retinal membranes. In cortical or striatal slices from mouse brain, these acids had a negligible stimulatory effect on GABA and dopamine release.
Animals↗
Molecular pharmacology of homologues of ibotenic acid at cloned metabotropic glutamic acid receptors.
We have studied the effects of the enantiomers of 2-amino-3-(3-hydroxyisoxazol-5-yl)propionic acid (homoibotenic acid, HIBO) and analogues substituted with a methyl, bromo or butyl group in the four position of the ring at cloned metabotropic glutamate (mGlu) receptors expressed in Chinese hamster ovary (CHO) cells. In contrast to the parent compound ibotenic acid, which is a potent group I and II agonist, the (S)-forms of homoibotenic acid and its analogues are selective and potent group I antagonists whereas the (R)-forms are inactive both as agonists and antagonists at group I, II, and III mGlu receptors. Interestingly, (S)-homoibotenic acid and the analogues display equal potency at both mGlu1alpha and mGlu5a with Ki values in the range of 97 to 490 microM, (S)-homoibotenic acid and (S)-2-amino-3-(4-butyl-3-hydroxyisoxazol-5-yl)propionic acid [(S)-4-butylhomoibotenic acid] displaying the lowest and highest potency, respectively. The homoibotenic acid analogues thereby differ from mGlu receptor antagonists derived from phenylglycine such as (S)-4-carboxyphenylglycine which only antagonizes mGlu1alpha (Ki = 18 microM) showing no effect at mGlu5a (Ki > 300 microM).
Animals↗
Transport of amino acids (L-valine, L-lysine, L-glutamic acid) and sucrose into plasma membrane vesicles isolated from cotyledons of developing pea seeds.
Transport of the amino acids L-valine, L-lysine, and L-glutamic acid and of sucrose was studied in plasma membrane vesicles isolated from developing cotyledons of pea (Pisum sativum L. cv. Marzia). The vesicles were obtained by aqueous polymer two-phase partitioning of a microsomal fraction and the uptake was determined after the imposition of a H(+)-gradient (DeltapH, inside alkaline) and/or an electrical gradient (Deltapsi, inside negative) across the vesicle membrane. In the absence of gradients, a distinct, time-dependent uptake of L-valine was measured, which could be enhanced about 2-fold by the imposition of DeltapH. The imposition of Deltapsi stimulated the influx of valine by 20%, both in the absence and in the presence of DeltapH. Uptake of L-lysine was more strongly stimulated by Deltapsi than by DeltapH, and its DeltapH-dependent uptake was enhanced about 6-fold by the simultaneous imposition of Deltapsi. In the absence of gradients the uptake of L-glutamic acid was about 2-fold higher than that of L-valine, but it was not detectably affected by DeltapH or Deltapsi. Although the transport of sucrose was very low, a stimulating effect of DeltapH could be clearly demonstrated. The results lend further support to the contention that during seed development cotyledonary cells employ H(+)-symporters for the active uptake of sucrose and amino acids.
Amino Acids↗
The role of glutamic acid in the pathogenesis of stroke and the development of neuroprotective drugs.
The role of glutamic acid (glutamate) in the pathogenesis of stroke is now fairly well established. As a result, many drugs which act on glutamate receptors are currently under investigation for their ability to prevent the damage induced by glutamate under ischaemic conditions. The efficacy of these compounds in protecting central neurones from the effects of stroke may be indicative of the importance of the role that glutamate plays in this process.
Brain Damage, Chronic↗
Thermotropic liquid-crystalline peptide derivatives: oligo(glutamic acid)s forming hydrogen-bonded columns.
We report on new thermotropic liquid-crystalline oligo(amino acid) derivatives forming columnar structures. These are based on branched oligo(glutamic acid)s and 2-(3,4-dialkyloxyphenyl)ethyl moieties. An oligo(glutamic acid) derivative, alpha,gamma-bis(L-glutamoyl) L-glutamic acid tetra[2-(3,4-dioctadecyloxyphenyl)ethyl]ester, shows a hexagonal columnar phase, whilst a glutamic acid derivative, alpha,gamma-bis[2-(3,4-dioctadecyloxyphenyl)ethyl] L-glutamate, does not show a mesophase. Hydrogen bonds formed by the oligo(glutamic acid) moieties should contribute to the induction of the columnar liquid-crystalline properties. In addition, we have examined the effects of the molecular chirality of the oligo(glutamic acid) parts and the functionalisation at the focal position of the taper shaped molecules on the liquid-crystalline properties of the compounds.
Alkanes↗
Comparative distribution of messenger RNAs encoding glutamic acid decarboxylases (Mr 65,000 and Mr 67,000) in the basal ganglia of the rat.
Glutamic acid decarboxylase, the enzyme required for GABA synthesis, exists as distinct isoforms, which have recently been found to be encoded by different genes. The relative expression of messenger RNAs encoding two isoforms of glutamic acid decarboxylase (Mr 67,000 and Mr 65,000) was measured at the single-cell level in neurons of the rat basal ganglia with in situ hybridization histochemistry. Both messenger RNAs were expressed in neurons of the striatum, pallidum, and substantia nigra pars reticulata, but marked differences in the relative level of labelling were observed with the two probes. In striatum, efferent neurons were more densely labelled for the messenger RNA encoding glutamic acid decarboxylase (Mr 65,000) than for the messenger RNA encoding glutamic acid decarboxylase (Mr 67,000), whereas the reverse was observed for GABA-ergic interneurons. Neurons of the entopeduncular nucleus were much more densely labelled for messenger RNA encoding glutamic acid decarboxylase (Mr 65,000) than for messenger RNA encoding glutamic acid decarboxylase (Mr 67,000). In addition, labelling for messenger RNA encoding glutamic acid decarboxylase (Mr 65,000) was higher in the entopeduncular nucleus (internal pallidum) than in the globus pallidus (external pallidum), a structure which expressed similar levels of both mRNAs. In contrast to neurons of the internal pallidum, efferent neurons of the substantia nigra pars reticulata expressed slightly more messenger RNA encoding glutamic acid decarboxylase (Mr 67,000) than that encoding the other isoform of the enzyme. The results suggest a differential expression of the messenger RNAs encoding the two isoforms of glutamic acid decarboxylase in subpopulations of basal ganglia neurons in rats.
Animals↗
Glutamic acid, twenty years later.
This review examines progress in understanding the physiologic functions of glutamic acid in the body since the first symposium on glutamic acid physiology and biochemistry was held at the Mario Negri Institute in Milan in 1978. The topics reviewed, although not exhaustive, include the metabolism of glutamic acid, umami taste, the role of glutamic acid as a neurotransmitter, glutamate safety and the development of new drugs resulting from the knowledge of the neurodegeneration induced by high doses of glutamic acid.
Animals↗
High affinity uptake and Ca2+-dependent release of glutamic acid in the developing cerebellum.
This study was undertaken in order to evaluate the postulated role of glutamic acid as the neurotransmitter for the parallel fibers of the cerebellar cortex. We studied the Ca2+-dependent release and the high affinity uptake of glutamic acid in the developing cerebellum. The Ca2+-dependent release of glutamic acid from cerebellar molecular layer during development closely follows the time course of parallel fibers synaptogenesis. Little glutamic acid release was observed at 15 days, then it increased to the adult values at the 21st postnatal day. In the rat the bulk of synapses of the parallel fibers appear between the 15th and the 21st postnatal days, the time at which the nerve terminals of the climbing fibers, the other excitatory input to the Purkinje cells, are already developed. An enhanced Na+-dependent, high affinity uptake of glutamic acid was observed in the developing cerebellum relative to the adult rat. That this higher accumulation of glutamic acid is not related to a releasable pool is suggested by the fact that an enhanced glutamic acid, Ca2+-dependent release relative to the adult was not observed. These results support the view that glutamic acid is the transmitter for the cerebellar parallel fibers.
Animals↗
Isolation by anion-exchange of immunologically and enzymatically active human islet glutamic acid decarboxylase 65 overexpressed in Sf9 insect cells.
The enzyme L-glutamic acid decarboxylase is a major autoantigen of the beta cell. Autoantibodies against this enzyme are observed before the onset of insulin-dependent diabetes mellitus (IDDM) in man and may be of predictive value. There is evidence that this enzyme is involved in the development of autoimmune diabetes in animals. In order to facilitate the investigation of the role of L-glutamine acid decarboxylase in IDDM, we expressed the 65 kDa isoform of human islet L-glutamic acid decarboxylase in insect cells using a baculovirus-based vector. The material was expressed at high levels (up to 50 mg/l of cells). Partially purified metabolically labelled L-glutamic acid decarboxylase bound to immunoglobulins in the sera from 20 of 49 subjects with newly-diagnosed IDDM. The enzyme was isolated in high yields (up to 26 mg/l cell culture) with fully maintained enzymatic activity by either ion-exchange chromatography or immunoaffinity chromatography. Purified L-glutamic acid decarboxylase inhibited the binding of radioactive L-glutamic acid decarboxylase, prepared by in vitro translation of mRNA, to immunoglobulins in the sera of subjects with IDDM. Recombinant human islet L-glutamic acid decarboxylase, isolated from Sf9 cells, is a suitable material for the large scale investigation of the utility of this enzyme in the prediction and prevention of autoimmune diabetes.
Adolescent↗
Synthesis of 9-membered dilactams derived from 1,3-diaminopropionic and glutamic acids.
Previously unknown 9-membered bridged dipeptides derived from l or d isomers of 1,3-diaminopropionic acids and l-glutamic acid were synthesized using aminoacyl incorporation reaction. Key intermediates containing internal pyroglutamyl moiety were prepared via side chain to backbone cyclization of related protected dipeptide derivatives of glutamic acid.
Combinatorial Chemistry Techniques↗