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At least 415 records · Page 23Linked to original sources
PubMed1986

Cardiac metabolism and performance during L-glutamic acid infusion in postoperative cardiac failure.

Intravenous infusion of L-glutamic acid results in the augmentation of the cardiac output and an improvement of the circulation in patients with postoperative cardiac failure. This effect is not accompanied by increased myocardial oxygen demand. Arterial plasma glutamate level rises 10-fold and arterial-coronary sinus plasma glutamate difference increases fivefold during intravenous L-glutamic acid infusion. This leads to cessation of ammonia release from the myocardium, probably due to augmentation of glutamine synthesis and to an increase in alanine formation coupled with a change from lactate release to lactate uptake by the myocardium. The data obtained suggest that the beneficial effect of L-glutamic acid on depressed cardiac function in postoperative patients is related to changes in myocardial metabolism. Glutamic acid may be useful in treatment of circulatory and metabolic disturbances in cardiac failure.

Alanine↗
PubMed1981

Effects of level of dietary glutamic acid and thiamin on food intake, weight gain, plasma amino acids, and thiamin status of growing kittens.

Specific pathogen-free kittens were individually fed purified amino acid diets containing 4.4 mg of thiamin and 3.0, 4.5, 6.0, 9.0 or 12.0% glutamic acid (Glu) in a balanced 5 x 5 latin square design. Kittens fed either the 9.0% followed by the 12.0% glutamate diets or vice versa developed severe clinical signs of thiamin deficiency and two kittens died. Other affected kittens given 5 mg additional thiamin per day for 3 days promptly recovered. In a subsequent experiment, the effect of a diet containing 12.0% glutamic acid with either 4.4 or 25.0 mg thiamin per kilogram diet was compared with a diet containing 3.0% glutamic acid with either 0.0 or 4.4 mg thiamin per kilogram. Kittens fed the diet containing the high level of glutamic acid with 4.4 mg thiamin exhibited depressed food intake and body weight gain and an elevated level of plasma glutamic acid compared to diets containing 3.0% glutamic acid. Red blood cells from this group of kittens also showed a transitory incomplete saturation of transketolase with thiamin pyrophosphate. Kittens fed the high glutamate diets vomited occasionally during the 1st month of the dietary regimen. Although increased thiamin (25 mg/kg diet) decreased the severity of the adverse effects of the high glutamate diet, maximal growth was not obtained in kittens fed the high glutamate, high thiamin diet.

Amino Acids↗
PubMed1997

Biosensor for neurotransmitter L-glutamic acid designed for efficient use of L-glutamate oxidase and effective rejection of interference.

An amperometric biosensor for L-glutamic acid (Glu) was constructed by the adsorption and dip coating of L-glutamate oxidase (GluOx, 200 U ml-1 phosphate buffer, pH 7.4) onto 60-micron radius Teflon-coated Pt wire (1 mm exposed length). The enzyme was then trapped on the surface by electropolymerisation of o-phenylenediamine that also served to block electroactive interference. This procedure afforded electrodes with similar substrate sensitivity compared with the classical approach of immobilising enzyme from a solution of monomer, and represents an approximately 10,000-fold increase in the yield of biosensors from a batch of enzyme. A number of strategies were examined to enhance the sensitivity and selectivity of the Pt/PPD/GluOx sensors operating at 0.7 V versus SCE. Pre-coating the Pt with lipid and incorporation of the protein bovine serum albumin into the polymer matrix were found to improve the performance of the electrode. The sensors had a fast response time, high sensitivity to Glu, with an LOD of about 0.3 mumol l-1, and possessed selectivity characteristics suggesting that monitoring Glu in biological tissues in vivo may be feasible.

Amino Acid Oxidoreductases↗
PubMed2004

Molecular profile of the T cell receptors of regulatory and effector CD4+ T cells recognizing overlapping determinants on glutamic acid decarboxylase (524-543).

Glutamic acid decarboxylase (GAD65) is one of the autoantigens that initiates pathogenic T cell responses against insulin-secreting pancreatic beta cells in Type 1 diabetes (T1D). Previously it was shown that spontaneously arising pathogenic T cell responses in the NOD mouse model are confined to GAD530-543 (p530). However, regulatory T cell subpopulations, which can prevent diabetes, can also be generated, for example, by immunization with GAD524-538 (p524) or GAD524-543. Interestingly, two functionally distinct subpopulations of T cells which recognize overlapping determinants of GAD524-543, p524 and p530, utilize distinct TCR Vbeta families, Vbeta4 for pathogenic, and Vbeta12 for regulatory T cells. We characterized T cell receptors (TCRs) from each subpopulation of T cells and visualized p524-specific TCR/p524/I-A(g7) and p530-specific TCR/p530/I-A(g7) complexes via molecular modeling to help us understand, at a molecular level, the in vivo expansion of p524- or p530-specific T cells in the NOD model of T1D. The absolute restriction in Vbeta usage but not Valpha usage and conserved CDR3beta lengths for both T cell subpopulations demonstrates that the beta chains are main contributors in shaping both p524/I-A(g7) and p530/I-A(g7) restricted TCRs. However, only Vbeta4+ T cells but not Vbeta12+ T cells contain a common motif (DWG) in CDR3beta and may involve all of CDR1beta, CDR2beta, and CDR3beta in the recognition of the C-terminus of p530. These observations imply that the spontaneously arising p530-restricted TCRs may be selected under stringent structural frameworks to bind p530/I-A(g7) with high affinity. Thus, the pathogenic p530-specific T cells may arise from a small pool of autoreactive T cells upon breaking tolerance.

Amino Acid Motifs↗
PubMed1990

Drosophila GABAergic systems: sequence and expression of glutamic acid decarboxylase.

A mammalian glutamic acid decarboxylase (GAD) cDNA probe has been utilized to isolate Drosophila cDNA clones that represent a genomic locus in chromosome region 64A. Deletion analysis indicates that this chromosomal locus encodes an enzymatically active GAD protein. The in vitro translation of cRNA representing a Drosophila cDNA clone yields a 57-kDa protein that can be immunoprecipitated by an anti-GAD antiserum. A GAD-immunoreactive protein of the same size can also be detected in Drosophila head extracts. The nucleotide sequence derived from two overlapping Drosophila cDNA clones predicts a 57,759-dalton protein composed of 510 residues that is 53% identical to mammalian GAD. Sequence comparisons of mammalian and Drosophila GAD identify two highly conserved regions (greater than or equal to 70% identity), one of which encompasses a putative co-factor-binding domain. Transcriptional analyses show that expression of the Drosophila Gad gene commences early in embryonic development (4-8 h) and continues in all later developmental stages. A 3.1-kb class of mRNA is detected throughout embryogenesis, in all three larval stages, in pupae, and in adults. This transcript class has a widespread distribution in the adult CNS. A smaller 2.6-kb transcript is expressed in a developmentally regulated manner; it is detected only in embryos and pupae.

Amino Acid Sequence↗