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At least 847 records · Page 47Linked to original sources
PubMed1985

Effects of excitatory amino acids on calcium transport by brain membranes.

The effect of excitatory amino acids on the uptake of 45Ca was studied in crude mitochondrial (P2) fractions prepared from mouse brain. L-Glutamate stimulated calcium uptake, but this action was not shared by other amino acids including D-glutamate, L-aspartate, N-methyl-aspartate or kainate. The glutamate-stimulated calcium uptake was, however, blocked by inhibitors of glutamate dehydrogenase, such as D-glutamate, glutarate and triiodothyronine. Subcellular fractionation demonstrated that the uptake was enriched in the mitochondrial fraction. Furthermore, most of the uptake found in the synaptosomal fraction was inhibited by triiodothyronine. These results indicate that the glutamate-stimulated uptake of calcium by brain membranes is due mainly to mitochondrial uptake of calcium that is driven by the metabolism of glutamate by glutamate dehydrogenase. Previous suggestions of coupling of glutamate receptors to calcium channels based on uptake of 45Ca by brain membranes must now be reevaluated.

Amino Acids↗
PubMed1975

Alpha-ketoadipic aciduria: degradation studies with fibroblasts,.

Observation of one patient with alpha-ketoadipic aciduria initiated degradation studies with radiolabelled lysine metabolites in fibroblasts in order to localise the metabolic defect. Liberation of 14-CO-2 from alpha-D,L-(1-14-C) aminoadipate and alpha-(1-14-C) ketoadipate was considerably less in the patient's fibroblasts than in the patient's fibroblasts than in normal controls, whereas 14-CO-2 production from (1,5-14-C) glutarate was in the normal range. These results indicate a defect in the oxidative decarboxylation of alpha-ketoadipate as the probable cause of alpha-ketoadipic aciduria; Cultured amniotic fluid cells from pregnancies of the 15th and 16th week of gestation degrade alpha-(1-14-C) ketoadipate with a similar activity to fibroblast cultures from normal humans after birth.

Adipates↗
PubMed1976

Identification of ethylmalonic acid in urine of two patients with the vomitting sickness of Jamaica.

Large amounts of ethylmalonic acid have been identified in urines from two patients with the vomitting sickness of Jamaica. The amounts were 178 and 882 mug per mg creatinine which are 70 and 350 times, respectively, over control values. Other short and medium chain dicarboxylic acids including glutaric and adipic acids and those with eight and ten carbon chain, saturated and cis-unsaturated, were also detected in large quantities as in the case of hypoglycin treated rats; urine. However, the large increase of urinary ethylmalonic acid in these two human cases is in a sharp contrast to the findings in hypoglycin treated rats in which urinary ethylmalonic acid increased only 3 times over control. It appears that ethylmalonic acid is produced in the cases with the vomiting sickness of Jamaica by carboxylation of n-butyryl-CoA which is not oxidized further due to the inhibition by hypoglycin A. In case of hypoglycin-treated rats, n-butyryl-CoA is mainly conjugated with glycine or deacylated to free butyric acid.

Animals↗
PubMed1977

Identification of urinary metabolites of sodium dipropylacetate in man; potential sources of interference in organic acid screening procedures.

Organic acid screening of urine samples from two children with neurological disease demonstrated the presence of two unknown metabolites. The children were receiving an antiepileptic drug, sodium dipropylacetate. The major abnormal compound has been shown by gas chromatography-mass spectrometry to be 3-oxodipropylacetic acid, a previously unidentified metabolite of dipropylacetate in man, while the minor metabolite was indentified as 2-(n-propyl)-glutaric acid.

Acids↗
PubMed1977

Demonstration of N-dicarboxyl-mono-glycines in dicarboxylic acidurias by mass fragmentography.

Urine samples from 18 individuals with various types of dicarboxylic acidurias have been investigated by mass fragmentography for N-dicarboxyl-mono-glycines (dicarboxylglycines). One patient with methylmalonic acidemia excreted 14-20 microgram methylmalonylglycine/mg creatinine, three patients with glutaric aciduria excreted 20-60 microgram glutarylglycine/creatinine, and one patient with C6-C10-dicarboxylic aciduria excreted 120-365 microgram succinylglycine/mg creatinine. Excretion of C6-C10-dicarboxylic acids in patients with ketosis and glycogenosis and in neonates were not accompanied by excretion of C8-C10-dicarboxylglycines in measurable amounts (greater than 1 microgram/mg creatinine). Nor did patients with succinic aciduria excrete succinylglycine in amounts larger than 1 microgram/mg creatinine. On the basis of these data it is argued that production of short- and medium-chain dicarboxylglycines is not a metabolic pathway of biological significance for the elimination of short- and medium-chain dicarboxylic acids from individuals with dicarboxylic acidurias.

Adolescent↗
PubMed1992

A specific method for determination of peroxisomal beta-oxidation activity in cultured human skin fibroblasts using a specific substrate, C9: a possible application for screening of peroxisomal disorders.

We developed a specific method for direct determination of peroxisomal beta-oxidation activity in cultured human skin fibroblasts. When control fibroblasts were incubated with N-(alpha-methylbenzyl)azelaamic acid (C9), a specific peroxisomal substrate, C5 and C7, the chain-shortened products, were detected with cell concentration and incubation time dependencies and no other products including C3 were detected. In glutaric aciduria type I and type II fibroblasts, the formation rates of C2 units liberated from C9 were almost similar to that in control cells. In contrast to these cell types, the fibroblasts from patient of Zellweger syndrome, in which peroxisomal beta-oxidation was impaired, showed no conversion of C9 to C5 and C7. The lack of the C2 units liberation in Zellweger fibroblasts was not due to an impairment of mitochondrial beta-oxidation and/or activation of C9 to C9-CoA derivative for subsequent beta-oxidation reaction, but rather, appeared to be due to the specific defect of peroxisomal beta-oxidation system. These results indicate that C9 is a useful substrate for the estimation of peroxisomal beta-oxidation activity in cultured human skin fibroblasts.

Cells, Cultured↗
PubMed1993

Enzyme reactor for urinary acylcarnitines assay by reversed-phase high-performance liquid chromatography.

An immobilized enzyme reactor, made up acylcarnitine hydrolase, carnitine dehydrogenase and diaphorase in sequence, was developed for the sensitive and selective determination of urinary free and individual acylcarnitines by a reversed-phase high-performance liquid chromatography. A 100-microliter urine sample was directly injected onto the TSKgel ODS 80Ts column and eluted by a step-gradient procedure. The eluent was mixed with the substrate solution of beta-NAD+ (1.0 mmol/l), resazurin (25 mumol/l) and Tris acetate (0.2 mol/l, pH 9.0). The mixture was passed through the immobilized enzyme reactor at 40 degrees C. Acylcarnitines were hydrolyzed and the converted to rezorufin which was measured by monitoring the fluorescence intensity at lambda EX = 560 nm and lambda EM = 580 nm. Free, acetyl-, glutaryl-, propionyl-, butyryl-, isobutyryl-, valeryl- and isovalerylcarnitine were determined within 55 min with detection limits (< 1 mumol/l) and within-run and day-to-day imprecision (C.V. < 6%). Free, acetyl- and isobutyrylcarnitine were found in normal urine. On the other hand, propionylcarnitine was detected in the urine of children with propionic aciduria and methylmalonic aciduria and multiple acylcarnitines were found in the urine of children with glutaric aciduria (type II).

Acetylcarnitine↗
PubMed1984

The stereochemistry of the formation of the methyl group in the glutamate mutase-catalysed reaction in Clostridium tetanomorphum.

The adenosylcobalamin-dependent enzyme glutamate mutase from Clostridium tetanomorphum catalyses the reversible rearrangement of (2S)-glutamate to (2S,3S)-3- methylaspartate . In this conversion 6 carbon centers are involved. The stereochemistry of 4 has been elucidated whereas the formation of the methyl group from the methylene group remains to be established. To solve this problem, (2S,3R)- and (2S,3S)-[3,3-2H1,3H]glutamates were prepared via the 2-oxo[3,3-2H2 or 3H] glutarates by incubation with isocitrate dehydrogenase in deuterium oxide or tritiated water. The labelled glutamates were fermented with growing cells of C. tetanomorphum to butyrate and acetate. Butyrate was further degraded to acetate in which methyl group over 90% of the tritium of the starting glutamate was retained. The chirality of the acetates was determined with malate synthase and fumarase. In both samples complete racemisation was found. This result confirms the rule that racemisation occurs in all adenosylcobalamin-dependent rearrangements in which methyl groups are formed. A methylene radical as intermediate could explain these observations. In a control experiment inversion of configuration in the formation of the methine group of (2S,3S)-3-methylaspartate from the methylene group of (2S)-glutamate was confirmed. Glutamates stereospecifically labelled at C-4 were synthesized from chiral acetates via citrate.

Amino Acid Isomerases↗
PubMed1987

Amino acid sequence surrounding the lipoic acid cofactor of bovine kidney 2-oxoglutarate dehydrogenase complex.

The 2-oxoglutarate dehydrogenase complex was succinylated using 2-oxo[5-14C]glutarate in the presence of N-ethylmaleimide to label the lipoic acid cofactor of the transuccinylase (E2) component. Following peptic digestion, 14C-lipoate-containing peptides were purified and subjected to automated Edman degradation and amino acid analysis. The amino acid sequence surrounding the lipoyllysine residue is reported.

Amino Acid Sequence↗
PubMed1989

Glutamate degradation in the ischemic dog heart: contribution to anaerobic energy production.

The present study investigated the conversion of amino acids to succinate and the contribution of this pathway to anaerobic energy production during regional ischemia in the dog heart in situ. The relation between regional myocardial blood flow, estimated by the tracer microsphere technique, and myocardial contents of metabolites (glutamate, alanine, succinate, lactate) as well as their local arterio-venous differences (A-V) were determined. During 30 min of coronary artery occlusion, myocardial glutamate decreased from 2.3 mumol/g wet wt in control tissue to 1.2 mumol/g wet wt in severely ischemic areas, while aspartate was unaffected. Myocardial alanine increased in a 1: 1 stoichiometry compared to glutamate, and succinate accumulated. During control perfusion (118 mmHg), A-V of lactate, succinate and glutamate were +470, -0.7 and -3.9 nmol/ml, respectively. Stepwise reduction of perfusion pressure led to the release of lactate and succinate from the underperfused area; extraction of glutamate occurred at the lowest perfusion pressure investigated (34 mmHg; A-V: -500, -10.4 and +4.2 nmol/ml, respectively). The data indicate that during regional ischemia in vivo, succinate is synthetized exclusively from glutamate via 2-oxo-glutarate, following transamination with glycolytic pyruvate yielding alanine, while the contribution of aspartate is negligible. Using tissue levels of glutamate and lactate together with the local arterio-venous concentration differences of these compounds, it can be estimated that degradation of glutamate delivers 20% of the ATP generated by substrate level phosphorylation reactions. Thus energy production by the glutamate degradation pathway is significant in vivo under conditions of flow deprivation.

Adenosine Triphosphate↗
PubMed1990

Antimitochondrial autoantibodies of primary biliary cirrhosis as a novel probe in the study of 2-oxo acid dehydrogenases in patients with mitochondrial myopathies.

Autoantibodies present in the autoimmune disease primary biliary cirrhosis react by immunoblotting with four human skeletal muscle mitochondrial antigens of 70 kDa, 52 kDa, 50 kDa and 45 kDa, identified as the lipoate acetyl transferases (E2) of the pyruvate dehydrogenase, component X of E2 pyruvate dehydrogenase, E2 of 2-oxo glutarate dehydrogenase and E2 of branched-chain 2-oxo acid dehydrogenase complexes respectively. These autoantibodies have been employed as a novel probe to study whether there is a defect in the synthesis of the 2-oxo acid dehydrogenase complexes in patients with mitochondrial respiratory chain disorders. The reactive antigens are present normally in four patients with oculomyopathy in whom partial deletions of the mtDNA have been detected, and in two patients with MERRF and MELAS encephalomyopathy. Thus, unlike in the yeast Saccharomyces cerevisiae, there appear to be no regulatory interactions which coordinate the assembly of the mitochondrial respiratory chain with the development of the pyruvate dehydrogenase complex, which plays an important role in regulating the flow of metabolic intermediates to oxidative energy metabolism.

3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)↗
PubMed1994

A riboflavin-responsive lipid storage myopathy due to multiple acyl-CoA dehydrogenase deficiency: an adult case.

A 62-year-old man was admitted to our hospital because of easy fatigability of the lower limbs during walking. The biopsied muscle specimen showed excessive lipid accumulation. The carnitine concentration in the muscle was at the lower level of the normal range. Organic acid urinalysis was consistent with the diagnosis of multiple acyl-CoA dehydrogenase deficiency or glutaric acidemia type II. In cultured lymphoblastoid cells from this patient there was impaired beta-oxidation, but the activities of acyl-CoA dehydrogenases were normal. Riboflavin therapy resulted in a dramatic improvement in both clinical and biochemical aspects. In this patient, the defect in coenzyme binding to electron transfer flavoprotein (ETF) or ETF-dehydrogenase was suspected. In the adult case of lipid storage myopathy, multiple acyl-CoA dehydrogenase deficiency should be suspected as one of its pathogenesis and riboflavin therapy should be considered.

Acyl-CoA Dehydrogenases↗
PubMed1995

The metabolism of n-nonane in male Fischer 344 rats.

The urinary metabolites of n-nonane in male Fischer 344 rats, after administering the hydrocarbon by gavage, included gamma-valerolactone, delta-hexanolactone, 2,5-hexanedione, delta-heptanolactone, 1-heptanol, 2-nonanol, 3-nonanol, 4-nonanol, 4-nonanone and 5-methyl-2-(3-oxobutyl)furan. Metabolism strongly favored the formation of monoalcohols and lactones, which are the products of appropriately substituted hydroxy carboxylic acids. The metabolites were identified using gas chromatography (GC) and gas chromatography/mass spectrometry (GC/MS). High pressure liquid chromatography (HPLC) permitted the detection of the dicarboxylic acids malonic acid and glutaric acid in the n-nonane dosed rat urines.

Alcohols↗
PubMed1994

Biochemical diagnosis of fatty acid oxidation disorders by metabolite analysis of postmortem liver.

At least 12 fatty acid oxidation disorders are known to be responsible for cases of sudden and unexpected death in early childhood. A specific diagnosis of these disorders is essential for genetic counseling and for the screening of siblings potentially at risk for life-threatening episodes of fasting intolerance. Postmortem blood and urine samples often are not available for further biochemical studies, and currently only medium-chain acyl-CoA dehydrogenase (MCAD) deficiency can be diagnosed by the molecular analysis of tissues. We developed a postmortem screening method for fatty acid oxidation disorders by the simultaneous measurement of C8-C20 fatty acids, glucose, lactate, and other metabolites from the methanol wash of a pellet obtained by ultracentrifugation of liver homogenate. Cis-4-decenoic acid was present in five confirmed cases with MCAD deficiency and in one case with glutaric aciduria type II and was absent in 97 of 100 randomly chosen sudden death cases, at least 81 of which were diagnosed as sudden infant death syndrome (SIDS). C14-C18 monounsaturated fatty acids were significantly elevated in the one examined case affected with long-chain acyl-CoA dehydrogenase (LCAD) deficiency. The metabolite profiles in two cases with carnitine uptake deficiency were less informative, but they shared with all the other disease controls a very low glucose concentration, a finding compatible with premortem hypoglycemia. This method is proposed as a simple and practical means of biochemical screening to follow up the postmortem finding of liver fat infiltration.

Acyl-CoA Dehydrogenase↗
PubMed1984

Succinate potentiates the action of platelet agonists.

Succinate potentiated the actions of ADP, epinephrine, and the endoperoxide analog U46619 on platelets in plasma. Potentiation was observed at concentrations as low as 400 microM. Potentiation occurred immediately and did not change during incubations as long as five min. It was also observed with maleate and malonate but not with fumarate, oxalate, glutarate or succinate analogs with one or both carboxyls blocked. Succinate was able to reverse the inhibition of platelet activation due to elevated cAMP, and succinate and maleate were comparable to ADP in their ability to inhibit PGI2-induced synthesis of cAMP.

15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5↗
PubMed1984

In vivo evaluation of a new polyurethane-coated catgut suture.

Plain catgut sutures were coated with different polyester-based polyurethanes. The sutures were implanted subcutaneously in rats and tested for tensile strength loss and tissue reactions. A polyurethane coating based on an oxalic acid polyester was hydrolysed too fast to protect the catgut against proteolysis. However, a 2-0 plain catgut having a 50 micron polyurethane coating based on glutaric acid polyester maintained its original tensile strength for 8 days. The tensile strength then decreased as for plain catgut. Histological examination of the surrounding tissues showed that the strong inflammatory reaction observed in the first three days with non-coated catguts is decreased, but occurs again later, although to a lesser extent.

Animals↗
PubMedDate not supplied

Spectrophotometric determination of proteolytic activity in coloured solutions.

A simple procedure for spectrophotometric determination of proteolytic activity in coloured solutions is described. Gelatin cross-linked with glutaric dialdehyde or formaldehyde in the presence of black drawing ink is used as an insoluble chromolytic substrate. The absorbances of reaction mixture filtrates are read in the near infra-red region (at 800-900 nm) where the majority of coloured substances does not absorb; on the contrary black drawing ink released from the substrate during the proteolysis absorbs strongly even at these wavelengths.

Hydrolysis↗
PubMed1992

Nucleotide sequence and expression in Escherichia coli of the cephalosporin acylase gene of a Pseudomonas strain.

The gene encoding cephalosporin acylase, which hydrolyzes 7-beta-(4-carboxybutanamido)-cephalosporanic acid (GL-7ACA) to 7-aminocephalosporanic acid (7ACA) and glutaric acid, was cloned from a Pseudomonas sp. strain V22 and expressed in Escherichia coli, in a two-cistron system, and the enzyme was purified and characterized. The purified enzyme was composed of two non-identical subunits, their molecular weights were estimated by SDS-PAGE to be 40,000 and 22,000, and had a pI of 4.6. The amino acid sequence of the enzyme, deduced from the nucleotide sequence, showed high similarity (97%) with that of a previously reported acyI-encoded cephalosporin acylase. Cephalosporin acylase also resembles the bacterial gamma-glutamyl transpeptidases (GGTs) with respect to their molecular organization and amino acid sequence, but differs from them with respect to catalytic and immunological properties. Purified enzyme exhibited not only cephalosporin acylase activity, but also GGT activity. The Km values of the enzyme for GL-7ACA and L-gamma-glutamyl-p-nitroanilide were 6.1 and 3.8 mM, respectively. Cephalosporin acylase was not recognized by antibodies prepared against bacterial GGTs.

Amidohydrolases↗