Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.6.1.2 (alanine aminotransferase)
 26,722 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The subcellular localization of NAD- and NADP-linked glutamate dehydrogenases (GDH-NAD and GDH-NADP), alanine aminotransferase (ALAT) and aspartate aminotransferase (ASAT) in epimastigotes of Trypanosoma cruzi was studied by digitonin extraction from whole cells, subcellular fractionation by differential centrifugation and isopycnic ultracentrifugation. All enzymes presented both a cytosolic and a mitochondrial form; in addition, GDH-NADP seems to have a third, still undefined, localization. The results are compatible with the existence of two pathways for the production of L-alanine linked to the reoxidation of glycolytic NADH, one operative in the mitochondrion and the other in the cytosol, and perhaps responsible for the existence of the two alanine pools detected by 13C-nuclear magnetic resonance (B. Frydman et al., Eur. J. Biochem. 192 (1990) 363-368).
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PMID:Subcellular localization of glutamate dehydrogenases and alanine aminotransferase in epimastigotes of Trypanosoma cruzi. 177 28

The 3-years efficacy and safety of the 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitor simvastatin (S) (previously called synvinolin or MK-733) has been studied in single and combined therapy with cholestyramine (C) in 48 hypercholesterolaemic patients. Plasma lipids, lipoproteins and apolipoproteins A-I and B, and blood safety tests (haematology, liver function, creatine phosphokinase (CPK), creatinine, blood glucose and thyroid function) were determined regularly throughout the study. Extensive ophthalmological examinations with particular focus on the lens were done before initiation of therapy and at every 6 months during drug treatment. Maximal reductions of mean plasma total cholesterol concentration (34% with S; 47% with S + C) and low-density lipoprotein (LDL)-cholesterol concentration (42% with S; 56% with S + C) were achieved after 4 weeks on full-dose therapy. During continued treatment, years 1 through 3, the reduction of mean plasma total cholesterol was 26-29% with S alone, and 31-41% with S + C. Significant reductions of plasma triglycerides (15-27%) and very low density lipoprotein (VLDL) triglycerides (10-27%) were achieved in the group treated with S as single therapy. In this group there was also a significant increase (10-14%) of high-density lipoprotein (HDL)-cholesterol. In liver aspartate (AST) and alanine (ALT) aminotransferases, as well as alkaline phosphatase (ALP), minor and variable, but usually transient, increases were seen. Repeated ophthalmological examinations did not demonstrate any drug-related side effects. It is concluded that simvastatin is a safe and efficient cholesterol-lowering drug for long-term therapy, both as a single drug and in combination with cholestyramine.
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PMID:Long-term efficacy and safety of simvastatin alone and in combination therapy in treatment of hypercholesterolaemia. 178 13

The influence of Z-4,4-bis(4-ethylphenyl)-2,3-dibromo-2-butenoic acid, the compound originally synthetized as a cytostatic edikron and showing inhibitory effect on several pyridoxal enzymes, on absorption and circular dichroism spectra of alanine and aspartate aminotransferases (ALT, AST) in the region of coenzyme absorption characteristics was studied. In the case of AST, the compound decreased absorption and CD maxima at 360 nm, which represents the active form of the enzyme, but it did not seem to prevent formation of the pyridoxamine form of the enzyme, produced in the presence of L-aspartate. Edikron caused insignificant spectral changes of ALT, but it partially denatured the enzyme. Circular dichroism measurement of both enzymes uncovered some effects of edikron at 250-300 nm, which suggests conformational changes in the aromatic amino acids of the apoenzymes due to the compound studied.
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PMID:Interaction of Z-4,4-bis(4-ethylphenyl)-2,3-dibromo-2-butenoic acid with aminotransferases: changes in absorption and circular dichroism spectra. 182 79

The influence of repeated s.c. administration of the cytostatic 5-[2-(N,N-dimethylamino)ethoxy]-7-oxo-7H-benzo(c)fluorene hydrochloride (benflurone, 25 mg/kg body weight daily) on the activities of aspartate and alanine aminotransferases (AST, ALT) per g of tissue, and protein concentration in the liver of adult male rats was studied. During the first week of benflurone administration, the activities of ALT and AST decreased by 2/3 and 1/3, respectively, in comparison with controls while the protein concentration did not show any substantial change. No in vitro influence of benflurone on AST and ALT was found even at the highest concentration tested (10(-4) M). The significance of the aminotransferase decrease after treatment with benflurone and possible participation of these changes in the side- or cytostatic effects of the compound are considered.
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PMID:Influence of 5-[2-(N,N-dimethylamino)ethoxy]-7-oxo-7H-benzo(C)fluorene hydrochloride (benflurone) on the activity of rat liver aspartate and alanine aminotransferases. 182 83

L-alanine aminotransferase was demonstrated in a range of gastrointestinal, free-living and entomophagous nematodes. As in mammals, nematode L-alanine aminotransferase was found to exist in the form of mitochondrial and cytosolic isoenzymes. Whilst the majority of nematode enzymes exhibited a greater overall capacity for L-alanine synthesis than for L-alanine catabolism in vitro, the opposite was true for rat liver L-alanine aminotransferase. In contrast with rat liver, certain gastrointestinal nematodes were apparently able to transaminate D-alanine at low rates. H. contortus cytosolic L-alanine aminotransferase differed significantly from the mammalian enzyme with respect to both thermal stability and response to potential protective reagents.
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PMID:Studies on alanine aminotransferase in nematodes. 189 37

Effects of an 18 min exercise test, on three separate occasions during a one year jump-training programme, was studied in seven horses. Determinations were carried out on venous blood for packed cell volume, haemoglobin, total protein, lactate and pyruvate, glucose, free fatty acids, insulin, glucagon, blood gases, bicarbonate, pH, aldolase, aspartate aminotransferase and alanine amino-transferase. Exercise caused a slight increase in lactate and pyruvate, total protein, aldolase, alanine aminotransferase, pO2, bicarbonate and pH. Glucose, free fatty acids and pCO2 levels decreased. Training caused no significant difference in these changes. However, during the year, increases in lactate and decreases in pH (resting levels) were observed.
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PMID:Changes in some haematological and metabolic indices in young horses during the first year of jump-training. 191 34

Human and rat erythrocytes were found to generate 3HOH from D-[6(N)-3H]glucose. The rate of 3HOH production represented 7-10% of the glycolytic flux. The generation of 3HOH appeared attributable, in part at least, to the detritiation of [3-3H]pyruvate during the interconversion of the 2-keto acid and L-alanine in the reaction catalyzed by glutamate-pyruvate transaminase. Indeed, purified pig heart glutamate-pyruvate transaminase, as well as homogenates prepared from rat erythrocytes or pancreatic islets, catalyzed the generation of 3HOH from L-[3-3H]alanine. When the production of tritiated pyruvate from L-[3-3H]alanine was coupled to the conversion of the 2-keto acid to L-lactate, the production of 3HOH accounted for one-third of the reaction velocity, the latter failing to display isotopic discrimination. In these experiments, the production of 3HOH was abolished by amino-oxyacetate. Likewise, in intact rat erythrocytes, aminooxyacetate inhibited the generation of 3HOH and tritiated L-alanine from D-[6-3H]glucose (or D-[1-3H]glucose), as well as the generation of 3HOH from L-[3-3H]alanine. In pancreatic islets, however, aminooxyacetate failed to affect significantly the generation of 3HOH from D-[6-3H]glucose. These findings indicate that the generation of 3HOH from D-[6-3H]glucose is mainly attributable to an intermolecular tritium transfer in transaminase reaction, at least in cells devoid of mitochondria.
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PMID:Generation of 3HOH from D-[6-3H]glucose by erythrocytes: role of pyruvate alanine interconversion. 193 Nov 57

Protein is not normally an important energy fuel for exercising muscle. In spite of this, there is a significant increase in the rate of amino acid catabolism during exercise. This is secondary to the exercise-induced increase in several metabolic processes, such as hepatic gluconeogenesis and the citric acid cycle, where amino acid carbon is utilized. The suppression of protein synthesis during an exercise bout leaves amino acids available for catabolism. There is some evidence that basal amino acid concentrations in plasma and muscle may be higher in trained than in untrained individuals. In the rat, the concentration of free amino acids is higher in slow-twitch than in fast-twitch muscles. With short-term exercise, the transamination of glutamate by alanine aminotransferase leads to increased levels of alanine in muscle and plasma, and an increased release of alanine from the muscle. At the same time, the muscle and plasma glutamate concentrations are markedly decreased. The plasma glutamine level is elevated with short-term exercise, but changes in muscle glutamine concentration are more variable. With prolonged exercise, there is a depletion of the plasma amino acid pool, which may be explained by an increased consumption in organs other than muscle. With the exception of alanine, we found, however, that the muscle levels of free amino acids are kept stable throughout a 3.5-h exercise period. There is a significant activation of branched-chain amino acid metabolism with prolonged exercise, and the current data indicate that this is more pronounced in endurance-trained subjects than in untrained controls.
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PMID:Effect of exercise on amino acid concentrations in skeletal muscle and plasma. 196 May 12

The effects of Glu and Asp on calcium stone formation was evaluated in three experiments. Studies using mixed suspension, mixed product removal crystallization and scanning electron microscopy showed that Glu and Asp inhibited the nucleation rate, growth rate and suspension density (crystal mass produced) in proportion to the concentration. The main amino acids in calcium oxalate stones and calcium phosphate stones were Glu and Asp. However, the main amino acids in uric acid stones were glycine and urea, and there were no specific amino acids in struvite stones. The activity of urinary GOT and GPT, which convert Asp and alanine, respectively, to Glu in normal subjects was significantly greater than in calcium stone formation.
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PMID:Inhibitory effect of glutamic acid and aspartic acid on calcium oxalate crystal formation. 196 35

Lipid peroxidation (LPO) and alterations in cellular systems protecting against oxidative damage were determined in the liver, kidney and skeletal muscle of male F344/NCr rats, 1 h to 3 days after a single intraperitoneal (i.p.) injection of 107 mumol nickel(II)acetate per kg body weight. At 3 h, when tissue nickel concentrations were highest, the following significant (at least, P less than 0.05) effects were observed: in kidney, increased LPO (by 43%), increased renal iron (by 24%), decreased catalase (CAT) and glutathione peroxidase (GSH-Px) activities (both by 15%), decreased glutathione (GSH) concentration (by 20%), decreased glutathione reductase (GSSG-R) activity (by 10%), and increased glutathione-S-transferase (GST) activity (by 44%); the activity of superoxide dismutase (SOD) and gamma-glutamyl transferase (GGT), as well as copper concentration, were not affected. In the liver, nickel effects included increased LPO (by 30%), decreased CAT and GSH-Px activities (both by 15%), decreased GSH level (by 33%), decreased GSSG-R activity (by 10%) and decreased GST activity (by 35%); SOD, GGT, copper, and iron remained unchanged. In muscle, nickel treatment decreased copper content (by 43%) and the SOD activity (by 30%) with no effects on other parameters. In blood, nickel had no effect on CAT and GSH-Px, but increased the activities of alanine-(ALT) and aspartate-(AST) transaminases to 330% and 240% of the background level, respectively. In conclusion, nickel treatment caused profound cell damage as indicated by increased LPO in liver and kidney and leakage of intracellular enzymes, ALT and AST to the blood. The time pattern of the resulting renal and hepatic LPO indicated a possible contribution to its magnitude from an increased concentration of nickel and concurrent inhibition of CAT, GSH-Px and GSSG-R, but not from increased iron or copper levels. The oxidative damage expressed as LPO was highest in the kidney and lowest in the muscle, which concurs with the corresponding ranking of nickel uptake by these tissues.
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PMID:Nickel induced lipid peroxidation in the rat: correlation with nickel effect on antioxidant defense systems. 197 9


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