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 content of free amino acids, activity of aspartate and alanine transaminase, number of sulphydryl groups in fish tissues were studied as affected by lethal amounts (3.2 g/l) of blue-green algae. Blue-green algae have a certain affect on fishes not only by excreting biologically active substances in the process of vital activity and decay but also changing the gas regime of the medium (the oxygen content lowers, the amount of carbon dioxide increases). Under the algae effect the total content of free amino acids in the fish liver, intestine and muscles increases, mainly due to a rise in the content of glutamic acid with threonine and aspartic acid with serine. These changes are most essential in the liver, intestine and are less pronounced in the muscles. Under the effect of blue-green algae the activity of aspartate transaminase increases in the heart, brain and decreases in the intestine. The activity of alanine transaminase enhances in the heart, intestine and brain. The ration value for these enzymes changes significantly in the brain, liver, intestine, but does not differ from the control in the muscles.
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PMID:[Amino acid composition and transaminase activity in fish tissues, in a medium containing Cyanophyceae]. 10 39

Protein hydrolysate-containing parenteral solutions have been reported to be hepatotoxic. Ten infants who were treated with a 20 percent glucose solution containing either 2.5 percent or 3.25 percent protein hydrolysate are reviewed. Their gestational ages were 30 to 40 weeks and births weights 1000 to 35000 g. Serum glutamate-oxaloacetate transaminase (GOT), glutamate-pyruvate transaminase (GPT), leucine amino peptidase (LAP) and bilirubin were measured serially. Serum amino acids were measured and consistently demonstrated decreased levels of isoleucine and increased aspartic acid, glutamic acid, serine, proline, glycine, alanine, threonine and lysine. The amino acid imbalances were associated with transaminase elevations in eight infants. Serum bilirubin levels increased in six patients and LAP in four. Liver biopsies from three patients showed minimal to moderate hepatic parenchymal disease with cholestasis.
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PMID:The hepatotoxicity of parenteral protein hydrolysate-containing solutions. 82 62

1. The concentrations of alanine, aspartate, glutamate, glutamine and serine plus threonine have been measured by enzymic methods in ;quick-frozen' livers from normal, starved, alloxan-diabetic and phlorrhizin-treated rats. 2. The hepatic concentrations of alanine and serine plus threonine were decreased in rats starved for 48hr. Treatment of these rats with phlorrhizin resulted in a rapid fall (within 2(1/2)hr.) in the concentrations of all the glucogenic amino acids except serine plus threonine, which increased. The pattern for alloxan-diabetic rats was similar to that for phlorrhizin-treated animals, except that here serine plus threonine also decreased in concentration. 3. The effects of anoxia on the hepatic concentrations of the glucogenic amino acids are reported. 4. Inhibition of glutamate-pyruvate transaminase in vivo by l-cycloserine resulted in the accumulation of alanine in situations involving high rates of gluconeogenesis from endogenous amino acids. 5. Measurements of the concentrations of the reactants of the glutamate-pyruvate transaminase and glutamate-oxoglutarate transaminase systems in various metabolic states suggest that they are both at or near equilibrium in rat liver. 6. New enzymic methods are described for the determination of serine plus threonine and alanine.
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PMID:Concentrations of free glucogenic amino acids in livers of rats subjected to various metabolic stresses. 604 91

Effects of varying protein level on hepatic utilization of serine, threonine and glycine were examined by measurements of metabolic fluxes across the liver. Feeding a high protein (HP) diet markedly enhanced hepatic extraction of serine, threonine and glycine, in parallel to alanine. After 20 hours starvation, activity of alanine aminotransferase and serine dehydratase still reflected the induction of these enzymes in fed rats. Thus, in starved rats previously adapted to HP diets, hepatic uptake of serine, threonine and glycine remained very efficient. With a normal diet, gluconeogenesis from alanine may be very active during starvation, in contrast to serine. The present results suggest that serine, and, to a lesser extent glycine, are very efficient glucogenic substrates with HP diets. The serine aminotransferase pathway might be important in rats fed HP diets, particularly for utilization of serine synthesized from glycine in mitochondria. With HP diets, the drop in hepatic alanine, serine and threonine suggest that transport across the plasma membrane might limit their utilization.
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PMID:Control of hepatic utilization of serine, glycine and threonine in fed and starved rats. 640 4

Some experimental and clinical studies were done from the metabolic viewpoint to elucidate the characteristics of myonephropathic-metabolic syndrome. In experimental dogs with their femoral arteries ligated and two third of femoral muscles divided, aldolase and myoglobin showed remarkable increase without significant changes in electrolytes. Slight increase of GPT and GOT was observed. Amino acids showed elevation in urea, taurin, leucin, isoleucin, valine, threonine, 3-methylhistidine, phenylalanine, histidine, lysine, methionine, tyrosine and anserin and decrease in glutamine, alanine, glycine, proline, carnosine, citrullin and arginine. In patients with acute arterial occlusion, potassium, GOT, LDH, CPK, lactate and pyruvate increased moderately and myoglobin showed remarkable increase and aldolase slight increase. Amino acids showed remarkable increase in 3-methylhistidine and beta-amino-isobutyric acid and moderate increase in phenylalanine and arginine. These results revealed that measurement of free amino acid concentration, especially that of methylhistidine as well as myoglobin, pyruvate, lactate and some other enzymes might be of great help to predict the prognosis of patients with acute arterial occlusion of the extremities.
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PMID:[Metabolic study on acute arterial occlusion of the extremities]. 667 89

Serum amino acid (AA) profiles are altered in epilepsy. It is not clear whether this is due to the disease process itself or to other variables such as seizure type, seizure frequency, duration of illness, medication, or altered liver function. We investigated serum AA profiles and liver enzymes in 73 epileptic patients and 90 healthy subjects and evaluated the data by analysis of variance to discriminate between age, sex, seizure type, duration of illness, seizure frequency, antiepileptic drug (AED) and increased serum liver enzyme levels, and their putative interaction with the serum AA profile. There was no correlation between the changes in the AA profile and age, duration of illness, seizure frequency, and seizure type. Seventy-two percent of the AED-treated patients and 33% of the unmedicated patients showed an increase in one or several serum liver enzymes [alanine aminotransferase (ALT), aspartate aminotransferase (AST), and/or gamma-glutamyl transferase (gamma-GT)]; particularly gamma-GT. We observed a significant increase in serum concentrations of glutamine and glycine and decreased levels of taurine, threonine, serine, valine, methionine, isoleucine, leucine, phenylalanine, histidine, tryptophan, and arginine in AED-treated patients but not in unmedicated patients. These results show that the changes in the serum AA profiles of epileptic patients treated with AEDs occur in patients with alteration of serum liver enzymes; whether this implies a causal relation is still uncertain.
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PMID:Serum amino acids, liver status, and antiepileptic drug therapy in epilepsy. 809 92

The effect of long-term 'corn peptide (CP)' ingestion on alcohol metabolism was investigated in stroke-prone spontaneously hypertensive rats (SHR-SP) with alcohol loading. Long-term CP ingestion in the EtOH/CP group did not significantly increase plasma GOT and GPT activities but markedly increased hepatic ADH and ALDH activities. Intragastric CP administration prior to a dose of 1.0 g/kg ethanol significantly lowered the blood ethanol concentration in SHR-SP which had been loaded with ethanol for a long time. Compared with non-loaded SHR-SP (control group), the rats loaded for a long time with ethanol (EtOH group) showed high concentrations of taurine, glycine and histidine in the plasma. The plasma threonine and proline concentrations were significantly elevated by long-term CP ingestion (EtOH/CP group), but the plasma alanine concentration was rather decreased. These results suggest that short- or long-term CP ingestion may enhance the alcohol metabolism within the body because of an increase in ADH and ALDH activities as well as the alleviation of alcohol-related hepatic injury.
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PMID:Effect of long-term 'corn peptide' ingestion on alcohol metabolism in stroke-prone spontaneously hypertensive rats with alcohol loading. 908 82

Chronic occupational exposure to organophosphorus and carbamate-type pesticides significantly inhibits acetylcholinesterase activity and causes morbidity. This study on mice was designed to evaluate their amino profile and to identify signs of hepatic dysfunction following their chronic exposure to mixtures of organophosphorus pesticides. Laboratory mice were exposed to a formulated mixture of the six organophosphorus pesticides (Dimethoate, Chlorpyrifos, Profenofos, Pirimiphos methyl, Triazophos and Dimethoate) most commonly used in agriculture in this region of the Middle East. Doses (10% of LD50 of the mixture) were given once a week by gavage in corn oil for 7 weeks; the control group was given only corn oil. At the end of the exposure period, mice were culled and blood samples were collected to determine erythrocyte acetylcholinesterase activity, biochemical markers of liver function and concentrations of serum amino acids. Erythrocyte acetylcholinesterase activity and total serum proteins decreased significantly in the exposed group. Serum concentrations of alanine aminotransferase and aspartate aminotransferase, alanine, glutamic acid, glycine, isoleucine, leucine, methionine, ornithine, proline, serine, threonine and valine were significantly increased in the exposed mice, while serum levels of cystine were decreased significantly. There were also non-significant increases in serum alkaline phosphatase, gama-glutamyl transpeptidase and some of the other amino acids. Chronic exposure to mixtures of organophosphorus pesticides is associated with decreased acetylcholinesterase activity, hepatic dysfunction and disturbance of amino acids profile. Biochemical indices of hepatocellular injury and disturbed amino acid metabolism may be of value as markers of chronic exposure to such pesticides.
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PMID:Hepatic injury and disturbed amino acid metabolism in mice following prolonged exposure to organophosphorus pesticides. 1002 66

The aims of the present study were to assess the changes of individual plasma amino acid levels in relation (1) to the severity of liver damage and (2) to the process of liver recovery. Acute liver injury was induced by an intragastric administration of CCl4 diluted in olive oil in doses of 2, 4 and/or 6 g of CCl4 per kg b.w. The control rats received olive oil only. Animals were sacrificed at 16, 24, 48 and 96 hours after treatment. The severity of liver injury was assessed by histological examination, by changes in ALT and AST in the blood plasma and by changes in liver weight. Statistical analysis was carried by ANOVA, p < 0.05 was considered significant. The Spearman rank correlation coefficient was used as a measure of the degree of linear relationship between variable and dose. In the period of the development of acute liver damage, i.e. at 16 and 24 hours after treatment, an increase in blood plasma amino acid levels and positive correlations with the dose of CCl4 were observed for most individual amino acids. The only exception was arginine which decreased in a dose dependent manner. At a phase of liver recovery, i.e. at 48 and 96 hours after CCl4 treatment, the concentrations of some individual amino acids decreased below the control values. The negative correlation with the dose of CCl4 occurred for taurine and isoleucine (at 48 hours) and taurine, threonine, valine, methionine, isoleucine and leucine (at 96 hours).
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PMID:Plasma amino acid levels after carbon tetrachloride induced acute liver damage. A dose-response and time-response study in rats. 1007 29

Cystalysin, isolated from the oral pathogen Treponema denticola, is an L-cysteine desulfhydrase (producing pyruvate, ammonia and hydrogen sulfide from cysteine) that can modify hemoglobin and has hemolytic activity. Here, we show that enzymatic activity of recombinant cystalysin depends upon stochiometric pyridoxal phosphate. The enzyme was not functional as an L-alanine transaminase, and had a strong preference for L-cysteine over D-cysteine. Cystalysin preferred small alpha-L-amino acids as substrates or inhibitors and was far more active towards L-cysteine than towards the other standard amino acids that undergo pyridoxal phosphate-dependent beta-elimination reactions (serine, threonine, tryptophan and tyrosine). Cystalysin tolerated small modifications to the carboxylate of L-cysteine (i.e., the methyl and ethyl esters of L-cysteine were good substrates), but the smallest possible peptide with an N-terminal cysteine, L-cysteinylglycine, was a very poor substrate. These results, combined with the implicit requirement for a free amine for pyridoxal phosphate-dependent reactions, imply that cystalysin cannot catabolize cysteine residues located within peptides. Cystalysin has Michaelis-Menten kinetics towards L-cysteine, and there was little or no inhibition by ammonia, H2S, pyruvate and acetate. Human erythrocytes incubated with H2S or with cystalysin and cysteine primarily accumulated sulfhemoglobin and methemoglobin, along with minor amounts of choleglobin and protein aggregates. Erythrocytes retained the ability to reduce methemoglobin in the presence of H2S. Cystalysin could not modify hemoglobin when beta-chloroalanine was the substrate, indicating an absolute requirement for H2S production. Cystalysin appears to be an unregulated L-cysteine catabolizing enzyme, with the resulting H2S production being essential to the atypical hemolytic activity.
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PMID:Sulfhemoglobin formation in human erythrocytes by cystalysin, an L-cysteine desulfhydrase from Treponema denticola. 1049 9


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