Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P17174 (aspartate aminotransferase)
 14,872 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have examined the value of serum type III procollagen amino propeptide (PIIINP) measurement both in evaluation of disease activity and in estimation of prognosis in primary biliary cirrhosis (PBC). 55 paired sera from 32 PBC patients not receiving treatment known to affect PIIINP levels not with non-hepatic inflammatory conditions were used to estimate serum PIIINP by radioimmunoassay. Significant correlations were found between serum PIIINP and serum albumin (P less than 0.001), bilirubin (P less than 0.002) and aspartate transaminase (P = 0.01). The mean serum PIIINP level rose with advancing histological stage (P less than 0.001). In 18 patients in whom more than 1 serum was assayed (mean follow-up 42 months) PIIINP often fell, particularly in patients with established cirrhosis and advanced disease. The independent prognostic value of PIIINP was examined using Cox's proportional hazards model with three other prognostic co-variables (bilirubin, albumin, patient age). Stepwise regression analysis selected albumin (P less than 0.001) and bilirubin (P = 0.002) as the most important prognostic factors. PIIINP did not give independent prognostic information. We conclude that PIIINP is another marker of disease activity in PBC which confers no benefit over existing conventional measurements in routine management of this disease.
J Hepatol 1989 Sep
PMID:Is measurement of type III procollagen amino propeptide useful in primary biliary cirrhosis? 280 58

Cutaneous LD50 of N,N-diethylphenylacetamide (DEPA), a new multi insect repellent was 2200, 3200 and 7100 mg/kg body weight in female mice, rats and guinea pigs; and 1600 and 4000 mg/kg in male mice and rats indicating a high degree of safety on skin contact. Dermal application of DEPA to young growing rats for 21 days at a dose of 50 mg/kg did not exert any adverse effects while massive doses of 500 and 1000 mg/kg caused marked reduction of body weight gain and lowering of activities of serum alanine aminotransferase, aspartate aminotransferase and cholinesterase. Along with DEPA, N-ethylphenylacetamide, phenylacetamide and phenylacetic acid were detected in the urine of DEPA treated mice, rats and guinea pigs.
Toxicology 1989 Sep
PMID:Toxicity and metabolism of a new insect repellent N,N-diethylphenylacetamide in mice, rats and guinea pigs on cutaneous application. 281 93

Haematological and biochemical investigations were performed on 14 koalas with uncomplicated cystitis, 8 with complicated cystitis, 8 with conjunctivitis, 8 with lymphosarcoma, and 14 with miscellaneous diseases. Changes were limited and inconsistent in individual koalas with uncomplicated cystitis and conjunctivitis. In contrast, individual koalas with complicated cystitis were more likely to have anaemia, leukocytosis due to neutrophilia, hypoproteinaemia due to hypoalbuminaemia, and azotaemia due to elevated urea concentration. Although these changes were non-specific they did allow assessment of prognosis for survival and response to treatment. Koalas with lymphosarcoma were invariably anaemic, leukaemic, azotaemic and hypoalbuminaemic. Elevated enzymes (aspartate transaminase [AST]. lactate dehydrogenase [LD] and gamma glutamyl transferase [GGT]) were more common in koalas with lymphosarcoma. Koalas affected by miscellaneous conditions showed variable changes but once again anaemia, leukocytosis, azotaemia, elevated AST and LD, and hypoalbuminaemia were not uncommon. On the basis of these findings a minimal profile is suggested for the investigation of sick koalas and would include haematocrit, total and differential leukocyte counts, urea, total protein and albumin concentrations and AST, GGT and LD activities.
Aust Vet J 1989 Sep
PMID:Haematological and biochemical investigations of diseased koalas (Phascolarctos cinereus). 281 69

We have previously shown that the rapid clearance of intravenously injected lactate dehydrogenase M4 from plasma is mainly due to endocytosis by macrophages in liver, spleen, and bone marrow. We have now studied endocytosis of lactate dehydrogenase M4 in detail, using freshly isolated rat liver macrophages (Kupffer cells) in vitro. 125I-lactate dehydrogenase M4 rapidly accumulated in the cells and was subsequently degraded to trichloroacetic acid-soluble material. Degradation was inhibited by leupeptin, an inhibitor of lysosomal proteases. Breakdown of the protein was also greatly diminished by treatment of the cells with chloroquine, a weak base which inhibits proteolysis by raising the pH in endosomes and lysosomes. High concentrations of chloroquine inhibited uptake. Lactate dehydrogenase M4 was not endocytosed by liver endothelial cells, although, under the same conditions, these cells were shown to accumulate horse radish peroxidase via a mannose-specific receptor. Uptake of lactate dehydrogenase M4 by Kupffer cells was strongly reduced after pretreatment of the cells with low concentrations of proteases. Endocytosis of lactate dehydrogenase M4 exhibited saturation kinetics (Km = 0.8 microM) and was competitively inhibited by mitochondrial and cytosolic malate dehydrogenase, alcohol dehydrogenase, adenylate kinase, and creatine kinase MM, enzymes which are rapidly cleared in vivo. Enzymes with long half-lives in plasma, namely lactate dehydrogenase H4, alanine aminotransferase, and cytosolic aspartate aminotransferase did not compete at concentrations up to 10 microM. Our results indicate that Kupffer cells contain a receptor that is involved in the clearance of lactate dehydrogenase M4 and a number of other tissue-derived enzymes from plasma. Uptake of lactate dehydrogenase M4 does not occur via a receptor that recognizes carbohydrate residues, for the enzyme is not a glycoprotein.
J Biol Chem 1987 Sep 25
PMID:Receptor-mediated endocytosis of lactate dehydrogenase M4 by liver macrophages: a mechanism for elimination of enzymes from plasma. Evidence for competition by creatine kinase MM, adenylate kinase, malate, and alcohol dehydrogenase. 282 Sep 61

Physical interactions between pyridoxal kinase and aspartate aminotransferase were detected by means of emission anisotropy and affinity chromatography techniques. Binding of aspartate aminotransferase (apoenzymes) to pyridoxal kinase tagged with a fluorescent probe was detected by emission anisotropy measurements at pH 6.8 (150 mM KCl). Upon saturation of the kinase with the aminotransferase, the emission anisotropy increases 22%. The protein complex is characterized by a dissociation constant of 3 microM. Time-dependent emission anisotropy measurements conducted with the mixture 5-naphthylamine-1-sulfonic acid-kinase aspartate aminotransferase (apoenzyme), revealed the presence of two rotational correlation times of phi 1 = 36 and phi 2 = 62 ns. The longer correlation time is attributed to the stable protein complex. By immobilizing one enzyme (pyridoxal kinase) through interactions with pyridoxal-Sepharose, it was possible to demonstrate that aspartate aminotransferase releases pyridoxal kinase. A test of compartmentation of pyridoxal-5-phosphate within the protein complex using alkaline phosphatase as trapping agent, indicates that the cofactor generated by the catalytic action of the kinase is channeled to the apotransaminase. The main function of the stable complex formed by the kinase and the aminotransferase is to hinder the release of free pyridoxal-5-phosphate into the bulk solvent.
J Biol Chem 1988 Sep 25
PMID:Interactions of pyridoxal kinase and aspartate aminotransferase emission anisotropy and compartmentation studies. 284 32

The serum activities of the liver enzymes alanine aminotransferase, aspartate aminotransferase, ornithine carbamyl transferase, and gamma-glutamyl transferase were examined in 47 paint industry workers and unexposed age matched referents. The workers were exposed to a mixture of industrial solvents, of which xylene was the main component in most cases. The median total exposure was about 50% of Swedish 1981 threshold limit values according to measurements of individual solvent exposure performed at the same time. No differences in enzyme activities were shown either when the whole exposed and referent groups were compared or when the five workers with outstanding solvent exposures of five times the TLV or more were compared with their referents. It is concluded that in most workers the liver seems to remain largely undamaged from inhalation exposure to a commonly used mixture of non-chlorinated solvents. In many workers this seems to hold true even for high exposures for limited periods.
Br J Ind Med 1985 Sep
PMID:Normal serum activities of liver enzymes in Swedish paint industry workers with heavy exposure to organic solvents. 286 77

The isolated perfused rat kidney was shown to synthesize serine from aspartate or glutamate, both of which are also precursors of glucose. The major products of aspartate metabolism were ammonia, serine, glutamate, glucose, glutamine and CO2. Perfusion of kidneys with aspartate in the presence of amino-oxyacetate resulted in a near-complete inhibition of aspartate metabolism, illustrating the essential role of aspartate aminotransferase in the metabolism of this substrate. Radioactivity from 14C-labelled aspartate and from 14C-labelled glycerol was incorporated into serine and glucose. Production of both glucose and serine from aspartate was suppressed in the presence of 3-mercaptopicolinic acid. These data provide evidence for the operation of the phosphorylated and/or non-phosphorylated pathway for serine production to the presence of 3-mercaptopicolinic acid. This is explained by simultaneous glycolysis. The rate of glucose production, but not that of serine, was greater in kidneys perfused with glutamate or with aspartate plus glycerol than the rates obtained by perfusion with aspartate alone. These data are taken to suggest that serine synthesis occurred at a near-maximal rate, and that the capacity of the kidney for serine synthesis from glucose precursors is lower than that for glucose synthesis.
Biochem J 1985 Sep 01
PMID:Serine synthesis by an isolated perfused rat kidney preparation. 286 20

A comparative study of the metabolic effects of two combined oral contraceptive preparations was undertaken in seven WHO Collaborating Centres for Research in Human Reproduction. A total of 847 subjects were randomly allocated to one of two pill groups - norethisterone lmg/ethinyl estradiol 35 micrograms (NET/EE) or levonorgestrel 150 micrograms/ethinyl estradiol 30 micrograms (LNG/EE). An additional 195 women using an IUD served as a comparison group. Blood samples were taken on admission, and at 3 and 12 months thereafter. Both pills induced changes in fasting and 2-hour glucose, triglycerides, total cholesterol, HDL-cholesterol, bilirubin, alkaline phosphatase, albumin, and total protein, but not aspartate aminotransferase. The most dramatic and probably most clinically important changes were an increase in triglycerides and a decrease in HDL-cholesterol. The NET/EE preparation appeared to induce a greater increase in triglycerides, but no significant difference was found between the two pill preparations with respect to HDL-cholesterol changes.
Contraception 1985 Sep
PMID:A randomized double-blind study of the effects of two low-dose combined oral contraceptives on biochemical aspects. Report from a seven-centred study. WHO Special Programme of Research, Development and Research Training in Human Reproduction. Task force on Oral Contraceptives. 286 58

Plasma levels of glutamate, alanine, free fatty acids (FFA), citrate, glucose, insulin, lactate, creatine kinase and aspartate aminotransferase were determined frequently during the first 2-48 h after onset of chest pain in 10 patients who developed acute myocardial infarction (AMI) and in 8 who did not (non-AMI). An initial decrease in plasma glutamate and increase in alanine was found in AMI compared to non-AMI patients. The AMI group showed early, moderate rises of plasma FFA and citrate concentrations, positively related to the initial ST-segment elevation and to the enzymatic estimated infarct size. The AMI patients were continuously hyperglycaemic, but their relative insulin response i.e. plasma glucose/insulin ratio was identical to that of non-AMI patients. Lactate values did not differ between the two groups. Via participation in the malate-aspartate shuttle and by shunting pyruvate to alanine instead of lactate, glutamate is of importance for maintaining myocardial glucose utilization. Our finding of initial low plasma glutamate concentrations after onset of myocardial infarction suggests insufficient glutamate supply to the ischaemic myocardium. On basis of this and animal experiments, an external supply of glutamate might be a 'metabolic' treatment of AMI, alternative or additional to glucose-insulin-potassium infusion in order to promote myocardial glucose oxidation.
Eur Heart J 1986 Sep
PMID:Altered plasma concentrations of glutamate, alanine and citrate in the early phase of acute myocardial infarction in man. 287 95

Pathways of glutamine metabolism in resting and proliferating rat thymocytes were evaluated by in vitro incubations of freshly prepared or 60-h cultured cells for 1-2 h with [U14C]glutamine. Complete recovery of glutamine carbons utilized in products allowed quantification of the pathways of glutamine metabolism under the experimental conditions. Partial oxidation of glutamine via 2-oxoglutarate in a truncated citric acid cycle to CO2 and oxaloacetate, which then was converted to aspartate, accounted for 76 and 69%, respectively, of the glutamine metabolized beyond the stage of glutamate by resting and proliferating thymocytes. Complete oxidation to CO2 in the citric acid cycle via 2-oxoglutarate dehydrogenase and isocitrate dehydrogenase accounted for 25 and 7%, respectively. In proliferating cells a substantial amount of glutamine carbons was also recovered in pyruvate, alanine, and especially lactate. The main route of glutamine and glutamate entrance into the citric acid cycle via 2-oxoglutarate in both cells is transamination by aspartate aminotransferase rather than oxidative deamination by glutamate dehydrogenase. In the presence of glucose as second substrate, glutamine utilization and aspartate formation markedly decreased, but complete oxidation of glutamine carbons to CO2 increased to 37 and 23%, respectively, in resting and proliferating cells. The dipeptide, glycyl-L-glutamine, which is more stable than free glutamine, can substitute for glutamine in thymocyte cultures at higher concentrations.
J Cell Physiol 1987 Sep
PMID:Pathways of glutamine and glutamate metabolism in resting and proliferating rat thymocytes: comparison between free and peptide-bound glutamine. 288 73


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