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)

Serum alanine aminotransferase, aspartate aminotransferase and gamma-glutamyltransferase activities were monitored in psychiatric patients receiving normal doses of phenothiazine neuroleptics over a 30-day period. The first two enzymes showed slight initial increases and a subsequent return to normal, while the third showed a slight increase. In rats, dosage levels exceeding those used in human therapy produced much larger increases in the catalytic concentrations of all three enzymes in serum (1.4, 0.7 and 0.5 above the control value, respectively), and somewhat smaller increases in the liver homogenates of these animals.
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PMID:Effects of neuroleptic phenothiazines on the activities of aminotransferases and gamma-glutamyltransferase in serum and liver. 287 49

Following a major environmental accident near Seveso, Italy, on July 10, 1976, we attempted to determine if the 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) released into the atmosphere had any effect on the liver function and lipid metabolism of exposed children. From July 1976 to June 1982, we analyzed the results of more than 4500 laboratory tests (alanine aminotransferase, aspartate aminotransferase, gamma-glutamyltransferase, alkaline phosphatase, cholesterol, and triglycerides in plasma and delta-aminolevulinic acid in urine) in a population of about 1500 children aged 6 to 10 years at the moment of the accident. The children exposed to the highest concentration of TCDD showed alterations in serum gamma-glutamyltransferase and alanine aminotransferase activity compared with the control group. These differences were restricted to values inside limits set from the lower end of the normal range to slightly above it. The observed abnormalities were slight and disappeared with time.
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PMID:Clinical laboratory manifestations of exposure to dioxin in children. A six-year study of the effects of an environmental disaster near Seveso, Italy. 287 2

Serial blood samples were obtained from 16 Standardbred foals from time of birth to postpartum day 28. Sera were obtained and analyzed for gamma-glutamyltransferase (GGT), aspartate transaminase, and immunoglobulin (Ig) G. Presuckle colostrum from the respective mares of these foals was analyzed for GGT activity. Mean serum aspartate transaminase activities were significantly increased above presuckle values by postpartum hour 48 (P less than 0.01) and increased gradually over the first 14 days. Mean serum IgG concentrations were significantly greater than presuckle values by 5 hours after foals first suckled (P less than 0.01) and remained significantly increased during the 28-day sampling period. Serum GGT activity did not differ significantly over the period sampled. The SD were large, since there was a large degree of interindividual variation. Serum GGT activity in the foals was significantly increased over that in the mares throughout the period of the study. The profile of serum GGT activity over time in each foal did not show a pattern of change. There was no postsuckle increase in serum GGT activity nor a correlation between serum GGT activities and IgG concentrations at 24 hours after foals first suckled. Evidence was not obtained to support a colostric source of GGT involved in the increase of serum GGT activity in foals. Serum GGT activity seems to be increased in foals due to endogenous sources.
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PMID:Increase of serum gamma-glutamyltransferase in neonatal Standardbred foals. 287 35

The average biological intra-individual CV in 20 patients with chronic liver diseases (CLD), estimated for 14 analytes during a stationary phase, significantly exceeded that for a normal group in the cases of Na+, K+, Cl-, total protein, albumin, cholinesterase, hemoglobin, and alpha-amylase; it did not differ significantly from the normal group for cholesterol, alkaline phosphatase, aspartate aminotransferase, and alanine aminopeptidase; and it was significantly lower than in the normal group for alanine aminotransferase and gamma-glutamyltransferase. There were no significant sex-related differences in mean intra-individual variation in CLD patients. Individual values were gaussian-distributed for all analytes, including enzymes. The estimated biological component of intra-individual variation and the analytical variation as determined for each laboratory can be used to derive decision-making criteria in monitoring CLD.
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PMID:Intra-individual variation of analytes in serum from patients with chronic liver diseases. 288 11


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PMID:Peripheral markers in the female "hidden alcoholic". 288 89

Glucuronidation of 4-nitrophenol, nopol (a monoterpenoid alcohol) and bilirubin, which in the rat, are catalyzed by three different enzymes, has been examined in liver biopsies from patients with various liver diseases, in particular cholestasis. These different activities were not correlated, which strongly suggests that at least three independently regulated forms of UDP-glucuronosyltransferases were present in the microsomes. Non ionic detergents (Triton X100, Emulgen 911) and deoxycholate produced similar activation (more than 2-fold) of the glucuronidation of 4-nitrophenol. Amphipathic substances, such as CHAPS (3-[3-cholamidopropyl-dimethylammonio]-1-propane sulfonate), and lysophosphatidylcholines maximally increased this UDP-glucuronosyltransferase activity, the most potent being oleoyl lysophosphatidylcholine (4-fold increase). Discriminant analysis of the data revealed no correlation between the three different UDP-glucuronosyltransferase activities and the age or sex of the patients. A good correlation was found on multidimensional analysis between form 1 of the enzyme (4-nitrophenol glucuronidation) and, in decreasing order of magnitude, epoxide hydrolase (measured with benzo(a)pyrene-4,5-oxide as substrate), cytochrome P-450, 7-ethoxycoumarin deethylase, aspartate aminotransferase and gamma-glutamyltransferase (r = 0.89); and between Form 3 of the enzyme (bilirubin glucuronidation) and NADPH cytochrome c reductase, alkaline phosphatase, (r = 0.81). These relationships may reflect the differential variation in enzymatic activities in various hepato-biliary diseases.
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PMID:Properties of human hepatic UDP-glucuronosyltransferases. Relationship to other inducible enzymes in patients with cholestasis. 288 32

We evaluated the performance of the Kodak DTSC Module for determination of alanine aminotransferase (ALT; EC 2.6.1.2), aspartate aminotransferase (2.5.1.2), alkaline phosphatase (3.1.3.1), creatine kinase (2.7.3.2), gamma-glutamyltransferase (2.3.2.2), and lactate dehydrogenase (1.1.1.27). The DTSC is a "special chemistry" accessory for the DT60 analyzer; the same multilayer film technology as that of the Ektachem 700 is used. The overall precision, assessed over a three-month period with two serum-based quality control materials, ranged from 2.2 to 8.0%. DTSC results for patients' specimens correlated well with those by the Technicon RA-1000 analyzer. The performance of the analyzer in linearity and interference studies was satisfactory for clinical use. The DTSC is simple to operate and has no technique-dependent step; it should be useful for the physician's office laboratory.
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PMID:Measurement of six enzymes with the Kodak DTSC Module, a physician's office analyzer. 288 44

We evaluated the Kodak Ektachem DT60/DTSC and the Boehringer Mannheim Reflotron for measuring activity concentrations of six enzymes. The Ektachem CVs for low concentrations of aspartate aminotransferase and alanine aminotransferase were high. As compared with the Ektachem and a routine "wet-chemistry" system, values for aspartate aminotransferase and alanine aminotransferase were lower as measured by the Reflotron, because no pyridoxal 5'-phosphate is included in the Reflotron slides. Activity concentrations of gamma-glutamyltransferase and creatine kinase measured with the Ektachem and with the routine procedure did not agree well, possibly because the Ektachem gave too-high results for the enzyme activities. Assays of several commercial test sera indicated that test results by the dry-chemistry and routine procedures are not interconvertible. This contrasts with our previous experience, in which between-test agreement for several analytes was acceptable.
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PMID:Two dry-reagent systems evaluated for determinations of enzyme activities. 289 95

This study provides quantitative toxicological data on potassium dichromate-induced renal damage and considers the possible difficulties arising from the non-invasive in vivo assessment of renal damage, with particular attention to enzymuria. Renal damage induced in male Wistar rats by single sc injections of potassium dichromate was assessed 52 to 72 hr after doses ranging from 3 to 20 mg potassium dichromate/kg body weight and throughout a 9-day period following a dose of 20 mg potassium dichromate/kg. The earliest and most sensitive non-invasive functional change in the dose-response and time-response studies was an elevation in the rate of urinary excretion of protein. Evidence of tissue damage was observed with elevations in the urinary excretion rates of the brush border enzymes, gamma-glutamyltransferase, alkaline phosphatase and leucine aminopeptidase, the cytosolic enzymes, aspartate aminotransferase and lactate dehydrogenase and the lysosomal enzyme, N-acetyl-beta-D-glucosaminidase. Such changes occurred as early as the abnormal urinary protein excretion, but returned to control or sub-control values sooner. Urinary brush border enzyme excretion returned to control values within 48 hr following potassium dichromate injection, despite histological and histochemical evidence of extensive renal damage and renal dysfunction. Elevations in plasma aspartate aminotransferase and lactate dehydrogenase levels were observed, but histochemical and isoenzyme studies would be needed to determine the source of these increases. The simplest and most persistent indicators of renal damage were the urinary excretion of protein and N-acetyl-beta-D-glucosaminidase.
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PMID:Dose-response and time-response biochemical and histological study of potassium dichromate-induced nephrotoxicity in the rat. 289 38

Solid phase chemistry can be used for clinical analysis at the bedside, and it is even applicable to whole blood. We compared precision, accuracy, method linearity, and practicability of two solid phase chemistry analysers. Reflotron (Boehringer Mannheim, W. Germany) and Ektachem DT 60 (Eastman Kodak Co, USA). Eight analytes, glucose, cholesterol, triacylglycerols, urea, uric acid, alanine aminotransferase, aspartate aminotransferase, and gamma-glutamyltransferase were investigated. The precision of both instruments was good. Coefficients of variation for within run and day to day precision were below 10% for all analytes. Methods were compared by analysing 88 to 105 patients sera for each investigated analyte on Reflotron, on Ektachem DT 60 and on a wet chemistry reference instrument. Linear regression analysis showed good agreement between wet chemistry and solid phase chemistry results. Coefficients of correlation (r) ranged from 0.957 to 0.999. Reflotron and Ektachem are desk top analysers. Reflotron is the smaller instrument. Currently, it offers 9 analytes and rapid single test performance. Whole blood can be used for all tests. Test strips can be stored at room temperature. Ektachem DT 60 has a modular design, and 22 analytes are available. Series of up to 100 tests per hour are possible. Whole blood can be used for the preparation of glucose and haemoglobin test slides. The slides must be deep frozen for prolonged storage. Reflotron may be suitable for the physician's office, Ektachem for small laboratories. The problem of quality control has not yet been satisfactorily solved for either instrument, as only analyser-specific control specimens can be used. Reagent costs of solid phase chemistry tests are high, especially when large test series are performed. Operation of both instruments requires well trained personnel.
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PMID:Comparison of two solid phase chemistry systems: Reflotron and Ektachem DT 60. 289 3


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