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)

Rats were fed for 23 d diets adequate or deficient in vitamin B-6 and containing selenium as either sodium selenite, selenocysteine (SeCys) or selenomethionine (SeMet). They were then injected with 75Se of the same chemical form and killed 2 d later. Tissue deposition of stable and radiotracer selenium and the activity of glutathione peroxidase (GSHPx) were used to assess selenium utilization. Erythrocyte levels of selenium and GSHPx were lower in vitamin B-6--deficient animals for all forms of selenium; however, 75Se deposition in erythrocytes was not affected by vitamin B-6 status. The activities of cystathionine lyase, aspartate aminotransferase and selenocysteine lyase were lower in livers of vitamin B-6--deficient rats than in vitamin B-6--supplemented rats. The proportion of liver and kidney 75Se soluble in 5% trichloroacetic acid and 0.1 M 2-mercaptoethanol was consistently lower in vitamin B-6--deficient animals, but cation-exchange chromatography of tissue extracts did not identify a specific low-molecular-weight species. Tissue retention of 75Se provided as SeMet was increased in vitamin B-6--deficient animals, but the proportion of 75Se retained in muscle and liver as SeCys was significantly reduced. These findings suggest that the conversion of SeMet to a form available for GSHPx synthesis is reduced by vitamin B-6 deficiency.
J Nutr 1989 Dec
PMID:Effects of vitamin B-6 deficiency on selenium metabolism in the rat. 262 89

The health status of broilers fed diets with varying protein contents in the presence of ochratoxin A (OA) were evaluated using clinical-chemistry techniques for blood analysis. A completely randomized, 3 x 4 factorial design was utilized: 14, 18, 22, and 26% of dietary protein and 0, 2, and 4 mg/kg of OA. The broilers were raised to 3 wk of age, at which time blood was collected and various hematological parameters were evaluated. The serum was analyzed for various enzyme activities and for concentrations of metabolites and minerals using an automated, clinical-chemistry analyzer and an atomic-absorption spectrophotometer. Adding OA to the diets of broilers decreased the hemoglobin concentration, corpuscular volume, and the activity of serum alkaline and phosphatase but increased the activity of gamma-glutamyl transferase. Adding protein to the diet increased the activity of the serum aspartate aminotransferase, creatine kinase, and alkaline phosphatase. Adding OA to the diet of broilers decreased the concentrations of serum total protein, as well as the concentrations of albumen and cholesterol and increased the concentrations of serum creatinine and uric acid. The concentrations of serum total protein, albumin, urea nitrogen, and triglyceride were increased by adding protein to the diet. The concentrations of calcium, potassium, and inorganic phosphorus in the serum decreased when OA was added to the diet; but the concentrations of calcium and potassium content in the serum increased along with dietary protein. A regression analysis suggested that dietary protein was synergistic toward OA with regard to the blood levels of cholinesterase, lactate dehydrogenase, and glucose.(ABSTRACT TRUNCATED AT 250 WORDS)
Poult Sci 1989 Dec
PMID:Ochratoxin A and dietary protein. 2. Effects on hematology and various clinical chemistry measurements. 262 21

Toxin produced by Pasteurella multocida type D was investigated for its effect on serum complement and serum biochemistry in rats. Rats were given a sublethal single subcutaneous injection of D toxin equivalent to 0.2 microgram/kg of body weight. Serum obtained 1, 3, 5 and 7 days post-treatment was tested for complement activity, total bilirubin, aspartate aminotransferase (AST), alanine aminotransferase (ALT) and alkaline phosphatase (ALP). Serum complement titers were significantly elevated (P less than 0.05) at all times after injection of toxin compared to rats injected with diluent and tested at the same intervals. Bilirubin was decreased but both control and D toxin-treated rats had low concentrations of bilirubin in their sera. The other biochemical constituents measured had no consistent pattern that would indicate liver damage in the rats.
Vet Immunol Immunopathol 1989 Dec
PMID:Serum complement activity and serum enzymes in rats after a subcutaneous injection of toxin prepared from Pasteurella multocida type D. 262 1

Several subforms of cytosolic aspartate aminotransferase (AspATc) in the crude extracts of rat liver and kidney were separated by isoelectric focusing using immunoblotting and staining of activity to detect the enzyme protein and activity, respectively. Vitamin B6-deficiency resulted in decrease in the subforms with higher isoelectric points and increase in those with lower ones both in the liver and in the kidney. When pyridoxal phosphate was added to those preparations from vitamin B6-deficient rats, the isoelectric focusing pattern of kidney was recovered to the similar one to that of the controls. However, the liver preparation was affected only partially by the addition of PLP. The pattern of subforms was altered during in vitro incubation at 37 degrees C for 24 h in both liver and kidney preparations, and their patterns were very similar to that of liver preparation from VB6-deficient rats. The enzyme activity also decreased during this incubation, especially in preparations of the enzyme from the liver of vitamin B6-deficient rats. This loss of enzyme activity was not affected by addition of PLP alone, but was almost completely prevented by addition of substrate. The inactivation was recovered by addition of substrate and pyridoxal phosphate simultaneously. This finding suggests that the inactivation may be related with a conformational change around the catalytic site of the AspATc molecule.
J Nutr Sci Vitaminol (Tokyo) 1989 Dec
PMID:Increase in negative charge of cytosolic aspartate aminotransferase in vitamin B6 deficiency and during incubation. 263 35

Cholestatic liver injury was experimentally induced in rats by administration of chlorpromazine (CPZ). The peak activity of mitochondrial aspartate aminotransferase (AST) released in serum was found to precede the peak of total AST activity. The liver mitochondria obtained from rats treated with CPZ was fractionated into two subfractions: one containing the intermembrane space, and the other containing the matrix and the membranes. As a results, the relative activity of AST in the intermembrane space was significantly increased at 12 h after CPZ administration. This result suggests that mitochondrial AST, which is dominantly located in the mitochondrial matrix, transmigrated to the intermembrane space via the inner membrane under the effect of CPZ administration.
Kitasato Arch Exp Med 1989 Dec
PMID:Effect of chlorpromazine on transmigration of mitochondrial aspartate aminotransferase in rat liver. 264 Feb 58

Beating rat heart cultures were prepared in vitro and infected with Coxsackie B-2 virus. The cells were evaluated in the post-infected period for changes in cardiac enzymes, alterations in beating frequency and cytotoxicity as measured by chromium 51 (51Cr) release. The cardiac enzymes, lactate dehydrogenase (LDH) and aspartate aminotransferase (AST) were measured in infected and uninfected controls over a period of 120 h. Enzyme levels in the infected cells remained essentially the same for the first 42 h as compared to the controls. At this time, the LDH levels increased rapidly reaching 116 +/- 24.8 U/l while the controls remained at 46.9 +/- 9.7 U/l. Aspartate aminotransferase levels increased at a slower rate and obtained a level of 104 +/- 20.2 U/l compared to 66.6 +/- 13.2 U/l in the control. Visual evidence of cellular damage as measured by decreased beating frequencies and the appearance of cytopathic effect was first noted at 42 h post-infection. Complete loss of cardiac beats and maximal viral cytopathic effect occurred at 96 h post-infection. Cardiac cellular damage as measured by cytotoxicity assay was found to parallel those changes seen in cardiac enzymes. No significant changes in cytotoxicity were observed for the first 24 h; however, at 48 h increased release of 51Cr was noted and visual evidence of viral replication also was present. The cardiac enzyme changes noted in beating rat heart cells appear to be similar to those changes reported in patients with viral-induced myocardial disease.(ABSTRACT TRUNCATED AT 250 WORDS)
J Virol Methods 1985 Dec
PMID:Coxsackie B-2 virus infection in rat beating heart cell culture. 300 12

Reversible endotoxic shock was induced in adult rats by i.v. injection of Escherichia coli O111:B4 lipopolysaccharide (1.6 mg/100 g). The shock progression was evaluated by measuring serum glucose levels as well as activities of aspartate aminotransferase (GOT) and alkaline phosphatase in serum. A rapid increase of serum glucose levels occurs, after LPS injection, followed by hypoglycaemia (minimum values at 6 h) with progressive reversion to control values. Serum GOT activity increased (twofold) 6 h after endotoxin administration and returned to control values at 72 h. No appreciable changes occurred in serum alkaline phosphatase activity. Endotoxaemia produced a decrease in the cytochrome P-450 levels in all target organs considered: lung, adrenal glands and liver. The progressive decrease in the serum albumin concentration as well as changes of the physical properties of the plasma membranes observed in vivo, can not be explained only by direct interaction of endotoxin with the target organs, underlining the importance of serum mediators in the induction of the shock response.
Br J Exp Pathol 1988 Dec
PMID:Induction of reversible shock by Escherichia coli lipopolysaccharide in rats. Changes in serum and cell membrane parameters. 306

Because it remains debatable whether all patients with a clinical diagnosis of alcoholic liver disease should have a liver biopsy to help confirm the diagnosis, we evaluated the diagnostic value of liver biopsy in alcoholic liver disease. Studied were 108 consecutive patients who had a percutaneous liver biopsy for the first time. In all cases the patient's clinical diagnosis recorded before biopsy was compared with the histological diagnosis of an experienced histopathologist. Prebiopsy clinical data (reported alcohol intake, signs of chronic liver disease) and laboratory data (liver function tests, mean corpuscular volume, ferritin, hepatitis B serology) were reviewed. We found that a prebiopsy clinical diagnosis of alcoholic liver disease (n = 35) was confirmed by biopsy in all but one case. The prebiopsy diagnosis of alcoholic liver disease was significantly associated with a histological diagnosis of alcoholic liver disease (specificity 98%, sensitivity 79%). Individually, alcohol intake, signs of chronic liver disease, the alanine aminotransferase (ALT), the aspartate aminotransferase to ALT ratio, and the mean corpuscular volume were significantly associated with a histological diagnosis of alcoholic liver disease. When clinical and laboratory parameters were considered jointly using stepwise logistic regression, only reported alcohol intake and mean corpuscular volume were significant. Liver biopsy may not always be necessary for the identification of that broad group of patients with alcoholic liver disease.
J Clin Gastroenterol 1988 Dec
PMID:Diagnostic value of liver biopsy in alcoholic liver disease. 306 3

The effect of various proteases (trypsin, chymotrypsin, subtilisin, protease 401, and thermolysin) on the mitochondrial isoenzyme (m-AST) and cytoplasmic isoenzyme (c-AST) of human and swine aspartate aminotransferase (AST;EC 2.6.1.1) was evaluated. All procedures including the reaction with proteases and the subsequent determination of the AST activity were carried out in an automatic analyzer. The mammalian c-AST was efficiently inactivated by chymotrypsin, subtilisin and protease 401 while m-AST activity decreased very slowly with these proteases. Thermolysin and trypsin showed much less effect on c-AST activity. Especially, chymotrypsin at concentrations of 0.5-1.0 g/L inactivated human c-AST almost completely but showed no detectable inactivating effect on m-AST. Thus chymotrypsin appears to be the most suitable protease for the differential determination of AST isoenzymes in human serum. Further studies on the effects of proteases with AST from other species showed that Escherichia coli AST resembled mammalian m-AST while Pseudomonas AST resembled c-AST.
Clin Biochem 1988 Dec
PMID:Determination of human aspartate aminotransferase isoenzymes by their differential sensitivity to proteases. 306 46

Ursodiol, a naturally occurring bile acid, has gained Food and Drug Administration approval for the dissolution of cholesterol gallstones. Ursodiol inhibits hepatic cholesterol synthesis and secretion. Lithocholic acid, a potentially hepatotoxic metabolite of ursodiol and chenodiol, may accumulate to a lesser extent with ursodiol than with chenodiol. Enterohepatic recirculation of ursodiol and its metabolites occurs and is essential to the dissolution of cholesterol gallstones. Complete dissolution has been achieved in 17 percent of patients with noncalcified, radiolucent, floating, cholesterol gallstones. Recurrence of cholesterol gallstones may occur in over one-half of initial responders. Diarrhea reported in up to 50 percent of the patients on chenodiol has been reported in only 4 percent of patients treated with ursodiol. Increased mean aspartate aminotransferase levels to more than twice the pretreatment level seen with chenodiol therapy have not been reported with ursodiol. Reportedly fewer adverse reactions may give ursodiol a major advantage over chenodiol in hospital formulary considerations.
Drug Intell Clin Pharm 1988 Dec
PMID:Ursodiol: a cholesterol gallstone solubilizing agent. 307 72


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