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)

Male Sprague-Dawley rats were treated with a single ip injection of dimethyl sulfoxide (DMSO), phenanthrene, nitrated products of phenanthrene, pyrene, or nitrated products of pyrene. Phenanthrene, pyrene and their nitrated products were dissolved in DMSO. Phenanthrene produced a significant elevation of serum aspartate aminotransferase (AST) and alanine aminotransferase (ALT) levels relative to DMSO-injected rats 24 hr after injection. Gamma-glutamyl transpeptidase (GGTP) levels were significantly increased for groups treated with phenanthrene when compared with the DMSO group 72 hr after injection. Nitrated products of phenanthrene produced a significant elevation of serum AST, ALT, sorbitol dehydrogenase (SDH), and GGTP levels when compared with groups treated with DMSO and phenanthrene 24 hr after injection. Four of six rats in the nitrated phenanthrene treatment group died between 48 and 72 hr after the injection. Injection of pyrene caused no significant increases in serum enzyme activities. Significant changes in the serum AST, SDH and LDH levels were observed with the nitrated products of pyrene at 24 hr. Only SDH levels were significantly different when pyrene and its nitrated products were compared. No significant differences were detected at 72 hr with the nitrated products of pyrene. As supported by serum chemistry, this study suggests that the products of the reaction of NO2 with two model polynuclear aromatic hydrocarbons (PAH) are hepatotoxic. Both pyrene and phenanthrene form nitrated products that are more toxic than the parent PAH, but the nitrated products of phenanthrene appear to be more toxic than the nitration products of pyrene.
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PMID:Toxicity of polycyclic aromatic hydrocarbons. II. Effect of NO2-nitrated phenanthrene and pyrene on blood chemistry in rats. 382 71

The effects of sodium selenite on bromobenzene hepatotoxicity were examined in male rats. Rats pretreated with sodium selenite (12.5 or 30 mumol/kg, ip) 72 hr prior to injection of bromobenzene (7.5 mmol/kg, ip) showed a marked reduction in bromobenzene-induced liver injury as evidenced by decreased plasma alanine and aspartate transaminase values, sorbitol dehydrogenase activity, and reduced histologic damage. Administration of bromobenzene did not affect the selenium content of blood or liver. At 72 hr after treatment with selenite, hepatic reduced (GSH) and oxidized (GSSG) glutathione values or GSH synthetic and degradation enzyme activities were not altered. However, from 3 to 12 hr following bromobenzene administration, hepatic GSH and cysteine amounts declined less rapidly in selenite-treated rats compared to control. Thus, acute selenite treatment ameliorated bromobenzene hepatotoxicity in a manner suggesting facilitation of hepatic GSH production by selenite for use in bromobenzene detoxication.
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PMID:Effect of sodium selenite upon bromobenzene toxicity in rats. I. Hepatotoxicity. 396 15

A trotter stallion showing symptoms of emaciation was suspected of disease of the liver associated with cholestasis in view of clinical symptoms (poor appetite, sluggishness, jaundice and oedema) and the results of examination of the blood (increased concentrations of gamma-glutamyl, transpeptidase, sorbitol dehydrogenase, alkaline phosphatase, aspartate aminotransferase and markedly increased conjugated bilirubin). A specimen removed at biopsy of the liver revealed the presence of portal fibrosis and severe cholestasis. At autopsy, it was found that very extensive fibrosis of the pancreas (probably due to migrating larvae of parasites) had caused extrahepatic cholestasis accompanied by fibrosis of the liver. The lesions of the coronary border, which were also present in this horse, could not be accounted for.
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PMID:[Extrahepatic cholestasis due to pancreas fibrosis in a trotter]. 397 93

Pretreatment with Mn2+ is known to produce tolerance to Cd2+-induced lethality. This study was designed to determine the mechanism of tolerance to Cd2+-induced lethality and hepatotoxicity following Mn2+ pretreatment. Rats given 36 mumoles Cd2+/kg, i.v., died within 10-20 hr while only one of nine rats pretreated with Mn2+ (250 mumoles/kg, s.c., 48 and 24 hr prior to Cd2+ challenge) died. Ten hours after Cd2+, plasma aspartate aminotransferase and sorbitol dehydrogenase activities were elevated markedly, and extensive histopathologic lesions of the liver were evident in control rats but not in Mn2+-pretreated rats. To examine the mechanism of this tolerance, distribution of Cd2+ to fourteen organs and the subcellular distribution in six organs were determined in control and Mn2+-pretreated rats. Two hours after challenge (31 mumoles Cd2+/kg, i.v., 0.75 microCi 109Cd2+/mumol Cd2+), the distribution of Cd2+ to liver markedly increased after Mn2+ pretreatment with concomitant decreases in other tissues. Mn2+ pretreatment also resulted in a marked difference in the hepatic subcellular distribution of Cd2+ with more present in cytosol and less associated with organelles. Gel-filtration chromatography indicated that most cytosolic Cd2+ was bound to a low molecular weight protein. Isolation and partial characterization of this protein suggest that it is identical to metallothionein (MT); it had a similar relative elution following gel-filtration chromatography, had low absorbance at 280 nm and, after separation into two isoproteins by DEAE A-25 anion exchange chromatography, had the same mobility after electrophoresis on non-denaturing polyacrylamide gels as Cd2+-induced metallothioneins. These data suggest that Mn2+ pretreatment reduces Cd2+-induced hepatotoxicity by altering the hepatic subcellular distribution of Cd2+ with more Cd2+ binding to MT in the cytosol. This decreased hepatotoxicity is probably responsible for tolerance to Cd2+-induced lethality.
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PMID:Mechanism of manganese-induced tolerance to cadmium lethality and hepatotoxicity. 399 53

Vitamin D-depleted and vitamin D-replete rats were treated with allyl alcohol (AA) or bromobenzene (BB). The severity of the hepatotoxicity was evaluated by the serum concentrations of aspartate aminotransferase, alanine aminotransferase and sorbitol dehydrogenase, the histomorphological appearance of the lesions, and the amount of cytochrome P-450 destroyed. The activity of the monooxygenases was also evaluated. All parameters indicated that vitamin D depletion alone did not lead to any signs of liver toxicity nor did it modify the pattern of toxicity of either AA or BB. However, the intensity of the response in the periportal (AA treatment) and in the centrilobular (BB treatment) zones was modified by the depletion. Vitamin D depletion was accompanied by increased hepatic damage due to AA while BB resulted in less hepatic damage in vitamin D-depleted compared to vitamin D-replete animals. The metabolic profile of the liver mixed function oxidases indicated that its intraacinar distribution was modified by the depletion. Although the overall activity toward the substrates studied was not changed by vitamin D depletion, two out of the three enzyme activities studied suggested that vitamin D-depleted rats were poorer "centrilobular metabolizers" and better "periportal metabolizers" than vitamin D-replete rats. These observations correspond to increased periportal and decreased centrilobular toxicity in vitamin D-depleted animals. These results suggest that vitamin D depletion associated with severe hypocalcemia may be associated with an intraacinar modulation of enzyme systems as well as with an intraacinar difference in the susceptibility of the liver to certain chemicals.
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PMID:Comparative hepatic response to bromobenzene and allyl alcohol in the vitamin D-replete and vitamin D-depleted rat. 399 32

The electrophoretic separations of some human and pig liver enzymes on cellulose acetate and Cellogel were investigated, with reference to their joint occurrence in serum of patients undergoing treatment by extracorporeal pig liver perfusion. In every case it was possible to distinguish between the human and pig enzymes. Pig lactate dehydrogenase isoenzymes occupy a position slightly anodic to the corresponding human bands. The aspartate transaminase band of human is more anodic than that of pig, but their cathodic bands have the same mobility. Alanine transaminase of both human and pig liver extract is shown to exist as two bands each towards the anode. The faster moving human band is more anodic than the corresponding pig band, while the other human band is less anodic. Sorbitol dehydrogenase, alkaline phosphatase, and ornithine carbamoyltransferase all exist as one band each. Human sorbitol dehydrogenase is more cathodic than the pig enzyme, human alkaline phosphatase more anodic than the pig enzyme, while human ornithine carbamoyltransferase is less anodic than the pig enzyme.
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PMID:Electrophoretic separation and differentiation of enzymes from human and from porcine liver. 504 73

The effects of a diet containing a high proportion of rapeseed meal on the activity of certain plasma enzymes were studied in laying birds. The enzymes studied were alkaline phosphatase (AP), aspartate transaminase (AST), L-gamma-glutamyl-transferase (gamma-GT), isocitrate dehydrogenase (ICDH), leucine arylamidase (LAP), malate dehydrogenase (MDH) and sorbitol dehydrogenase (SDH). No notable differences were observed between the plasma AP, LAP or SDH activities of the birds given the rapeseed meal and the birds receiving a soyabean meal control diet throughout the experiment. However, the plasma AST and gamma-GT activities of the treated birds showed slight elevations while their plasma ICDH and MDH activities showed more marked elevations, which are indicative of liver damage, in response to the diet. Macroscopic observations of the livers of the birds at the end of the experiment were in fairly good accord with the elevation in plasma ICDH and MDH activities noted for the individual birds.
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PMID:Plasma enzyme activities indicative of liver cell damage in laying fowl given a diet containing 20 per cent of rapeseed meal. 610 67

Feeder pigs weighing 12 to 15 kg each were given a single oral dose of aflatoxin, 1.2 mg/kg of body weight. Liver-specific serum enzyme activities were compared with gross, microscopic, and ultrastructural hepatic changes in individual pigs euthanatized at 24, 48, and 72 hours after they were given aflatoxin. The greater the morphologic change in liver of the treated pigs, the greater the increase in liver-specific serum enzyme activities. Isocitric dehydrogenase, alkaline phosphatase, sorbitol dehydrogenase, and aspartate aminotransferase activities increased in 6 of 8 treated pigs by 24 hours. Increase in gamma-glutamyl transpeptidase activity was not significant. Microscopic and ultrastructural changes in centrilobular hepatocytes included glycogen deletion, mitochondrial and endoplasmic reticulum swelling, membrane disruption, and nuclear fragmentation at 24 hours. The centrilobular areas had marked extravasation of erythrocytes at 24 hours without basal lamina changes. At 72 hours, the centrilobular hepatocytes had increased lipid vacuoles and acceptable amounts of glycogen. Marked infiltrations of monocytes, plasma cells, and lymphocytes were also present at this time.
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PMID:Acute aflatoxicosis in swine: clinical pathology, histopathology, and electron microscopy. 612 94

The activities of aspartate aminotransferase (AST), alanine aminotransferase (ALT), ornithine carbamoyltransferase (OCT), sorbitol dehydrogenase (SDH), gamma-glutamyl transferase (GGT), alkaline phosphatase (AP), lactate dehydrogenase (LDH) and creatine kinase (CK), were determined in eight organs of 10 healthy male blue foxes. OCT was absolutely liver specific and ALT was also found to be liver specific. SDH was also found primarily in the liver but its activity was relatively low. GGT was found almost exclusively in the kidneys. The highest levels of AP were observed in the kidneys and in the intestines. LDH together with AST was present in high activities in all the tissues tested. CK activity was highest in skeletal and cardiac muscles.
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PMID:Activities of some enzymes in the tissues of the blue fox (Alopex lagopus). 613 May 87

Serum alkaline phosphatase (ALP), gamma-glutamyl transferase (GGT), 5'nucleotidase (5'NT), sorbitol dehydrogenase (SDH), and aspartate transaminase activities were measured in 10 clinically healthy foals, 10 yearlings, and 10 two-year-old Quarter Horses. Enzyme activities in foals at 0.5 to 3 days, 2 to 3 weeks, and 5 to 7 weeks of age were compared with enzyme activities from yearling and 2-year-old horses. Multivariate analyses of variance revealed significantly higher enzyme values in foals (P less than 0.002). This increase was mainly a result of higher ALP and GGT activities, with lesser effects due to higher SDH and 5'NT activities. Standard deviations for ALP and GGT were also larger in foals than in adult horses. The wide variation of ALP and GGT activities may limit their usefulness in the diagnosis of hepatic disease in foals. Standard deviations for serum AST, SDH, and 5'NT activities were smaller. These enzymes may be indicators of hepatobiliary disease in foals. The high serum enzyme activities in healthy foals may reflect a physiologic difference between foals and adult horses. Relative hepatic mass (as a percentage of body weight) and enzyme activity per gram of hepatic tissue are high in young animals, indicating that the high serum enzyme activities in foals are due partly to a high rate of enzyme production and release.
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PMID:Effect of age on liver enzyme activities in serum of healthy quarter horses. 614 23


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