Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.6.1.2 (alanine aminotransferase)
 26,722 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

High concentration of inorganic phosphate in the culture medium of Aspergillus fumigatus inhibited ergot alkaloid synthesis. Addition of L-tryptophan but not mevalonate or 5-methyltryptophan to the above culture restored the alkaloid synthesis to the level found in normal cultures. The decrease in alkaloid synthesis in the fungus accompanies an increase in cell mass, cellular protein and sterol content. Aspartate aminotransferase and alanine aminotransferase activities were significantly increased in the high-phosphate culture.
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PMID:Effect of phosphate on ergot alkaloid synthesis in Aspergillus fumigatus. 33 88

Coenzymes participate in many of the enzyme analyses performed in the clinical laboratory. Supplementation of assay systems with optimal levels of coenzymes has recently been recommended as part of efforts to achieve interlaboratory standardization of enzyme measurements. Aspartate aminotransferase and alanine aminotransferase require pyridoxal phosphate for expression of enzyme activity. The role of this coenzyme in enzymatic transamination and the effects of its supplementation on the clinical estimation of these two enzymes is reviewed. Other coenzymes discussed are flavins, coenzymes for glutathione reductase, glucose oxidase, cholesterol oxidase and diaphorase, as well as thiamine pyrophosphate, coenzyme for transketolase. Catalase and peroxidase are used as examples of hemoproteins utilized in clinical measurements. Two peptide coenzymes, colipase and glutathione, are also considered. Measurement of apoenzyme stimulation upon supplementation with specific coenzymes is discussed as a valuable technique for quantitative coenzyme measurements or assessment of vitamin nutritional status.
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PMID:Review: the role of coenzymes in clinical enzymology. 33 88

Twenty calves were infected with 1000 metacercariae of Fasciola hepatica, the activities of 10 enzymes in plasma or serum were assayed and concentrations in serum of proteins, urea and bilirubin were determined. These values were compared with control data obtained from 14 uninfected calves. Aspartate aminotransferase, lactate dehydrogenase, sorbitol dehydrogenase, glutamate dehydrogenase, ornithine carbamoyl transferase and gamma-glutamyl transpeptidase activities increased in infected calves. Total serum protein increased, albumin decreased, globulin increased and the albumin/globulin ratio was decreased in infected calves. Plasma alanine aminotransferase, leucine aminopeptidase, alkaline phosphatase and cholinesterase activities and serum concentration of urea and bilirubin were unaffected. It was concluded that glutamate dehydrogenase and gamma-glutamyl transpeptidase were the most sensitive indicators of liver cell damage in fascioliasis.
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PMID:Biochemical indicators of liver injury in calves with experimental fascioliasis. 83 11

The rate of distribution of cell enzymes between the intravascular and extravascular space was studied, following a sudden decrease of enzyme activities in plasma. This rapid decrease of enzyme activities was achieved in rats by a rapid exchange of the blood with a twofold volume of a suspension of homologous erythrocytes in isoosmolar bovine serum albumin solution. After this plasmapheresis, the activities of seven cell enzymes in the plasma were decreased to 14 to 22% of their original values. The subsequent increase in activities showed different kinetics, depending on the enzyme. After 120 min, creatine kinase had reached the starting activity; malate dehydrogenase and aldolase reached their original activities after 180 min. Aspartate aminotransferase, glutamate dehydrogenase, alanine aminotransferase and pyruvate kinase increased more slowly and they had still not reached their starting values after 240 min. Repetition of the plasmapheresis after 90 min had no obvious effect on the kinetics of the subsequent activity increase. During the first minutes after plasmapheresis the adjustment of the activity equilibrium between the interstitial and the intravascular compartments depends mainly on the capillary permeability. It is therefore possible to determine half-life constants for the distribution of enzymes within the extracellular space. The constants for malate dehydrogenase and aldolase are almost identical with those determined by intravenous injection, whereas there are discrepancies in the constants for the remaining enzymes. The constants for pyruvate kinase and glutamate dehydrogenase are significantly lower, while those for aspartate aminotransferase, alanine aminotransferase and creatine kinase are significantly higher, than those determined after intravenous injection. Possible reasons for these differences are disucssed.
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PMID:[Plasmapheresis as an experimental model for studies on the extracellular distribution of enzymes. Distribution and transport of cell enzymes within the extracellular space. IV (author's transl)]. 93 47

An acute or fulminant adenovirus hepatitis developed in 5 of 224 pediatric patients who were recipients of orthotopic liver transplants. All had received prednisolone, azathioprine, and cyclosporine as basal immunosuppression, and four received monoclonal (OKT3) or polyclonal (antithymocyte globulin) antibodies for steroid-resistant rejection episodes. These patients initially had high fever and a worsening condition for a mean of 73 days after transplantation (range 44 to 140 days). Results of biochemical tests showed very high serum levels of lactate dehydrogenase. Aspartate aminotransferase values were always markedly more elevated than those of alanine aminotransferase. Two patients had severe leukopenia. Results of histologic studies of the liver showed extensive areas of confluent necrosis and targetlike hepatocyte nuclei. Typical intranuclear viral inclusions were observed on electron microscopy. Adenovirus was cultured in all patients and in two relatives. Two patients died of liver failure; others recovered after cessation of immunosuppression. We conclude that adenovirus hepatitis can be fatal in liver transplant recipients. There is no specific treatment, and immunosuppression must be discontinued.
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PMID:Acute adenovirus hepatitis in liver transplant recipients. 173 Oct 21

Rats were pretreated with a single iv dose of chlorpromazine (CPZ) 3 mg/kg, verapamil 1 mg/kg, or quinacrine 2 mg/kg. Livers were taken out and perfused with University of Wisconsin (UW) preservation solution and stored on ice for 48 h in the UW solution before reperfusion with erythrocyte-free and colloid-free Krebs-Hanseleit buffer at 38 degrees C in a nonrecirculating perfusion system for 2 h. CPZ- and quinacrine-pretreated livers produced significantly more bile than control livers and also released significantly less alanine aminotransferase into the perfusate at 30, 60, and 120 min of reperfusion. Aspartate aminotransferase levels were lower at 30 and 60 min of reperfusion for CPZ-pretreated livers but not at 120 min. The only difference between groups concerning lactate dehydrogenase (LDH) release into the perfusate was that CPZ decreased the amount of LDH released at 60 min. Total tissue water or tissue electrolyte content of the liver tissue at the end of the reperfusion did not differ between groups. In conclusion, verapamil was ineffective when given as single dose iv pretreatment to the liver donor but pretreatment with CPZ or quinacrine appeared to improve the function of the preserved liver.
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PMID:Chlorpromazine, quinacrine, and verapamil as donor pretreatment in liver preservation, tested in the isolated perfused rat liver. 175 29

Patients with severe Lassa fever have high serum levels of liver enzymes. Studies of the histology of the liver have shown only minor alterations, seemingly insufficient to account for death. Pichinde virus is an arenavirus which causes severe illness similar to Lassa fever in strain 13 guinea pigs, but does not cause severe illness in man. This can serve as a relatively safe model for studying the pathology and pathophysiology of fatal arenaviral infection. We used this infection to evaluate the effect of arenavirus on liver morphology and function. When guinea pigs were infected with Pichinde virus, all developed severe disease and died within 14 days of infection. The animals lost large amounts of weight. Higher levels of virus were detected in the liver than in serum. Aspartate aminotransferase and alanine aminotransferase were elevated late in the course of the disease; no elevations were seen in gamma glutamyl transpeptidase or bilirubin. Alkaline phosphatase, initially high in these growing animals, was markedly decreased early in infection. Prothrombin time and activated partial thromboplastin time were increased late in the disease, and decreased levels of Factors VIII and IX were seen relatively early. Fatty metamorphosis, indicating problems in lipid processing, occurred by day 11, but necrosis was minor and occurred late. Pichinde virus infection results in significant alterations in the metabolic and synthetic capacities of the hepatocytes early in infection in the absence of significant necrosis.
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PMID:The effect of an arenavirus infection on liver morphology and function. 197 92

Aspartate aminotransferase, alanine aminotransferase and gamma-glutamyl transferase activities were measured in sera from 411 diabetic outpatients and were raised in 26 (6.4%), 34 (8.3%) and 62 (15.2%) patients, respectively. Serum total bile acid concentrations were raised in 4 patients (1%). Percentage glycated hemoglobin A1, serum fructosamine concentration and plasma glucose concentration were also measured. No relationship between the presence of raised enzyme activity and mature age, short duration of diabetic treatment regimen or glycemic control was found. Twenty-six patients with an alanine aminotransferase activity greater than 60 U/l were reviewed at 23 +/- 6.5 weeks. The activity of this enzyme had fallen to within the reference interval in 15 (58%). In the other 11 patients, its median activity was 75 U/l (range 51-181 U/l). Median gamma-glutamyl transferase activity had risen in these 11 patients from 78 U/l to 93 U/l (P less than 0.01). No statistical differences in treatment regimen or glycemic control were found between these two groups. Raised liver-associated enzyme activity in treated stabilised diabetic outpatients should therefore not be attributed to poor glycemic control or diabetic treatment regimen.
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PMID:Raised liver associated enzyme activity and post-prandial bile acid concentrations in sera from treated diabetic outpatients. 197 26

In human liver, unlike in rat liver, there is no apparent acinar heterogeneity of total cellular activity of phosphoenolpyruvate carboxykinase [Wimmer, Luttringer & Columbi (1990) Histochemistry 93, 409-415]. Since the intracellular compartmentation of phosphoenolpyruvate carbonxykinase differs in rat and human liver, we examined the acinar heterogeneity of cytosolic and organelle-bound activities of this enzyme in the guinea pig, which shows a more similar intracellular compartmentation of enzyme activity to human liver than does the rat. Cytosolic phosphoenolpyruvate carboxykinase activity was higher in periportal than in perivenous hepatocytes, whereas the organelle-bound activity was similar in the two cell populations. Aspartate aminotransferase and alanine aminotransferase activities showed a similar distribution to phosphoenolpyruvate carboxykinase, with a higher cytosolic activity in periportal than in perivenous hepatocytes but a similar organelle-bound activity in the two cell populations. Data on the acinar zonation of enzymes determined in whole cells or tissue should be interpreted cautiously if the enzyme activity is present in more than one subcellular compartment.
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PMID:Acinar zonation of cytosolic but not organelle-bound activities of phosphoenolpyruvate carboxykinase and aspartate aminotransferase in guinea-pig liver. 224 21

Aminotransferase activities were measured in the serum of two- to three-year-old Thoroughbred fillies and colts during a four week period of peak training for flat racing. Aspartate aminotransferase (AspAT, EC 2.6.1.1), mitochondrial aspartate aminotransferase (m-AspAT) and alanine aminotransferase (AlaAT, EC 2.6.1.2) activities in serum were measured and the relative proportions of apoenzyme and holoenzyme were determined. The aminotransferase activities were increased only slightly immediately following exercise. This small and immediate post exercise increase in activity did not vary greatly over the period of peak training. Measured in the presence of exogenous pyridoxal 5'-phosphate, mean enzyme activities (iu/litre at 30 degrees C) before exercise were: AspAT, 291; m-AspAT, 13; AlaAT, 18. After exercise they were: AspAT, 317; m-AspAT, 16; AlaAT, 23. Nearly all of the AspAT activity was present in the holoenzyme form (94 per cent holoenzyme) indicating excellent vitamin B6 status in these animals. Paradoxically, the AlaAT in serum from the same highly trained Thoroughbred horses was poorly saturated with pyridoxal phosphate, with nearly half of the AlaAT in most horses present in the inactive apoenzyme form (61 per cent that of holoenzyme). It is critical therefore, that exogenous pyridoxal phosphate be included in aminotransferase assays to determine the amounts of enzyme release into the peripheral circulation.
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PMID:Effects of exercise on serum amino-transferase activity and pyridoxal phosphate saturation in Thoroughbred racehorses. 236 10


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