Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Subcellular distribution and some physicochemical properties of alanine aminotransferase in striated muscles of the crayfish, trout, carp, frog, pigeon and rabbit were studied. It was established that: (1) Alanine aminotransferase activity in all mentioned animals occurred almost entirely in the cytosolic fraction of the muscles. Total activity and activity per mg protein were highest in crayfish and pigeon muscles and lowest in carp and trout muscles. (2) The pH optimum for the muscles of homoiotherms and poikilotherms ranged from 7.5 to 8, Km values for L-alanine were of the order 10(-3)--10(-2) M and those for alpha-ketoglutarate 10(-4) M. (3) A 10 degree C temperature increase of the incubation medium was accompanied by a 70--90% increase in activity. (4) The higher the alanine aminotransferase activity of the muscles, the relatively higher their alanine production during electrical stimulation. (5) From the above results it is concluded that alanine aminotransferase in striated muscles regulates the rate of glycolysis and energy production under conditions of anaerobiosis through the formation of alanine.
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PMID:Subcellular distribution and some properties of alanine aminotransferase in striated muscles of the crayfish, trout, carp, frog, pigeon and rabbit. 3 68

In the adult rat kidney, alanine aminotransferase (EC 2.6.1.2), aspartate aminotransferase (EC 2.6.1.1) and D-amino acid oxidase (EC 1.4.3.3) were measured in glomeruli, 4 parts of the proximal tubule, 2 parts of the distal tubule and in patches from the thin limb area and the papilla. These enzymes were measured in more limited parts of the nephron during postnatal development. Adult aspartate aminotransferase activities (percentage of the highest) ranged from 100 in the distal straight segment to 25 in the late part of the proximal straight segment to 10 in the thin limb and papillary area. Alanine aminotransferase (lower by a factor of 100 in absolute terms) was distributed as the mirror image of aspartate aminotransferase within proximal and distal tubules. D-Amino acid oxidase was 850-fold higher in proximal straight segments than in medullary structures. During development alanine aminotransferase increased 6-fold and D-amino acid oxidase, 4.5-fold in proximal straight tubules but aspartate aminotransferase increased in distal straight tubles 8-fold.
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PMID:Distribution of two aminotransferases and D-amino acid oxidase within the nephron of young and adult rats. 3 98

Alanine aminotransferase activity is present in mitochondria and the cell sap fraction of the rat myocardium. As distinct from the cell sap form, mitochondrial alanine aminotransferase was significantly inhibited by chloride ions, maleate and incubation medium temperatures of over 40 degrees C. Activity of the cell sap enzyme was inhibited by phosphate and stimulated by temperatures of over 40 degrees C. The pH optimum for cell sap alanine aminotransferase was in the region of 8, while for the mitochondrial enzyme it had a wider range (pH 7.3-8.2). D,L-penicillamine, and antagonist of vitamin B6, inhibited alanine aminotransferase activity equally in intact and tritonized mitochondria and in the cell sap fraction. The activity of mitochondrial and cell sap alanine aminotransferease rose in correlation to the stage of ontogenesis, the maximum increase being observed in the cell sap fraction 14-20 days after birth. The addition of coenzyme to the incubation medium did not affect the activity of either mitochondrial or cell sap alanine aminotransferase. The results indicate that there are two different alanine aminotransferase enzymes in the rat heart, with different intracellular localizations and probably with different regulative functions.
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PMID:Some properties of mitochondrial and cell sap alanine aminotransferase of the rat heart. 13 62

In an experimental study, employing anaesthetized dogs, it was investigated whether cellular enzymes from peripheral skeletal muscle get into the circulating blood by diffusion across capillary membranes or by lymphatic transport. In the experimental group 1, the animals were anaesthetized only. The plasma activities of the four enzymes measured--lactate dehydrogenase, aspartate aminotransferase, alanine aminotransferase, creatine kinase--did not show any mentionable change during a time period of 6 h. In group 2 one hind limb of each animal was moved passively for 1 h. Alanine aminotransferase remained unchanged in plasma, the activities of the three other enzymes increased significantly. In group 3 one hind limb was made hypoxic by clamping the femoral blood vessels for 1 h. No activity changes were observed. When the period of hypoxia was followed by a 1-hour period of passive movement in group 4, the alterations in plasma activities were almost identical to those observed in group 2. In group 5 the experimental procedure was as in group 4, in addition the lymph from the thoracic duct was quantitatively withdrawn. The enzyme activities in plasma revealed a tendency to decrease rather than increase. Lymph flow increased significantly as well as the lymphatic activities of those enzymes which have high intracellular activities in muscle. The results prove, that enzymes from muscle are transported from the interstitial into the intravascular compartment mainly by lymphatic transport. Indications were found that the interruption of blood flow in one hind limb did not result in an enzyme release from muscle cells. It is discussed how changes in lymph flow, occurring during physical exercise for example, affect enzyme activities in plasma.
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PMID:Lymphatic transport of cellular enzymes from muscle into the intravascular compartment. 45 37

Alanine aminotransferase activity in serum increases significantly when serum is incubated with pyridoxal phosphate. The increase depends on the L-alanine concentration in the final assay mixture, being greatest at 800 mmol/liter. Preincubation of 22 normal sera, in a 10:1 ratio with an 8.09 mmol/liter pyridoxal phosphate solution, resulted in an increase in the alanine aminotransferase activity from 10.5 +/- 4.9 U/liter (mean +/- SD) to 28.4 +/- 5.3 U/liter, an increase of 170%. The absolute amount of apoalanine aminotransferase is relatively constant over a wide range of enzyme activities.
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PMID:Activation of alanine aminotransferase in serum by pyridoxal phosphate. 83 80

The effects of interferon therapy on liver histologic findings were assessed in a randomized controlled trial consisting of 80 patients with chronic non-A,non-B hepatitis. Twenty-eight patients received 1 million units of recombinant interferon alpha-2b; 25 patients received 3 million units, subcutaneously, three times a week for 24 weeks; and 21 patients were observed as untreated controls; all of them underwent liver biopsy within 6 months from the beginning of the study and on the last day of therapy. Six patients were withdrawn from the study because of inadequate liver biopsy specimens. Alanine aminotransferase levels were determined before, during, and after therapy. For each biopsy, a semiquantitative score of histologic features, the histologic activity index, and the overall histologic assessment were performed. Ninety-five percent of patients tested positive for hepatitis C virus antibody. Portal inflammation, piecemeal and spotty necrosis, and bile duct proliferation were significantly decreased in patients with normalized alanine aminotransferase. The effectiveness of therapy was dose dependent: piecemeal and spotty necrosis and the histologic activity index showed a significant decrease only in 3-million-unit-treated patients. Hepatocellular degeneration and fibrosis did not change significantly after treatment.
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PMID:Histologic changes in liver biopsy specimens produced by recombinant interferon alpha-2b therapy for chronic non-A,non-B viral hepatitis. A randomized controlled trial. 141 21

Plasma alanine aminotransferase, aspartate aminotransferase, creatine kinase and alkaline phosphatase activities were studied in clinically healthy Danish landrace and dwarf kids in seven herds from birth to 12 months of age. The purpose was to evaluate the influence of age, breed and herd on reference values. The mean enzyme levels +/- standard deviation (s) in neonatal dwarf kids were 0.09 +/- 0.04, 1.23 +/- 0.24, 2.79 +/- 1.50 and 18.3 +/- 11.0 mu kat/l respectively. The respective values in landrace kids were 0.13 +/- 0.06, 1.06 +/- 0.22, 2.44 +/- 1.60 and 37.6 +/- 23.6 mu kat/l. In 8-12 months old dwarf kids they were 0.30 +/- 0.11, 1.49 +/- 0.13, 3.28 +/- 0.44 and 11.1 +/- 2.4 mu kat/l respectively and 0.23 +/- 0.05, 1.12 +/- 0.34, 3.68 +/- 1.63 and 14.1 +/- 8.40 mu kat/l respectively in landrace kids of the same age. The 5th to 95th percentile intervals of the enzyme activities were within mean +/- 2s for most age groups in both breeds except alkaline phosphatase. The means and medians were close to each other for the values of alanine aminotransferase, aspartate aminotransferase and creatine kinase but not for alkaline phosphatase. Alanine aminotransferase, aspartate aminotransferase and creatine kinase levels were low at birth and increased with age, whereas for alkaline phosphatase it was vice versa. Significant differences were observed in mean enzyme activities between kids of different ages (within breeds), breeds (in same age kids) and herds (within same breed and age kids). Sex variations (within the breeds) were not observed. It was concluded that plasma enzyme activities are dependent on age, breed and environment.
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PMID:Profile of some plasma enzyme activities in growing dwarf and landrace kids. 177 78

Ninety patients with histologically documented chronic non-A, non-B hepatitis were randomly allocated to receive SC injections of placebo or of 1 or 3 MU of recombinant interferon alfa-2b three times weekly for 24 weeks. Complete normalization of alanine aminotransferase levels occurred posttreatment in 43.3% of patients receiving 3 MU, in 20% of those receiving 1 MU, and in 6.7% of untreated patients (P less than 0.0005 vs. those treated with 3 MU). Alanine aminotransferase normalization was sustained for 6 months after therapy in 13.3% of the patients treated with 3 MU and in 3.3% of those given 1 MU or placebo. The decline of alanine aminotransferase levels following interferon therapy showed independent, positive correlations with female sex (P less than 0.03) and younger age (P less than 0.05). The Knodell's fibrosis score was strongly positively correlated with age (P less than 0.0001). It is concluded that 3 MU of interferon is a more effective dose than 1 MU for controlling disease activity in non-A, non-B chronic hepatitis patients. Women and younger and noncirrhotic patients are more likely to respond.
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PMID:Comparison of 1 or 3 MU of interferon alfa-2b and placebo in patients with chronic non-A, non-B hepatitis. 190 28

Alanine aminotransferase is an enzyme produced mainly in the liver. When serum activity is measured, it provides a marker of hepatic disease. This review explores the biochemistry and laboratory analysis of alanine aminotransferase in terms of its significance in human health and disease. Cut-off levels that define abnormality are rather arbitrary and this decreases the specificity of the test in apparently healthy patients. A small, but important, group of patients with alanine aminotransferase abnormality have underlying liver disease that may be treatable. Most can be diagnosed based on history, physical examination, and biochemical-serological profiles. Liver biopsy can complement the diagnostic process in selected circumstances. Literature pertaining to this is critically reviewed.
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PMID:Alanine aminotransferase in clinical practice. A review. 172 20

Because of the liver's dependence on arterial blood to exert its metabolic functions in cirrhosis of the liver, with or without thrombosis of the portal vein, the interruption of hepatic arterial flow for the palliative treatment of malignant tumors of the liver is counterindicated. However, the effects of arterial devascularization on the cholestatic liver are not fully understood. The objective of the present study was to investigate hepatic alterations due to hepatic artery ligation in rats with chronic extrahepatic cholestasis. Serum alkaline phosphatase, bilirubin and alanine aminotransferase were measured in rats 3 h after sham operation (group A, N = 29) or ligation of the hepatic artery (group B, N = 29). Alanine aminotransferase activity was significantly higher (P less than 0.05) in group B, demonstrating acute hepatocellular damage in animals with chronic extrahepatic cholestasis.
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PMID:Effect of hepatic artery ligation in rats with chronic extrahepatic cholestasis. 210 Oct 73


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