scholarly journals The effect of cytosine arabinoside and bromodeoxyuridine on the appearance of tyrosine aminotransferase in cultured foetal hepatocytes of the rat

1980 ◽  
Vol 188 (3) ◽  
pp. 929-932 ◽  
Author(s):  
G C Yeoh ◽  
I T Oliver
Keyword(s):  
Cell Differentiation ◽  
Rat Liver ◽  
Cytosine Arabinoside ◽  
Culture Medium ◽  
Tyrosine Aminotransferase ◽  
Aminotransferase Activity ◽  
Inhibitory Effects ◽  
Foetal Liver ◽  
Foetal Rat

1. The acquisition of dexamethasone-inducibility of tyrosine aminotransferase activity by hepatocytes cultured from 15-day-foetal rat liver is blocked in the presence of cytosine arabinoside. 2. Similar results are obtained in the presence of bormodeoxyuridine. 3. No effects on steroid-inducibility of tyrosine aminotransferase are obtained with either of the above compounds in hepatocytes cultured from 19-day-foetal liver. 4. the inhibitory effects of the agents are substantially reversed after their removal from the culture medium. 5. The effects of bromodeoxyuridine suggest that cell differentiation, with respect to tyrosine aminotransferase-inducibility, occurs in cultures of 15-day-doetal hepatocytes. 6. The effects of cytosine arabinoside suggest that such an event is dependent on mitosis.

scholarly journals Tyrosine aminotransferase induction in hepatocytes cultured from rat foetuses treated with dexamethasone in utero

1979 ◽  
Vol 180 (3) ◽  
pp. 545-549 ◽  
Author(s):  
G C T Yeoh ◽  
T Arbuckle ◽  
I T Oliver
Keyword(s):  
Culture Medium ◽  
Actinomycin D ◽  
Tyrosine Aminotransferase ◽  
In Utero ◽  
Aminotransferase Activity ◽  
Foetal Liver ◽  
Translational Block ◽  
Cells Cultured ◽  
Specific Mrna

1. The administration of dexamethasone to foetal rats in utero does not result in the appearance of specific tyrosine aminotransferase activity even after 24 h. 2. When foetal hepatocytes are cultured in vitro from animals treated in utero with dexamethasone, significantly higher activities of specific tyrosine aminotransferase are found than in untreated controls. 3. Dexamethasone in vitro induces specific tyrosine aminotransferase in cells cultured from control animals and the effect is maximal at 10 nM in the culture medium. 4. Actinomycin D at 0.2 microgram/ml in the culture medium completely prevents the induction of activity in vitro. 5. In cultures established from animals treated with dexamethasone in utero, the increase in specific tyrosine aminotransferase activity over the control cultures is only marginally decreased in the presence of actinomycin D. 6. The results can be interpreted to mean that dexamethasone in utero stimulates the transcription of enzyme-specific mRNA, which is not rranslated until a translational block in the foetal liver is removed by the conditions of culture in vitro.

scholarly journals Biphasic effect of acute ethanol administration on rat liver tyrosine-2-oxoglutarate aminotransferase activity

1980 ◽  
Vol 186 (3) ◽  
pp. 755-761 ◽  
Author(s):  
A A B Badawy ◽  
B M Snape ◽  
M Evans
Keyword(s):  
Enzyme Activity ◽  
Rat Liver ◽  
Actinomycin D ◽  
Tyrosine Aminotransferase ◽  
Ethanol Metabolism ◽  
Ethanol Administration ◽  
Aminotransferase Activity ◽  
Biphasic Effect ◽  
Initial Decrease ◽  
Acute Ethanol

1. Acute ethanol administration causes a biphasic change in rat liver tyrosine aminotransferase activity. 2. The initial decrease is significant with a 200 mg/kg dose of ethanol, is prevented by adrenoceptor-blocking agnets and by reserpine, but not by inhibitors of ethanol metabolism, and exhibits many of the characteristics of the inhibition caused by noradrenaline. 3. The subsequent enhancement of the enzyme activity by ethanol is not associated with stabilization of the enzyme, but is sensitive to actinomycin D and cycloheximide. 4. It is suggested that the initial decrease in aminotransferase activity is caused by the release of catecholamines, whereas the subsequent enhancement may be related to the release of glucocorticoids.

scholarly journals The development of gluconeogenesis in rat liver. Effects of glucagon and ether

1970 ◽  
Vol 120 (2) ◽  
pp. 385-392 ◽  
Author(s):  
Helen Philippidis ◽  
F. J. Ballard
Keyword(s):  
Rat Liver ◽  
Redox State ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Fold Increase ◽  
Similar Increase ◽  
Ether Anaesthesia ◽  
Foetal Liver ◽  
Foetal Rat ◽  
Newborn Animals

1. Administration of glucagon to foetal rats produced a 10–15-fold increase in hepatic phosphoenolpyruvate carboxykinase activity together with a similar increase in the overall pathway of pyruvate conversion into glycogen in liver slices. 2. Glucagon was without effect on gluconeogenesis in vivo, which remained at approx. 0.1% of the incorporation as measured in newborn animals. 3. The apparent discrepancy between these results was due to the ether anaesthesia that was required for experimentation in vivo. Under conditions when minimal ether was used, the rates of labelling of glycogen from [3-14C]pyruvate in vivo were increased 10–20-fold and there was an additional stimulus by glucagon. 4. Ether anaesthesia produced a more reduced redox state of the foetal liver cytosol and lowered the ATP/ADP concentration ratio. 5. It is proposed that these effects are significant in the limitation of gluconeogenesis in the foetal rat liver, so that only with high phosphoenolpyruvate carboxykinase activity, high ATP concentration and a relatively oxidized cytosol redox state will a functional gluconeogenic pathway be present.

scholarly journals The adaptive behaviour of isoenzyme forms of rat liver alanine amino transferases during development

1972 ◽  
Vol 128 (2) ◽  
pp. 403-413 ◽  
Author(s):  
Keith Snell ◽  
Deryck G. Walker
Keyword(s):  
Cyclic Amp ◽  
Rat Liver ◽  
In Utero ◽  
Adaptive Behaviour ◽  
Intragastric Administration ◽  
Aminotransferase Activity ◽  
Dibutyryl Cyclic Amp ◽  
Neonatal Development ◽  
Foetal Liver ◽  
Glyoxylate Aminotransferase

1. The activities of the mitochondrial and cytosol isoenzyme forms of l-alanine–glyoxylate and l-alanine–2-oxoglutarate aminotransferases were determined in rat liver during foetal and neonatal development. 2. The mitochondrial glyoxylate aminotransferase activity begins to develop in late-foetal liver, increases rapidly at birth to a peak during suckling and then decreases at weaning to the adult value. 3. The cytosol glyoxylate aminotransferase and the mitochondrial and cytosol 2-oxoglutarate aminotransferase activities first appear prenatally, increase further after birth and then rise to the adult values during weaning. 4. In foetal liver the mitochondrial glyoxylate aminotransferase and the cytosol 2-oxoglutarate aminotransferase activities are increased after injection in utero of glucagon, dibutyryl cyclic AMP (6-N,2′-O-dibutyryladenosine 3′:5′-cyclic monophosphate) or thyroxine. The cytosol glyoxylate aminotransferase and the mitochondrial 2-oxoglutarate aminotransferase activities are increased after injection in utero of cortisol or thyroxine. 5. After birth the further normal increases in the mitochondrial and cytosol 2-oxoglutarate aminotransferase activities can be hastened by cortisol injection, whereas the increase in cytosol glyoxylate aminotransferase activity requires cortisol treatment together with the intragastric administration of casein. 6. The results are discussed with reference to the metabolic patterns and the changes in regulatory stimuli (hormonal and dietary) that occur during the period of development.

scholarly journals Development of adenylate kinase isoenzymes in rat liver

1971 ◽  
Vol 122 (4) ◽  
pp. 553-555 ◽  
Author(s):  
R. Filler ◽  
W. E. Criss
Keyword(s):  
Rat Liver ◽  
Liver Cell ◽  
Adenylate Kinase ◽  
Energy Flow ◽  
Kinase Activity ◽  
Adult Liver ◽  
Foetal Liver ◽  
Foetal Rat ◽  
Wet Weight ◽  
Developing Rat

Total adenylate kinase activity was determined in developing rat liver. The activity was 18 units/g wet weight of tissue in foetal liver; this increased to 41 units/g immediately after birth and continued increasing until adult activities of 150 units/g were reached after two weeks. The adenylate kinase activity was separated into four isoenzymes. Only isoenzymes II and III were observed in foetal rat liver. Isoenzyme II activity was 2 units/g in the foetal liver and increased to 25 units/g in adult liver. Adenylate kinase III activity was 20 units/g in the foetal liver and increased to 118 units/g in adult liver. The possible role that adenylate kinase might have in regulating the energy flow in the developing liver cell is discussed.

scholarly journals Tryptophan aminotransferase activity in rat liver

1984 ◽  
Vol 220 (1) ◽  
pp. 341-344 ◽  
Author(s):  
J C Stanley ◽  
A R Nicholas ◽  
A J Dickson ◽  
I M Thompson ◽  
C I Pogson
Keyword(s):  
Rat Liver ◽  
Enzyme Induction ◽  
Tyrosine Aminotransferase ◽  
The Other ◽  
Aminotransferase Activity

By using an antiserum raised against rat liver tyrosine aminotransferase, it was shown that about 60% of tryptophan aminotransferase activity in rat liver extracts is catalysed by this enzyme. Induction of tryptophan aminotransferase activity by intraperitoneal injections of tryptophan or triamcinolone can be entirely attributed to the effects of these agents on tyrosine aminotransferase. The origin of the other 40% of tryptophan aminotransferase activity remains to be established. This activity increases after starvation for 48 h. It is unlikely that tryptophan transamination plays a quantitatively important role in the metabolism of tryptophan by the liver.

Diurnal variations in inducibility of rat liver tyrosine aminotransferase activity

Life Sciences ◽  
1978 ◽  
Vol 23 (12) ◽  
pp. 1301-1308 ◽  
Author(s):  
James A. Gurr ◽  
Robert S. Elvehjem ◽  
Van R. Potter
Keyword(s):  
Rat Liver ◽  
Tyrosine Aminotransferase ◽  
Diurnal Variations ◽  
Aminotransferase Activity

scholarly journals Ontogeny of the glucocorticoid receptor and its relationship to tyrosine aminotransferase induction in cultured foetal hepatocytes

1981 ◽  
Vol 198 (2) ◽  
pp. 301-307 ◽  
Author(s):  
M H Cake ◽  
G C T Yeoh ◽  
I T Oliver
Keyword(s):  
Glucocorticoid Receptor ◽  
Cytosine Arabinoside ◽  
Tyrosine Aminotransferase ◽  
Receptor Activity ◽  
Cultured Hepatocytes ◽  
Foetal Liver ◽  
Receptor Concentration ◽  
Steroid Responsiveness ◽  
Haemopoietic Cells ◽  
Rate Of Accumulation

The glucocorticoid receptor activity that can be detected in the liver from 15-day foetal rats would appear to be associated with the haemopoietic cells. In hepatocytes, purified by culture for 1-2 days from 15-day foetal rats, the glucocorticoid receptor activity is low and dexamethasone does not induce the enzyme tyrosine aminotransferase. If culture is continued both receptor activity and steroid responsiveness are acquired. Cultured hepatocytes from 19-day foetal liver contain receptor from the first day of culture and, furthermore, the subsequent level of response to glucocorticoids is directly correlated with the actual receptor concentration. It would appear that the glucocorticoid receptor is not acquired by hepatocytes until after 18 days of gestation. Nevertheless, the fact that bromodeoxyuridine has no effect on the rate of accumulation of receptor in hepatocytes suggests that the differentiative event leading to the subsequent appearance of the receptor has already occurred before day 15 of gestation. However, the acquisition of the receptor would appear to be dependent on mitosis as cytosine arabinoside can inhibit the process.

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