The effect of acute ethanol administration on the activity of membrane-bound enzymes of rat liver

1980 ◽  
Vol 12 (8) ◽  
pp. 739-749 ◽  
Author(s):  
Lanfranco Corazzi ◽  
Giuseppe Arienti ◽  
Giuseppe Porcellati
Keyword(s):  
Rat Liver ◽  
Ethanol Administration ◽  
Acute Ethanol ◽  
Membrane Bound ◽  
Membrane Bound Enzymes

Effects of ethanol administration on rat liver plasma membrane-bound enzymes

1985 ◽  
Vol 34 (15) ◽  
pp. 2685-2689 ◽  
Author(s):  
Jorge L. Gonzalez-Calvin ◽  
John B. Saunders ◽  
Ian R. Crossley ◽  
Christopher J. Dickenson ◽  
Heather M. Smith ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Rat Liver ◽  
Ethanol Administration ◽  
Liver Plasma Membrane ◽  
Membrane Bound ◽  
Membrane Bound Enzymes

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.

Transglutaminase activity in rat liver after acute ethanol administration

1995 ◽  
Vol 1245 (3) ◽  
pp. 371-375 ◽  
Author(s):  
Angela Sessa ◽  
Patrizia Tunici ◽  
Edoardo Perilli ◽  
Antonio Perin
Keyword(s):  
Rat Liver ◽  
Ethanol Administration ◽  
Transglutaminase Activity ◽  
Acute Ethanol

scholarly journals Effects of acute ethanol administration on rat liver 5-aminolaevulinate synthase activity

1989 ◽  
Vol 262 (2) ◽  
pp. 491-496 ◽  
Author(s):  
A A B Badawy ◽  
C J Morgan ◽  
N R Davis
Keyword(s):  
Alcohol Dehydrogenase ◽  
Rat Liver ◽  
Intraperitoneal Administration ◽  
Reciprocal Relationship ◽  
Ethanol Administration ◽  
Simultaneous Increase ◽  
Acute Ethanol ◽  
Tryptophan Pyrrolase ◽  
Dose Dependent Decrease ◽  
Dose Dependent

1. Liver 5-aminolaevulinate (ALA) synthase activity of 24 h-starved rats is maximally increased at 4 h after intraperitoneal administration of a 1.6 g/kg body wt. dose of ethanol. Larger doses cause a dose-dependent decrease in the extent of this stimulation, exhibiting a reciprocal relationship with an elevation of hepatic haem concentration, as suggested by the simultaneous increase in the haem saturation of tryptophan pyrrolase. 2. ALA synthase induction by ethanol is abolished if the above increase in pyrrolase saturation with haem is enhanced by theophylline, but is potentiated when the increase in the haem saturation is inhibited by anti-lipolytic agents. 3. ALA synthase induction by ethanol is also inhibited by inhibitors of alcohol dehydrogenase and aldehyde dehydrogenase. Acetaldehyde and acetate are, however, not responsible; they both decrease ALA synthase activity and increase the haem saturation of tryptophan pyrrolase. These latter effects of acetaldehyde are not mediated by acetate. 4. ALA synthase activity is also stimulated by succinate, which, however, also increases the haem saturation of tryptophan pyrrolase. 5. Ethanol does not influence the rate of ALA synthase degradation. 6. It is suggested that ethanol increases rat liver ALA synthase activity as a result of its own metabolism by the alcohol dehydrogenase-dependent pathway by a mechanism not involving decreased degradation of the former enzyme or the participation of the metabolites acetaldehyde and acetate.

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