Effects of inducers of drug metabolism on basic hepatic forms of mouse glutathione transferase

The cytosolic glutathione transferases (GSTs) with basic pI values have been studied in mouse liver after treatment with 2,3-t-butylhydroxyanisole (BHA), cafestol palmitate (CAF), phenobarbital (PB), 3-methylcholanthrene (3-MC) and trans-stilbene oxide (t-SBO). The cytosolic GST activity was induced...

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Bibliographic Details
Published in:Biochemical journal 1989-11, Vol.263 (3), p.679-685
Main Authors: Di Simplicio, P, Jensson, H, Mannervik, B
Format: Article
Language:English
Subjects:
Animals
Butylated Hydroxyanisole - pharmacology
Cytosol - enzymology
Diterpenes - pharmacology
Enzyme Induction - drug effects
Glutaredoxins
Glutathione Peroxidase - metabolism
Glutathione Reductase - metabolism
Glutathione Transferase - biosynthesis
Glutathione Transferase - metabolism
Isoenzymes - biosynthesis
Isoenzymes - metabolism
Lactoylglutathione Lyase - metabolism
liver
Liver - anatomy & histology
Liver - enzymology
Methylcholanthrene - pharmacology
Mice
Organ Size - drug effects
Oxidoreductases - metabolism
Phenobarbital - pharmacology
Protein Disulfide Reductase (Glutathione)
Stilbenes - pharmacology
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Summary:The cytosolic glutathione transferases (GSTs) with basic pI values have been studied in mouse liver after treatment with 2,3-t-butylhydroxyanisole (BHA), cafestol palmitate (CAF), phenobarbital (PB), 3-methylcholanthrene (3-MC) and trans-stilbene oxide (t-SBO). The cytosolic GST activity was induced by all compounds except for 3-MC. Three forms of GST were isolated by means of affinity chromatography and f.p.l.c. The examination of protein profiles and enzymic activities with specific substrates showed that the three GSTs correspond to those found in control animals, i.e. GSTs MI, MII and MIII. The class Mu GST MIII accounted for the major effect of induction, whereas the class Alpha GST MI and the class Pi GST MII were unchanged or somewhat down-regulated. The greatest induction was obtained with BHA, PB and CAF. The activities of other glutathione-dependent enzymes were also studied. An increase in glutathione reductase and thioltransferase activities was observed after BHA, PB or CAF treatment; glyoxalase I and Se-dependent glutathione peroxidase were depressed in comparison with the control group in all cases studied.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2630679