Abstract
Known inducers of the hepatic glutathione (GSH) S-transferases were tested at the limits of their solubility as inducers of the enzyme in cultured human keratinocytes. Neither phenobarbital, trans-stilbene oxide, propylthiouracil, nor butylated hydroxyanisole increased GSH S-transferase activity or led to the appearance of alpha- or mu-forms of the enzyme, as judged by Western blotting. Only the pi-form of the enzyme was found before and after all treatments. Thus, the enzyme is not inducible in keratinocytes. However, 4 mM propylthiouracil did lead to a 50% increase in GSH reductase activity, and phenobarbital at 4 mM completely abolished GSH peroxidase and GSH reductase activity and led to a significant loss of viability.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Butylated Hydroxyanisole / pharmacology
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Cells, Cultured
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Enzyme Induction* / drug effects
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Glucosephosphate Dehydrogenase / biosynthesis
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Glucosephosphate Dehydrogenase / drug effects
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Glutathione / metabolism*
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Glutathione Peroxidase / biosynthesis
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Glutathione Peroxidase / drug effects
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Glutathione Reductase / biosynthesis
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Glutathione Reductase / drug effects
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Glutathione Transferase / biosynthesis*
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Glutathione Transferase / drug effects
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Humans
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Keratinocytes / drug effects
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Keratinocytes / enzymology*
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Phenobarbital / pharmacology
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Propylthiouracil / pharmacology
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Stilbenes / pharmacology
Substances
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Stilbenes
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Butylated Hydroxyanisole
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Propylthiouracil
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Glucosephosphate Dehydrogenase
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Glutathione Peroxidase
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Glutathione Reductase
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Glutathione Transferase
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Glutathione
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stilbene oxide
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Phenobarbital