Effect of inducers on the activity of glutathione S-transferase and other enzymes of the glutathione pathway in cultured human keratinocytes

D. A. Vessey, K. H. Lee, K. L. Blacker, Thomas D Boyer

Research output: Contribution to journalArticle

3 Scopus citations

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 α- or μ-forms of the enzyme, as judged by Western blotting. Only the π-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.

Original languageEnglish (US)
Pages (from-to)241-245
Number of pages5
JournalSkin Pharmacology
Volume6
Issue number4
Publication statusPublished - 1993
Externally publishedYes

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Keywords

  • Butylated hydroxyanisole
  • Glutathione peroxidase
  • Glutathione reductase
  • Glutathione S-transferases
  • Induction
  • Keratinocytes
  • Phenobarbital
  • Propylthiouracil
  • Trans-stilbene oxide

ASJC Scopus subject areas

  • Dermatology
  • Pharmacology (medical)
  • Pharmacology, Toxicology and Pharmaceutics(all)

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