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

Donald A. Vessey, Kyung Hee Lee, Kerry L. Blacker, Thomas D. Boyer

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

Known inducers of the hepatic glutathione (GSH) S-transfcr-ases were tested at the limits of their solubility as inducers of the enzyme in cultured human keratinocytes. Neither pheno-barbital. 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 pheno-barbital 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 and Physiology
Volume6
Issue number4
DOIs
StatePublished - Jan 1 1993

Keywords

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

ASJC Scopus subject areas

  • Physiology
  • Pharmacology
  • Dermatology

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