Chlorinated trans stilbenes: Competitive binding to the ah receptor, induction of cytochrome p-450 monooxygenase activity and partial 2, 3, 7, 8-TCDD antagonism

Nigel J. Bunce, James P. Landers, Uwe A. Schneider, S. H. Safe, Tim R. Zacharewski

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

Chlorinated trans stilbenes bind with high affinity to the cytosolic Ah receptor from Wistar rat liver. The EC50values for competition with [3H]-2, 3, 7, 8-tetrachlorodibenzo-p-dioxin (TCDD) cover a range from 10–400 nM, but with no apparent relationship between molecular structure and binding activity. These compounds induce monooxygenase enzyme activity in rat hepatoma H-4-II E cells in culture only weakly, again with no apparent dependence on molecular structure, and the weakest enzyme inducers act as antagonists for the induction of these enzymes by TCDD. In vivo administration of 3, 3′, 4, 4′-tetrachloro-trans-stilbene in the rat leads to decreased Ah receptor levels.

Original languageEnglish (US)
Pages (from-to)217-229
Number of pages13
JournalToxicological & Environmental Chemistry
Volume28
Issue number4
DOIs
StatePublished - Aug 1 1990

ASJC Scopus subject areas

  • Environmental Chemistry
  • Pollution
  • Health, Toxicology and Mutagenesis

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