Structural differences between the glucocorticoid, dioxin and oxysterol receptors from rat liver cytosol

Marc Denis, Anna Wilhelmsson, Scott Cuthill, Lorenz Poellinger, Jan Åke Gustafsson

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


The rat hepatic glucocorticoid, dioxin and oxysterol receptors were subjected to high performance liquid chromatography on size-exclusion and anion-exchange columns. Both the glucocorticoid receptor and the dioxin receptor had a Stokes radius Rs ∼ 7.5 nm, expected value for heteromeric complexes containing a dimer of the Mr ∼ 90,000 heat shock protein, hsp90 (Rs ∼ 7.0 nm). The oxysterol receptor represented a much smaller entity (Rs ∼ 6.0 nm). When analyzed on a Mono Q anion-exchange column, the molybdate-stabilized glucocorticoid receptor and dioxin receptor eluted as single peaks at ∼0.30 M and 0.26-0.28 M NaCl, respectively, whereas the oxysterol receptor represented a less negatively charged species (0.11-0.14 M NaCl). Following washing of the Mono Q column with molybdate-free buffer, the activated monomeric glucocorticoid receptor was detected (0.10-0.12 M NaCl). In contrast, no modification in the elution pattern of the dioxin receptor and the oxysterol receptor was observed. These data demonstrate differences in the physico-chemical properties of the glucocorticoid, dioxin and oxysterol receptors, respectively, which might reflect structural differences.

Original languageEnglish (US)
Pages (from-to)444-451
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Aug 30 1989

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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