The hepatic Ah receptor for 2,3,7,8-Tetrachlorodibenzo-p-dioxin: Species differences in subunit dissociation

Michael S. Denison, Lynn M. Vella

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Abstract

2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD, dioxin) produces many of its biological effects by binding to a soluble, intracellar protein (the Ah receptor (AhR)). The hepatic AhR, from a variety of species, is present in low salt cytosol as a form which sediments at 8-10 S. High salt (0.4 m KCL) dissociates the rat, guinea pig, and rabbit cytosolic TCDD:AhR complex to a form which sediments at 5-6 S. In contrast, high salt conditions failed to dissociate the 8-10 S TCDD:AhR complex present in any of the mouse strains studied. Incubation of cytosol with heparin resulted in a shift of the [3H]TCDD:AhR complex to a smaller sedimenting form in all species. Mouse TCDD:AhR complex sedimented at 8-10 S when cytosol was simultaneously incubated with high salt and heparin, indicating that the interaction of heparin with the AhR was electrostatic in nature. Incubation of heparin-dissociated mouse TCDD: AhR complex (5-6 S) with high salt resulted in reassociation of AhR to a form which sediments at 8-10 S. Our data suggests that the resistance of mouse AhR to salt-mediated dissociation may be due to a property of the receptor protein itself and also indicates that mouse hepatic cytosolic AhR is distinctly different from that present in all other species examined to date.

Original languageEnglish (US)
Pages (from-to)382-388
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume277
Issue number2
DOIs
StatePublished - 1990
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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