Send to

Choose Destination
Biochem Biophys Res Commun. 1988 Sep 15;155(2):801-7.

Association of the dioxin receptor with the Mr 90,000 heat shock protein: a structural kinship with the glucocorticoid receptor.

Author information

Department of Medical Nutrition, Karolinska Institute, Huddinge University Hospital, Sweden.


The Mr approximately equal to 90,000 heat shock protein, hsp90, readily interacts with the glucocorticoid receptor to form the 9 S, non-DNA-binding receptor complex. This receptor is stabilized in cytosolic preparations by sodium molybdate. In analogy, sodium molybdate stabilizes a 9 S form of the dioxin receptor. Polyclonal antibodies raised against the purified glucocorticoid receptor-associated hsp90 interact with the molybdate-stabilized 9 S dioxin-receptor complex but not with the 4 S dioxin receptor monomer, as assessed by sedimentation shift analysis on sucrose gradients. Thus we conclude that both the dioxin and glucocorticoid receptor can form heteromeric complexes which share a common non-ligand-binding component. These results represent the first demonstration of a structural relationship between the dioxin and glucocorticoid receptors.

[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center