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Demonstration that the 90-Kilodalton Heat Shock Protein is Bound to the Glucocorticoid Receptor in its 9S Nondeoxynucleic Acid Binding Form

Department of Pharmacology, University of Michigan Medical School Ann Arbor, Michigan 48109
The Department of Microbiology, Washington University School of Medicine St. Louis, Missouri 63110

Address requests for reprints to: William B. Pratt, Department of Pharmacology, University of Michigan Medical School, Ann Arbor, Michigan 48109.

Abstract

The 9S molybdate-stabilized form of the glucocorticoid receptor of mouse L cell lysates was immunoadsorbed to protein-A-Sepharose with antiserum directed against the 89-kilodalton chicken heat shock protein (anti-hsp89). In order to achieve this, "free" (nonreceptor associated) hsp90 was first separated from the molybdate-stabilized 9S receptor by sucrose gradient sedimentation. Incubation of the 9S [³H]triamcinolone acetonide-labeled receptor peak with anti-hsp89 results in the immune-specific adsorption of 20% of the specifically bound radioactivity and adsorption of the 100-kilodalton receptor protein, as detected by Western-blotting, using the GR49 antireceptor monoclonal antibody as probe. These observations provide the only direct proof that hsp90 is a component of the 9S form of a steroid receptor.

FOOTNOTES

This investigation was supported by Grant CA-28010 from NCI (to W.B.P.) and by a grant from the National Science Foundation (to M.J.S.).

Received for publication August 25, 1987. Accepted for publication October 6, 1987.

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