Relationship between glucocorticoid receptor steroid-binding capacity and association of the Mr 90,000 heat shock protein with the unliganded receptor
1988; Pergamon Press; Volume: 30; Issue: 1-6 Linguagem: Inglês
10.1016/0022-4731(88)90104-5
ISSN1878-2353
AutoresEmery H. Bresnick, Edwin R. Sánchez, William B. Pratt,
Tópico(s)Hormonal Regulation and Hypertension
ResumoTreatment of rat liver cytosol with hydrogen peroxide (H2O2) or sodium molybdate (MoO42−) inhibits thermal inactivation of glucocorticoid receptor steroid-binding capacity at 25°C. Dithiothreitol (DTT) prevents the stabilization of receptors by H2O2. Heating (25°C) of immune pellets formed by immunoadsorption of L-cell murine glucocorticoid receptor complexes to protein-A-Sepharose with an anti-receptor monoclonal antibody (BuGR2) results in dissociation of the M 90,000 heat shock protein (hsp90) from the steroid binding protein. Such thermal-induced dissociation of hsp90 is inhibited by H2O2. Pretreatment of immunoadsorbed receptor complexes with the thiol derivatizing agent, methyl methanethiosulfonate (MMTS) prevents the ability of H2O2 to stabilize the hsp90-receptor interaction. These data suggest a role for hsp90 in maintaining an active steroid-binding conformation of the glucocorticoid receptor.
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