Abstract
The primary goal of these studies was to determine whether the cytosolic glucocorticoid receptor is dephosphorylated during activation in the intact cell. To address this question WEHI-7 mouse thymoma cells were grown with [32P]orthophosphoric acid or [35S]methionine to label the receptor. The nonactivated (non-DNA-binding) and activated (DNA-binding) complexes, formed by incubation of the cells with 200 nM triamcinolone acetonide (TA) at 37 C. were separated on DNA-cellulose. purified using the BuGRl monoclonal antibody, and analyzed by Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS-PAGE). In some experiments. steroid-binding proteins were identified by their specific association with the affinity label [3H]dexamethasone 21-mesylate (DM).
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