Evidence for an association of a ribonucleic acid with the purified, unactivated glucocorticoid receptor.
The unactivated glucocorticoid-receptor complex (GRC) was purified from rat hepatic cytosol (approximately 4000-fold by specific activity) by a procedure developed in our laboratory. Following elution of unactivated GRC from DEAE-cellulose with a 0.05-0.5 M potassium phosphate gradient, a second gradient of 0.5-1.0 M potassium chloride was started. This gradient eluted material at 0.6 M potassium chloride that incorporated [32P] in vivo and stained with ethidium bromide. A predominant ethidium bromide stained band of 100-110 nucleotides was observed. The presence of this material was dependent on the presence of highly purified GRC since presaturation of cytosol with 50 microM unlabeled triamcinolone acetonide (TA) precluded the appearance of this material. Experiments with partially purified GRC from CEM-C7 cells incubated in vivo with [14C]uridine indicated that the material eluted at 0.6 M potassium chloride incorporated [14C]uridine. Collectively, these data suggest that a RNA is associated with the purified, unactivated form of the GRC.
D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D008297:Male; D012313:RNA / Q000032:analysis*; D051381:Rats; D011919:Rats, Inbred Strains; D011965:Receptors, Glucocorticoid / Q000032:analysis* / Q000302:isolation & purification; D014222:Triamcinolone Acetonide / Q000494:pharmacology
D011965:Receptors, Glucocorticoid; D012313:RNA; D014222:Triamcinolone Acetonide