title: Activation of rat liver glucocorticoid receptor bound to the antiglucocorticoid RU38486.
abstract: The kinetics of steroid binding to rat liver glucocorticoid receptor (GR) and receptor denaturation were dependent upon the nature of the molecule occupying GR. Both the agonist [triamcinolone acetonide (TA)] and the antagonist (Ru38486) however competed for the same saturable binding site. Despite opposing physiological action, both steroid analogues permitted receptor activation as evident by binding to DNA-cellulose and 9S to 4S shift on sucrose gradient sedimentation. It therefore seems necessary to reevaluate a current notion that antagonist action of RU38486 in rat liver is a result of impaired receptor activation.
mesh_terms: D000818:Animals; D001667:Binding, Competitive; D002499:Centrifugation, Density Gradient; D003600:Cytosol / Q000378:metabolism; D004963:Estrenes / Q000378:metabolism* / Q000494:pharmacology; D005938:Glucocorticoids / Q000037:antagonists & inhibitors*; D008099:Liver / Q000378:metabolism*; D008297:Male; D015735:Mifepristone; D011489:Protein Denaturation; D051381:Rats; D011919:Rats, Inbred Strains; D011965:Receptors, Glucocorticoid / Q000187:drug effects* / Q000378:metabolism; D014222:Triamcinolone Acetonide / Q000378:metabolism
chemical_list: D004963:Estrenes; D005938:Glucocorticoids; D011965:Receptors, Glucocorticoid; D015735:Mifepristone; D014222:Triamcinolone Acetonide