Agarwal M K, Lombardo G, Eliezer N, Moudgil V K
Biochem Biophys Res Commun. 1985 Dec 17;133(2):745-52. doi: 10.1016/0006-291x(85)90967-2.
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.
类固醇与大鼠肝脏糖皮质激素受体（GR）结合的动力学以及受体变性取决于占据GR的分子的性质。然而，激动剂[曲安奈德（TA）]和拮抗剂（RU38486）都竞争同一个可饱和结合位点。尽管生理作用相反，但两种类固醇类似物都能使受体激活，这在与DNA-纤维素结合以及蔗糖梯度沉降时从9S到4S的转变中很明显。因此，似乎有必要重新评估当前的一种观点，即RU38486在大鼠肝脏中的拮抗作用是受体激活受损的结果。
