ACTIVATION OF RAT-LIVER GLUCOCORTICOID RECEPTOR BOUND TO THE ANTIGLUCOCORTICOID RU38486

被引：31

作者：

AGARWAL, MK ^{[1
]}

LOMBARDO, G ^{[1
]}

ELIEZER, N ^{[1
]}

MOUDGIL, VK ^{[1
]}

机构：

[1] OAKLAND UNIV, DEPT BIOL SCI, ROCHESTER, MI 48063 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1985年 / 133卷 / 02期

关键词：

D O I：

10.1016/0006-291X(85)90967-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 acentonide (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.

引用

页码：745 / 752

页数：8

共 9 条

[1]

AGARWAL MK, 1977, MULTIPLE MOL FORMS S

[2]

Alberts B., 1971, Methods Enzymol, V21, P198

[3] ENDOMETRIAL AND PITUITARY RESPONSES TO THE STEROIDAL ANTIPROGESTIN RU-486 IN POSTMENOPAUSAL WOMEN [J].