Activation of the glucocorticoid-receptor complex

1982 ◽  
Vol 20 (1) ◽  
pp. 15-27 ◽  
Author(s):  
Thomas J. Schmidt ◽  
Carol A. Barnett ◽  
Gerald Litwack
1980 ◽  
Vol 255 (9) ◽  
pp. 3866-3870
Author(s):  
D.M. DiSorbo ◽  
D.S. Phelps ◽  
V.S. Ohl ◽  
G. Litwack

1982 ◽  
Vol 204 (3) ◽  
pp. 777-786 ◽  
Author(s):  
N Murakami ◽  
S P Healy ◽  
V K Moudgil

Effects of sodium tungstate on various properties of rat liver glucocorticoid receptor were examined at pH7 and pH 8. At pH 7, [3H]triamcinolone acetonide binding in rat liver cytosol preparations was completely blocked in the presence of 10-20 mM-sodium tungstate at 4 degrees C, whereas at 37 degrees C a 30 min incubation of cytosol receptor preparation with 1 mM-sodium tungstate reduced the loss of unoccupied receptor by 50%. At pH 8.0, tungstate presence during the 37 degrees C incubation maintained the steroid-binding capacity of unoccupied glucocorticoid receptor at control (4 degrees C) levels. In addition, heat-activation of cytosolic glucocorticoid-receptor complex was blocked by 1 mM- and 10 mM-sodium tungstate at pH 7 and pH 8 respectively. The DNA-cellulose binding by activated receptor was also inhibited completely and irreversibly by 5 mM-tungstate at pH 7, whereas at pH 8 no significant effect was observed with up to 20 mM-tungstate. The entire DNA-cellulose-bound glucocorticoid-receptor complex from control samples could be extracted by incubation with 1 mM- and 20 mM-tungstate at pH 7 and pH 8 respectively, and appeared to sediment as a 4.3-4.6 S molecule, both in 0.01 M- and 0.3 M-KCl-containing sucrose gradients. Tungstate effects are, therefore, pH-dependent and appear to involve an interaction with both the non-activated and the activated forms of the glucocorticoid receptor.


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