scholarly journals Identification of the region of glucocorticoid-receptor complex binding in the structural part of rat tryptophan oxygenase gene

1990 ◽  
Vol 6 (6) ◽  
pp. 80-83 ◽  
Author(s):  
V. M. Merkulov ◽  
T. I. Merkulova
Keyword(s):  
Glucocorticoid Receptor ◽  
Receptor Complex ◽  
Structural Part ◽  
Tryptophan Oxygenase

scholarly journals Comparative analysis of tryptophan oxygenase activity and glucocorticoid receptor under the influence of insulin

2008 ◽  
pp. 101-107
Author(s):  
ER Isenović ◽  
Z Zakula ◽  
G Koricanac ◽  
NR Stepić
Keyword(s):  
Glucocorticoid Receptor ◽  
Wistar Rats ◽  
Receptor Complex ◽  
Complex Stability ◽  
Cell Nuclei ◽  
Tryptophan Oxygenase ◽  
Oxygenase Activity ◽  
Male Wistar Rats ◽  
Hepatic Regulation ◽  
Different Doses

This investigation addresses the interaction of insulin (INS) and glucocorticoid (GC) signaling in the hepatic regulation of tryptophan oxygenase (TO) enzyme activity in the rat. Male Wistar rats (200-250 g b.w) received an injection of the different doses of INS (10, 25, 50, 70 and 100 μg/200 g b.w., i.p.) and were used for experiments 3 h and 18 h after INS administration. This study shows that maximum of TO activity was found at dose of 50 μg of INS with peak increases observed at 3 h and 18 h after injection of INS, while INS had no effect on TO activity in adrenalectomized rats. The analysis of INS effects on glucocorticoid receptor-complex (GC/GR complex) stability shows that complexes from INS-treated rats are less stable than those from control animals. In addition, INS-stimulated stability of glucocorticoid receptor (GR) protein was significantly increased from the controls. Furthermore, the results show that GC/GR complexes from INS-treated rats could be activated and accumulated at higher rate in cell nuclei of control animals. These data support the involvement of INS in modulation of GC signaling pathway which mediates, in part, the activity of TO.

scholarly journals Pyridoxine deficiency influences the behavior of the glucocorticoid . receptor complex.

1980 ◽  
Vol 255 (9) ◽  
pp. 3866-3870
Author(s):  
D.M. DiSorbo ◽  
D.S. Phelps ◽  
V.S. Ohl ◽  
G. Litwack
Keyword(s):  
Glucocorticoid Receptor ◽  
Receptor Complex ◽  
Pyridoxine Deficiency

Activation of the glucocorticoid-receptor complex

1982 ◽  
Vol 20 (1) ◽  
pp. 15-27 ◽  
Author(s):  
Thomas J. Schmidt ◽  
Carol A. Barnett ◽  
Gerald Litwack
Keyword(s):  
Glucocorticoid Receptor ◽  
Receptor Complex

scholarly journals Interaction of rat liver glucocorticoid receptor with sodium tungstate

1982 ◽  
Vol 204 (3) ◽  
pp. 777-786 ◽  
Author(s):  
N Murakami ◽  
S P Healy ◽  
V K Moudgil
Keyword(s):  
Glucocorticoid Receptor ◽  
Rat Liver ◽  
Sodium Tungstate ◽  
Binding Capacity ◽  
Receptor Complex ◽  
Heat Activation ◽  
Ph Dependent ◽  
Steroid Binding ◽  
Cellulose Binding ◽  
Rat Liver Cytosol

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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