Influence of Gonads on the Sulfurylation of 11-Deoxycorticosterone and Corticosterone by Rat Liver Cytosol

1971 ◽  
Vol 49 (4) ◽  
pp. 437-440 ◽  
Author(s):  
J. S. Torday ◽  
G. P. Klein ◽  
C. J. P. Giroud
Keyword(s):  
Body Weight ◽  
Rat Liver ◽  
Cytosol Fraction ◽  
Liver Cytosol ◽  
Daily Dose ◽  
17Β Estradiol ◽  
Rat Liver Cytosol ◽  
Gut Homogenate

When incubated in the presence of ATP, the cytosol fraction of rat liver, kidney, and gut homogenate is capable of sulfurylating 11-deoxycorticosterone, the extent of sulfurylation by liver cytosol being three to four times more efficient in the female than in the male. This sex-linked difference in liver sulfokinase activity is further demonstrated by the finding that sulfurylation of corticosterone is decreased by ovariectomy and brought back to the level observed in normal females by injection of 17β-estradiol (at the daily dose of 6 μg/100 g body weight) to castrated females; this effect is increased by orchidectomy and further enhanced by the administration of the same dose of 17β-estradiol to orchidectomized rats.

scholarly journals p-Nitrophenol sulfate conjugation with substrate inhibition in rat liver cytosol fraction.

1983 ◽  
Vol 31 (12) ◽  
pp. 4565-4567 ◽  
Author(s):  
TAKASHI MIZUMA ◽  
HIROYUKI YAMAGUCHI ◽  
MASAHIRO HAYASHI ◽  
SHOJI AWAZU
Keyword(s):  
Rat Liver ◽  
Substrate Inhibition ◽  
Cytosol Fraction ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

scholarly journals Reduction of ubiquinone in membrane lipids by rat liver cytosol and its involvement in the cellular defence system against lipid peroxidation

1995 ◽  
Vol 309 (3) ◽  
pp. 883-890 ◽  
Author(s):  
T Takahashi ◽  
T Yamaguchi ◽  
M Shitashige ◽  
T Okamoto ◽  
T Kishi
Keyword(s):  
Lipid Peroxidation ◽  
Rat Liver ◽  
Membrane Lipids ◽  
Reductase Activity ◽  
Egg Yolk ◽  
Cytosol Fraction ◽  
Liver Cytosol ◽  
Intracellular Fraction ◽  
Endogenous Antioxidant ◽  
Rat Liver Cytosol

Rat liver homogenates reduced ubiquinone (UQ)-10 to ubiquinol (UQH2)-10 in the presence of NADPH rather than NADH. This NADPH-dependent UQ reductase (NADPH-UQ reductase) activity that was not inhibited by antimycin A and rotenone, was located mainly in the cytosol fraction and its activity accounted for 68% of that of the homogenates. Furthermore, the NADPH-UQ reductase from rat liver cytosol efficiently reduced both UQ-10 incorporated into egg yolk lecithin liposomes, and native UQ-9 residing in rat microsomes, to the respective UQH2 form in the presence of NADPH. The gross redox ratios of UQH2-9/(UQ-9 + UQH2-9) in individual tissues of rat correlated positively with the log of their respective cytosolic NADPH-UQ reductase activities, while the redox ratios in every intracellular fraction from liver were at about the same level, irrespective of NADPH-UQ reductase activities in the respective fractions. The combined addition of rat liver cytosol and NADPH inhibited to a great extent 2,2′-azobis(2,4-dimethyl-valeronitrile)-induced lipid peroxidation of UQ-10-fortified lecithin liposomes and completely inhibited such peroxidation in the liposomes in which UQH2-10 replaced UQ-10. The NADPH-UQ reductase activity was clearly separated from DT-diaphorase (EC 1.6.99.2) activity by means of Cibacron Blue-immobilized Bio-Gel A-5m chromatography. In conclusion, the NADPH-UQ reductase in cytosol, which is a novel enzyme to our knowledge, was presumed to be responsible for maintaining the steady-state redox levels of intracellular UQ and thereby to act as an endogenous antioxidant in protecting intracellular membranes from lipid peroxidation that is inevitably induced in aerobic metabolism.

scholarly journals Alterations in translatable messenger RNA coding for phosphoenolpyruvate carboxykinase (GTP) in rat liver cytosol during deinduction.

1978 ◽  
Vol 253 (12) ◽  
pp. 4327-4332
Author(s):  
D. Kioussis ◽  
L. Reshef ◽  
H. Cohen ◽  
S.M. Tilghman ◽  
P.B. Iynedjian ◽  
...  
Keyword(s):  
Rat Liver ◽  
Messenger Rna ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

scholarly journals Transformation of the glucocorticoid receptor in rat liver cytosol by lysosomal enzymes.

1979 ◽  
Vol 254 (5) ◽  
pp. 1537-1539 ◽  
Author(s):  
J. Carlstedt-Duke ◽  
O. Wrange ◽  
E. Dahlberg ◽  
J.A. Gustafsson ◽  
B. Högberg
Keyword(s):  
Glucocorticoid Receptor ◽  
Rat Liver ◽  
Lysosomal Enzymes ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

Development of an [3H] glucocorticoid exchange assay in rat liver cytosol

Steroids ◽  
1981 ◽  
Vol 37 (4) ◽  
pp. 409-421 ◽  
Author(s):  
Ashutosh Banerji ◽  
Mohammed Kalimi
Keyword(s):  
Rat Liver ◽  
Liver Cytosol ◽  
Rat Liver Cytosol
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