Age-associated changes in the estrogen receptor-active proteases of female rabbit liver

1990 ◽  
Vol 68 (7-8) ◽  
pp. 1065-1070
Author(s):  
Denis G. Williamson ◽  
Marie M. Song

Female rabbit liver cytosol contains a receptor-modifying activity that converts the 250 000 estrogen receptor of liver and uterine cytosol to a 37 000 form. There is an age-dependent increase in this receptor-active protease and in the general protease activity of rabbit liver cytosol, measured with [14C]casein. Sephacryl S-200 chromatography of liver cytosol shows that in the young animal (5 weeks old) the major receptor-modifying activity elutes near the void volume, while in the older animal (13 weeks old) activities having lower molecular weights are present. The general protease activity elution profile is similar to the receptor-active protease profile for the 5-week-old rabbit but not the 13-week-old rabbit. The liver cytosol of the older animal has a high molecular weight protease active toward [14C]casein but not toward the estrogen receptor. The changes in the estrogen receptor forms and the receptor-modifying activity profiles of liver cytosol that occur during development in the rabbit suggest that receptor-modifying activity may initially be associated with the estrogen receptor to form a high molecular weight complex.Key words: liver, estrogen receptor, proteolysis, age dependent.

1985 ◽  
Vol 225 (2) ◽  
pp. 391-398 ◽  
Author(s):  
G R Antoun ◽  
D G Williamson

The soluble NADP-dependent 17 beta-hydroxysteroid dehydrogenase activity of female rabbit liver increases with the age of the animal, the specific activity of the enzyme in the 56-day-old rabbit being 3 times that of the 28-day-old animal. The increase in activity is accompanied by a change in the molecular heterogeneity of the enzyme. Three forms (enzymes I, II and III) were identified in the liver cytosol of the 56-day-old female rabbit, whereas only one major form (enzyme IIIY) was present in the 28-day-old animal. Peptide maps of the four purified enzymes showed that there were minor differences in structure. The enzyme present in the liver of the 28-day-old rabbit was distinct from the three enzymes of the 56-day-old animal. All of the enzymes exhibited bifunctional activity, having 17 beta-hydroxysteroid dehydrogenase activity towards androgen and oestrogen substrates and 3 alpha-hydroxysteroid dehydrogenase activity towards androgens of the 5 beta-androstane series. The differences in substrate specificity of the enzymes paralleled their differences in structure. The data suggest that one enzyme (enzyme III) may have a special role in steroid metabolism during development in the female rabbit.


Biochimie ◽  
1972 ◽  
Vol 54 (1) ◽  
pp. 83-91 ◽  
Author(s):  
Hélène Thaler-Dao ◽  
Bernard Descomps ◽  
Monique Saintot ◽  
André Crastes de Paulet

1985 ◽  
Vol 53 (02) ◽  
pp. 245-248 ◽  
Author(s):  
W Rogatti ◽  
K Yokoigawa ◽  
T Kobayashi

SummaryFive commercially available German Urokinase (UK) preparations were examined for purity, fibrinolytic activity, and molecular weight composition. With the exception of one preparation (B) all samples showed comparable fibrinolytic activity (91-107% of the activity declared). Preparations A, D, and E contained almost exclusively high-molecular-weight UK (HMW-UK), i.e., 82-86%. However, preparation C (from kidney tissue cultures) contained 95% of low-molecular-weight-UK (LMW-UK), and sample B consisted of nearly equal amounts of both HMW-UK and LMW-UK (47:53). Purity criteria (coagulative and lysozyme activity, endotoxin content, protease activity, HBS antigen) were fulfilled by preparation E, and, with certain restrictions, also by preparations A and C.


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