ORGAN-SPECIFIC ONTOGENESES OF STEROID HORMONE METABOLIZING ENZYME ACTIVITIES IN THE RAT

1975 ◽  
Vol 79 (1) ◽  
pp. 192-201 ◽  
Author(s):  
Rüdiger Ghraf ◽  
Ulrich Vetter ◽  
Jeane Marie Zandveld ◽  
Herbert Schriefers
Keyword(s):  
Enzyme Activity ◽  
Sexual Differentiation ◽  
Microsomal Fraction ◽  
Steroid Hormone ◽  
Hydroxysteroid Dehydrogenase ◽  
Dependent Development ◽  
Enzymes Activities ◽  
Age Dependent ◽  
Organ Specific ◽  
Liver And Kidney

ABSTRACT The development and sexual differentiation of 11β- and 17β-hydroxysteroid dehydrogenase activities was investigated in the liver, kidney, adrenal and gonads of rats over a period of 15–120 days of life. 11β-Hydroxysteroid dehydrogenase in the adrenal and ovary was at the limit of detectibility at all the stages of life investigated. In the liver, kidney and testis the enzyme activity is restricted to the microsomal fraction and demonstrates an age-dependent development; in the liver, kidney and in the gonads it is additionally characterized by a sexual differentiation to higher values in the male sex. In all the organs investigated the cytoplasmic and microsomal fractions contain 17β-hydroxysteroid dehydrogenase activity; the activities are very low in the microsomal fraction of the kidney and in the cytosol of the testis. In all the organs the enzyme activity of at least one cell fraction displays an age-dependent development. The only activities, not demonstrating an ontogenesis are those of the cytosol of the adrenal and those of the microsomal fraction of the kidney. The age-dependent development is accompanied by a sexual differentiation of the enzymes activities. The only exception is the microsomal activity of the liver. The female sex shows the higher activity in the kidney, adrenal and gonads; whereas the male animal shows the higher activity only in the cytosol of the liver. The developmental processes of 11β- and 17β-hydroxysteroid dehydrogenase have the following properties in common: In the immature phase (day 15–30) the activities of the enzymes develop either very rapidly to manifold higher values or remain constant at the low neonatal level; no sexual differentiation of the enzymes activities occurs at this stage of life. The rapid increase in activity is found only in the liver and kidney, that is in the steroid hormone catabolizing organs. It does not occur in the steroid hormone producing glands.

Histoarchitecture and Δ5-3β hydroxysteroid dehydrogenase profile in ovaries of the non-pregnant, pregnant and lactating insectivorous rat-tailed bat, Rhinopoma microphyllum kinneari

2007 ◽  
Vol 57 (1) ◽  
pp. 97-114 ◽  
Author(s):  
Seema Trivedi ◽  
Suresh Bihari Lall
Keyword(s):  
Enzyme Activity ◽  
Annual Cycle ◽  
Steroid Hormone ◽  
Post Partum ◽  
Hydroxysteroid Dehydrogenase ◽  
Follicular Atresia ◽  
Ovarian Stroma ◽  
Thecal Cells ◽  
Hormone Biosynthesis ◽  
Seasonally Breeding

AbstractThe histoarchitecture and profile of Δ5-3β hydroxysteroid dehydrogenase were studied in an insectivorous seasonally-breeding microchiropteran, Rhinopoma microphyllum kinneari (rattailed bat) ovaries during non-pregnant, pregnant and lactation phases. Mid-sections of follicles and ova showed variation in their diameter (0.013-0.182 mm and 0.010-0.075 mm, respectively). Though dextral and sinistral ovaries are functionally equivalent, ovulation occurs only once (alternately from one ovary) in each annual cycle. An extroverted corpus luteum (0.792 mm) was observed in either the dextral or sinistral ovary of a pregnant R. m. kinneari. This exhibited two types of cells. Follicular atresia was pronounced in ovaries during these reproductive stages. No post-partum 'heat' was discerned. Δ5-3β HSDH is a crucial catalyst in steroid hormone biosynthesis and the reaction product indicates status of steroidogenesis in different follicle types. Differential Δ5-3β HSDH activity evident from reaction product staining in three reproductive states and in different ovarian components was seen. Consistent sites of enzyme activity were thecal cells and ovarian stroma. However, intensity varied in different reproductive states.

scholarly journals Effect ofLuteolinon 11Beta-Hydroxysteroid Dehydrogenase in Rat Liver and Kidney

2015 ◽  
Vol 2015 ◽  
pp. 1-7
Author(s):  
Lei Tang ◽  
Bin Deng ◽  
Lijuan Shi ◽  
Binghua Wei ◽  
Bin Ren ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Rat Liver ◽  
Drug Effect ◽  
Kidney Tissue ◽  
Drug Effects ◽  
Hydroxysteroid Dehydrogenase ◽  
Clinical Value ◽  
Eclipta Prostrata ◽  
Protein Expressions ◽  
Liver And Kidney

11Beta-hydroxysteroid dehydrogenase (11β-HSD) enzymes control the glucocorticoid (GC) signaling, which is essential in regulating homeostasis. Our previous study revealed thatEclipta prostrata(EP) affected the activity and expression of 11β-HSD enzymes which might improve the efficacy and reduce the adverse drug effects of glucocorticoid in patients undergoing combinational therapy. However, it is still unclear which composition of EP plays a major role and how it works. In this paper, we choseLuteolinwhich is one of the main ingredients of EP and evaluated its effect and metabolism in combination with prednisone. The effects of different concentrations ofLuteolinextract on prednisone/prednisolone metabolism indicated the enzyme activity of 11β-HSD, so the production rate (pmol/min per mg protein) of metabolites was used to indicate enzyme activity. Furthermore, we explored the influence ofLuteolinon gene and protein expressions of 11β-HSD I/II in rat liver and kidney tissue. Our results showed that oral administration ofLuteolinsignificantly increased the gene and protein expressions of hepatic 11β-HSD I and renal 11β-HSD II, which may improve the efficacy and reduce the adverse drug effect of glucocorticoid in clinical application. A potential clinical value ofLuteolinwould also be indicated in combination therapy with prednisone for the treatment of nephrotic syndrome.

THE INFLUENCE OF HAEMOGLOBIN-S AND G6PD DEFICIENCY ON THE ACTIVITY OF THE 17β-HYDROXYSTEROID DEHYDROGENASE OF INTACT HUMAN ERYTHROCYTES

1974 ◽  
Vol 75 (4) ◽  
pp. 793-800
Author(s):  
A. O. Sogbesan ◽  
O. A. Dada ◽  
B. Kwaku Adadevoh
Keyword(s):  
Enzyme Activity ◽  
Dehydrogenase Activity ◽  
Sex Steroids ◽  
G6pd Deficiency ◽  
Incubation Medium ◽  
Hydroxysteroid Dehydrogenase ◽  
G6pd Activity ◽  
Reverse Transformation ◽  
Oxidative Transformation ◽  
Haemoglobin S

ABSTRACT The 17β-hydroxysteroid dehydrogenase activity in intact erythrocytes of Nigerian patients, in particular with regard to haemoglobin genotypes and G6PD* activity was studied. The G6PD activity of the erythrocyte did not affect the oxidative transformation of testosterone to androstenedione and of oestradiol to oestrone. The reduction (reverse transformation) was inhibited in G6PD-deficient erythrocytes but this inhibition was offset by the addition of 0.025 m glucose to the incubation medium. The per cent oxidation transformation of testosterone was higher in Hb-AA than in Hb-SS erythrocytes. It is suggested that the differences may be a result of either lower enzyme activity in the Hb-SS erythrocytes or of differences in the uptake and possibly binding of sex steroids by intact Hb-SS and Hb-AA erythrocytes.

scholarly journals Age dependent accumulation of N-acyl-ethanolamine phospholipids in ischemic rat brain: a 31P NMR and enzyme activity study

2000 ◽  
Vol 41 (6) ◽  
pp. 985-990 ◽  
Author(s):  
Birthe Moesgaard ◽  
Gitte Petersen ◽  
Jerzy W. Jaroszewski ◽  
Harald S. Hansen
Keyword(s):  
Enzyme Activity ◽  
Rat Brain ◽  
31P Nmr ◽  
Age Dependent

scholarly journals Adrenal microsomal C19-steroid 5α-reductase activity in the Snell transplantable rat adrenocortical tumour 494 and the effect of oestradiol, testosterone propionate and adrenocorticotrophin in intact and gonadectomized rats

1973 ◽  
Vol 132 (2) ◽  
pp. 293-300 ◽  
Author(s):  
Paul V. Maynard ◽  
Euan H. D. Cameron
Keyword(s):  
Enzyme Activity ◽  
Steroid Hormones ◽  
Microsomal Fraction ◽  
Testosterone Propionate ◽  
Reductase Activity ◽  
Intact Control ◽  
Adrenal Tissue ◽  
Males And Females ◽  
Adrenocortical Tumour ◽  
Hormonal Treatments

The C19-steroid 5α-reductase activity in the microsomal fraction of rat adrenal tissue under various hormonal treatments was examined. In intact control rats the activity is similar in both males and females, and after gonadectomy it is markedly increased. Treatment with oestradiol (150μg/day per animal for 7 days) or testosterone propionate (2mg/day per animal for 7 days) lowered the activity of 5α-reductase in castrated animals to approximately the values for intact animals in both sexes, and in intact animals the activity was also decreased by these treatments. The enzyme activity was also decreased by adrenocorticotrophin treatment but to a lesser extent than by the steroid hormones. The activity of the 5α-reductase enzyme in the Snell adrenocortical tumour 494 is very low when incubated as a whole homogenate, but the activity in microsomal material of the tumour was measured and unexpectedly found to be similar to that in intact controls.

scholarly journals Induction of carnitine acetyltransferase by clofibrate in rat liver

1981 ◽  
Vol 194 (1) ◽  
pp. 249-255 ◽  
Author(s):  
B Mittal ◽  
C K R Kurup
Keyword(s):  
Protein Synthesis ◽  
Enzyme Activity ◽  
Rat Liver ◽  
Time Lag ◽  
Mitochondrial Protein ◽  
Carnitine Acetyltransferase ◽  
Enzyme Protein ◽  
General Protein Synthesis ◽  
Liver And Kidney ◽  
General Protein

Administration of the anti-hypercholesterolaemic drug clofibrate to the rat increases the activity of carnitine acetyltransferase (acetyl-CoA-carnitine O-acetyltransferase, EC 2.3.1.7) in liver and kidney. The drug-mediated increase in enzyme activity in hepatic mitochondria shows a time lag during which the activity increases in the microsomal and peroxisomal fractions. The enzyme induced in the particulate fractions is identical with one normally present in mitochondria. The increase in enzyme activity is prevented by inhibitors of RNA and general protein synthesis. Mitochondrial protein-synthetic machinery does not appear to be involved in the process. Immunoprecipitation shows increased concentration of the enzyme protein in hepatic mitochondria isolated from drug-treated animals. In these animals, the rate of synthesis of the enzyme is increased 7-fold.

Hormone-induced differentiation of antheridial branches in Achlya ambisexualis: dependence on ribonucleic acid synthesis

1974 ◽  
Vol 20 (7) ◽  
pp. 977-980 ◽  
Author(s):  
David K. Horowitz ◽  
Peter J. Russell
Keyword(s):  
Sexual Differentiation ◽  
Ribonucleic Acid ◽  
Rna Synthesis ◽  
Actinomycin D ◽  
Steroid Hormone ◽  
Acid Synthesis ◽  
Aquatic Fungus ◽  
Induced Differentiation ◽  
Sexual Steroid ◽  
Achlya Ambisexualis

Sexual differentiation in male strains of the aquatic fungus Achlya ambisexualis Raper is induced by antheridiol, a sexual steroid hormone secreted by female strains. Antheridiol-induced initiation of the morphologically distinct antheridial branches in male Achlya is completely prevented when DNA-dependent RNA synthesis is inhibited by actinomycin D. In addition antheridial branch elongation is inhibited to a degree proportional to the concentration of actinomycin D added. Thus, evidence indicates that RNA synthesis is required for antheridiol-induced initiation of antheridial branching and that continued RNA synthesis is required for elongation of antheridial branches.

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