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.

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

2014 ◽  
Vol 2014 ◽  
pp. 1-9 ◽  
Author(s):  
Chenshu Xu ◽  
Binghua Wei ◽  
Xiaohua Fu ◽  
Meijuan Luo ◽  
Shidai Liu ◽  
...  
Keyword(s):  
Rat Liver ◽  
Hydroxysteroid Dehydrogenase ◽  
Underlying Mechanism ◽  
Drug Reactions ◽  
Eclipta Prostrata ◽  
Glomerular Nephritis ◽  
The Family ◽  
Protein Expressions ◽  
Liver And Kidney ◽  
Microsomal Incubation

Eclipta prostrata(EP) is often prescribed in combination with glucocorticoid to treat glomerular nephritis, nephrotic syndrome, and IgA nephropathy in clinical practice of Traditional Chinese Medicine. Previous studies from our laboratory revealed that coadministration of EP significantly increased the plasma concentration of prednisolone while decreased the level of cotreated prednisone in rats. However, the underlying mechanism remains unclear. 11β-Hydroxysteroid dehydrogenase (11β-HSD) belongs to the family of oxidoreductases that catalyze the interconversion of prednisone to active prednisolone. Therefore, the current study aimed to investigate the effects of EP on the activity and expression of 11β-HSD in rat liver and kidney. The results showed that oral administration of EP significantly increased the activity of 11β-HSD I in the liver and 11β-HSD II in the kidney by employing the microsomal incubation system. Moreover, gene and protein expressions of 11β-HSD I and 11β-HSD II were also increased in rat liver and kidney, respectively. These results suggest that the effects of EP on 11β-HSD may attribute to the mechanism that administration of EP improves the efficacy and reduces adverse drug reactions of glucocorticoid in patients undergoing combinational therapy.

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.

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.

The protective effect of pomegranate extract against cisplatin toxicity in rat liver and kidney tissue

2015 ◽  
Vol 121 (4) ◽  
pp. 152-156 ◽  
Author(s):  
Salih Bakır ◽  
Ümit Can Yazgan ◽  
İbrahim İbiloğlu ◽  
Bilal Elbey ◽  
Murat Kızıl ◽  
...  
Keyword(s):  
Protective Effect ◽  
Rat Liver ◽  
Kidney Tissue ◽  
Liver And Kidney

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.

REGULATION OF THE ACTIVITIES OF THE ENZYMES INVOLVED IN THE METABOLISM OF STEROID HORMONES IN RAT LIVER: THE EFFECT OF 19-NORTESTOSTERONE AND THE INFLUENCE OF CYPROTERONE ACETATE ON THE ACTION OF TESTOSTERONE AND 5α-DIHYDROTESTOSTERONE

1974 ◽  
Vol 77 (2) ◽  
pp. 287-297 ◽  
Author(s):  
Rüdiger Ghraf ◽  
Edmund Rodney Lax ◽  
Hanns-Georg Hoff ◽  
Herbert Schriefers
Keyword(s):  
Weight Loss ◽  
Body Weight ◽  
Rat Liver ◽  
Enzyme Activities ◽  
Cyproterone Acetate ◽  
Hydroxysteroid Dehydrogenase ◽  
Seminal Vesicles ◽  
Normal Male ◽  
Steroid Hydroxylases ◽  
Drug Leads

ABSTRACT The androgens testosterone and 5α-dihydrotestosterone, the anabolic drug 19-nortestosterone and the anti-androgen cyproterone acetate were investigated with regard to their modifying action on the sexual differentiation of the activities of rat liver enzymes involved in steroid hormone metabolism. The activities of the enzymes (Δ4-5α-hydrogenase, 20-ketoreductase, 3α-and 3β-hydroxysteroid dehydrogenase, NAD- and NADP-dependent Δ4-3β-hydroxysteroid dehydrogenase, total steroid hydroxylases, 7α- and 16α-hydroxylase) were determined in cell-free liver fractions of male animals castrated on day 25 of life and killed on day 90; and of castrated animals which, from day 75 to 89 received daily sc injections (0.3 mg/100 g body weight) of the anabolic drug or the androgen only or in combination with cyproterone acetate (3 mg/100 g body weight). With the exception of 7α-hydroxylase castration leads to a feminization of the enzyme activity pattern. However, the degree of feminization varies from enzyme to enzyme. The administration of testosterone or of 5α-dihydrotestosterone reverses the effect of castration. With 5α-dihydrotestosterone activity values were reached which in some cases were significantly higher than those obtained with testosterone. Although both androgens restored the enzyme activities to the normal male values, neither androgen was able to compensate for the weight loss of the seminal vesicles in the dose administered. The administration of 19-nortestosterone in the same dose as testosterone is only 30 % as effective in restoring the weight loss of the seminal vesicles, but leads to identical activities of Δ4-5α-hydrogenase and of hydroxysteroid dehydrogenases as are found for testosterone. 19-Nortestosterone is without influence on the activities of total steroid hydroxylases and of 16α-hydroxylase. 16α-Hydroxylase is the only enzyme in which the activity enhancing effects of testosterone or of 5α-dihydrotestosterone can be completely blocked by the simultaneous administration of the anti-androgen cyproterone acetate. In all other enzyme activities the anti-androgen does not interfere with the effect of the androgens although it blocks their action on the weight restitution of the seminal vesicles by 60–70 %. 7α-Hydroxylase does not exhibit any androgen dependency. Neither castration nor the subsequent administration of the two androgens, or of the anabolic drug leads to any alterations in activity. However, it is interesting to note that the administration of cyproterone acetate does cause an increase in activity.

scholarly journals Arylamidases of Rat Liver and Kidney

1967 ◽  
Vol 242 (10) ◽  
pp. 2369-2374
Author(s):  
S. Mahadevan ◽  
A.L. Tappel
Keyword(s):  
Rat Liver ◽  
Liver And Kidney
Sign in / Sign up

Export Citation Format

Share Document