scholarly journals Increase in the amount of glutathione transferase 4-4 in the rat adrenal gland after hypophysectomy and down-regulation by subsequent treatment with adrenocorticotrophic hormone

1990 ◽  
Vol 265 (1) ◽  
pp. 147-154 ◽  
Author(s):  
L Mankowitz ◽  
V M Castro ◽  
B Mannervik ◽  
J Rydström ◽  
J W DePierre
Keyword(s):  
Adrenal Gland ◽  
Adrenocorticotropic Hormone ◽  
Glutathione Transferase ◽  
Fold Increase ◽  
Subsequent Treatment ◽  
Glutathione Transferases ◽  
Pituitary Hormone ◽  
Down Regulation ◽  
Trans Stilbene ◽  
Hypophysectomized Rats

The effect of hypophysectomy and subsequent treatment with adrenocorticotropic hormone (adrenocorticotropin, ACTH) on the isoenzymes of glutathione transferase in the rat adrenal gland was investigated. A large increase (approx. 11-fold) in the level of transferase subunit 4 was observed in hypophysectomized animals by immunoblotting. When the activity of glutathione transferase 4-4 was measured in adrenal cytosol using trans-stilbene oxide as a selective substrate, a 15-fold increase was noted. Lack of the pituitary hormone ACTH is apparently related to this increase, since treatment of hypophysectomized animals with ACTH for 2 weeks partially down-regulated subunit 4. Glutathione transferase subunits 3 and 8 in the adrenal were also increased in amount by hypophysectomy, but not at all to the same extent. The activity of glutathione transferase 4-4 was elevated also in the liver and ovary (5 and 1.5 times respectively) after hypophysectomy. These elevated enzyme levels were, however, not affected by ACTH treatment. This down-regulation of glutathione transferases in the rat adrenal by ACTH may be related to the fact that, under normal conditions, this organ is highly susceptible to the toxic effects of various polycyclic hydrocarbons, whereas under circumstances where there is no ACTH production, as in hypophysectomized rats, the adrenal is resistant to these same hydrocarbons.

scholarly journals Glutathione transferases in rat hepatoma cells. Effects of ascites cells on the isoenzyme pattern in liver and induction of glutathione transferases in the tumour cells

1989 ◽  
Vol 257 (1) ◽  
pp. 215-220 ◽  
Author(s):  
M K Tahir ◽  
C Guthenberg ◽  
B Mannervik
Keyword(s):  
Glutathione Transferase ◽  
Hepatoma Cell ◽  
Normal Liver ◽  
Hepatoma Cells ◽  
Glutathione Transferases ◽  
Trans Stilbene ◽  
Cytosolic Glutathione ◽  
Fold Induction ◽  
Rat Hepatoma ◽  
Rat Hepatoma Cells

Rat hepatoma cells grown intraperitoneally as an ascites tumour were analysed with respect to their contents of cytosolic glutathione transferases. In contrast with normal liver tissue, the hepatoma cells were dominated by the class Pi glutathione transferase 7-7. All the major hepatic enzyme forms were down-regulated to almost undetectable concentrations. Livers of rats bearing ascites-hepatoma cells expressed low, but significant, amounts of protein which, by electrophoretic and immunochemical properties, appeared identical with transferase 7-7. This enzyme is not detectable in normal hepatocytes. Treatment of rats with trans-stilbene oxide induced the expression of transferase 7-7 in the livers of normal rats as well as in hepatoma-cell-bearing animals. In addition, a 2-fold induction of transferase 7-7 was measured in the hepatoma ascites cells. No significant elevation of any other enzyme forms in the hepatoma cells was noted.

scholarly journals Effects of inducers of drug metabolism on basic hepatic forms of mouse glutathione transferase

1989 ◽  
Vol 263 (3) ◽  
pp. 679-685 ◽  
Author(s):  
P Di Simplicio ◽  
H Jensson ◽  
B Mannervik
Keyword(s):  
Mouse Liver ◽  
Glutathione Transferase ◽  
Major Effect ◽  
Glutathione Transferases ◽  
Control Group ◽  
Glyoxalase I ◽  
Protein Profiles ◽  
Trans Stilbene ◽  
Cytosolic Glutathione ◽  
Gst Activity

The cytosolic glutathione transferases (GSTs) with basic pI values have been studied in mouse liver after treatment with 2,3-t-butylhydroxyanisole (BHA), cafestol palmitate (CAF), phenobarbital (PB), 3-methylcholanthrene (3-MC) and trans-stilbene oxide (t-SBO). The cytosolic GST activity was induced by all compounds except for 3-MC. Three forms of GST were isolated by means of affinity chromatography and f.p.l.c. The examination of protein profiles and enzymic activities with specific substrates showed that the three GSTs correspond to those found in control animals, i.e. GSTs MI, MII and MIII. The class Mu GST MIII accounted for the major effect of induction, whereas the class Alpha GST MI and the class Pi GST MII were unchanged or somewhat down-regulated. The greatest induction was obtained with BHA, PB and CAF. The activities of other glutathione-dependent enzymes were also studied. An increase in glutathione reductase and thioltransferase activities was observed after BHA, PB or CAF treatment; glyoxalase I and Se-dependent glutathione peroxidase were depressed in comparison with the control group in all cases studied.

1,25-Dihydroxyvitamin D3-induced upregulation of the thyrotropin-releasing hormone receptor in clonal rat pituitary GH3 cells

1995 ◽  
Vol 147 (3) ◽  
pp. 397-404 ◽  
Author(s):  
L M Atley ◽  
N Lefroy ◽  
J D Wark
Keyword(s):  
Vitamin D ◽  
Fold Increase ◽  
Thyrotropin Releasing Hormone ◽  
Gh3 Cells ◽  
Pituitary Hormone ◽  
Pituitary Cells ◽  
Hormone Production ◽  
Releasing Hormone ◽  
Rat Pituitary ◽  
Trh Receptor

Abstract 1,25-Dihydroxyvitamin D3 (1,25-(OH)2D3) is active in primary dispersed and clonal pituitary cells where it stimulates pituitary hormone production and agonist-induced hormone release. We have studied the effect of 1,25-(OH)2D3 on thyrotropin-releasing hormone (TRH) binding in clonal rat pituitary tumour (GH3) cells. Compared with vehicle-treated cells, 1,25-(OH)2D3 (10 nmol/l) increased specific [3H]MeTRH binding by 26% at 8 h, 38% at 16 h, 35% at 24 h and reached a maximum at 48 h (90%). In dose–response experiments, specific [3H]MeTRH binding increased with 1,25-(OH)2D3 concentration and reached a maximum at 10 nmol/l. Half-maximal binding occurred at 0·5 nmol 1,25-(OH)2D3/l. The vitamin D metabolite, 25-OH D3, increased [3H]MeTRH binding but was 1000-fold less potent than 1,25-(OH)2D3. In equilibrium binding assays, treatment with 10 nmol 1,25-(OH)2D3/l for 48 h increased the maximum binding from 67·4 ± 8·8 fmol/mg protein in vehicle-treated cells to 96·7 ± 12·4 fmol/mg protein in treated cells. There was no difference in apparent Kd (1·08 ± 0·10 nmol/l for 1,25-(OH)2D3-treated and 0·97 ± 0·11 nmol/l for vehicle-treated cells). Molecular investigations revealed that 10 nmol 1,25-(OH)2D3/l for 24 h caused an 8-fold increase in TRH receptor-specific mRNA. Actinomycin D (2 μg/ml, 6 h) abrogated the 1,25-(OH)2D3-induced increase in [3H]MeTRH binding. Cortisol also increased [3H]MeTRH binding but showed no additivity or synergism with 1,25-(OH)2D3. TRH-stimulated prolactin release was not enhanced by 1,25-(OH)2D3. We conclude that the active vitamin D metabolite, 1,25-(OH)2D3, caused a time- and dose-dependent increase in [3H]MeTRH binding. The effect was vitamin D metabolite-specific and resulted from an upregulation of the TRH receptor. Further studies are needed to determine the functional significance of this novel finding. Journal of Endocrinology (1995) 147, 397–404

Porcine glutathione transferase Alpha 2-2 is a human GST A3-3 analogue that catalyses steroid double-bond isomerization

2010 ◽  
Vol 431 (1) ◽  
pp. 159-167 ◽  
Author(s):  
Natalia Fedulova ◽  
Françoise Raffalli-Mathieu ◽  
Bengt Mannervik
Keyword(s):  
Double Bond ◽  
Glutathione Transferase ◽  
Biological Species ◽  
Glutathione Transferases ◽  
Special Role ◽  
Primary Role ◽  
The Novel ◽  
Protective Function ◽  
Isomerase Activity

A primary role of GSTs (glutathione transferases) is detoxication of electrophilic compounds. In addition to this protective function, hGST (human GST) A3-3, a member of the Alpha class of soluble GSTs, has prominent steroid double-bond isomerase activity. The isomerase reaction is an obligatory step in the biosynthesis of steroid hormones, indicating a special role of hGST A3-3 in steroidogenic tissues. An analogous GST with high steroid isomerase activity has so far not been found in any other biological species. In the present study, we characterized a Sus scrofa (pig) enzyme, pGST A2-2, displaying high steroid isomerase activity. High levels of pGST A2-2 expression were found in ovary, testis and liver. In its functional properties, other than steroid isomerization, pGST A2-2 was most similar to hGST A3-3. The properties of the novel porcine enzyme lend support to the notion that particular GSTs play an important role in steroidogenesis.

Direct effect of hypothalamic neuropeptides on the release of catecholamines by adrenal medulla in sheep – study ex vivo

2017 ◽  
Vol 20 (2) ◽  
pp. 339-346 ◽  
Author(s):  
D. Wrońska ◽  
B.F. Kania ◽  
M. Błachuta
Keyword(s):  
Adrenal Gland ◽  
Adrenal Medulla ◽  
Noradrenaline Release ◽  
Adrenocorticotropic Hormone ◽  
Ex Vivo ◽  
Adrenal System ◽  
Adrenaline Release ◽  
Hormone Control

Abstract Stress causes the activation of both the hypothalamic-pituitary-adrenocortical axis and sympatho-adrenal system, thus leading to the release from the adrenal medulla of catecholamines: adrenaline and, to a lesser degree, noradrenaline. It has been established that in addition to catecholamines, the adrenomedullary cells produce a variety of neuropeptides, including corticoliberine (CRH), vasopressin (AVP), oxytocin (OXY) and proopiomelanocortine (POMC) – a precursor of the adrenocorticotropic hormone (ACTH). The aim of this study was to investigate adrenal medulla activity in vitro depending, on a dose of CRH, AVP and OXY on adrenaline and noradrenaline release. Pieces of sheep adrenal medulla tissue (about 50 mg) were put on 24-well plates and were incubated in 1 mL of Eagle medium without hormone (control) or supplemented only once with CRH, AVP and OXY in three doses (10−7, 10−8 and 10−9 M) in a volume of 10 μL. The results showed that CRH stimulates adrenaline and noradrenaline release from the adrenal medulla tissue. The stimulating influence of AVP on adrenaline release was visible after the application of the two lower doses of this neuropeptide; however, AVP reduced noradrenaline release from the adrenal medulla tissue. A strong, inhibitory OXY effect on catecholamine release was observed, regardless of the dose of this hormone. Our results indicate the important role of OXY in the inhibition of adrenal gland activity and thus a better adaptation to stress on the adrenal gland level.

Role of the pituitary in the effects of tonin on adrenal secretion of the rat

1983 ◽  
Vol 61 (3) ◽  
pp. 201-206 ◽  
Author(s):  
Ernesto L. Schiffrin ◽  
Raul Garcia ◽  
Jolanta Gutkowska ◽  
Jacques Genest
Keyword(s):  
Plasma Renin ◽  
Plasma Corticosterone ◽  
Plasma Aldosterone ◽  
High Rate ◽  
Pituitary Hormone ◽  
Plasma Aldosterone Concentration ◽  
Plasma Angiotensin ◽  
Hypophysectomized Rats ◽  
Adrenal Secretion

Chronically catheterized conscious rats were infused intravenously with tonin at 2.4 and 12 μg∙kg−1∙min−1 for 2 h. Plasma aldosterone concentration (PAC) at the end of the experiment was 11.2 ± 2.4 ng% in controls, 8.5 ± 2.8 ng% in rats infused with tonin at the lower rate, and 26.2 ± 3.6 ng% (p < 0.01 vs. controls) in rats infused at the higher rate. Plasma corticosterone (PC) was significantly higher (p < 0.05) in the group infused at the high rate while plasma renin activity (PRA) was significantly reduced in this group of rats. Plasma angiotensin II (AII) concentration was similar in all three groups. PAC was elevated after tonin infusion in the presence of AII blockade. PAC in conscious sodium-depleted rats infused with tonin was not significantly changed, but PRA was significantly reduced (p < 0.01). In chronically hypophysectomized rats, PAC remained unchanged by tonin infusion. The failure of tonin to stimulate aldosterone in hypophysectomized animals indicates a role of a pituitary hormone (probably ACTH) in the effect of tonin on adrenal secretion.

PREPARATION OF HUMAN GROWTH HORMONE

1961 ◽  
Vol 23 (3) ◽  
pp. 285-NP ◽  
Author(s):  
A. L. C. WALLACE ◽  
K. A. FERGUSON
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth ◽  
High Yield ◽  
Pituitary Hormone ◽  
Simple Method ◽  
Anterior Pituitary Hormone ◽  
Epiphysial Cartilage ◽  
Diethylaminoethyl Cellulose ◽  
Hypophysectomized Rats

SUMMARY A simple method for the preparation of human growth hormone using chromatography on diethylaminoethyl-cellulose is described. Material prepared in this way, when assayed by growth of the tibial epiphysial cartilage in hypophysectomized rats, is at least as active as material prepared by published methods and is obtained in high yield. The only other anterior pituitary hormone activity present in any concentration is prolactin.

scholarly journals CUSHING DISEASE MASQUERADING AS GLAUCOMA

2019 ◽  
Vol 5 (5) ◽  
pp. e290-e293
Author(s):  
Yumiko Tsushima ◽  
Lubna Bashir Munshi ◽  
Charit Taneja ◽  
Se-min Kim
Keyword(s):  
Adrenocorticotropic Hormone ◽  
Case Reports ◽  
Elevated Serum ◽  
Serum Cortisol ◽  
Thyroid Stimulating Hormone ◽  
Pituitary Hormone ◽  
Cushing Disease ◽  
Corticosteroid Administration ◽  
Late Night ◽  
Stimulating Hormone

Objective: Glaucoma is a well-recognized side effect of corticosteroids. However, steroid-induced glaucoma typically refers to that caused by exogenous corticosteroid administration. Glaucoma secondary to endogenous overproduction of corticosteroids has only been reported in a few case reports. We aim to bring attention to glaucoma as a rare but important manifestation of endogenous hypercortisolism. Methods: Patient history, physical exam, laboratory results, and imaging studies were reviewed. Results: We report a case of glaucoma as the initial presentation of Cushing disease (CD). The patient was diagnosed with glaucoma 16 months prior to his endocrinology evaluation. At our initial encounter, the patient had a cushingoid appearance. Levels of 24-hour urinary cortisol and late-night salivary cortisol were elevated. Serum cortisol was not suppressed by 1 mg of dexamethasone overnight, but it was suppressed by 8 mg of dexamethasone. Adrenocorticotropic hormone was also elevated. All other pituitary hormone axes were unremarkable (thyroid-stimulating hormone, free thyroxine, follicle-stimulating hormone, luteinizing hormone, growth hormone, prolactin, and insulin-like growth factor). Pituitary magnetic resonance imaging suggested a small adenoma (2 to 3 mm); therefore, the patient underwent inferior petrosal sinus sampling. The results were consistent with CD. Transsphenoidal resection was performed and final pathology confirmed an adrenocorticotropic hormone-positive adenoma. Hypercortisolism and intraocular pressures improved after the surgery. Conclusion: Glaucoma can lead to irreversible blindness if left untreated or uncontrolled. However, endogenous hypercortisolism-induced glaucoma can be reversed with treatment of the underlying CD. Thus, heightened awareness of extraocular manifestations of secondary causes of glaucoma such as endogenous hypercortisolism is necessary in order to promote prompt evaluation and treatment.

METABOLISM IN VITRO OF TRITIATED ADRENOCORTICOTROPIC HORMONE

1965 ◽  
Vol 43 (9) ◽  
pp. 1489-1498 ◽  
Author(s):  
Edward E. Nishizawa ◽  
R. B. Billiar ◽  
J. Karr ◽  
Kristen B. Eik-Nes
Keyword(s):  
Biological Activity ◽  
Adrenal Gland ◽  
Adrenal Cortex ◽  
Enzymatic Degradation ◽  
Adrenocorticotropic Hormone ◽  
Specific Radioactivity ◽  
Adrenocorticotrophic Hormone ◽  
Serine Residue

Adrenocorticotrophic hormone (ACTH) labeled with tritium has been prepared with a specific radioactivity of approximately 4000 d.p.m./μg. The tritiated trophin showed biological activity and appeared to be bound to the cells of the adrenal gland. Data indicating that the adrenal cortex can inactivate ACTH were obtained; whether such inactivation is due to binding or enzymatic degradation has not been illustrated. Attempts to demonstrate that the adrenal gland could acetylate the N-terminal serine residue of ACTH failed.

PHOSPHORUS METABOLISM OF THE ADRENAL GLAND: THE MECHANISM OF THE CHANGE AFTER HYPOPHYSECTOMY

1954 ◽  
Vol 32 (3) ◽  
pp. 261-270 ◽  
Author(s):  
B. E. Riedel ◽  
R. J. Rossiter
Keyword(s):  
Adrenal Gland ◽  
Specific Activity ◽  
Extracellular Fluid ◽  
Phosphorus Metabolism ◽  
Time Intervals ◽  
Inorganic P ◽  
Fluid Compartment ◽  
Hypophysectomized Rats ◽  
Specific Activities ◽  
Isotope Equilibrium

The specific activity of the intracellular inorganic phosphate (P) of the adrenal gland relative to that of the inorganic P of the plasma is significantly decreased in hypophysectomized rats at time intervals as long as 16 hr. after the injection of inorganic P labelled with P32. The specific activity of the intracellular inorganic P was determined (1) by measuring the specific activity of the easily-hydrolyzable acid-soluble P, which rapidly comes into isotope equilibrium with the intracellular inorganic P, (2) by calculation, from the specific activity of the inorganic P of the whole adrenal, assuming values for the specific activity and the concentration of the inorganic P of the extracellular fluid and the volume of the extracellular fluid compartment, and (3) by measuring the specific activities of the inorganic P of both the adrenal gland and the plasma at a series of time intervals after the injection of the P32. It is concluded that the decrease in the relative specific activity of the intracellular inorganic P of the adrenal is the result of a slowing in the passage of inorganic P32 across the cell membrane, i.e. from the extracellular to the intracellular fluid.

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