CORTISOL UTILIZATION BY SALIVARY GLAND, KIDNEY AND ADRENAL CORTEX

1970 ◽  
Vol 47 (4) ◽  
pp. 511-515 ◽  
Author(s):  
M. M. FERGUSON ◽  
J. B. GLEN ◽  
D. K. MASON
Keyword(s):  
Enzyme Activity ◽  
Sex Differences ◽  
Salivary Gland ◽  
Salivary Glands ◽  
Dehydrogenase Activity ◽  
Adrenal Cortex ◽  
Hydroxysteroid Dehydrogenase ◽  
Histochemical Technique ◽  
Hydroxysteroid Dehydrogenases ◽  
Convoluted Tubules

SUMMARY Cortisol utilization by salivary glands, kidneys and adrenals of various mammals has been compared by using a standard histochemical technique for the demonstration of hydroxysteroid dehydrogenases. 11β-Hydroxysteroid dehydrogenase activity was localized in salivary gland ducts, renal collecting and convoluted tubules and in the adrenal cortex of some species. There was no obvious relationship between the levels of enzyme activity in the salivary glands, kidneys and adrenals. Neither was the presence of 11β-hydroxysteroid dehydrogenase in salivary glands particularly associated with mucous or serous secretion, nor were sex differences in levels of activity evident.

ONTOGENETIC AND PHYLOGENETIC DISTRIBUTION OF HYDROXYSTEROID DEHYDROGENASES IN THE VERTEBRATE KIDNEY

1966 ◽  
Vol 36 (1) ◽  
pp. 29-NP ◽  
Author(s):  
A. H. BAILLIE ◽  
M. M. FERGUSON ◽  
D. McK. HART
Keyword(s):  
Dehydrogenase Activity ◽  
Sex Steroids ◽  
Hydroxysteroid Dehydrogenase ◽  
Phylogenetic Distribution ◽  
Hydroxysteroid Dehydrogenases ◽  
Collecting Tubules ◽  
Convoluted Tubules

SUMMARY The human pronephros showed no hydroxysteroid dehydrogenase activity. The human mesonephros, like piscine and amphibian mesonephroi had 16β- and 17β-hydroxysteroid dehydrogenase activity and a possible function of the human mesonephros is suggested. Metanephric kidneys had 3α-, Δ5-3β-, 3β-, 6β-, 16α-, 16β-, and 17β-hydroxysteroid dehydrogenases; 11β-hydroxysteroid dehydrogenase was present in all adult mammalian metanephric kidneys surveyed. 3α-Hydroxysteroid dehydrogenase was selectively present and very active in the proximal and distal convoluted tubules, particularly of the juxta-medullary glomeruli. This function is thought to be related to the excretion of 3α-ketosteroids. 11β-Hydroxysteroid dehydrogenase was confined to the collecting tubules and its possible involvement in the metabolism of cortisol, aldosterone or androgens in the kidney is noted. 17β-Hydroxysteroid dehydrogenase may be concerned in the excretion of the sex steroids; it occurs throughout the nephron. Δ5-3β-, 16α-, and 16β-hydroxysteroid dehydrogenases were not as active histochemically in the kidney as the 3α-, 3β-, 11β- and 17β-hydroxysteroid dehydrogenases.

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.

ACUTE ENZYME HISTOCHEMICAL CHANGES IN THE ZONA GLOMERULOSA OF THE RAT ADRENAL CORTEX

1968 ◽  
Vol 59 (3) ◽  
pp. 508-518
Author(s):  
J. D. Elema ◽  
M. J. Hardonk ◽  
Joh, Koudstaal ◽  
A. Arends
Keyword(s):  
Peritoneal Dialysis ◽  
Succinate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Adrenal Cortex ◽  
Isocitrate Dehydrogenase ◽  
Hydroxysteroid Dehydrogenase ◽  
Zona Glomerulosa ◽  
Acute Changes ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Histochemical Changes

ABSTRACT Acute changes in glucose-6-phosphate dehydrogenase and isocitrate dehydrogenase activity in the zona glomerulosa of the rat adrenal cortex were induced by peritoneal dialysis with 5 % glucose. Although less clear, the activity of 3β-ol-hydroxysteroid dehydrogenase also seemed to increase as well. No changes were seen in the activity of succinate dehydrogenase. Dialysis with 0.9 % NaCl had no effect on any of the enzymes investigated. The possible significance of these observations is discussed.

ALTERATION OF 3β-HYDROXYSTEROID DEHYDROGENASE ACTIVITY IN RAT OVARIES DURING THE OESTROUS CYCLE

1974 ◽  
Vol 60 (3) ◽  
pp. 441-443 ◽  
Author(s):  
A. M. GAWIENOWSKI ◽  
J. N. CLARK ◽  
C. N. SRINIVASAN
Keyword(s):  
Enzyme Activity ◽  
Dehydrogenase Activity ◽  
Hydroxysteroid Dehydrogenase ◽  
Oestrous Cycle

SUMMARY The activity of 3β-hydroxysteroid dehydrogenase has been determined during various stages of the oestrous cycle in rats. The enzyme activity was high during pro-oestrus and oestrus but low during dioestrus I and II.

scholarly journals Human Cytosolic 3α-Hydroxysteroid Dehydrogenases of the Aldo-keto Reductase Superfamily Display Significant 3β-Hydroxysteroid Dehydrogenase Activity

2003 ◽  
Vol 279 (11) ◽  
pp. 10784-10795 ◽  
Author(s):  
Stephan Steckelbroeck ◽  
Yi Jin ◽  
Sridhar Gopishetty ◽  
Busola Oyesanmi ◽  
Trevor M. Penning
Keyword(s):  
Dehydrogenase Activity ◽  
Hydroxysteroid Dehydrogenase ◽  
Hydroxysteroid Dehydrogenases

3β-HYDROXYSTEROID DEHYDROGENASE ACTIVITY IN THE HUMAN FOETAL ADRENAL CORTEX

1965 ◽  
Vol 48 (3) ◽  
pp. 423-428 ◽  
Author(s):  
M. Niemi ◽  
A. H. Baillie
Keyword(s):  
Dehydrogenase Activity ◽  
Adrenal Cortex ◽  
Substrate Binding ◽  
Hydroxysteroid Dehydrogenase ◽  
List Type ◽  
Histochemical Reaction ◽  
Enzyme Substrate ◽  
Human Male ◽  
Foetal Life ◽  
Free Steroid

ABSTRACT 3β-Hydroxysteroid dehydrogenase activity was studied histochemically in the adrenal cortex of ten human male foetuses, ranging in crownrump length from 3.0 cm to 18.3 cm, with the following steroids: 3β-hydroxy-pregn-5-en-20-one (pregnenolone). 3β,17α-dihydroxy-pregn-5-en-20-one (17α-hydroxypregnenolone). 3β-hydroxy-androst-5-en-17-one (DHA). 3β,17β-dihydroxy-androst-5-ene (androstenediol). 3β-sulphoxy-pregn-5-en-20-one (pregnenolone sulphate). 3β-sulphoxy-17α-hydroxy-pregn-5-en-20-one (17α-hydroxy-pregnenolone sulphate) 3β-sulphoxy-androst-5-en-17-one (DHAsulphate). 3β-hydroxy-5α-androstan-17-one (epiandrosterone). After incubation with pregnenolone, 17α-hydroxypregnenolone, DHA and androstenediol a positive histochemical reaction was obtained in the inner part of the »definitive« cortex and throughout the foetal cortex of all adrenals studied. Initially very weak, the reaction became strongly positive about the twelfth week of foetal life. Pregnenolone sulphate and 17α-hydroxypregnenolong sulphate also gave a histochemical reaction in all the adrenals investigated, but DHA sulphate differed significantly from the free steroid by giving a very poor reaction. Formazan deposition followed incubation with epiandrosterone in all adrenals used and this may imply that a δ5 configuration is not necessary for enzyme-substrate binding.

scholarly journals A HISTOCHEMICAL METHOD FOR THE DEMONSTRATION OF 20α-HYDROXYSTEROID DEHYDROGENASE ACTIVITY IN RAT OVARIES

1964 ◽  
Vol 12 (9) ◽  
pp. 670-673 ◽  
Author(s):  
KÁROLY BALOGH
Keyword(s):  
Enzyme Activity ◽  
Corpus Luteum ◽  
Dehydrogenase Activity ◽  
Present Method ◽  
Hydroxysteroid Dehydrogenase ◽  
Microscopic Level ◽  
Corpora Lutea ◽  
Endocrine Glands ◽  
Progesterone Metabolism ◽  
Rat Ovary

20α-Hydroxysteroid dehydrogenase activity was localized histochemically in the corpus luteum of the rat by using Nitro-BT as an indicator. Intensive enzyme activity was obseryed in the corpus luteum cells, especially during involution. The placenta and corpora lutea of pregnancy failed to reveal enzyme activity during the last week of gravidity. Other tissues, including endocrine glands, liver and kidneys were also negative. The Present method offers a possibility to identify the sites of progesterone metabolism in the rat ovary at the microscopic level.

Purification and Properties of the Soluble 17β-Hydroxysteroid Dehydrogenase of Rabbit Uterus

1979 ◽  
Vol 34 (9-10) ◽  
pp. 726-737 ◽  
Author(s):  
Kunhard Pollow ◽  
Walter Eiger ◽  
Herrmann Heßlinger ◽  
Barbara Pollow
Keyword(s):  
Enzyme Activity ◽  
Dehydrogenase Activity ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Hydroxysteroid Dehydrogenase ◽  
Maximal Velocity ◽  
Ammonium Sulfate Precipitation ◽  
Ph Optimum ◽  
Mobility Data ◽  
Purification And Properties

Abstract 17 β-Hydroxysteroid dehydrogenase activity towards estradiol-17 β has been demonstrated in the 105,000 X g supernatant of rabbit uterus. Hydroxylapatite chromatography of the enzyme activity isolated by ammonium sulfate precipitation, gel filtration and DEAE-cellulose chromato­graphy yielded a single 17 β-hydroxysteroid dehydrogenase activity. Further purification of the enzyme preparation by isoelectric focusing resulted in multiple peaks of activity. The molecular weight or the enzyme, calculated from mobility data on Sephadex gel, is approximately 64,000. Some properties of partially purified 17 β-hydroxysteroid dehydrogenase activity have been studied. Estradiol-17 β reacts at a faster rate than testosterone. The Km for estradiol is 4.16X 10-5 mol/1 for the NAD-linked enzyme activity and 4.37 X 10-5 mol/1 when NADP as cofactor was used. The ratio of the maximal velocity for NADP to that for NAD was 1.42. The pH-optimum for estradiol appears between 9.5 and 10.5 and for estrone between 5.5 and 6.5. The enzyme appears to be of the sulfhydryl type.

HYDROXYSTEROID DEHYDROGENASES IN THE HUMAN ADRENAL CORTEX

1966 ◽  
Vol 34 (4) ◽  
pp. 439-NP ◽  
Author(s):  
K. C. CALMAN ◽  
A. H. BAILLIE ◽  
M. M. FERGUSON ◽  
D. McK. HART
Keyword(s):  
Dehydrogenase Activity ◽  
Cushing’S Syndrome ◽  
Adrenal Glands ◽  
Adrenal Adenoma ◽  
Hydroxysteroid Dehydrogenase ◽  
Cushing's Syndrome ◽  
Normal Adult ◽  
Zona Fasciculata ◽  
Adult Human ◽  
Hydroxysteroid Dehydrogenases

SUMMARY The histochemical utilization of 3α-, 3β-, 6β-, 11α-, 11β-, 12α-, 16α-, 16β-, 17α-, 17β-, 20α-, 21- and 24-hydroxysteroids by three normal adult human adrenal glands, two human foetal adrenal glands, three adrenals from patients with Cushing's syndrome and one adrenal adenoma are described. The normal adult human adrenal showed high 16β-hydroxysteroid dehydrogenase activity in the zona glomerulosa. Activity restricted to the outer part of the zona fasciculata was recorded with 3α-, 3β-, 6β-, 11β-, 16α-, 16β-, and 17β-hydroxysteroids. The zona reticularis utilized 3α-, 3β-, 11β-, 16β- and 17β-hydroxysteroids less well than the zona fasciculata. The adrenals of Cushing's syndrome showed activity only for 3β- and 16β-hydroxysteroid dehydrogenases; this activity was noted in all three zones. The activity pattern of the adrenal adenoma resembled that of the normal adult human adrenal except that greater activity for 16α-hydroxysteroid dehydrogenase was noted. The foetal part of the human foetal cortex was extremely active, showing 3α-, 3β-, 6β-, 11β-, 12α-, 16α-, 16β-, 17β-, 20β- and 21-hydroxysteroid dehydrogenase activity. The definitive cortex behaved similarly to the adult gland and possessed 3α-, 3β-, 11β-, 16β- and 17β-hydroxysteroid dehydrogenases; some evidence of zoning of the definitive cortex was seen with the 16β-hydroxysteroid. The relevance of these findings in the light of current knowledge of adrenal zonation is discussed.

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