scholarly journals The zona reticularis is the site of biosynthesis of dehydroepiandrosterone and dehydroepiandrosterone sulfate in the adult human adrenal cortex resulting from its low expression of 3 beta-hydroxysteroid dehydrogenase.

1996 ◽  
Vol 81 (10) ◽  
pp. 3558-3565 ◽  
Author(s):  
A Endoh ◽  
S B Kristiansen ◽  
P R Casson ◽  
J E Buster ◽  
P J Hornsby
Keyword(s):  
Adrenal Cortex ◽  
Dehydroepiandrosterone Sulfate ◽  
Hydroxysteroid Dehydrogenase ◽  
Zona Reticularis ◽  
Adult Human ◽  
Low Expression

Immunohistochemical studies on 3β-hydroxysteroid dehydrogenase in the adult human adrenal

1998 ◽  
Vol 5 (1) ◽  
pp. 94A-94A
Author(s):  
R MIXON ◽  
R BRISSIE ◽  
W GRIZZLE ◽  
J THOMAS ◽  
O FAYEPELERSEN ◽  
...  
Keyword(s):  
Hydroxysteroid Dehydrogenase ◽  
Adult Human ◽  
Immunohistochemical Studies

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.

PROPERTIES OF RAT ADRENAL ZONA RETICULARIS CELLS: PRODUCTION AND STIMULATION OF CERTAIN STEROIDS

1979 ◽  
Vol 83 (3) ◽  
pp. 435-447 ◽  
Author(s):  
J. B. G. BELL ◽  
R. P. GOULD ◽  
P. J. HYATT ◽  
J. F. TAIT ◽  
S. A. S. TAIT
Keyword(s):  
Adrenal Cortex ◽  
Significant Role ◽  
Zona Fasciculata ◽  
Cell Type ◽  
Acth Stimulation ◽  
Specific Stimulus ◽  
Zona Reticularis ◽  
Cell Pool ◽  
Stimulation Of

The outputs of corticosterone, deoxycorticosterone and androstenedione from dispersed, purified rat adrenal zona reticularis and zona fasciculata cells have been measured by radioimmunoassay. Preferential production of deoxycorticosterone by zona reticularis cells was demonstrated by their higher basal deoxycorticosterone: corticosterone ratio when compared with zona fasciculata cells. Adrenocorticotrophin (ACTH) stimulated corticosterone output by all cell pools prepared by unit gravity (1 g) sedimentation, zona fasciculata cells being stimulated 130-fold compared with 20-fold for the zona reticularis cells in relation to their basal corticosterone output. In every cell pool, ACTH stimulated the output of corticosterone more than it stimulated the output of deoxycorticosterone. In parallel cell preparations, it was shown that ACTH increased the conversion of tracer amounts of radioactive deoxycorticosterone to corticosterone and decreased the conversion of radioactive corticosterone to 11-dehydrocorticosterone. Adrenocorticotrophin did not increase the conversion of radioactive deoxycorticosterone to total 11-oxygenated steroids (corticosterone+ 11-dehydrocorticosterone). It is unlikely therefore that ACTH stimulates 11 β-hydroxylation. Data indicate that the ratio of deoxycorticosterone to total 11-oxygenated steroids (corticosterone +11-dehydrocorticosterone) is characteristic for each cell type, and that this ratio will be relatively independent of ACTH stimulation or the amount of pregnenolone substrate available. Basal androstenedione outputs were similar for both types of cell, and ACTH stimulation was very small, being slightly greater for zona fasciculata than for zona reticularis cells. The contribution of the zona reticularis cells to the basal output of any steroid by the cells of the inner two zones of the adrenal cortex of the rat was relatively small (20% for deoxycorticosterone and 10% for corticosterone) and was even less after stimulation by ACTH. Unless a specific stimulus can be found, therefore, a significant role for the zona reticularis cannot yet be established.

scholarly journals Dehydroepiandrosterone Sulfate and Allopregnanolone Directly Stimulate Catecholamine Production via Induction of Tyrosine Hydroxylase and Secretion by Affecting Actin Polymerization

Endocrinology ◽  
2005 ◽  
Vol 146 (8) ◽  
pp. 3309-3318 ◽  
Author(s):  
I. Charalampopoulos ◽  
Ε. Dermitzaki ◽  
L. Vardouli ◽  
C. Tsatsanis ◽  
C. Stournaras ◽  
...  
Keyword(s):  
Tyrosine Hydroxylase ◽  
Actin Filament ◽  
Chromaffin Cells ◽  
Actin Polymerization ◽  
Dehydroepiandrosterone Sulfate ◽  
Neuroactive Steroids ◽  
Zona Reticularis ◽  
Catecholamine Synthesis ◽  
Catecholamine Levels

Abstract Adrenal cortical cells of zona reticularis produce the neuroactive steroids dehydroepiandrosterone (DHEA), its sulfate ester dehydroepiandrosterone sulfate (DHEAS), and allopregnanolone (ALLO). An interaction between zona reticularis and adrenal medulla has been postulated based on their close proximity and their interwoven borders. The aim of this paper was to examine in vitro the possible paracrine effects of these steroids on catecholamine production from adrenomedullary chromaffin cells, using an established in vitro model of chromaffin cells, the PC12 rat pheochromocytoma cell line. We have found the following: 1) DHEA, DHEAS, and ALLO increased acutely (peak effect between 10–30 min) and dose-dependently (EC50 in the nanomolar range) catecholamine levels (norepinephrine and dopamine). 2) It appears that the acute effect of these steroids involved actin depolymerization/actin filament disassembly, a fast-response cellular system regulating trafficking of catecholamine vesicles. Specifically, 10−6m phallacidin, an actin filament stabilizer, completely prevented steroid-induced catecholamine secretion. 3) DHEAS and ALLO, but not DHEA, also affected catecholamine synthesis. Indeed, DHEAS and ALLO increased catecholamine levels at 24 h, an effect blocked by l-2-methyl-3-(-4hydroxyphenyl)alanine and 3-(hydrazinomethyl)phenol hydrochloride, inhibitors of tyrosine hydroxylase and l-aromatic amino acid decarboxylase, respectively, suggesting that this effect involved catecholamine synthesis. The latter hypothesis was confirmed by finding that DHEAS and ALLO increased both the mRNA and protein levels of tyrosine hydroxylase. In conclusion, our findings suggest that neuroactive steroids exert a direct tonic effect on adrenal catecholamine synthesis and secretion. These data associate the adrenomedullary malfunction observed in old age and neuroactive steroids.

Ultrastructural and immunohistochemical studies on the zona-reticularis cells of the adrenal cortex of normal and 3-methylcholanthrene-treated mice

1985 ◽  
Vol 83 (3-4) ◽  
pp. 207-211
Author(s):  
M. Usa ◽  
K. Ishimura ◽  
H. Fujita ◽  
S. Sugano ◽  
M. Okamoto ◽  
...  
Keyword(s):  
Adrenal Cortex ◽  
Zona Reticularis ◽  
Immunohistochemical Studies

scholarly journals Immunoelectron microscopic localization of three key steroidogenic enzymes (cytochrome P450(scc), 3 beta-hydroxysteroid dehydrogenase and cytochrome P450(c17)) in rat adrenal cortex and gonads

2001 ◽  
Vol 171 (2) ◽  
pp. 373-383 ◽  
Author(s):  
G Pelletier ◽  
S Li ◽  
V Luu-The ◽  
Y Tremblay ◽  
A Belanger ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Steroid Hormones ◽  
Adrenal Cortex ◽  
Leydig Cells ◽  
Ultrastructural Localization ◽  
Hydroxysteroid Dehydrogenase ◽  
Cytochrome P450 Enzymes ◽  
Steroidogenic Enzymes ◽  
Adrenocortical Cells ◽  
Theca Interna

The biosynthesis of steroid hormones in endocrine steroid-secreting glands results from a series of successive steps involving both cytochrome P450 enzymes, which are mixed-function oxidases, and steroid dehydrogenases. So far, the subcellular distribution of steroidogenic enzymes has been mostly studied following subcellular fractionation, performed in placenta and adrenal cortex. In order to determine in situ the intracellular distribution of some steroidogenic enzymes, we have investigated the ultrastructural localization of the three key enzymes: P450 side chain cleavage (scc) which converts cholesterol to pregnenolone; 3 beta-hydroxysteroid dehydrogenase (3 beta-HSD) which catalyzes the conversion of 3 beta-hydroxy-5-ene steroids to 3-oxo-4-ene steroids (progesterone and androstenedione); and P450(c17) which is responsible for the transformation of C(21) into C(19) steroids (dehydroepiandrosterone and androstenedione). Immunogold labeling was used to localize the enzymes in rat adrenal cortex and gonads. The tissues were fixed in 1% glutaraldehyde and 3% paraformaldehyde and included in LR gold resin. In the adrenal cortex, both P450(scc) and 3 beta-HSD immunoreactivities were detected in the reticular, fascicular and glomerular zones. P450(scc) was exclusively found in large mitochondria. In contrast, 3 beta-HSD antigenic sites were mostly observed in the endoplasmic reticulum (ER) with some gold particles overlying crista and outer membranes of the mitochondria. P450(c17) could not be detected in adrenocortical cells. In the testis, the three enzymes were only found in Leydig cells. Immunolabeling for P450(scc) and 3 beta-HSD was restricted to mitochondria, while P450(c17) immunoreactivity was exclusively observed in ER. In the ovary, P450(scc) and 3 beta-HSD immunoreactivities were found in granulosa, theca interna and corpus luteum cells. The subcellular localization of the two enzymes was very similar to that observed in adrenocortical cells. P450(c17) could also be detected in theca interna cells of large developing and mature follicles. As observed in Leydig cells, P450(c17) immunolabeling could only be found in the ER. These results indicate that in different endocrine steroid-secreting cells P450(scc), 3 beta-HSD and P450(c17) have the same association with cytoplasmic organelles (with the exception of 3 beta-HSD in Leydig cells), suggesting similar intracellular pathways for biosynthesis of steroid hormones.

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