Stromal 5α-reductase activity is elevated in benign prostatic hyperplasia

1980 ◽  
Vol 94 (2) ◽  
pp. 284-288 ◽  
Author(s):  
R. P. Wilkin ◽  
N. Bruchovsky ◽  
T. K. Shnitka ◽  
P. S. Rennie ◽  
T. L. Comeau
Keyword(s):  
Benign Prostatic Hyperplasia ◽  
Specific Activity ◽  
Reductase Activity ◽  
Hydroxysteroid Dehydrogenase ◽  
Prostatic Hyperplasia ◽  
Primary Site ◽  
Human Prostate ◽  
The Mean ◽  
Abnormal Condition

Abstract. The activities of 5α-reductase and 3α(β)-hydroxysteroid dehydrogenase were assayed in homogenates of stroma and epithelium obtained from 3 normal, 9 hyperplastic and 2 carcinomatous human prostates. Irrespective of the normal or abnormal condition of the prostate, the localization of 5α-reductase was predominantly in stroma whereas the reductive and oxidative activities of 3α(β)-hydroxysteroid dehydrogenase were more evenly divided between stroma and epithelium. Furthermore, the mean specific activity of 5α-reductase in hyperplastic stroma at 84.6 ± 13.1 (± sem) pmol 30 min−1 mg protein−1 was almost 3 times greater (Student's t-test, P < 0.05) than the corresponding value in normal stroma, 31.6 ± 7.2 pmol mg protein−1 30 min−1. We conclude that the stroma is the primary site of conversion of testosterone to dihydrotestosterone in the human prostate owing to the prevalence in stroma of 5α-reductase, and that benign prostatic hyperplasia is characterized by an increased amount of stromal 5α-reductase activity.

Localization of angiotensin-converting enzyme in the human prostate: pathological expression in benign prostatic hyperplasia

2001 ◽  
Vol 195 (5) ◽  
pp. 571-579 ◽  
Author(s):  
Labrini Nassis ◽  
Albert G. Frauman ◽  
Mitsuru Ohishi ◽  
Jialong Zhuo ◽  
David J. Casley ◽  
...  
Keyword(s):  
Benign Prostatic Hyperplasia ◽  
Angiotensin Converting Enzyme ◽  
Prostatic Hyperplasia ◽  
Human Prostate ◽  
Converting Enzyme

scholarly journals Ghrelin Aggravates Prostate Enlargement in Rats with Testosterone-Induced Benign Prostatic Hyperplasia, Stromal Cell Proliferation, and Smooth Muscle Contraction in Human Prostate Tissues

2019 ◽  
Vol 2019 ◽  
pp. 1-14 ◽  
Author(s):  
Xiaolong Wang ◽  
Yiming Wang ◽  
Christian Gratzke ◽  
Christian Sterr ◽  
Qingfeng Yu ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Benign Prostatic Hyperplasia ◽  
Muscle Contraction ◽  
Stromal Cell ◽  
Molecular Mechanisms ◽  
Smooth Muscle Contraction ◽  
Prostatic Hyperplasia ◽  
Human Prostate ◽  
Mrna Levels ◽  
Prostate Enlargement

Epidemiologic studies revealed a context between lower urinary tract symptoms (LUTS) suggestive of benign prostatic hyperplasia (BPH) and metabolic syndrome. However, molecular mechanisms underlying this relationship are largely unknown. Prostate enlargement and increased prostate smooth muscle tone are important factors in the pathophysiology of LUTS suggestive of BPH. In the present study, we studied effects of the metabolic hormone ghrelin on prostate enlargement in rats with experimentally induced BPH, growth of cultured stromal cells from human prostate (WPMY-1), and smooth muscle contraction of human prostate tissues. Ghrelin (20 nmol/kg daily, p.o., 2 weeks) increased prostate size in rats with testosterone-induced BPH. Microarray identified 114 ghrelin-upregulated genes (2-fold or more) in these prostates, with possible roles in growth, smooth muscle contraction, or metabolism. 12 genes were selected for further analyses. In human prostate tissues, mRNA levels of 11 of them correlated positively with ghrelin receptor (GHSR) expression, but only two with the degree of BPH. Accordingly, no correlation was evident between GHSR expression level and BPH in human prostate tissues. In WPMY-1 cells, the GHRS agonist MK0677 upregulated 11 of the selected genes. MK0677 induced proliferation of WPMY-1 cells, shown by EdU assay, colony formation, proliferation markers, flow cytometry, and viability. In myographic measurements, GHSR agonists enhanced contractions of human prostate strips. Together, ghrelin may aggravate prostate enlargement, stromal cell growth, and prostate smooth muscle contraction in BPH. Ghrelin may deteriorate urethral obstruction independently from BPH, qualifying the ghrelin system as an attractive new target to be tested for LUTS treatment in BPH.

Stroma of human benign prostatic hyperplasia: preferential tissue for androgen metabolism and oestrogen binding

1981 ◽  
Vol 96 (3) ◽  
pp. 422-432 ◽  
Author(s):  
M. Krieg ◽  
G. Klötzl ◽  
J. Kaufmann ◽  
K. D. Voigt
Keyword(s):  
Benign Prostatic Hyperplasia ◽  
Binding Sites ◽  
Reductase Activity ◽  
Enzyme Reaction ◽  
Prostatic Hyperplasia ◽  
Binding Studies ◽  
Normal Prostate ◽  
Layer Chromatography ◽  
Androgen Binding ◽  
Tissue Fraction

Abstract. Because of the well known stromal-epithelial interaction of various urogenital organs, it was of interest to compare quantitatively steroid metabolism and binding in epithelium (E) and stroma (S) of the human benign prostatic hyperplasia (BPH). Testosterone 5α-reductase activity was determined by thin-layer chromatography and androgen as well as oestrogen binding sites by a charcoal adsorption technique after a steroid incubation period of 18 h at 0°C, using methyltrienolone (R1881) and oestradiol-17β as tritiated ligands and unlabelled R1881 and diethylstilboestrol as the respective competitors. The main results were as follows: (1) using biochemical markers (acid phosphatase, hydroxyproline), an on average 17% contamination of E by S and 6% of S by E was found, (2) the molar optimum of NADPH for the enzyme reaction was nearly identical in E and S, ranging between 1 and 0.1 mm, (3) the apparent Michaelis constant (Km) of 5α-reductase was in both fractions identical, the mean being 0.15 (μm, (4) the maximal rate of 5α-reductase activity (pmol 5α-reduced metabolites · mg protein−1 · 1 h−1) was 161 ± 28 (sem; n = 20), 66 ± 4.6 and 148 ± 6.6 in S, E and whole tissue fraction of BPH, respectively. In two normal prostates the means were: 88, 53 and 73, respectively, (5) the androgen binding sites were evenly distributed between the cytosol of E and S, while measurable oestrogen binding sites were found in 42% of the analyzed S but only in 5% of analyzed E. In conclusion: the 2.4 times higher 5·-reductase activity in S compared to E of the BPH is responsible for the about 2 to 2.5 times higher activity in the whole tissue fraction of BPH if compared with the normal prostate. Furthermore, due to our preliminary binding studies, oestrogens might play an important role in the S fraction of BPH.

Ultrastructural aspects of human prostate in benign prostatic hyperplasia

The Prostate ◽  
1982 ◽  
Vol 3 (1) ◽  
pp. 99-108 ◽  
Author(s):  
Graziella Biagini ◽  
Paola Preda ◽  
Michele Lo Cigno ◽  
Marcello Soli ◽  
Edward Bercovich
Keyword(s):  
Benign Prostatic Hyperplasia ◽  
Prostatic Hyperplasia ◽  
Human Prostate

Differential nuclear matrix-intermediate filament expression in human prostate cancer in respect to benign prostatic hyperplasia

1996 ◽  
Vol 109 (1-2) ◽  
pp. 193-198 ◽  
Author(s):  
Ingles Alberti ◽  
Silvio Parodi ◽  
Paola Barboro ◽  
Paola Sanna ◽  
Guido Nicolò ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Benign Prostatic Hyperplasia ◽  
Nuclear Matrix ◽  
Intermediate Filament ◽  
Prostatic Hyperplasia ◽  
Human Prostate ◽  
Human Prostate Cancer
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