| Autor: |
Wilkin, R. P., Bruchovsky, N., Shnitka, T. K., Rennie, P. S., Comeau, T. L. |
| Zdroj: |
European Journal of Endocrinology; June 1980, Vol. 94 Issue: 2 p284-288, 5p |
| Abstrakt: |
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−1mg protein−1was 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−130 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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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