17beta-estradiol treatment decreases steroidogenic enzyme messenger ribonucleic acid levels in the rainbow trout testis. 2001

M Govoroun, and O M McMeel, and H Mecherouki, and T J Smith, and Y Guiguen
Institut National de la Recherche Agronomique, Laboratoire Institut National de la Recherche Agronomique-Station Commune de Recherches en Ichtyophysiologie, Biodiversité et Environement, Campus de Beaulieu, 35042 Rennes Cedex, France.

In fish, estrogens are well known for their involvement in ovarian differentiation and have been shown to be very potent feminizing agents when administrated in vivo during early development. However, the mechanism of action of exogenous estrogens is poorly understood. We report here on the feminizing effects of estrogen treatment on the testicular levels of some steroidogenic enzyme messenger RNAs [mRNAs; cholesterol side-chain cleavage (P450scc), 17-hydroxylase/lyase (P450c17), 3beta-hydroxysteroid dehydrogenase (3betaHSD), 11beta-hydroxylase (P45011beta), and aromatase (P450aro)] in the rainbow trout, Oncorhynchus mykiss. Treatment was carried out by dietary administration of 17beta-estradiol (E(2); dosage of 20 mg/kg diet) to a genetically all male population. Steroidogenesis in the differentiating testis was demonstrated to be strongly altered by E(2), as this treatment resulted in considerable decrease in P450c17, 3betaHSD, and P45011beta mRNAs after only 10 days of treatment. In contrast, P450scc and P450aro mRNA levels were unaffected by E(2), with P450scc mRNA levels remaining unaltered and P450aro not stimulated by this feminizing estrogen treatment. To better characterize this E(2) effect, the same treatment was applied on postdifferentiating males, and roughly the same expression pattern was detected with a considerable decrease in testicular P450c17, 3betaHSD, and P45011beta mRNAs and a significant, but reduced, decrease in P450scc mRNA. In the interrenal, these steroidogenic enzyme mRNAs were not significantly affected by this E(2) treatment, except for a slight, but significant, decrease in P450scc mRNA. These results clearly demonstrate that estrogens have profound effects on testicular steroidogenesis and that they are acting specifically on the testis by decreasing mRNA steady state levels of many steroidogenic enzyme genes. The decrease in P45011beta mRNA, and thus inhibition of the synthesis of testicular 11-oxygenated androgens, may be an important step required for the active feminization of these genetic males.

UI MeSH Term Description Entries
D008297 Male Males
D002786 Cholesterol Side-Chain Cleavage Enzyme A mitochondrial cytochrome P450 enzyme that catalyzes the side-chain cleavage of C27 cholesterol to C21 pregnenolone in the presence of molecular oxygen and NADPH-FERRIHEMOPROTEIN REDUCTASE. This enzyme, encoded by CYP11A1 gene, catalyzes the breakage between C20 and C22 which is the initial and rate-limiting step in the biosynthesis of various gonadal and adrenal steroid hormones. CYP11A1,Cholesterol Desmolase,Cholesterol Monooxygenase (Side-Chain-Cleaving),Cytochrome P-450 CYP11A1,Cytochrome P-450(scc),20,22-Desmolase,CYP 11A1,Cytochrome P450 11A1,Cytochrome P450scc,20,22 Desmolase,Cholesterol Side Chain Cleavage Enzyme,Cytochrome P 450 CYP11A1
D004958 Estradiol The 17-beta-isomer of estradiol, an aromatized C18 steroid with hydroxyl group at 3-beta- and 17-beta-position. Estradiol-17-beta is the most potent form of mammalian estrogenic steroids. 17 beta-Estradiol,Estradiol-17 beta,Oestradiol,17 beta-Oestradiol,Aerodiol,Delestrogen,Estrace,Estraderm TTS,Estradiol Anhydrous,Estradiol Hemihydrate,Estradiol Hemihydrate, (17 alpha)-Isomer,Estradiol Monohydrate,Estradiol Valerate,Estradiol Valeriante,Estradiol, (+-)-Isomer,Estradiol, (-)-Isomer,Estradiol, (16 alpha,17 alpha)-Isomer,Estradiol, (16 alpha,17 beta)-Isomer,Estradiol, (17-alpha)-Isomer,Estradiol, (8 alpha,17 beta)-(+-)-Isomer,Estradiol, (8 alpha,17 beta)-Isomer,Estradiol, (9 beta,17 alpha)-Isomer,Estradiol, (9 beta,17 beta)-Isomer,Estradiol, Monosodium Salt,Estradiol, Sodium Salt,Estradiol-17 alpha,Estradiol-17beta,Ovocyclin,Progynon-Depot,Progynova,Vivelle,17 beta Estradiol,17 beta Oestradiol,Estradiol 17 alpha,Estradiol 17 beta,Estradiol 17beta,Progynon Depot
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001141 Aromatase An enzyme that catalyzes the desaturation (aromatization) of the ring A of C19 androgens and converts them to C18 estrogens. In this process, the 19-methyl is removed. This enzyme is membrane-bound, located in the endoplasmic reticulum of estrogen-producing cells of ovaries, placenta, testes, adipose, and brain tissues. Aromatase is encoded by the CYP19 gene, and functions in complex with NADPH-FERRIHEMOPROTEIN REDUCTASE in the cytochrome P-450 system. CYP19,Cytochrome P-450 CYP19,Cytochrome P-450(AROM),Androstenedione Aromatase,CYP 19,CYP19 Protein,Cytochrome P450 19,Estrogen Synthase,Estrogen Synthetase,P450AROM,Aromatase, Androstenedione,Cytochrome P 450 CYP19,Protein, CYP19
D012333 RNA, Messenger RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm. Messenger RNA,Messenger RNA, Polyadenylated,Poly(A) Tail,Poly(A)+ RNA,Poly(A)+ mRNA,RNA, Messenger, Polyadenylated,RNA, Polyadenylated,mRNA,mRNA, Non-Polyadenylated,mRNA, Polyadenylated,Non-Polyadenylated mRNA,Poly(A) RNA,Polyadenylated mRNA,Non Polyadenylated mRNA,Polyadenylated Messenger RNA,Polyadenylated RNA,RNA, Polyadenylated Messenger,mRNA, Non Polyadenylated
D013250 Steroid Hydroxylases Cytochrome P-450 monooxygenases (MIXED FUNCTION OXYGENASES) that are important in steroid biosynthesis and metabolism. Steroid Hydroxylase,Steroid Monooxygenases,Hydroxylase, Steroid,Hydroxylases, Steroid,Monooxygenases, Steroid
D013252 Steroid 11-beta-Hydroxylase A mitochondrial cytochrome P450 enzyme that catalyzes the 11-beta-hydroxylation of steroids in the presence of molecular oxygen and NADPH-FERRIHEMOPROTEIN REDUCTASE. This enzyme, encoded by CYP11B1 gene, is important in the synthesis of CORTICOSTERONE and HYDROCORTISONE. Defects in CYP11B1 cause congenital adrenal hyperplasia (ADRENAL HYPERPLASIA, CONGENITAL). CYP11B1,Cytochrome P-450 CYP11B1,Cytochrome P-450(11 beta),Steroid 11-beta-Monooxygenase,11 beta-Hydroxylase,CYP 11B1,Cytochrome P450 11B1,Steroid 11 Hydroxylase,Steroid 11-Hydroxylase,Steroid-11-Hydroxylase,11 beta Hydroxylase,Cytochrome P 450 CYP11B1,Steroid 11 beta Hydroxylase,Steroid 11 beta Monooxygenase
D013254 Steroid 17-alpha-Hydroxylase A microsomal cytochrome P450 enzyme that catalyzes the 17-alpha-hydroxylation of progesterone or pregnenolone and subsequent cleavage of the residual two carbons at C17 in the presence of molecular oxygen and NADPH-FERRIHEMOPROTEIN REDUCTASE. This enzyme, encoded by CYP17 gene, generates precursors for glucocorticoid, androgen, and estrogen synthesis. Defects in CYP17 gene cause congenital adrenal hyperplasia (ADRENAL HYPERPLASIA, CONGENITAL) and abnormal sexual differentiation. 17 alpha-Hydroxylase,17,20-Lyase,CYP17,Cytochrome P-450(17 alpha),P450(c17),Steroid 17 alpha-Monooxygenase,Steroid 17-Hydroxylase,Steroid 17-Monooxygenase,17 alpha-Hydroxylase Cytochrome P-450,17 alpha-Hydroxyprogesterone Aldolase,17,20-Desmolase,Cytochrome P-450(17-alpha),Cytochrome P450(17 alpha),Hydroxyprogesterone Aldolase,Steroid 17 alpha-Hydroxylase,Steroid-17-Hydroxylase,17 alpha Hydroxylase,17 alpha Hydroxylase Cytochrome P 450,17 alpha Hydroxyprogesterone Aldolase,17 alpha-Hydroxylase, Steroid,17 alpha-Monooxygenase, Steroid,17,20 Desmolase,17,20 Lyase,17-Hydroxylase, Steroid,17-Monooxygenase, Steroid,17-alpha-Hydroxylase, Steroid,Aldolase, 17 alpha-Hydroxyprogesterone,Aldolase, Hydroxyprogesterone,Steroid 17 Hydroxylase,Steroid 17 Monooxygenase,Steroid 17 alpha Hydroxylase,Steroid 17 alpha Monooxygenase,alpha-Hydroxyprogesterone Aldolase, 17,alpha-Monooxygenase, Steroid 17
D013256 Steroids A group of polycyclic compounds closely related biochemically to TERPENES. They include cholesterol, numerous hormones, precursors of certain vitamins, bile acids, alcohols (STEROLS), and certain natural drugs and poisons. Steroids have a common nucleus, a fused, reduced 17-carbon atom ring system, cyclopentanoperhydrophenanthrene. Most steroids also have two methyl groups and an aliphatic side-chain attached to the nucleus. (From Hawley's Condensed Chemical Dictionary, 11th ed) Steroid,Catatoxic Steroids,Steroids, Catatoxic

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