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Data on the localization of EGFP and 20α-hydroxysteroid dehydrogenase (20α-HSD) in the placenta and testes of transgenic mice.

ABSTRACT: In order to investigate the function of monkey 20α-hydroxysteroid dehydrogenase (20α-HSD), transgenic mice (tg) were produced, expressing enhanced green fluorescent protein (EGFP) under the control of the monkey 20α-HSD promoter. The expression levels and localization of EGFP and 20α-HSD were analyzed in immature testis and in placenta. In support of our recent publication, "Characterization of transgenic mice expressing EGFP under control of monkey 20α-hydroxysteroid dehydrogenase promoter" (Park et al., 2018) [1], it was important to characterize the function of EGFP and 20α-HSD in the ovarian luteal cells of tg mice. Here, the expression of EGFP and 20α-HSD in immature testis and placenta are presented. The expression level of EGFP and 20α-HSD were detected in the testes 1 week after birth, and increased dramatically at 8 weeks. Both of proteins strongly detected in the placenta on days 14, 16, and 18 of pregnancy. Immunohistochemical analysis revealed that EGFP was detected in the seminiferous epithelium and 20α-HSD was specifically localized in the seminiferous tubule at 8 weeks.

SUBMITTER: Yoo MH

PROVIDER: S-EPMC5997899 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature

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Data on the localization of EGFP and 20α-hydroxysteroid dehydrogenase (20α-HSD) in the placenta and testes of transgenic mice.

Yoo Mi-Hyang MH Park Chae-Won CW Byambaragchaa Munkhzaya M Kang Myung-Hwa MH Min Kwan-Sik KS

Data in brief 20180519

In order to investigate the function of monkey 20α-hydroxysteroid dehydrogenase (20α-HSD), transgenic mice (tg) were produced, expressing enhanced green fluorescent protein (EGFP) under the control of the monkey 20α-HSD promoter. The expression levels and localization of EGFP and 20α-HSD were analyzed in immature testis and in placenta. In support of our recent publication, "Characterization of transgenic mice expressing EGFP under control of monkey 20α-hydroxysteroid dehydrogenase promoter" (Pa ...[more]

PMID: 29900362

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Project description:Metabolic inactivation of progesterone within uterine myocytes by 20α-hydroxysteroid dehydrogenase (20α-HSD) has been postulated as a mechanism contributing to functional progesterone withdrawal at term. In humans, 20α-HSD is encoded by the gene AKR1C1. Myometrial AKR1C1 mRNA abundance has been reported to increase significantly during labor at term. In spontaneous preterm labor, however, we previously found no increase in AKR1C1 mRNA level in the myometrium except for preterm labor associated with clinical chorioamnionitis. This suggests that increased 20α-HSD activity is a mechanism through which inflammation drives progesterone withdrawal in preterm labor. In this study, we have determined the effects of various treatments of therapeutic relevance on AKR1C1 expression in pregnant human myometrium in an ex vivo culture system. AKR1C1 expression increased spontaneously during 48 h culture (p < 0.0001), consistent with the myometrium transitioning to a labor-like phenotype ex vivo, as reported previously. Serum supplementation, prostaglandin F2α, phorbol myristate acetate, and mechanical stretch had no effect on the culture-induced increase, whereas progesterone (p = 0.0058) and cAMP (p = 0.0202) further upregulated AKR1C1 expression. In contrast, culture-induced upregulation of AKR1C1 expression was dose-dependently repressed by three histone/protein deacetylase inhibitors: trichostatin A at 5 (p = 0.0172) and 25 µM (p = 0.0115); suberoylanilide hydroxamic acid at 0.5 (p = 0.0070), 1 (p = 0.0045), 2.5 (p = 0.0181), 5 (p = 0.0066) and 25 µM (p = 0.0014); and suberoyl bis-hydroxamic acid at 5 (p = 0.0480) and 25 µM (p = 0.0238). We propose the inhibition of histone/protein deacetylation helps to maintain the anti-inflammatory, pro-quiescence signaling of progesterone in pregnant human myometrium by blocking its metabolic inactivation. Histone deacetylase inhibitors may represent a class of agents that preserve or restore the progesterone sensitivity of the pregnant uterus.

Project description:BackgroundEpi-testosterone (epiT) is the 17alpha-epimer of testosterone. It has been found at similar level as testosterone in human biological fluids. This steroid has thus been used as a natural internal standard for assessing testosterone abuse in sports. EpiT has been also shown to accumulate in mammary cyst fluid and in human prostate. It was found to possess antiandrogenic activity as well as neuroprotective effects. So far, the exact pathway leading to the formation of epiT has not been elucidated.ResultsIn this report, we describe the isolation and characterization of the enzyme 17alpha-hydroxysteroid dehydrogenase. The name is given according to its most potent activity. Using cells stably expressing the enzyme, we show that 17alpha-HSD catalyzes efficienty the transformation of 4-androstenedione (4-dione), dehydroepiandrosterone (DHEA), 5alpha-androstane-3,17-dione (5alpha-dione) and androsterone (ADT) into their corresponding 17alpha-hydroxy-steroids : epiT, 5-androstene-3beta,17alpha-diol (epi5diol), 5alpha-androstane-17alpha-ol-3-one (epiDHT) and 5alpha-androstane-3alpha,17alpha-diol (epi3alpha-diol), respectively. Similar to other members of the aldo-keto reductase family that possess the ability to reduce the keto-group into hydroxyl-group at different position on the steroid nucleus, 17alpha-HSD could also catalyze the transformation of DHT, 5alpha-dione, and 5alpha-pregnane-3,20-dione (DHP) into 3alpha-diol, ADT and 5alpha-pregnane-3alpha-ol-20-one (allopregnanolone) through its less potent 3alpha-HSD activity. We also have over-expressed the 17alpha-HSD in Escherichia coli and have purified it by affinity chromatography. The purified enzyme exhibits the same catalytic properties that have been observed with cultured HEK-293 stably transfected cells. Using quantitative Realtime-PCR to study tissue distribution of this enzyme in the mouse, we observed that it is expressed at very high levels in the kidney.ConclusionThe present study permits to clarify the biosynthesis pathway of epiT. It also offers the opportunity to study gene regulation and function of this enzyme. Further study in human will allow a better comprehension about the use of epiT in drug abuse testing; it will also help to clarify the importance of its accumulation in breast cyst fluid and prostate, as well as its potential role as natural antiandrogen.

Dataset Information

Data on the localization of EGFP and 20α-hydroxysteroid dehydrogenase (20α-HSD) in the placenta and testes of transgenic mice.

Publications

Data on the localization of EGFP and 20α-hydroxysteroid dehydrogenase (20α-HSD) in the placenta and testes of transgenic mice.

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