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Molecular characterization of bovine placental and ovarian 20?-hydroxysteroid dehydrogenase.

ABSTRACT: The enzyme 20?-hydroxysteroid dehydrogenase (20?-HSD) catalyzes the conversion of progesterone to its inactive form, 20?-hydroxyprogesterone. This enzyme plays a critical role in the regulation of luteal function in female mammals. In this study, we conducted the characterization and functional analyses of bovine 20?-HSD from placental and ovarian tissues. The nucleotide sequence of bovine 20?-HSD showed significant homology to that of goats (96%), humans (84%), rabbits (83%), and mice (81%). The mRNA levels increased gradually throughout the estrous cycle, the highest being in the corpus luteum (CL) 1 stage. Northern blot analysis revealed a 1.2? kb mRNA in the bovine placental and ovarian tissues. An antibody specific to bovine 20?-HSD was generated in a rabbit immunized with the purified, recombinant protein. Recombinant 20?-HSD protein produced in mammalian cells had a molecular weight of ?37? kDa. Bacterially expressed bovine 20?-HSD protein showed enzymatic activity. The expression pattern of the 20?-HSD protein in the pre-parturition placenta and the CL1 stage of the estrous cycle was similar to the level of 20?-HSD mRNA expression. Immunohistochemical analysis also revealed that bovine 20?-HSD protein was intensively localized in the large luteal cells during the late estrous cycle.

SUBMITTER: Naidansuren P

PROVIDER: S-EPMC3207728 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature

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Molecular characterization of bovine placental and ovarian 20α-hydroxysteroid dehydrogenase.

Naidansuren Purevjargal P Park Cha-Won CW Kim Sang-Hwan SH Nanjidsuren Tseeleema T Park Jong-Ju JJ Yun Seong-Jo SJ Sim Bo-Woong BW Hwang Seongsoo S Kang Myung-Hwa MH Ryu Buom-Yong BY Hwang Sue-Yun SY Yoon Jong-Taek JT Yamanouchi Keitaro K Min Kwan-Sik KS

Reproduction (Cambridge, England) 20110909 5

The enzyme 20α-hydroxysteroid dehydrogenase (20α-HSD) catalyzes the conversion of progesterone to its inactive form, 20α-hydroxyprogesterone. This enzyme plays a critical role in the regulation of luteal function in female mammals. In this study, we conducted the characterization and functional analyses of bovine 20α-HSD from placental and ovarian tissues. The nucleotide sequence of bovine 20α-HSD showed significant homology to that of goats (96%), humans (84%), rabbits (83%), and mice (81%). Th ...[more]

PMID: 21908655

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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.

Dataset Information

Molecular characterization of bovine placental and ovarian 20?-hydroxysteroid dehydrogenase.

Publications

Molecular characterization of bovine placental and ovarian 20α-hydroxysteroid dehydrogenase.

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