Author:
Naidansuren Purevjargal,Park Cha-Won,Kim Sang-Hwan,Nanjidsuren Tseeleema,Park Jong-Ju,Yun Seong-Jo,Sim Bo-Woong,Hwang Seongsoo,Kang Myung-Hwa,Ryu Buom-Yong,Hwang Sue-Yun,Yoon Jong-Taek,Yamanouchi Keitaro,Min Kwan-Sik
Abstract
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%). 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 20α-HSD was generated in a rabbit immunized with the purified, recombinant protein. Recombinant 20α-HSD protein produced in mammalian cells had a molecular weight of ∼37 kDa. Bacterially expressed bovine 20α-HSD protein showed enzymatic activity. The expression pattern of the 20α-HSD protein in the pre-parturition placenta and the CL1 stage of the estrous cycle was similar to the level of 20α-HSD mRNA expression. Immunohistochemical analysis also revealed that bovine 20α-HSD protein was intensively localized in the large luteal cells during the late estrous cycle.
Subject
Cell Biology,Obstetrics and Gynecology,Endocrinology,Embryology,Reproductive Medicine
Cited by
16 articles.
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