Topic
Hydroxysteroid dehydrogenase
About: Hydroxysteroid dehydrogenase is a research topic. Over the lifetime, 1087 publications have been published within this topic receiving 28468 citations. The topic is also known as: hydroxysteroid dehydrogenase.
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TL;DR: Models of the enzyme-coenzyme-substrate complexes suggest that Lys31, Gly225 and Gly226 are important for ligand recognition and orientation in the active site of AKR1C21.
Abstract: Mouse 3(17)α-hydroxysteroid dehydrogenase (AKR1C21) is a bifunctional enzyme that catalyses the oxidoreduction of the 3- and 17-hydroxy/keto groups of steroid substrates such as oestrogens, androgens and neurosteroids. The structure of the AKR1C21–NADPH binary complex was determined from an orthorhombic crystal belonging to space group P212121 at a resolution of 1.8 A. In order to identify the factors responsible for the bifunctionality of AKR1C21, three steroid substrates including a 17-keto steroid, a 3-keto steroid and a 3α-hydroxysteroid were docked into the substrate-binding cavity. Models of the enzyme–coenzyme–substrate complexes suggest that Lys31, Gly225 and Gly226 are important for ligand recognition and orientation in the active site.
7 citations
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TL;DR: New insights are given to the transcriptional regulation of 3 βHSD1 and 17βHSD7 and further hints to their involvement in steroid metabolism are given.
7 citations
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TL;DR: The interesting finding that 17β-HSD3 inhibitor RM-532-105 is concentrated inside tumors is fortuitously came across from experiments with LAPC-4 cells, where the levels of the androgens testosterone and dihydrotestosterone increased within the tumors.
Abstract: In the fight against androgen-sensitive prostate cancer, the enzyme 17β-hydroxysteroid dehydrogenase type 3 (17β-HSD3) is an attractive therapeutic target considering its key role in the formation of androgenic steroids. In this study, we attempted to assess the in vivo efficacy of the compound RM-532-105, an androsterone derivative developed as an inhibitor of 17β-HSD3, in the prostate cancer model of androgen-sensitive LAPC-4 cells xenografted in nude mice. RM-532-105 did not inhibit the tumor growth induced by 4-androstene-3,17-dione (4-dione); rather, the levels of the androgens testosterone (T) and dihydrotestosterone (DHT) increased within the tumors. In plasma, however, DHT levels increased but T levels did not. In troubleshooting experiments, the non-androgenic potential of RM-532-105 was confirmed by two different assays (LAPC-4 proliferation and androgen receptor transcriptional activity assays). The enzyme 5α-reductase was also revealed to be the predominant enzyme metabolizing 4-dione in LAPC-4 cells, yielding 5α-androstane-3,17-dione and not T. Other 17β-HSDs than 17β-HSD3 seem responsible in the androgen synthesis. From experiments with LAPC-4 cells, we fortuitously came across the interesting finding that 17β-HSD3 inhibitor RM-532-105 is concentrated inside tumors.
7 citations
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TL;DR: Results show that HSD17B11 transcription in PC cells is regulated by Sp1 and C/EBPα and this process was not mediated by the CCAAT boxes located within its proximal promoter region.
7 citations
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TL;DR: It is demonstrated that the testicular 20a-hydroxysteroid dehydrogenase is not assembled into a polymeric form even while performing its enzymic function.
7 citations