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: A significantly higher mRNA concentration in the subcortical white matter than in the cerebral cortex of women and men and reductive 17beta-HSD in vitro activity with 2 microM androstenedione as the substrate revealed no sex specific differences.
32 citations
TL;DR: Four patients with the 46,XY karyotype and 17-β-HSD3 deficiency are reported, showing different degrees of genital ambiguity, increased androstenedione and decreased testosterone levels, and testosterone to androstensione ratio < 0.8.
Abstract: The enzyme 17β-hydroxysteroid dehydrogenase type 3 (17-β-HSD3) catalyzes the conversion of androstenedione to testosterone in the testes, and its deficiency is a rare disorder of sex development in 46,XY individuals. It can lead to a wide range of phenotypic features, with variable hormonal profiles. We report four patients with the 46,XY karyotype and 17-β-HSD3 deficiency, showing different degrees of genital ambiguity, increased androstenedione and decreased testosterone levels, and testosterone to androstenedione ratio G novel mutation, and c.277+4A>T mutation, both located within the intron 3 splice donor site of the HSD17B3 gene, were identified in case 3. In addition, homozygosis for the missense p.Ala203Val, p.Gly289Ser, p.Arg80Gln mutations were found upon HSD17B3 gene sequencing in cases 1, 2, and 4, respectively.
32 citations
TL;DR: A dual steroidogenic activity of the 17βHSD2 enzyme is established after transfection of human 17β HSD2-transfected human embryonic kidney (293) cells to obtain a better understanding of the regulation of local steroid biosynthesis and metabolism in human tissues.
Abstract: The type 2 isoform of human 17β-hydroxysteroid dehydrogenase (17βHSD2) efficiently catalyzes the oxidative metabolism of androgens and estrogens, and it is expressed in a large series of human peripheral tissues. To obtain a better understanding of the regulation of local steroid biosynthesis and metabolism in human tissues, we have established a dual steroidogenic activity of the 17βHSD2 enzyme after transfection of human 17βHSD2-transfected human embryonic kidney (293) cells. After transient transfection, the metabolism of testosterone, pregnenolone, and dehydroepiandrosterone (DHEA) in intact transfected 293 cells was evaluated by TLC-based radiometric assays. 17βHSD2-transfected cells converted 91% of testosterone (1 μmol/L) into androstenedione in a 2-h incubation period. In addition, pregnenolone (1 μmol/L) was converted to progesterone (18.5%), whereas DHEA (1 μmol/L) was metabolized to androstenedione (8.3% conversion) in a 15-h incubation period. The kinetics of the 3β-hydroxysteroid dehydrogenas...
32 citations
TL;DR: Docking studies with 1-3 into the crystal structure of human 11beta-HSD1 reveal how the molecules may interact with the enzyme and cofactor and give further scope for structure based drug design in the optimisation of these series.
32 citations
TL;DR: It is proposed that the steroid recognition site on 17β-OH-steroid dehydrogenase evolved from an ancestral recognition site for polyols such as ribitol and glucitol-6-phosphate.
Abstract: The amino acid sequence of human placental 17β-hydroxysteroid dehydrogenase (17β-OH-steroid dehydrogenase) was found to be similar to that of the NodG protein of Rhizobium meliloti. The computer-based comparison score is 11.5 SD higher than that obtained with 2500 comparisons of randomized sequences of these proteins. The probability of getting such a score by chance is 6 × 10−31. 17β-OH-steroid dehydrogenase is also similar to Klebsiella aerogenes ribitol dehydrogenase and Escherichia coli glucitol-6-phosphate dehydrogenase. We propose that the steroid recognition site on 17β-OH-steroid dehydrogenase evolved from an ancestral recognition site for polyols such as ribitol and glucitol-6-phosphate.
32 citations