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.
Papers published on a yearly basis
Papers
More filters
••
24 Feb 2021TL;DR: In this article, the authors explore metabolism of BAs and glucocorticoids with a focus on biotransformation by microbial Hydroxysteroid dehydrogenases (HSDHs).
Abstract: Bile acids (BAs) and glucocorticoids are steroid hormones derived from cholesterol that are important signaling molecules in humans and other vertebrates. Hydroxysteroid dehydrogenases (HSDHs) are encoded both by the host and by their resident gut microbiota, and they reversibly convert steroid hydroxyl groups to keto groups. Pairs of HSDHs can reversibly epimerize steroids from α-hydroxy conformations to β-hydroxy, or β-hydroxy to ω-hydroxy in the case of ω-muricholic acid. These reactions often result in products with drastically different physicochemical properties than their precursors, which can result in steroids being activators or inhibitors of host receptors, can affect solubility in fecal water, and can modulate toxicity. Microbial HSDHs modulate sterols associated with diseases such as colorectal cancer, liver cancer, prostate cancer, and polycystic ovary syndrome. Although the role of microbial HSDHs is not yet fully elucidated, they may have therapeutic potential as steroid pool modulators or druggable targets in the future. In this review, we explore metabolism of BAs and glucocorticoids with a focus on biotransformation by microbial HSDHs.
27 citations
••
TL;DR: The cloning and characterization of the mouse type 5 17beta-HSD belonging to the aldo-keto reductase superfamily is reported, in contrast with types 1, 2, 3, 4, 6, and 7 17 beta-HSDs which belong to the short-chain alcohol dehydrogenase family.
27 citations
••
TL;DR: Findings suggest new roles for both peroxisome proliferator-activated receptor α and 17β-hydroxysterol dehydrogenase type 11 in lipid metabolism and/or detoxification in the intestine.
Abstract: In order to study the role of peroxisome proliferator-activated receptor α in mouse intestine, its agonist-induced proteins were identified by peptide mass fingerprinting followed by Northern blot analysis using their cDNAs One of the most remarkably induced proteins was identified as 17β-hydroxysterol dehydrogenase type 11 Its very rapid induction by various agonists was most efficient in intestine and then in liver These findings together with recently reported results showing the enzyme family's wide substrate spectrum, including not only glucocorticoids and sex steroids but also bile acids, fatty acids and branched chain amino acids, suggest new roles for both peroxisome proliferator-activated receptor α and 17β-hydroxysterol dehydrogenase type 11 in lipid metabolism and/or detoxification in the intestine
27 citations
••
TL;DR: Evidence is provided of powerful interactive effects between steroidal and paracrine control of human breast epithelial cells in vitro and a synergy between the 2 factors is indicated.
26 citations
••
TL;DR: Hydroxysteroid dehydrogenase activity was studied histochemically in the ovary and placenta of the rat, rabbit, guinea pig, cow and human, and in the testis of theRat.
Abstract: Hydroxysteroid dehydrogenase activity was studied histochemically in the ovary and placenta of the rat, rabbit, guinea pig, cow and human, and in the testis of the rat. Hydroxysteroids with the 3α, 3β, 17α, 17β, 20α and 20β configurations were used. The 3β-hydroxysteroid dehydrogenase activity was observed in the theca interna, corpus luteum and interstitial cells of the ovary, in the Leydig cells of the rat testis, in the syncytial trophoblast of the human placenta, and in the trophoblastic giant cells of the rat and guinea pig. The luteal cells of the rabbit showed less activity than did the interstitial cells except in early pregnancy, when their activities were equal. The cow placenta was negative. Activity with 17β-hydroxysteroids was found only in the ovary of the guinea pig and in the human syncytial trophoblast. No 20α- or 20β-hydroxysteroid dehydrogenase activity was observed. Increasing the alkalinity of the incubation medium to pH 9.5 or substituting TPN for DPN did not alter the results. (Endo...
26 citations