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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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Journal ArticleDOI
TL;DR: Open-reading-frame analysis and the deduced amino acid sequence predict a protein with a molecular mass of 32.3 kDa which belongs to the superfamily of the short-chain dehydrogenase proteins which points to an involvement of the 11 beta-HSD1A isoform in the reductive phase-I metabolism of xenobiotic compounds, besides its endocrinological functions.
Abstract: Screening of a mouse liver λgt 11 cDNA library with a rat liver 11β-hydroxysteroid dehydrogenase cDNA (11β-HSDr1A) and subsequent screening with an isolated mouse probe, resulted in the isolation and structure determination of a mouse cDNA encoding an amino acid sequence which is very similar to human and rat 11β-hydroxysteroid dehydrogenases (78% and 86% similar, respectively), and also to other known vertebrate 11β-hydroxysteroid dehydrogenase structures. Open-reading-frame analysis and the deduced amino acid sequence predict a protein with a molecular mass of 32.3 kDa which belongs to the superfamily of the short-chain dehydrogenase proteins. The amino acid sequence contains two potential glycosylation sites. These data are in agreement with information on the glycoprotein character of the native enzyme. This kind of post-translational modification seems to be a determining factor concerning the equilibrium of the catalyzed 11β-dehydrogenation/11-oxo reduction step [Obeid, J., Curnow, K. M., Aisenberg, J. & White, P. C. (1993) Mol. Endocrinol. 7, 154–160; Agarwal, A. K., Tusie-Luna, M. T., Monder, C. & White, P. C. (1990) Mol. Endocrinol. 4, 1827–18321. After in vitro transcription/translation of the mouse cDNA, immunoprecipitation with anti-(microsomal carbonyl reductase) serum and N-terminal sequence analysis of the purified protein confirms the identity of microsomal 11β-hydroxysteroid dehydrogenase with the previously described, microsomal-bound xenobiotic carbonyl reductase [Maser, E. & Bannenberg, G. (1994) Biochem. Pharmacol., 1805–1812], and points to an involvement of the 11β-HSD1A isofom in the reductive phase-I metabolism of xenobiotic compounds, besides its endocrinological functions. The alignment and comparison to other hydroxysteroid dehydrogenase forms of the same protein superfamily allows the identification of important residues in the 11β-HSD primary structure.

60 citations

Journal ArticleDOI
TL;DR: The results indicate that in both male and female mice, 17HSD type 2 is expressed mainly in the various epithelial cell types of the gastrointestinal and urinary tracts, and therefore suggest a role for the enzyme in steroid inactivation in a range of tissues and cell types not considered as classical sex steroid target tissues.
Abstract: Hydroxysteroid dehydrogenase (17HSD) type 2e Yciently catalyzes the conversion of the high activity 17‚-hydroxy forms of sex steroids into less potent 17-ketosteroids. In the present study in situ hybridization was utilized to analyze the cellular localization of 17HSD type 2 expression in adult male and female mice. The data indicate that 17HSD type 2 mRNA is expressed in several epithelial cell layers, including both absorptive and secretory epithelia as well as protective epithelium. In both males and females, strong expression of 17HSD type 2 was particularly detected in epithelial cells of the gastrointestinal and urinary tracts. The mRNA was expressed in the stratified squamous epithelium of the esophagus, and surface epithelial cells of the stomach, small intestine and colon. The hepatocytes of the liver and the thick limbs of the loops of Henle in the kidneys, as well as the epithelium of the urinary bladder, also showed strong expression of 17HSD type 2 mRNA in both male and female mice. In the genital tracts, low 17HSD type 2 expression was detected in the seminiferous tubules, the uterine epithelial cells and the surface epithelium of the ovary. Expression of the mRNA was also detected in the sebaceous glands of the skin. The results indicate that in both male and female mice, 17HSD type 2 is expressed mainly in the various epithelial cell types of the gastrointestinal and urinary tracts, and therefore suggest a role for the enzyme in steroid inactivation in a range of tissues and cell types not considered as classical sex steroid target tissues.

60 citations

Journal ArticleDOI
TL;DR: A specific, simple, and reliable method for the quantitative determination of 3 alpha-hydroxy bile acids in serum using a highly purified 3alpha-hydroxyl group of the steroid molecule and fluorimetric determination of NADH is described.
Abstract: A specific, simple, and reliable method for the quantitative determination of 3 alpha-hydroxy bile acids in serum in described. It is based on the specific enzymatic conversion of the 3alpha-hydroxyl group of the steroid molecule using a highly purified 3alpha-hydroxysteroid dehydrogenase and fluorimetric determination of NADH. A liquid-solid extraction employing Amberlite XAD-2 has been used. Overall recovery of the major human bile acids from normal and jaundiced serum averaged 91.2%. The range of normal values for serum bile acids was found to be 0.9-6.3 mumoles/1 (mean 3.0).

60 citations

Journal ArticleDOI
TL;DR: It was concluded that prolactin suppresses the synthesis of 20α-hydroxysteroid dehydrogenase in corpora lutea and that this hormone may owe part of its “luteotrophic” action in the rat to this effect.

59 citations

Journal ArticleDOI
TL;DR: This study describes the isolation, characterization, and tissue-specific expression of a sixth member of this gene family, 3β-HSD VI, which functions as an NAD+-dependent dehydrogenase/isomerase exhibiting very low Michaelis-Menten constant (Km) values for pregnenolone and dehydroepiandrosterone.
Abstract: The enzyme 3beta-hydroxysteroid dehydrogenase (3beta-HSD) is a key enzyme in the biosynthesis of steroid hormones. To date, this laboratory has isolated and characterized five distinct 3beta-HSD complementary DNAs (cDNAs) in the mouse (3beta-HSD I through V). These different forms are expressed in a tissue- and developmentally-specific manner and fall into two functionally distinct enzymes. 3beta-HSD I and III, and most likely II, function as dehydrogenase/isomerases, whereas 3beta-HSD IV and V function as 3-ketosteroid reductases. This study describes the isolation, characterization, and tissue-specific expression of a sixth member of this gene family, 3beta-HSD VI. This new isoform functions as an NAD+-dependent dehydrogenase/isomerase exhibiting very low Michaelis-Menten constant (Km) values for pregnenolone (approximately 0.035 microM) and dehydroepiandrosterone (approximately 0.12 microM). 3beta-HSD VI is the earliest isoform to be expressed during embryogenesis in cells of embryonic origin at 7 and 9.5 days postcoitum (pc), and is the major isoform expressed in uterine tissue at the time of implantation (4.5 days pc) and continues to be expressed in uterine tissue at 6.5, 7.5, and 9.5 days pc. 3beta-HSD VI is expressed in giant trophoblasts at 9.5 days pc and is expressed in the placenta through day 15.5 pc. In the adult mouse, 3beta-HSD VI appears to be the only isoform expressed in the skin and also is expressed in the testis, but to a lesser extent than 3beta-HSD I. Mouse 3beta-HSD VI cDNA is orthologous to human 3beta-HSD I cDNA. Human type I 3beta-HSD has been shown to be the only isoform expressed in the placenta and skin. The demonstration that mouse 3beta-HSD VI functions as a dehydrogenase/isomerase and is the predominant isoform expressed during the first half of pregnancy in uterine tissue and in embryonic cells suggests that this isoform may be involved in local production of progesterone, which is needed for successful implantation of the blastocyst and/or maintenance of early pregnancy.

59 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
202319
202217
20218
202016
201916
20186