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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01 Jan 2001
TL;DR: This chapter will examine how the activity of hydrocortisone may be controlled locally in various target tissues by the enzyme 11β-hydroxysteroid dehydrogenase (11β-HSD).
Abstract: The activity of hydrocortisone, the major endogenous glucocorticoid in humans, is determined at multiple levels along a complex metabolic pathway that begins with the release of corticotropin releasing hormone (CRH) at the hypothalamus and ends in the nucleus of target cells where the activated glucocorticoid receptor regulates cellular functions. Modulation of glucocorticoid synthesis by the hypothalamic-pituitary-adrenal axis is described in detail in the chapter by Cowell and Buckingham. This chapter will examine how the activity of hydrocortisone may be controlled locally in various target tissues by the enzyme 11β-hydroxysteroid dehydrogenase (11β-HSD).
TL;DR: In this paper , the authors highlight recent advances in basic research on the functional activities, major substrates, and key roles of 17β-hydroxysteroid dehydrogenase type 13 (HSD17B13) in the progression of NAFLD to develop innovative anti-NAFLD drugs targeting HSD17Bs.
Patent•
31 Oct 2019
TL;DR: In this paper, a 7B-hydroxysteroid dehydrogenase with co-substrate specificity of NAD+ instead of NADP+ was proposed, which can be used to convert cholic acid and/or chenodeoxycholic acid (CDCA) into URSOCHolic acid.
Abstract: The present invention relates to a NAD+ dependent 7B— hydroxysteroid dehydrogenases and to methods of providing a 7B— hydroxysteroid dehydrogenase with a co-substrate specificity of NAD+ instead of NADP+. The invention further relates to methods for converting cholic acid (CA) and/or chenodeoxycholic acid (CDCA) into ursocholic acid (UCA) and/or ursodeoxycholic acid (UDCA) respectively, and more specifically methods for converting 7-oxo-deoxycholic acid (7-oxo-DCA) and/or 7-oxo-lithocholic acid (7-oxo LCA) into ursocholic acid (UCA) and/or ursodeoxycholic acid (UDCA) respectively, by using an NAD+ dependent 7B— hydroxysteroid dehydrogenase.
TL;DR: This work examined maturational changes in the activities of two enzymes affecting testosterone accumulation, I7p-HSD and Sa-reductase, in two Leydig cell bands isolated on metrizamide gradients to partially address this question.
Abstract: Previous studies using Metrizamide or Percoll gradients identified two or more bands of Leydig cells in adult rodents, with different densities and functional characteristics.'-' Other studies suggest, however, that Leydig cells localizing at the less dense regions represent damaged cell^,^.^ thus implying only a single Leydig cell population. This question is difficult to resolve, because the methods of dispersion and isolation affect the quality and yield of cells i ~ o l a t e d . ~ . ~ To partially address this question, we examined maturational changes in the activities of two enzymes affecting testosterone accumulation, I7p-HSD and Sa-reductase, in two Leydig cell bands isolated on metrizamide gradients. We reasoned that if these Leydig cells were functionally different, there might be distinct developmental patterns for the two enzymes. Collagenase-dispersed interstitial cells, from Sprague-Dawley rats ( 18-73 days old), were centrifuged on continuous (0-32%) Metrizamide gradients to isolate band 3 cells (B3) and band 2 cells (B2), representing population I1 and population I Leydig cells, respective1y.I Sa-Reductase activity was estimated using 10 pM [3H]testosterone (0.5 pCi) as substrate and incubating intact cells for 30 min at 34°C. The products, dihydrotestosterone (DHT), Sa-androstan-3a, 17P-diol (3adiol), and Sa-androstan-3p, 17/3-diol(3p-diol) were isolated by thin-layer chromatography (TLC). Incubation conditions to estimate I7P-HSD activity were identical, except androstenedione was isolated. 5a-Reductase activity in B2 cells was 0.028 nmol/30 min/lOs cells on day 18, increased to peak at 0,148 * 0.007 nmol on day 35, decreased to 0.018 * 0.008 nmol on day 53, and then stabilized (FIG. 1 , panel A). The pattern of 5a-reductase activity for B3 cells was similar. Activity was 0.101 nmol/30 min/105 cells on day 18, increased to 1.404 ? 0.083 nmol on day 35, decreased to 0.084 ? 0.014 nmol on day 53, and then stabilized (FIG. I , panel B). Although the pattern of 5areductase was similar for both bands, for each age, a greater percentage of DHT was converted to 3aand 3P-diol in B2 cells. The developmental pattern of 17pHSD activity was similar to 5a-reductase for both B2 and B, cells. 17P-HSD activity in B2 cells was 0.010 nmol/30 min/lO5 cells on day 24, increased to 0.148 ? 0.028 nmol on day 35, and then decreased to 0.01 1 -t 0.002 nmol on day 73 (FIG.