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PubMed2004

Purification and characterization of 7beta-hydroxysteroid dehydrogenase from rabbit liver microsomes.

7beta-Hydroxysteroid dehydrogenase (7beta-HSD), a specific enzyme active in the metabolization of 7beta-hydroxycholesterol, was purified about 300-fold from male rabbit liver microsomes using ion exchange, hydroxylapatite, 2'5'ADP Sepharose 4B, and high-performance liquid chromatography on the basis of its catalytic activity. The specific activity of the purified enzyme was 276 nmol/min/mg protein. The molecular weight of the purified enzyme was 34,000. The preferred coenzyme was beta-NADP+. The optimum pH for oxidation was around 7.7 in potassium phosphate buffer, and 11.0 in glycine-NaOH buffer. The purified enzyme catalyzed the synthesis of not only 7beta-hydroxycholesterol but also corticosterone and hydrocortisone. Enzyme activities toward these three substrates accompanied all purification steps of 7beta-HSD. The amino acid sequence of the N-terminal of the purified enzyme showed that 7beta-HSD had sequence similarity to rabbit type I 11beta-hydroxysteroid dehydrogenase (11beta-HSD), indicating that 7beta-HSD may belong to the rabbit type I 11beta-HSD family and may play the same role in the metabolism of 11-hydroxysteroids and 7-hydroxysterols.

Amino Acid Sequence↗
PubMed2004

The role of 17 beta-hydroxysteroid dehydrogenases.

The biological activity of steroid hormones is regulated at the pre-receptor level by several enzymes including 17 beta-hydroxysteroid dehydrogenases (17 beta -HSD). The latter are present in many microorganisms, invertebrates and vertebrates. Dysfunctions in human 17 beta-hydroxysteroid dehydrogenases result in disorders of biology of reproduction and neuronal diseases, the enzymes are also involved in the pathogenesis of various cancers. 17 beta-hydroxysteroid dehydrogenases reveal a remarkable multifunctionality being able to modulate concentrations not only of steroids but as well of fatty and bile acids. Current knowledge on genetics, biochemistry and medical implications is presented in this review.

17-Hydroxysteroid Dehydrogenases↗
PubMed2005

11Beta-hydroxysteroid dehydrogenase type 1: purification from human liver and characterization as carbonyl reductase of xenobiotics.

11Beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1) catalyzes the interconversion of 11-oxo glucocorticoids to their 11-hydroxy metabolites, thereby controlling access of glucocorticoid hormones to the glucocorticoid receptor. Interestingly, evidence is emerging that 11beta-HSD1 fulfills an additional role in the metabolism of xenobiotic carbonyl compounds. In our studies, 11beta-HSD1 was identified as a microsomal reductase that initiates the final detoxification of xenobiotics by reducing them to alcohols that are easier to conjugate and eliminate. With its pluripotent substrate specificities for glucocorticoids and xenobiotics, 11beta-HSD1 adds to an expanding list of those hydroxysteroid dehydrogenases which, on the one hand, are capable of catalyzing the carbonyl reduction of non-steroidal carbonyl compounds, and which, on the other hand, exhibit great specificity to their physiological steroid substrates. It is conceivable that large interferences must occur between endogenous steroid metabolism and the detoxification of xenobiotic compounds on the level of hydroxysteroid dehydrogenases.

11-beta-Hydroxysteroid Dehydrogenase Type 1↗
PubMed2006

In silico Northern blot, an automated method to determine expression patterns from EST databases, reveals tissue specificity of murine 17beta-hydroxysteroid dehydrogenase type 11.

In this study, we developed an automated in silico Northern blot (ISNB) for analysis of gene expression patterns from EST databases. This kind of analysis can facilitate initial enzyme characterization by providing tissue distribution patterns. For proof of principle, we analyzed the expression pattern of well-characterized murine 17beta-hydroxysteroid dehydrogenases type 1 and 4. Less characterized murine 17beta-hydroxysteroid dehydrogenase type 11 (Dhrs 8) also was included and processed bioinformatically (ISNB) and further analyzed by Northern blot. The 17beta-hydroxysteroid dehydrogenase type 11 showed the same wide expression pattern by in silico and by wet laboratory approaches. The data point to its involvement of the enzyme in lipid metabolism. The quality of the ISNB relies on the quality of EST-databases. However, our approach is an easy and versatile tool of potentially universal application.

17-Hydroxysteroid Dehydrogenases↗
PubMed1999

Prevalence of 3beta-hydroxysteroid dehydrogenase-deficient nonclassic adrenal hyperplasia in hyperandrogenic women with adrenal androgen excess.

OBJECTIVE: We sought to determine the prevalence of 3beta-hydroxysteroid dehydrogenase-deficient nonclassic adrenal hyperplasia among adult hyperandrogenic women with dehydroepiandrosterone sulfate excess. STUDY DESIGN: Thirty consecutive hyperandrogenic women with hirsutism, oligomenorrhea, or both and dehydroepiandrosterone sulfate levels of >8.5 micromol/L and 24 control subjects were studied. Basal sex hormone binding globulin, total and free testosterone, dehydroepiandrosterone sulfate, 17-hydroxyprogesterone, and basal and 60-minute corticotropin-stimulated 17-hydroxypregnenolone and dehydroepiandrosterone were measured, and the increment (change from basal to 60-minute value) was calculated. RESULTS: Twenty-six (87%) and 25 (83%) of the 30 hyperandrogenic patients studied had 60-minute dehydroepiandrosterone and change in 0- to 60-minute dehydroepiandrosterone levels greater than the mean + 2 SD of control subjects, respectively. Six (20%) and 6 (20%) of the 30 hyperandrogenic patients had 60-minute 17-hydroxypregnenolone and 0- to 60-minute change in 17-hydroxypregnenolone levels greater than the mean + 2 SD of control subjects, respectively. However, none of the subjects had either 60-minute 17-hydroxypregnenolone levels or 60-minute dehydroepiandrosterone levels or both associated with the diagnosis of genetically proved 3beta-hydroxysteroid dehydrogenase deficiency (>5-fold of the control mean value). CONCLUSION: 3beta-Hydroxysteroid dehydrogenase-deficient nonclassic adrenal hyperplasia is rare even among adult hyperandrogenic patients with adrenal androgen excess.

17-alpha-Hydroxyprogesterone↗
PubMed1975

Hormonal activity of testes in aged rats with leydig cell hyperplasia: histochemical investigation of some hydroxysteroid dehydrogenases.

The following enzymes were employed in order to investigate the hormonal activity of the testes in aged rats: 3-beta hydroxysteroid-DH, 11-beta-hydroxysteroid-DH, and 17-beta-hydroxysteroid-DH. Our investigations show that in the non-altered testis of the aged rat the same enzyme activities can be observed as in young and sexually mature animals. A proliferation of the Leydig cells (L.c.), occurring in the aging rat, brings about an increased activity of the above-mentioned steroid-DHs. An augmented production of testosterone is quite probable.

Aging↗
PubMed1990

17 Beta-hydroxysteroid UDP-glucuronosyl transferase is expressed in bile ductular epithelial cells under physiological conditions.

Using an improved procedure to isolate pure bile ductular epithelial cells from rat liver, we were able to define UDP-glucuronosyl transferase (UDPGT) isozymes expressed in these cells under physiological conditions. The cells contained mRNA for a 17 beta-hydroxysteroid, a 3 alpha-hydroxysteroid and a phenol UDPGT. Concomitantly, a distinct pattern of UDPGT-immunoreactive proteins was expressed, including a putative 17 beta-hydroxysteroid UDPGT. The presence of this UDPGT isozyme was confirmed by a high level of testosterone glucuronidation activity. This is the first demonstration of a metabolic pathway in bile ductular epithelial cells that is primarily dedicated to the processing of endogenous compounds.

Animals↗
PubMed1986

Normal ovarian function in a mild form of late-onset 3 beta-hydroxysteroid dehydrogenase deficiency.

Late-onset 3 beta-hydroxysteroid dehydrogenase (HSD) deficiency was diagnosed in a 30-year-old woman with hirsutism and normal menstrual cycles. No genital abnormalities were present. Elevated basal serum levels of delta 5-3 beta-hydroxysteroids were demonstrated. Serum pregnenolone (P5) was 3.0 ng/ml, and dehydroepiandrosterone sulphate (DHEA-S) 3245 ng/ml. Basal serum levels of delta 4 steroids were low or within normal limits. Serum progesterone (P) was 0.5 ng/ml, 17 alpha-hydroxyprogesterone (17-OHP) 0.2 ng/ml, androstenedione (delta 4A) 0.4 ng/ml, and testosterone (T) 0.1 ng/ml. All delta 5/delta 4 steroid ratios were elevated. Dexamethasone (DEX) administration normalized the elevated levels of delta 5-3 beta-hydroxysteroids, whereas delta 4-3-ketometabolites exhibited only minor modifications. The DHEA-S/delta 4A ratio increased more than five times over the basal ratio, and P5/P and 17 alpha-hydroxypregnenolone (17-OHP5)/17-OHP ratios did not increase after adrenocorticotrophic hormone ACTH stimulation. Studies of basal ovarian function revealed 17 beta-estradiol (E2) and gonadotropins within normal limits according to the menstrual cycle. In the follicular phase, follicle-stimulating hormone (FSH) was 101.3 ng/ml, luteinizing hormone (LH) 46.0 ng/ml, and E2 49.7 pg/ml; in the luteal phase, FSH was 180.0 ng/ml, LH 69.3 ng/ml, and E2 50.1 pg/ml. The presence of ovulatory cycles was documented on the basis of the biphasic pattern of the basal body temperature cycles and the increment in P levels. This case demonstrates the existence of normal ovulatory function in a woman with late-onset of a mild form of HSD.

3-Hydroxysteroid Dehydrogenases↗
PubMed2001

Gene structure, chromosomal localization and analysis of 3-ketosteroid reductase activity of the human 3(alpha-->beta)-hydroxysteroid epimerase.

Following our previous characterization of the first human 3(alpha-->beta)hydroxysteroid epimerase (hHSE), we determined the genomic structure and chromosomal localization of the hHSE gene using fluorescent in situ hybridization (FISH) in this study. The gene spans 23 kb and contains five exons and four introns. FISH mapping assigned this gene to chromosome band 12q13. Primer extension analysis allowed the identification of a single transcription start site at 179 bp upstream from the ATG start codon. The 5'-flanking sequence lacks a typical TATA box in the proximal region of the transcription start site. However, analysis of the 2 kb promoter region revealed the presence of multiple potential transcription factor binding sites. Furthermore, we studied the 3-ketosteroid reductase activity demonstrated by hHSE in intact cells stably expressing the enzyme. It has been known that, in vitro, 3beta-hydroxysteroid dehydrogenase (3beta-HSD) shows both oxidative and reductive activity. Our results showed that hHSE catalyzes the reduction of 3-ketosteroids to form 3beta-hydroxysteroids while 3beta-HSD cannot catalyze this reaction in intact cells. However, hHSE showed 3-keto reductase activity in both microsomal fractions and intact cells. Since intact cells constitute a system which closely reflects in vivo intracellular conditions, we propose that hHSE might contribute to the cellular 3-ketosteroid reductase activity in the peripheral tissues.

3-Hydroxysteroid Dehydrogenases↗
PubMed2001

Hydroxysteroid dehydrogenases: ancient and modern regulators of adrenal and sex steroid action.

The adrenal and sex steroids receptor clade arose from an ancestral nuclear receptor in a primitive vertebrate at least 540 million years ago during the early Cambrian. At that time, these receptors had less specificity for their canonical ligands than their descendents in mammals have, which raises the question of how specificity for responses to different steroids was regulated. We propose that hydroxysteroid dehydrogenases that metabolized functional groups at different sites on steroids (e.g. C3, C11, C17 and C20) had a key role in providing specificity for steroid regulation of gene transcription in primitive vertebrates. Later, with increased physiological complexity in land animals due to innovations such as the placenta, hydroxysteroid dehydrogenases were recruited for new roles in regulating steroid-mediated physiological responses. Hydroxysteroid dehydrogenases in fish, amphibia and mammals are likely have different affinities for some xenobiotics, which needs to be considered in evaluating their hazards as endocrine disruptors.

Adrenal Cortex Hormones↗
PubMed2001

Human type 10 17 beta-hydroxysteroid dehydrogenase: molecular modelling and substrate docking.

17 beta-hydroxysteroid dehydrogenases catalyze the oxidoreduction of hydroxy/oxo groups at position C17 of steroid hormones, thereby constituting a prereceptor control mechanism of hormone action. At present, 11 different mammalian 17 beta-hydroxysteroid dehydrogenases have been identified, catalyzing the cell- and steroid-specific activation and inactivation of estrogens and androgens. The human type 10 17 beta-hydroxysteroid dehydrogenase (17 beta-HSD-10) is a multifunctional mitochondrial enzyme that efficiently catalyzes the oxidative inactivation at C17 of androgens and estrogens. However, it also mediates oxidation of 3 alpha-hydroxy groups of androgens, thereby reactivating androgen metabolites. Finally, it is involved in beta-oxidation of fatty acids by catalyzing the L-hydroxyacyl CoA dehydrogenase reaction of the beta-oxidation cycle. These features and expression profiles suggest a critical role of 17 beta-HSD-10 in neurodegenerative and steroid-dependent cancer forms. Since no three-dimensional structure of 17 beta-HSD-10 is available, homology modelling was carried out to understand the molecular basis of these substrate specificities. The structure obtained displays the properties of a one-domain, alpha/beta fold enzyme of the SDR family. The active site is located within a large, hydrophobic cleft, which forms optimal contacts with the different steroid surfaces. The data provide explanations for the substrate specificities toward the various classes of sex steroid hormones. The model is suitable to explore substrate and inhibitor characteristics that may be used in the development of novel strategies in the treatment of degenerative or malignant diseases.

17-Hydroxysteroid Dehydrogenases↗
PubMed1987

Inhibition of 3(17)beta-hydroxysteroid dehydrogenase from Pseudomonas testosteroni by steroidal A ring fused pyrazoles.

Several 2,3- and 3,4-steroidal fused pyrazoles have been investigated as potential inhibitors of NAD(P)H-dependent steroid oxidoreductases. These compounds are proven to be potent, specific inhibitors for 3(17) beta-hydroxysteroid dehydrogenase from Pseudomonas testosteroni with Ki values of 6-100 nM. In contrast, the activities of 3 alpha,20 beta-hydroxysteroid dehydrogenase from Streptomyces hydrogenans, steroid 5 alpha-reductase from rat prostate, and 3 alpha-hydroxysteroid dehydrogenase from rat liver were unaffected by micromolar concentrations of these compounds. Product and dead-end inhibition studies indicate an ordered association to the beta-dehydrogenase with the cofactor binding prior to substrate or inhibitor. From the results of double inhibition experiments, it is proposed that inhibition occurs through formation of an enzyme-NAD+-inhibitor ternate. On the basis of pH profiles of Vm/Km, Vm, and 1/Ki and of absorbance difference spectra, a hypothetical mechanism of inhibition by the steroidal pyrazoles, drawn by analogy from the inhibition of liver alcohol dehydrogenase by alkylpyrazoles [Theorell, H., & Yonetani, T. (1963) Biochem. Z. 338, 537-553; Andersson, P., Kvassman, J. K., Lindström, A., Oldén, B., & Pettersson, G. (1981) Eur. J. Biochem. 113, 549-554], is reconsidered. The pH studies and enzyme modification experiments by diethyl pyrocarbonate suggest the involvement of histidine in binding of the inhibitor. A modified proposal for the structure of the enzyme-NAD+-steroidal pyrazole complex is proposed.(ABSTRACT TRUNCATED AT 250 WORDS)

17-Hydroxysteroid Dehydrogenases↗
PubMed1989

Fetal lamb 3 beta, 20 alpha-hydroxysteroid oxidoreductase: dual activity at the same active site examined by affinity labeling with 16 alpha-(bromo[2'-14C]acetoxy)progesterone.

3 beta,20 alpha-Hydroxysteroid oxidoreductase was purified to homogeneity from fetal lamb erythrocytes. The Mr 35,000 enzyme utilizes NADPH and reduces progesterone to 4-pregnen-20 alpha-ol-3-one [Km = 30.8 microM and Vmax = 0.7 nmol min-1 (nmol of enzyme)-1] and 5 alpha-dihydrotestosterone to 5 alpha-androstane-3 beta, 17 beta-diol [Km = 74 microM and Vmax = 1.3 nmol min-1 (nmol of enzyme)-1]. 5 alpha-Dihydrotestosterone competitively inhibits (Ki = 102 microM) 20 alpha-reductase activity, suggesting that both substrates may be reduced at the same active site. 16 alpha-(Bromoacetoxy)progesterone competitively inhibits 3 beta- and 20 alpha-reductase activities and also causes time-dependent and irreversible losses of both 3 beta-reductase and 20 alpha-reductase activities with the same pseudo-first order kinetic t1/2 value of 75 min. Progesterone and 5 alpha-dihydrotestosterone protect the enzyme against loss of the two reductase activities presumably by competing with the affinity alkylating steroid for the active site of 3 beta,20 alpha-hydroxysteroid oxidoreductase. 16 alpha-(Bromo[2'-14C]acetoxy) progesterone radiolabels the active site of 3 beta,20 alpha-hydroxysteroid oxidoreductase wherein 1 mol of steroid completely inactivates 1 mol of enzyme with complete loss of both reductase activities. Hydrolysis of the 14C-labeled enzyme with 6 N HCl at 110 degrees C and analysis of the amino acid hydrolysate identified predominantly N pi-(carboxy[2'-14C]methyl)histidine [His(pi-CM)].(ABSTRACT TRUNCATED AT 250 WORDS)

Affinity Labels↗
PubMedDate not supplied

Solid-phase synthesis of hydroxysteroid derivatives using the diethylsilyloxy linker.

Four different types of hydroxysteroids (primary alcohol, secondary alcohols, and phenol), bearing either an oxirane or an azide as a precursor of molecular diversity, were linked in good yields to solid support using the butyldiethylsilane polystyrene (PS-DES) resin. These molecules were then used as scaffolds to generate hydroxysteroid derivatives containing two levels of diversity. The proposed libraries were tested by running steroidal alcohols through a model sequence of reactions (solid-phase coupling, aminolysis of oxirane or reduction of azide, amidation, and final cleavage). As a result, two linked secondary alcohols (17beta-hydroxy-spiro-3(R)-oxirane-5alpha-androstane and 3beta-hydroxy-spiro- 17(S)-oxirane-5alpha-androstane) and a primary alcohol (spiro-17(S)-oxirane-3-(hydroxymethyl)-1,3,5(10)-estratriene) afforded good overall yields (>45%) and high HPLC purities (>90%) of hydroxysteroids derivatized as alkylamides without purification. One limitation was noted for the fourth library: the phenolic steroid linked by the diethylsilyloxy linker gave a poor overall yield of 8% of the desired model compound. Finally, the diethylsilyloxy linker was used successfully for a rapid solid-phase synthesis of a model library of twenty C19-steroid derivatives (3beta-amido-3alpha-hydroxy-5alpha-androstane-17-ones), with an average yield of 53% and average HPLC purity of 97% without purification steps.

Chromatography, High Pressure Liquid↗
PubMed1985

Age-dependent changes in the multiple forms of the soluble 17 beta-hydroxysteroid dehydrogenase of female rabbit liver.

The soluble NADP-dependent 17 beta-hydroxysteroid dehydrogenase activity of female rabbit liver increases with the age of the animal, the specific activity of the enzyme in the 56-day-old rabbit being 3 times that of the 28-day-old animal. The increase in activity is accompanied by a change in the molecular heterogeneity of the enzyme. Three forms (enzymes I, II and III) were identified in the liver cytosol of the 56-day-old female rabbit, whereas only one major form (enzyme IIIY) was present in the 28-day-old animal. Peptide maps of the four purified enzymes showed that there were minor differences in structure. The enzyme present in the liver of the 28-day-old rabbit was distinct from the three enzymes of the 56-day-old animal. All of the enzymes exhibited bifunctional activity, having 17 beta-hydroxysteroid dehydrogenase activity towards androgen and oestrogen substrates and 3 alpha-hydroxysteroid dehydrogenase activity towards androgens of the 5 beta-androstane series. The differences in substrate specificity of the enzymes paralleled their differences in structure. The data suggest that one enzyme (enzyme III) may have a special role in steroid metabolism during development in the female rabbit.

17-Hydroxysteroid Dehydrogenases↗
PubMed2000

Dexamethasone-induced apoptosis of mouse thymocytes: prevention by native 7alpha-hydroxysteroids.

Dehydroepiandrosterone (DHEA) has been shown to decrease the dexamethasone (DEX)-induced apoptosis of thymocytes and to be one of the native 3beta-hydroxysteroids extensively 7alpha-hydroxylated in thymus. This led us to question whether DHEA or 7alpha-hydroxy-DHEA is responsible for the decrease in DEX-induced apoptosis of thymocytes and whether this property is shared with other native 3beta-hydroxysteroids and their 7alpha-hydroxylated metabolites. Treatment of mice with DHEA or 7alpha-hydroxy-DHEA prior to DEX led to a smaller decrease in thymus weight than with DEX alone and to a disappearance of the DEX-induced changes in thymocyte phenotypes. Thymocyte apoptosis induced by DEX treatment was significantly lowered in DHEA- and 7alpha-hydroxy-DHEA-treated thymi, even after 18 h culture with additional 10-6 mol/L DEX. Extensive apoptosis of thymocytes cultured with 10-7 mol/L DEX was brought back to control levels when 10-5 mol/L 7alpha-hydroxy-DHEA or 10-5 mol/L 7alpha-hydroxy-epiandrosterone was added. After use of DHEA and epiandrosterone or pregnenolone, less significant and no significant changes were obtained, respectively. These findings imply that the 7alpha-hydroxylation of 3beta-hydroxysteroids may be a prerequisite for an exquisite regulation of the thymocyte-positive selection driven by the glucocorticoids produced in thymic epithelial cells.

Androsterone↗
PubMedDate not supplied

[Severe 46,XY virilization deficit due to 17beta-hydroxysteroid dehydrogenase deficiency].

BACKGROUND: 17beta hydroxysteroid dehydrogenase deficiency is a presumable rare cause for a severe virilization disorder in children with 46,XY karyotype due to a defect in the testicular testosterone biosynthesis from androstenedione. PATIENT: We report on a 14 year old child with 46,XY karyotype with a predominantly female phenotype. RESULTS: Hormonal analysis showed low values for androstenedione and testosterone before and after stimulation with human chorionic gonadotropin, however, the androstenedione/testosterone ratio was elevated. Molecular genetic analysis proved the diagnosis of 17beta-hydroxysteroid dehydrogenase deficiency due to a homozygous mutation (325+4 A-T) in the HSD17B3-gene, which leads to an aberrant splicing process. CONCLUSIONS: This case demonstrates that in addition to a meticulous steroid analysis a direct molecular genetic analysis can be helpful in the diagnosis of 17beta-hydroxysteroid dehydrogenase deficiency.

17-Hydroxysteroid Dehydrogenases↗
PubMed2001

Characterization of a novel type of human microsomal 3alpha -hydroxysteroid dehydrogenase: unique tissue distribution and catalytic properties.

We report characterization of a novel member of the short chain dehydrogenase/reductase superfamily. The 1513-base pair cDNA encodes a 319-amino acid protein. The corresponding gene spans over 26 kilobase pairs on chromosome 2 and contains five exons. The recombinant protein produced using the baculovirus system is localized in the microsomal fraction of Sf9 cells and is an integral membrane protein with cytosolic orientation of its catalytic domain. The enzyme exhibits an oxidoreductase activity toward hydroxysteroids with NAD(+) and NADH as the preferred cofactors. The enzyme is most efficient as a 3alpha-hydroxysteroid dehydrogenase, converting 3alpha-tetrahydroprogesterone (allopregnanolone) to dihydroprogesterone and 3alpha-androstanediol to dihydrotestosterone with similar catalytic efficiency (V(max) values of 13-14 nmol/min/mg microsomal protein and K(m) values of 5-7 microm). Despite approximately 44-47% sequence identity with retinol/3alpha-hydroxysterol dehydrogenases, the enzyme is not active toward retinols. The corresponding message is abundant in human trachea and is present at lower levels in the spinal cord, bone marrow, brain, heart, colon, testis, placenta, lung, and lymph node. Thus, the new short chain dehydrogenase represents a novel type of microsomal NAD(+)-dependent 3alpha-hydroxysteroid dehydrogenase with unique catalytic properties and tissue distribution.

3-Hydroxysteroid Dehydrogenases↗