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Journal articles on the topic '3(or 17)-hydroxysteroid déhydrogénase'

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Published: 4 June 2021
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1

Olusanjo, M. S., and S. Ahmed. "Inhibitors of 17-hydroxysteroid dehydrogenase type 3 (17-beta-HSD 3)." Drugs of the Future 34, no. 7 (2009): 555. http://dx.doi.org/10.1358/dof.2009.034.07.1380625.

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2

Mendonca, B. B. "17 -Hydroxysteroid Dehydrogenase 3 Deficiency in Women." Journal of Clinical Endocrinology & Metabolism 84, no. 2 (February 1, 1999): 802–4. http://dx.doi.org/10.1210/jc.84.2.802.

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3

Lindqvist, A. "Substitution Mutation C268Y Causes 17 -Hydroxysteroid Dehydrogenase 3 Deficiency." Journal of Clinical Endocrinology & Metabolism 86, no. 2 (February 1, 2001): 921–23. http://dx.doi.org/10.1210/jc.86.2.921.

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4

Lee, Yung Seng, Jeremy M. W. Kirk, Richard G. Stanhope, Derek I. Johnston, Sharon Harland, Richard J. Auchus, Stefan Andersson, and Ieuan A. Hughes. "Phenotypic variability in 17?-hydroxysteroid dehydrogenase-3 deficiency and diagnostic pitfalls." Clinical Endocrinology 67, no. 1 (July 2007): 20–28. http://dx.doi.org/10.1111/j.1365-2265.2007.02829.x.

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5

Andersson, S., W. M. Geissler, L. Wu, D. L. Davis, M. M. Grumbach, M. I. New, H. P. Schwarz, et al. "Molecular genetics and pathophysiology of 17 beta-hydroxysteroid dehydrogenase 3 deficiency." Journal of Clinical Endocrinology & Metabolism 81, no. 1 (January 1996): 130–36. http://dx.doi.org/10.1210/jcem.81.1.8550739.

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6

Andersson, S. "Molecular genetics and pathophysiology of 17 beta-hydroxysteroid dehydrogenase 3 deficiency." Journal of Clinical Endocrinology & Metabolism 81, no. 1 (January 1, 1996): 130–36. http://dx.doi.org/10.1210/jc.81.1.130.

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7

Antoun, G. R., I. Brglez, and D. G. Williamson. "A 17 β-hydroxysteroid dehydrogenase of female rabbit liver cytosol. Purification and characterization of multiple forms of the enzyme." Biochemical Journal 225, no. 2 (January 15, 1985): 383–90. http://dx.doi.org/10.1042/bj2250383.

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Multiple forms of the soluble 17 beta-hydroxysteroid dehydrogenase of female rabbit liver were identified. NAD-dependent and NADP-dependent enzyme activities were separated by affinity chromatography on agarose-immobilized Procion Red HE3B, and three forms of the NADP-dependent enzyme activity were purified by chromatofocusing. These three enzyme forms are charge isomers and have no quaternary structure. The enzymes catalysed the C-17 oxidoreduction of oestrogens and androgens; with all enzyme forms the activity towards androgens was higher than that toward oestrogens. The enzymes also exhibited 3 alpha-hydroxysteroid dehydrogenase activity towards androgens of the 5 beta-androstane series. Comparison of the relative activities of the enzymes towards a number of oestrogen and androgen substrates revealed differences among the enzyme forms for both the oxidative and the reductive reactions. In particular, one enzyme form had a significantly lower Km for the 3 alpha-hydroxysteroid substrate and a higher 3 alpha-/17 beta-hydroxysteroid dehydrogenase activity ratio than the other two enzyme forms.
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8

Suzuki, T. "3 -Hydroxysteroid Dehydrogenase/ 5->4-Isomerase Activity Associated with the Human 17 -Hydroxysteroid Dehydrogenase Type 2 Isoform." Journal of Clinical Endocrinology & Metabolism 85, no. 10 (October 1, 2000): 3669–72. http://dx.doi.org/10.1210/jc.85.10.3669.

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9

Falany, C. N., M. D. Green, E. Swain, and T. R. Tephly. "Substrate specificity and characterization of rat liver p-nitrophenol, 3 α-hydroxysteroid and 17 β-hydroxysteroid UDP-glucuronosyltransferases." Biochemical Journal 238, no. 1 (August 15, 1986): 65–73. http://dx.doi.org/10.1042/bj2380065.

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Purified preparations of rat liver 17-hydroxysteroid, 3-hydroxyandrogen and p-nitrophenol (3-methylcholanthrene-inducible) UDP-glucuronosyltransferases were further characterized as to their substrate specificities, phospholipid-dependency and physical properties. The two steroid UDP-glucuronosyltransferases were shown to exhibit strict stereospecificity with respect to the conjugation of steroids and bile acids. These enzymes have been renamed 17 beta-hydroxysteroid and 3 alpha-hydroxysteroid UDP-glucuronosyltransferase to reflect this specificity for important endogenous substrates. An endogenous substrate has not yet been identified for the p-nitrophenol (3-methylcholanthrene-inducible) UDP-glucuronosyltransferase. The steroid UDP-glucuronosyltransferase activities were dependent on phospholipid for maximal catalytic activity. Complete delipidation rendered the UDP-glucuronosyltransferases inactive, and enzymic activity was not restored when phospholipid was added to the reaction mixture. After partial delipidation, phosphatidylcholine was the most efficient phospholipid for restoration of enzymic activity. Partial delipidation also altered the kinetic parameters of the 3 alpha-hydroxysteroid UDP-glucuronosyltransferase. The three purified UDP-glucuronosyltransferases are separate and distinct proteins, with different amino acid compositions and peptide maps generated by limited proteolysis with Staphylococcus aureus V8 proteinase. Some similarity was observed between the amino acid composition and limited proteolytic maps of the steroid UDP-glucuronosyltransferases, suggesting they are more closely related to each other than to the p-nitrophenol UDP-glucuronosyltransferase.
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10

Omrani, M. D., T. Adamovic, U. Grandell, S. Saleh-Gargari, and A. Nordenskjöld. "17-β-Hydroxysteroid Dehydrogenase Type 3 Deficiency in Three Adult Iranian Siblings." Sexual Development 5, no. 6 (2011): 273–76. http://dx.doi.org/10.1159/000335006.

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11

Dhagat, Urmi, Satoshi Endo, Akira Hara, and Ossama El-Kabbani. "Inhibition of 3(17)α-hydroxysteroid dehydrogenase (AKR1C21) by aldose reductase inhibitors." Bioorganic & Medicinal Chemistry 16, no. 6 (March 15, 2008): 3245–54. http://dx.doi.org/10.1016/j.bmc.2007.12.016.

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12

Payne, D. W., and P. Talalay. "Isolation of novel microbial 3 alpha-, 3 beta-, and 17 beta-hydroxysteroid dehydrogenases. Purification, characterization, and analytical applications of a 17 beta-hydroxysteroid dehydrogenase from an Alcaligenes sp." Journal of Biological Chemistry 260, no. 25 (November 1985): 13648–55. http://dx.doi.org/10.1016/s0021-9258(17)38774-4.

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13

Lee, Y. C., C. S. Park, and C. A. Strott. "Molecular cloning of a chiral-specific 3 alpha-hydroxysteroid sulfotransferase." Journal of Biological Chemistry 269, no. 22 (June 1994): 15838–45. http://dx.doi.org/10.1016/s0021-9258(17)40757-5.

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14

Araújo, Vitor Guilherme Brito de, Renata Santarem de Oliveira, Kallianna Paula Duarte Gameleira, Cátia Barbosa Cruz, and Adriana Lofrano-Porto. "3?-hydroxysteroid dehydrogenase type II deficiency on newborn screening test." Arquivos Brasileiros de Endocrinologia & Metabologia 58, no. 6 (August 2014): 650–55. http://dx.doi.org/10.1590/0004-2730000003098.

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3b-hydroxysteroid dehydrogenase II (3β-HSD) deficiency represents a rare CAH variant. Newborns affected with its classic form have salt wasting in early infancy and genital ambiguity in both sexes. High levels of 17-hydroxypregnenolone (Δ517OHP) are characteristic, but extra-adrenal conversion to 17-hydroxyprogesterone (17OHP) may lead to positive results on newborn screening tests. Filter paper 17OHP on newborn screening test was performed by immunofluorometric assay, and serum determinations of 17OHP and Δ517OHP, by radioimmunoassay. A 46,XY infant with genital ambiguity and adrenal crisis at three months of age presented a positive result on newborn screening for CAH. Serum determinations of 17OHP and Δ517OHP were elevated, and a high Δ517OHP/cortisol relation was compatible with the diagnosis of 3β-HSD deficiency. Molecular analysis of the HSD3B2 gene from the affected case revealed the presence of the homozygous p.P222Q mutation, whereas his parents were heterozygous for it. We present the first report of 3β-HSD type II deficiency genotype-proven detected at the Newborn Screening Program in Brazil. The case described herein corroborates the strong genotype-phenotype correlation associated with the HSD3B2 p.P222Q mutation, which leads to a classic salt-wasting 3β-HSD deficiency. Further evaluation of 17OHP assays used in newborn screening tests would aid in determining their reproducibility, as well as the potential significance of moderately elevated 17OHP levels as an early indicator to the diagnosis of other forms of classic CAH, beyond 21-hydroxylase deficiency.
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15

de Launoit, Y., J. Simard, F. Durocher, and F. Labrie. "Androgenic 17 beta-hydroxysteroid dehydrogenase activity of expressed rat type I 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase." Endocrinology 130, no. 1 (January 1992): 553–55. http://dx.doi.org/10.1210/endo.130.1.1309351.

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16

Zhang, Y., R. A. Word, S. Fesmire, B. R. Carr, and W. E. Rainey. "Human ovarian expression of 17 beta-hydroxysteroid dehydrogenase types 1, 2, and 3." Journal of Clinical Endocrinology & Metabolism 81, no. 10 (October 1996): 3594–98. http://dx.doi.org/10.1210/jcem.81.10.8855807.

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17

Zhang, Y. "Human ovarian expression of 17 beta-hydroxysteroid dehydrogenase types 1, 2, and 3." Journal of Clinical Endocrinology & Metabolism 81, no. 10 (October 1, 1996): 3594–98. http://dx.doi.org/10.1210/jc.81.10.3594.

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18

Biswas, R., NM Biswas, H. Mandal, and NM Biswas. "Effect of gonadotropins and alpha 2u-globulin on testicular steroidogenesis and spermatogenesis in melatonin-treated rats." Journal of College of Medical Sciences-Nepal 8, no. 1 (September 11, 2012): 7–12. http://dx.doi.org/10.3126/jcmsn.v8i1.6819.

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Administration of melatonin (400?g/100g bd.wt.) for 14 days caused a fall in weights of the testes and accessory sex organs and testicular 17?-hydroxysteroid dehydrogenase (17?-HSD) but rise in 3?-hydroxysteroid dehydrogenase (3?-HSD) activity, decreased spermatogenesis, serum level of gonadotropins, testosterone and alpha 2u-globulin, The animals treated with melatonin when received gonadotropins or alpha 2u-globulin for the last seven days reversed the weight of testis and accessory sex organs, 3?-HSD, 17?-HSD activities, serum level of gonadotropins, testosterone and alpha 2u-globulin when compared with melatonin-treated rats. It is concluded that alpha 2u-globulin prevents testicular degeneration in melatonin-treated rats by stimulating the synthesis of gonadotropins. Journal of College of Medical Sciences-Nepal,2012,Vol-8,No-1, 7-12 DOI: http://dx.doi.org/10.3126/jcmsn.v8i1.6819
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19

Ghosh, D., J. S. Punzi, and W. L. Duax. "Crystals of active tetramers of 3 alpha, 20 beta-hydroxysteroid dehydrogenase." Journal of Biological Chemistry 261, no. 3 (January 1986): 1306–8. http://dx.doi.org/10.1016/s0021-9258(17)36091-x.

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20

GELL, J., W. RAINEY, and B. CARR. "Immunohistocheniical localization of type 3 17-β hydroxysteroid dehydrogenase (17βHSD3) in human steroidogenic tissues." Journal of the Society for Gynecologic Investigation 5, no. 1 (January 1998): 95A. http://dx.doi.org/10.1016/s1071-5576(97)86301-0.

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21

El-Kabbani, Ossama, Syuhei Ishikura, Armin Wagner, Clemens Schulze-Briese, and Akira Hara. "Crystallization and preliminary X-ray diffraction analysis of mouse 3(17)α-hydroxysteroid dehydrogenase." Acta Crystallographica Section F Structural Biology and Crystallization Communications 61, no. 7 (June 23, 2005): 688–90. http://dx.doi.org/10.1107/s1744309105018427.

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22

Cara, José F., Thomas Moshang, Alfred M. Bongiovanni, and Barry S. Marx. "Elevated 17-Hydroxyprogesterone and Testosterone in a Newborn with 3-Beta-Hydroxysteroid Dehydrogenase Deficiency." New England Journal of Medicine 313, no. 10 (September 5, 1985): 618–21. http://dx.doi.org/10.1056/nejm198509053131007.

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23

Abalain, J. H., S. Di Stefano, Y. Amet, E. Quemener, M. L. Abalain-Colloc, and H. H. Floch. "Cloning, DNA sequencing and expression of (3–17)β hydroxysteroid dehydrogenase from Pseudomonas testosteroni." Journal of Steroid Biochemistry and Molecular Biology 44, no. 2 (February 1993): 133–39. http://dx.doi.org/10.1016/0960-0760(93)90020-w.

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24

ARAKAWA, SATOKO, MIZUE MITSUMA, MASATO IYO, RYOICHI OHKAWA, AKIRA KAMBEGAWA, SHOICHI OKINAGA, and KIYOSHI ARAI. "Inhibition of Rat Ovarian 3.BETA.-Hydroxysteroid Dehydrogenase (3.BETA.-HSD), 17.ALPHA.-Hydroxylase and 17, 20 Lyase by Progestins and Danazol." Endocrinologia Japonica 36, no. 3 (1989): 387–94. http://dx.doi.org/10.1507/endocrj1954.36.387.

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25

Antoun, G. R., and D. G. Williamson. "Age-dependent changes in the multiple forms of the soluble 17 β-hydroxysteroid dehydrogenase of female rabbit liver." Biochemical Journal 225, no. 2 (January 15, 1985): 391–98. http://dx.doi.org/10.1042/bj2250391.

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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.
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26

Moghrabi, N. "Deleterious Missense Mutations and Silent Polymorphism in the Human 17 -Hydroxysteroid Dehydrogenase 3 Gene (HSD17B3)." Journal of Clinical Endocrinology & Metabolism 83, no. 8 (August 1, 1998): 2855–60. http://dx.doi.org/10.1210/jc.83.8.2855.

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27

RAINEY, W. "Expression of 17$beta;-hydroxysteroid dehydrogenase types 1, 2, and 3 in the human ovary." Journal of the Society for Gynecologic Investigation 3, no. 2 (March 1996): 174A. http://dx.doi.org/10.1016/1071-5576(96)82679-7.

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28

S. Olusanjo, Moniola, Caroline P. Owen, and Sabbir Ahmed. "Esters of Dehydroepiandrosterone (DHEA) as Probes for the Active Site of Type 3 17β-Hydroxysteroid Dehydrogenase (17β-HSD3)." Letters in Drug Design & Discovery 7, no. 5 (June 1, 2010): 365–69. http://dx.doi.org/10.2174/157018010791163505.

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29

Inazu, A., K. Sato, T. Nakayama, Y. Deyashiki, A. Hara, and Y. Nozawa. "Purification and characterization of a novel dimeric 20 α-hydroxysteroid dehydrogenase from Tetrahymena pyriformis." Biochemical Journal 297, no. 1 (January 1, 1994): 195–200. http://dx.doi.org/10.1042/bj2970195.

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Tetrahymena pyriformis was found to exhibit high NADPH-dependent 20-oxosteroid reductase activity that converted 17 alpha-hydroxyprogesterone into 17 alpha,20 alpha-dihydroxypregn-4-en-3-one. The enzyme was purified 400-fold from the cytosolic fraction. The purified enzyme with a specific activity of 6.4 mumol/min per mg of protein had an isoelectric point of 4.9 and M(r) of 68,000, and was composed of two subunits of equal size. The N-terminal sequence was determined to be LAKTVPLNDGTNFPIFGG. The enzyme reduced pregnanes and pregnanes possessing a 17 alpha-hydroxy group to a greater extent than those without the hydroxy group, and oxidized 20 alpha-hydroxy groups of the steroids in the presence of NADP+. The Km values for 17 alpha-hydroxyprogesterone and 17 alpha-hydroxypregnenolone were 2.9 and 3.4 microM respectively. Although the enzyme was inactive towards androgens and oestrogens with 3- or 17-oxo groups, it reduced several nonsteroidal carbonyl compounds and oxidized trans-benzene dihydrodiol. The enzyme activity was inhibited by synthetic oestrogens, barbiturates, aldose reductase inhibitors and quercitrin. Thus, this enzyme is a novel form of 20 alpha-hydroxysteroid dehydrogenase (EC 1.1.1.149) which structurally and functionally differs from the mammalian and bacterial enzymes.
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30

Ricigliano, J. W., and T. M. Penning. "Active-site directed inactivation of rat ovarian 20 α-hydroxysteroid dehydrogenase." Biochemical Journal 240, no. 3 (December 15, 1986): 717–23. http://dx.doi.org/10.1042/bj2400717.

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Rat ovarian 20 alpha-hydroxysteroid dehydrogenase plays a pivotal role in leuteolysis and parturition by catalysing the reduction of progesterone to give the progestationally inactive steroid 20 alpha-hydroxyprogesterone. Putative mechanism based inhibitors of this enzyme were synthesized as potential progestational maintaining agents, including the epimeric allylic alcohol pair 3 beta-hydroxy-alpha-vinyl-5 alpha-androstane-17 beta-methanol and the related vinyl ketone 1-(3 beta-hydroxy-5 alpha-androstan-17 beta-yl)-2-propen-1-one. The vinyl ketone inactivates rat ovarian 20 alpha-hydroxysteroid dehydrogenase, semi-purified by poly(L-lysine)-agarose column chromatography, in a rapid time-dependent manner. Analysis of the pseudo-first-order inactivation plots gave a Ki of 2.0 microM for the inhibitor and a t1/2 for the enzyme of 20 s at saturation. These data indicate that the vinyl ketone is a potent and efficient inactivator of the ovarian dehydrogenase. Neither dialysis in the presence or absence of a competing nucleophile nor gel filtration reserves the inactivation, suggesting that a stable covalent bond is formed between the enzyme and steroid ligand. Both substrates (20 alpha-hydroxyprogesterone and NADP+) protect the enzyme from inactivation; moreover, initial velocity measurements in the presence of saturating concentrations of both substrates indicate that the vinyl ketone can behave as a competitive inhibitor, yielding a Ki value identical with that obtained in the inactivation experiments. Our results imply that the vinyl ketone is an active-site directed alkylating agent. By contrast the allylic alcohol pair 3 beta-hydroxy-alpha-vinyl-5 alpha-androstane-17 beta-methanol are neither substrates nor inhibitors of the ovarian enzyme and appear to be excluded from the catalytic site. The rapid inactivation observed with the vinyl ketone suggests that this compound may be useful as a progestational maintaining agent.
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31

Castro, Carla Cristina Telles de Sousa, Guilherme Guaragna-Filho, Flavia Leme Calais, Fernanda Borchers Coeli, Ianik Rafaela Lima Leal, Erisvaldo Ferreira Cavalcante-Junior, Isabella Lopes Monlleó, et al. "Clinical and molecular spectrum of patients with 17β-hydroxysteroid dehydrogenase type 3 (17-β-HSD3) deficiency." Arquivos Brasileiros de Endocrinologia & Metabologia 56, no. 8 (November 2012): 533–39. http://dx.doi.org/10.1590/s0004-27302012000800012.

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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 < 0.8. In three of the patients, diagnosis was only determined due to the presence of signs of virilization at puberty. All patients had been raised as females, and female gender identity was maintained in all of them. Compound heterozygosis for c.277+2T>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. Arq Bras Endocrinol Metab. 2012;56(8):533-9
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32

Levy, Mark A., Dennis A. Holt, Martin Brandt, and Brian W. Metcalf. "Inhibition of 3(17).beta.-hydroxysteroid dehydrogenase from Pseudomonas testosteroni by steroidal A ring fused pyrazoles." Biochemistry 26, no. 8 (April 1987): 2270–79. http://dx.doi.org/10.1021/bi00382a030.

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33

Nakagawa, Makoto, Fumitake Tsukada, Toshihiro Nakayama, Kazuya Matsuura, Akira Hara, and Hideo Sawada. "Identification of Two Dihydrodiol Dehydrogenases Associated with 3(17)a-Hydroxysteroid Dehydrogenase Activity in Mouse Kidney." Journal of Biochemistry 106, no. 4 (October 1989): 633–38. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a122908.

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34

Tremblay, Y. "Regulation of 3 beta-hydroxysteroid dehydrogenase and 17 beta- hydroxysteroid dehydrogenase messenger ribonucleic acid levels by cyclic adenosine 3',5'-monophosphate and phorbol myristate acetate in human choriocarcinoma cells." Molecular Endocrinology 7, no. 3 (March 1, 1993): 355–64. http://dx.doi.org/10.1210/me.7.3.355.

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35

Tremblay, Y., and C. Beaudoin. "Regulation of 3 beta-hydroxysteroid dehydrogenase and 17 beta-hydroxysteroid dehydrogenase messenger ribonucleic acid levels by cyclic adenosine 3',5'-monophosphate and phorbol myristate acetate in human choriocarcinoma cells." Molecular Endocrinology 7, no. 3 (March 1993): 355–64. http://dx.doi.org/10.1210/mend.7.3.8387158.

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36

Vrbikova, J., M. Hill, L. Starka, D. Cibula, B. Bendlova, K. Vondra, J. Sulcova, and M. Snajderova. "The effects of long-term metformin treatment on adrenal and ovarian steroidogenesis in women with polycystic ovary syndrome." European Journal of Endocrinology 144, no. 6 (June 1, 2001): 619–28. http://dx.doi.org/10.1530/eje.0.1440619.

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OBJECTIVE: To evaluate adrenal and ovarian steroidogenesis before and after long-term treatment with metformin in women with polycystic ovary syndrome (PCOS). DESIGN AND METHODS: Twenty-four women with PCOS were evaluated before and after treatment (27+/-4 weeks) with metformin (1000 mg/day) using adrenocorticotrophin (ACTH), GnRH analogue and oral glucose tolerance (oGTT) tests. For statistical evaluation, ANOVA and Wilcoxon's test were used. RESULTS: In 58% of the women a significant improvement in menstrual cyclicity was observed. No significant change in basal steroid levels was found. After ACTH stimulation, a significant decrease in the activity of 3 beta-hydroxysteroid dehydrogenase in C(21) steroids (P<0.05) and in 17 beta-hydroxysteroid dehydrogenase (P<0.01) was observed, as was an increase in the activity of C17,20-lyase in the Delta(4) pathway (P<0.01). A significant growth in the dehydroepiandrosterone (DHEA)/DHEA-sulfate ratio (P<0.05) was detected. With regard to ovarian steroidogenesis, a significant decrease in the stimulated levels of testosterone (P<0.05), index of free testosterone (P<0.01), LH (P<0.05) and oestradiol (P<0.01), and an increase in the levels of 17-hydroxypregnenolone (P<0.05) were detected. In the indices of ovarian enzyme activities, we observed a significant decrease in 3 beta-hydroxysteroid dehydrogenase in C21 steroids (P<0.01), in C17,20-lyase in the Delta 5 pathway (P<0.01), in 17 beta-hydroxysteroid dehydrogenase (P<0.05) and in aromatase. In glucose metabolism, a tendency towards reduction in the homeostasis model assessment (HOMA)-R (for insulin resistance) and HOMA-F (for beta cell function) was detected. In addition, an increase in the levels of C peptide during oGTT was observed (P<0.01). CONCLUSIONS: Long-term metformin treatment reduced various steroid enzymatic activities both in the ovary and the adrenal glands, without apparent changes in basal steroid levels and in insulin sensitivity.
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37

Feller, Klaus, and Lothar Tr�ger. "Steroid-induced regulation of 3?,20?- and 3?,17?-hydroxysteroid dehydrogenase activity in wild type and mutants of Streptomyces hydrogenans." Archives of Microbiology 143, no. 3 (December 1985): 256–59. http://dx.doi.org/10.1007/bf00411246.

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38

Zhang, Lihan, Qiushi Yang, Weitong Xu, Zhaojun Wu, and Dapeng Li. "Integrated Analysis of miR-430 on Steroidogenesis-Related Gene Expression of Larval Rice Field Eel Monopterus albus." International Journal of Molecular Sciences 22, no. 13 (June 29, 2021): 6994. http://dx.doi.org/10.3390/ijms22136994.

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The present study aims to reveal the mechanism by which miR-430s regulate steroidogenesis in larval rice field eel Monopterus albus. To this end, M. albus embryos were respectively microinjected with miRNA-overexpressing mimics (agomir430a, agomir430b, and agomir430c) or miRNA-knockdown inhibitors (antagomir430a, antagomir430b, and antagomir430c). Transcriptome profiling of the larvae indicated that a total of more than 149 differentially expressed genes (DEGs) were identified among the eight treatments. Specifically, DEGs related to steroidogenesis, the GnRH signaling pathway, the erbB signaling pathway, the Wnt signaling pathway, and other pathways were characterized in the transcriptome. We found that steroidogenesis-related genes (hydroxysteroid 17-beta dehydrogenase 3 (17β-hsdb3), hydroxysteroid 17-beta dehydrogenase 7 (17β-hsdb7), hydroxysteroid 17-beta dehydrogenase 12 (17β-hsdb12), and cytochrome P450 family 19 subfamily a (cyp19a1b)) were significantly downregulated in miR-430 knockdown groups. The differential expressions of miR-430 in three gonads indicated different roles of three miR-430 (a, b, and c) isoforms in regulating steroidogenesis and sex differentiation. Mutation of the miR-430 sites reversed the downregulation of cytochrome P450 family 17 (cyp17), cyp19a1b, and forkhead box L2 (foxl2) reporter activities by miR-430, indicating that miR-430 directly interacted with cyp17, cyp19a1b, and foxl2 genes to inhibit their expressions. Combining these findings, we concluded that miR-430 regulated the steroidogenesis and the biosynthesis of steroid hormones by targeting cyp19a1b in larval M. albus. Our results provide a novel insight into steroidogenesis at the early stage of fish at the molecular level.
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39

Bird, A. Daniel, Spencer Greatorex, David Reser, Gareth G. Lavery, and Timothy J. Cole. "Hydroxysteroid dehydrogenase HSD1L is localised to the pituitary–gonadal axis of primates." Endocrine Connections 6, no. 7 (October 2017): 489–99. http://dx.doi.org/10.1530/ec-17-0119.

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Steroid hormones play clinically important and specific regulatory roles in the development, growth, metabolism, reproduction and brain function in human. The type 1 and 2 11-beta hydroxysteroid dehydrogenase enzymes (11β-HSD1 and 2) have key roles in the pre-receptor modification of glucocorticoids allowing aldosterone regulation of blood pressure, control of systemic fluid and electrolyte homeostasis and modulation of integrated metabolism and brain function. Although the activity and function of 11β-HSDs is thought to be understood, there exists an open reading frame for a distinct 11βHSD-like gene; HSD11B1L, which is present in human, non-human primate, sheep, pig and many other higher organisms, whereas an orthologue is absent in the genomes of mouse, rat and rabbit. We have now characterised this novel HSD11B1L gene as encoded by 9 exons and analysis of EST library transcripts indicated the use of two alternate ATG start sites in exons 2 and 3, and alternate splicing in exon 9. Relatively strong HSD11B1L gene expression was detected in human, non-human primate and sheep tissue samples from the brain, ovary and testis. Analysis in non-human primates and sheep by immunohistochemistry localised HSD11B1L protein to the cytoplasm of ovarian granulosa cells, testis Leydig cells, and gonadatroph cells in the anterior pituitary. Intracellular localisation analysis in transfected human HEK293 cells showed HSD1L protein within the endoplasmic reticulum and sequence analysis suggests that similar to 11βHSD1 it is membrane bound. The endogenous substrate of this third HSD enzyme remains elusive with localisation and expression data suggesting a reproductive hormone as a likely substrate.
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40

Bilbao, L. Loridan, L. Audi, E. Gonzalo, and L. Castano. "A novel missense (R80W) mutation in 17-beta-hydroxysteroid dehydrogenase type 3 gene associated with male pseudohermaphroditism." European Journal of Endocrinology 139, no. 3 (September 1, 1998): 330–33. http://dx.doi.org/10.1530/eje.0.1390330.

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41

Benach, Jordi, Stefan Knapp, Udo C. T. Oppermann, Oskar Hagglund, Hans Jornvall, and Rudolf Ladenstein. "Crystallization and Crystal Packing of Recombinant 3 (or 17) beta-Hydroxysteroid Dehydrogenase from Comamonas testosteroni ATTC 11996." European Journal of Biochemistry 236, no. 1 (February 15, 1996): 144–48. http://dx.doi.org/10.1111/j.1432-1033.1996.t01-1-00144.x.

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42

Bird, I. M., M. M. Pasquarette, W. E. Rainey, and J. I. Mason. "Differential control of 17 alpha-hydroxylase and 3 beta-hydroxysteroid dehydrogenase expression in human adrenocortical H295R cells." Journal of Clinical Endocrinology & Metabolism 81, no. 6 (June 1996): 2171–78. http://dx.doi.org/10.1210/jcem.81.6.8964847.

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43

Ishikura, Syuhei, Noriyuki Usami, Satoko Nakajima, Akiko Kameyama, Hiroaki Shiraishi, Vincenzo Carbone, Ossama El-Kabbani, and Akira Hara. "Characterization of Two Isoforms of Mouse 3(17)α-Hydroxysteroid Dehydrogenases of the Aldo-Keto Reductase Family." Biological & Pharmaceutical Bulletin 27, no. 12 (2004): 1939–45. http://dx.doi.org/10.1248/bpb.27.1939.

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44

Bird, I. M. "Differential control of 17 alpha-hydroxylase and 3 beta-hydroxysteroid dehydrogenase expression in human adrenocortical H295R cells." Journal of Clinical Endocrinology & Metabolism 81, no. 6 (June 1, 1996): 2171–78. http://dx.doi.org/10.1210/jc.81.6.2171.

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45

Sawicki, M. W., M. Erman, T. Puranen, P. Vihko, and D. Ghosh. "Structure of the ternary complex of human 17 -hydroxysteroid dehydrogenase type 1 with 3-hydroxyestra-1,3,5,7-tetraen-17-one (equilin) and NADP+." Proceedings of the National Academy of Sciences 96, no. 3 (February 2, 1999): 840–45. http://dx.doi.org/10.1073/pnas.96.3.840.

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46

Djigoué, Guy, Béatrice Ngatcha, Jenny Roy, and Donald Poirier. "Synthesis of 5α-Androstane-17-spiro-δ-lactones with a 3-Keto, 3-Hydroxy, 3-Spirocarbamate or 3-Spiromorpholinone as Inhibitors of 17β-Hydroxysteroid Dehydrogenases." Molecules 18, no. 1 (January 11, 2013): 914–33. http://dx.doi.org/10.3390/molecules18010914.

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47

Dhagat, Urmi, Satoshi Endo, Hiroaki Mamiya, Akira Hara, and Ossama El-Kabbani. "Studies on a Tyr residue critical for the binding of coenzyme and substrate in mouse 3(17)α-hydroxysteroid dehydrogenase (AKR1C21): structure of the Y224D mutant enzyme." Acta Crystallographica Section D Biological Crystallography 66, no. 2 (January 22, 2010): 198–204. http://dx.doi.org/10.1107/s0907444909051464.

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Mouse 3(17)α-hydroxysteroid dehydrogenase (AKR1C21) is the only aldo–keto reductase that catalyzes the stereospecific reduction of 3- and 17-ketosteroids to the corresponding 3(17)α-hydroxysteroids. The Y224D mutation of AKR1C21 reduced theKmvalue for NADP(H) by up to 80-fold and completely reversed the 17α stereospecificity of the enzyme. The crystal structure of the Y224D mutant at 2.3 Å resolution revealed that the mutation resulted in a change in the conformation of the flexible loop B, including the V-shaped groove, which is a unique feature of the active-site architecture of wild-type AKR1C21 and is formed by the side chains of Tyr224 and Trp227. Furthermore, mutations (Y224F and Q222N) of residues involved in forming the safety belt for binding of the coenzyme showed similar alterations in kinetic constants for 3α-hydroxy/3-ketosteroids and 17-hydroxy/ketosteroids compared with the wild type.
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48

Blomquist, C. H., B. S. Leung, C. Beaudoin, D. Poirier, and Y. Tremblay. "Intracellular regulation of 17β-hydroxysteroid dehydrogenase type 2 catalytic activity in A431 cells." Journal of Endocrinology 153, no. 3 (June 1997): 453–64. http://dx.doi.org/10.1677/joe.0.1530453.

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Abstract There is growing evidence that various isoforms of 17β-hydroxysteroid dehydrogenase (17-HSD) are regulated at the level of catalysis in intact cells. A number of investigators have proposed that the NAD(P)/NAD(P)H ratio may control the direction of reaction. In a previous study, we obtained evidence that A431 cells, derived from an epidermoid carcinoma of the vulva, are enriched in 17-HSD type 2, a membrane-bound isoform reactive with C18 and C19 17β-hydroxysteroids and 17-ketosteroids. The present investigation was undertaken to confirm the presence of 17-HSD type 2 in A431 cells and to assess intracellular regulation of 17-HSD at the level of catalysis by comparing the activity of homogenates and microsomes with that of cell monolayers. Northern blot analysis confirmed the presence of 17-HSD type 2 mRNA. Exposure of cells to epidermal growth factor resulted in an increase in type 2 mRNA and, for microsomes, increases in maximum velocity (Vmax) with no change in Michaelis constant (Km) for testosterone and androstenedione, resulting in equivalent increases in the Vmax/Km ratio consistent with the presence of a single enzyme. Initial velocity data and inhibition patterns were consistent with a highly ordered reaction sequence in vitro in which testosterone and androstenedione bind only to either an enzyme–NAD or an enzyme–NADH complex respectively. Microsomal dehydrogenase activity with testosterone was 2- to 3-fold higher than reductase activity with androstenedione. In contrast, although cell monolayers rapidly converted testosterone to androstenedione, reductase activity with androstenedione or dehydroepiandrosterone (DHEA) was barely detectable. Lactate but not glucose, pyruvate or isocitrate stimulated the conversion of androstenedione to testosterone by monolayers, suggesting that cytoplasmic NADH may be the cofactor for 17-HSD type 2 reductase activity with androstenedione. However, exposure to lactate did not result in a significant change in the NAD/NADH ratio of cell monolayers. It appears that within A431 cells 17-HSD type 2 is regulated at the level of catalysis to function almost exclusively as a dehydrogenase. These findings give further support to the concept that 17-HSD type 2 functions in vivo principally as a dehydrogenase and that its role as a reductase in testosterone formation by either the Δ4 or Δ5 pathway is limited. Journal of Endocrinology (1997) 153, 453–464
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49

Albertini, Catherine, and Pierre Leroux. "A Botrytis cinerea Putative 3-keto Reductase Gene (ERG27) that is Homologous to the Mammalian 17 -Hydroxysteroid Dehydrogenase type 7 gene (17 -HSD7)." European Journal of Plant Pathology 110, no. 7 (August 2004): 723–33. http://dx.doi.org/10.1023/b:ejpp.0000041567.94140.05.

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50

Sullivan, Catherine A., Jodi D. Hoffman, and Joshua D. Safer. "17-β-hydroxysteroid dehydrogenase type 3 deficiency: Identifying a rare cause of 46, XY female phenotype in adulthood." Journal of Clinical and Translational Endocrinology: Case Reports 7 (March 2018): 5–7. http://dx.doi.org/10.1016/j.jecr.2017.10.002.

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