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

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Published: 4 June 2021

Last updated: 10 February 2022

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1

ADAMSKI, JERZY, JOSHUA CARSTENSEN, BETTINA HUSEN, MEYKE KAUFMANN, YVAN de LAUNOIT, FRAUKE LEENDERS, MONIKA MARKUS, and PETER W. JUNGBLUT. "New 17?-Hydroxysteroid Dehydrogenases." Annals of the New York Academy of Sciences 784, no. 1 Challenges an (April 1996): 124–36. http://dx.doi.org/10.1111/j.1749-6632.1996.tb16232.x.

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2

Poirier, Donald. "Inhibitors of 17β-Hydroxysteroid Dehydrogenases." Current Medicinal Chemistry 10, no. 6 (March 1, 2003): 453–77. http://dx.doi.org/10.2174/0929867033368222.

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3

Mindnich, R., G. Möller, and J. Adamski. "The role of 17 beta-hydroxysteroid dehydrogenases." Molecular and Cellular Endocrinology 218, no. 1-2 (April 2004): 7–20. http://dx.doi.org/10.1016/j.mce.2003.12.006.

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4

Penning, T. M. "17 -Hydroxysteroid dehydrogenase: inhibitors and inhibitor design." Endocrine Related Cancer 3, no. 1 (March 1, 1996): 41–56. http://dx.doi.org/10.1677/erc.0.0030041.

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5

Isomaa, Veli V., Sergio A. Ghersevich, Olli K. Mäentausta, E. Hellevi Peltoketo, Matti H. Poutanen, and Reijo K. Vihko. "Steroid Biosynthetic Enzymes: 17 β Hydroxysteroid Dehydrogenase." Annals of Medicine 25, no. 1 (January 1993): 91–97. http://dx.doi.org/10.3109/07853899309147864.

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6

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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7

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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8

Gobec, S., P. Brozic, and T. Rizner. "Inhibitors of 17β-Hydroxysteroid Dehydrogenase Type 1." Current Medicinal Chemistry 15, no. 2 (January 1, 2008): 137–50. http://dx.doi.org/10.2174/092986708783330629.

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9

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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10

VIHKO, R., O. MÄENTAUSTA, V. ISOMAA, V. P. LEHTO, K. BOMAN, and U. STENDAHL. "Human 17?-Hydroxysteroid Dehydrogenase in Normal and Malignant Endometrium." Annals of the New York Academy of Sciences 622, no. 1 The Primate E (May 1991): 392–401. http://dx.doi.org/10.1111/j.1749-6632.1991.tb37883.x.

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11

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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12

Kurosumi, M., K. Ishimura, T. Yoshinaga, H. Fujita, and B. Tamaoki. "Immunocytochemical localization of 17?-hydroxysteroid dehydrogenase in porcine testis." Histochemistry 85, no. 4 (1986): 287–89. http://dx.doi.org/10.1007/bf00493478.

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13

Ahmed, Sabbir, Moniola Olusanjo, Imran Shahid, and Caroline Owen. "Inhibition of 17β -Hydroxysteroid Dehydrogenase (17β -HSD) by Imidazole-Based Compounds." Letters in Drug Design & Discovery 5, no. 1 (January 1, 2008): 48–51. http://dx.doi.org/10.2174/157018008783406705.

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14

Zeitoun, K. "Deficient 17 -Hydroxysteroid Dehydrogenase Type 2 Expression in Endometriosis: Failure to Metabolize 17 -Estradiol." Journal of Clinical Endocrinology & Metabolism 83, no. 12 (December 1, 1998): 4474–80. http://dx.doi.org/10.1210/jc.83.12.4474.

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15

Poirier, Donald. "Advances in Development of Inhibitors of 17β-Hydroxysteroid Dehydrogenases." Anti-Cancer Agents in Medicinal Chemistry 9, no. 6 (July 1, 2009): 642–60. http://dx.doi.org/10.2174/187152009788680000.

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16

Sasano, Hironobu, Takashi Suzuki, Junji Takeyama, Hiroki Utsunomiya, Kiyoshi Ito, Naohiro Ariga, and Takuya Moriya. "17-Beta-Hydroxysteroid Dehydrogenase in Human Breast and Endometrial Carcinoma." Oncology 59, Suppl. 1 (2000): 5–12. http://dx.doi.org/10.1159/000055281.

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17

Baker, Michael E. "Unusual evolution of 11?- and 17?-hydroxysteroid and retinol dehydrogenases." BioEssays 18, no. 1 (January 1996): 63–70. http://dx.doi.org/10.1002/bies.950180112.

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18

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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19

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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20

Egorova, O. V., V. M. Nikolayeva, and M. V. Donova. "17-Hydroxysteroid dehydrogenases of Mycobacterium sp. VKM Ac-1815D mutant strain." Journal of Steroid Biochemistry and Molecular Biology 81, no. 3 (July 2002): 273–79. http://dx.doi.org/10.1016/s0960-0760(02)00076-6.

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21

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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22

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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23

Mäentausta, O., M. Menjivar, and R. Vihko. "Time-resolved immunofluorometric assay of 17 beta-hydroxysteroid dehydrogenase in plasma." Clinical Chemistry 37, no. 8 (August 1, 1991): 1412–15. http://dx.doi.org/10.1093/clinchem/37.8.1412.

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Abstract We describe a time-resolved immunofluorometric assay (TR-IFMA) for human 17 beta-hydroxysteroid dehydrogenase (17HSD) in which antibody-coated microtiter strip wells and europium chelate-labeled polyclonal antibodies are used. In preparing the label, a polyclonal antibody is affinity-purified and derivatized with diethylenetriamine-pentaacetic acid. With this derivative, five to eight europium ions can be combined with one antibody molecule without decreasing the antibody's immunoreactivity. The minimum detectable concentration of 17HSD is 0.13 microgram/L; the intra- and interassay CVs are less than 8% and less than 15%, respectively, for concentrations between 0.3 and 100 micrograms/L. There is no difference between the concentrations of 17HSD in plasma specimens taken during the proliferative and luteal phases of the menstrual cycle, the measured mean concentration being 0.22 microgram/L. We found no correlation between plasma 17HSD and progesterone concentrations. The plasma concentrations of 17HSD increase during pregnancy, the mean concentrations being 1.5, 4.4, and 12.5 micrograms/L, during the first, second, and third trimesters of pregnancy, respectively. In the specimens from 18 men, the mean concentration was 0.18 microgram/L. In six plasma specimens from patients with endometrial adenocarcinoma, the mean concentration was 0.20 micrograms/L. Pre-analytical aspects are important in the assay of 17HSD because of the lability of the enzyme protein. Preferably, blood should be sampled into EDTA-containing tubes, plasma should be separated within 15 min, and glycerol must be added without delay to a final volume of 200 mL/L.

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24

Dupont, E., F. Labrie, V. Luu-The, and G. Pelletier. "Localization of 17 beta-hydroxysteroid dehydrogenase throughout gestation in human placenta." Journal of Histochemistry & Cytochemistry 39, no. 10 (October 1991): 1403–7. http://dx.doi.org/10.1177/39.10.1940311.

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17 beta-Hydroxysteroid dehydrogenase (17 beta-HSD) is the enzyme responsible for the formation of all sex steroids in gonadal as well as extragonadal tissues. To obtain more information about the age-specific expression of 17 beta-HSD in the human placenta, we have localized this enzyme by immunocytochemistry at the light microscopic level at different periods of gestation. In the 7- and 9-week-old placenta, immunostaining was detected exclusively in the cytoplasm of the syncytiotrophoblast. Between the tenth and thirteenth weeks of gestation, immunolabeling was also observed in the cytoplasm of the cytotrophoblastic cells, suggesting that these cells could be transiently involved in the biosynthesis of sex steroids. Interestingly, between the fourteenth and twenty-fifth weeks of gestation, 17 beta-HSD was observed in both the cytoplasm and nucleus of the syncytiotrophoblast. The reaction product was much more intense in nuclei than in cytoplasm. During the last trimester of gestation, strong immunocytochemical staining was observed in all the nuclei of the syncytiotrophoblast, the cytoplasm being unstained. The meaning of this nuclear staining for 17 beta-HSD is still unclear and remains to be extensively investigated.

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25

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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26

Su, Emily, You-Hong Cheng, Robert Chatterton, Zhi-Hong Lin, Ping Yin, and Serdar Bulun. "Regulation of 17-hydroxysteroid dehydrogenase type 2 in placental endothelial cells." American Journal of Obstetrics and Gynecology 195, no. 6 (December 2006): S154. http://dx.doi.org/10.1016/j.ajog.2006.10.556.

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27

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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28

SUZUKI, T. "Regulation of 17$beta;-hydroxysteroid dehydrogenases (17$beta;-HSD) in T-47D human breast cancer cells." Journal of the Society for Gynecologic Investigation 3, no. 2 (March 1996): 376A. http://dx.doi.org/10.1016/1071-5576(96)83083-8.

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29

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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30

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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31

Adamski, J., T. Normand, F. Leenders, D. Monté, A. Begue, D. Stéhelin, P. W. Jungblut, and Y. de Launoit. "Molecular cloning of a novel widely expressed human 80 kDa 17β-hydroxysteroid dehydrogenase IV." Biochemical Journal 311, no. 2 (October 15, 1995): 437–43. http://dx.doi.org/10.1042/bj3110437.

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Reactions of oestrogens and androgens at position C-17 are catalysed by 17 beta-hydroxysteroid dehydrogenases (17 beta-HSDs). Cloning of the cDNA of a novel human 17 beta-HSD IV and expression of its mRNA are described. A probe derived from the recently discovered porcine 17 beta-oestradiol dehydrogenase (17 beta-EDH) was used to isolate a 2.6 kb human cDNA encoding a continuous protein of 736 amino acids of high (84%) similarity to the porcine 17 beta-EDH. The calculated molecular mass of the human enzyme is 79,595 Da. Other sequence similarities shared by the two enzymes are: an N-terminal sequence which is similar to that of members of the short-chain alcohol dehydrogenase family; amino acids 343-607 which are similar to the C-terminal domains of a trifunctional Candida tropicalis enzyme and the FOX2 gene product of Saccharomyces cerevisiae; amino acids 596-736 which are similar to human sterol carrier protein 2. The previously cloned human 17 beta-HSD I, II and III are less than 25% identical with 17 beta-HSD IV. mRNA for HSD IV is a single species of 3.0 kb, present in many tissues with highest concentrations in liver, heart, prostate and testes. When over-expressed in mammalian cells, the human 17 beta-HSD IV enzyme displays a specific unidirectional oxidative 17 beta-HSD activity.

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32

Aceves-Ramos, A., P. de la Torre, L. Hinojosa, A. Ponce, R. García-Villegas, J. P. Laclette, R. J. Bobes, and M. C. Romano. "Cloning, characterization and functional expression of Taenia solium 17 beta-hydroxysteroid dehydrogenase." General and Comparative Endocrinology 203 (July 2014): 186–92. http://dx.doi.org/10.1016/j.ygcen.2014.03.021.

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33

Lin, S. X., F. Yang, J. Z. Jin, R. Breton, D. W. Zhu, V. Luu-The, and F. Labrie. "Subunit identity of the dimeric 17 beta-hydroxysteroid dehydrogenase from human placenta." Journal of Biological Chemistry 267, no. 23 (August 1992): 16182–87. http://dx.doi.org/10.1016/s0021-9258(18)41984-9.

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34

Sasano, H., A. R. Frost, R. Saitoh, N. Harada, M. Poutanen, R. Vihko, S. E. Bulun, S. G. Silverberg, and H. Nagura. "Aromatase and 17 beta-hydroxysteroid dehydrogenase type 1 in human breast carcinoma." Journal of Clinical Endocrinology & Metabolism 81, no. 11 (November 1996): 4042–46. http://dx.doi.org/10.1210/jcem.81.11.8923858.

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35

Valentino, R., M. Wallace, M. Wallace, D. Burt, and C. R. W. Edwards. "17 Liquorice Induced Mineralocorticoid Excess: 11 ??- Hydroxysteroid Dehydrogenase Deficiency Comes of Age." Journal of Hypertension 5, no. 6 (December 1987): 768–69. http://dx.doi.org/10.1097/00004872-198712000-00038.

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36

Bellavance, E., V. Luu-The, and D. Poirier. "First Inhibitors of the Steroidogenic Enzyme Type 7 17β-Hydroxysteroid Dehydrogenase." Letters in Drug Design & Discovery 1, no. 3 (July 1, 2004): 194–97. http://dx.doi.org/10.2174/1570180043398867.

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37

Sasano, H. "Aromatase and 17 beta-hydroxysteroid dehydrogenase type 1 in human breast carcinoma." Journal of Clinical Endocrinology & Metabolism 81, no. 11 (November 1, 1996): 4042–46. http://dx.doi.org/10.1210/jc.81.11.4042.

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38

Barbieri, Robert L., and Xiaoying Gao. "17β-Hydroxysteroid Dehydrogenase: Enzymatic Activity and mRNA Species in Choriocarcinoma Cells." Gynecologic and Obstetric Investigation 37, no. 3 (1994): 210–14. http://dx.doi.org/10.1159/000292561.

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39

Rodens, K., J. Homoki, U. Schweikert, and W. M. Teller. "148 17-KETOREDUCTASE AND PARIAL ADRENAL 3β-HYDROXYSTEROID-DEHYDROGENASE (3β-HSD) DEFICIENCY." Pediatric Research 24, no. 4 (October 1988): 541. http://dx.doi.org/10.1203/00006450-198810000-00169.

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40

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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41

Takeyama, J. "17 -Hydroxysteroid Dehydrogenase Type 1 and 2 Expression in the Human Fetus." Journal of Clinical Endocrinology & Metabolism 85, no. 1 (January 1, 2000): 410–16. http://dx.doi.org/10.1210/jc.85.1.410.

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42

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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43

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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44

Wu, L., M. Einstein, W. M. Geissler, H. K. Chan, K. O. Elliston, and S. Andersson. "Expression cloning and characterization of human 17 beta-hydroxysteroid dehydrogenase type 2, a microsomal enzyme possessing 20 alpha-hydroxysteroid dehydrogenase activity." Journal of Biological Chemistry 268, no. 17 (June 1993): 12964–69. http://dx.doi.org/10.1016/s0021-9258(18)31480-7.

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45

Schöneshöfer, M., and M. Claus. "Multiple-sites of inhibition by intravenous metyrapone of human adrenal steroidogenesis." Acta Endocrinologica 109, no. 3 (July 1985): 378–85. http://dx.doi.org/10.1530/acta.0.1090378.

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Abstract. The in vivo influence of metyrapone on adrenal steroidogenesis has been studied by measuring plasma concentrations of pregnenolone, 17-OH-pregnenolone, progesterone, 17-OH-progesterone, 11-deoxycorticosterone, 11-deoxycortisol, corticosterone, cortisol, 18- OH -11- deoxycorticosterone, 18- OH -corticosterone and aldosterone before, during and after a 5 h infusion of metyrapone ditartrate at doses of 0.2 g/h and 0.8 g/h respectively. Time courses of plasma steroids and corticotrophin indicate an inhibitory effect of metyrapone on total adrenal steroidogenesis in addition to the known inhibition of the 11- and 18-monooxygenase. The effect on total adrenal steroidogenesis is pronounced at high concentrations of metyrapone and may be compensated by corticotrophin. This effect and a concomitant suppressive effect of metyrapone on plasma corticotrophin itself may account for the frequently described falsely abnormal responses to the metyrapone test. From the present 'in vivo' data, no significant, metyrapone induced alterations of the 3β-hydroxysteroid dehydrogenase/Δ5-isomerase, 17-monooxygenase, 21-monooxygenase or the 18-hydroxysteroid dehydrogenase are apparent.

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46

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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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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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

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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NÁRAY-FEJES-TÓTH, ANIKÓ, CHARLES O. WATLINGTON, and GÉZA FEJES-TÓTH. "llβ-Hydroxysteroid Dehydrogenase Activity in the Renal Target Cells of Aldosterone*." Endocrinology 129, no. 1 (July 1991): 17–21. http://dx.doi.org/10.1210/endo-129-1-17.

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