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Journal articles on the topic 'Type 5 17β-hydroxysteroid dehydrogenase'

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Published: 4 June 2021

Last updated: 4 February 2022

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1

Krazeisen, A., R. Breitling, G. Möller, and J. Adamski. "Phytoestrogens inhibit human 17β-hydroxysteroid dehydrogenase type 5." Molecular and Cellular Endocrinology 171, no. 1-2 (January 2001): 151–62. http://dx.doi.org/10.1016/s0303-7207(00)00422-6.

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2

Poirier, Donald, Patrick Bydal, Martin R. Tremblay, Kay-Mane Sam, and Van Luu-The. "Inhibitors of type II 17β-hydroxysteroid dehydrogenase." Molecular and Cellular Endocrinology 171, no. 1-2 (January 2001): 119–28. http://dx.doi.org/10.1016/s0303-7207(00)00427-5.

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3

Brožič, Petra, Barbara Golob, Nataša Gomboc, Tea Lanišnik Rižner, and Stanislav Gobec. "Cinnamic acids as new inhibitors of 17β-hydroxysteroid dehydrogenase type 5 (AKR1C3)." Molecular and Cellular Endocrinology 248, no. 1-2 (March 2006): 233–35. http://dx.doi.org/10.1016/j.mce.2005.10.020.

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4

Rheault, Patrick, Annie Charbonneau, and Van Luu-The. "Structure and activity of the murine type 5 17β-hydroxysteroid dehydrogenase gene." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1447, no. 1 (October 1999): 17–24. http://dx.doi.org/10.1016/s0167-4781(99)00106-2.

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5

Byrns, Michael C., Yi Jin, and Trevor M. Penning. "Inhibitors of type 5 17β-hydroxysteroid dehydrogenase (AKR1C3): Overview and structural insights." Journal of Steroid Biochemistry and Molecular Biology 125, no. 1-2 (May 2011): 95–104. http://dx.doi.org/10.1016/j.jsbmb.2010.11.004.

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6

Boutin, Sophie, and Donald Poirier. "Structure Confirmation and Evaluation of a Nonsteroidal Inhibitor of 17β-Hydroxysteroid Dehydrogenase Type 10." Magnetochemistry 4, no. 3 (July 23, 2018): 32. http://dx.doi.org/10.3390/magnetochemistry4030032.

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17β-Hydroxysteroid dehydrogenase type 10 (17β-HSD10) is a steroidogenesis enzyme known for its potential role in Alzheimer’s disease. For comparison purposes between steroidal and nonsteroidal 17β-HSD10 inhibitors 1 and 2, respectively, we attempted the chemical synthesis of benzothiazole phosphonate derivative 2. Instead of a one-pot synthesis, we report a two-step synthesis with characterization of both imine intermediate 5 and final compound 2. Furthermore, complete assignation of 1H and 13C nuclear magnetic resonance (NMR) signals of 2 is provided, as we observed a divergence of NMR data with those published previously. Finally, biological assays showed that 1 and 2 inhibited the oxidation of estradiol (E2) into estrone (E1) by the 17β-HSD10 recombinant protein. However, in human embryonic kidney (HEK)-293 intact cells transfected with 17β-HSD10, only the steroidal inhibitor 1 induced a dose-dependent inhibition of E2 to E1 transformation.

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7

Chai, Zhonglin, Phillip Brereton, Takashi Suzuki, Hironobu Sasano, Varuni Obeyesekere, Genevieve Escher, Richard Saffery, Peter Fuller, Carla Enriquez, and Zygmunt Krozowski. "17β-Hydroxysteroid Dehydrogenase Type XI Localizes to Human Steroidogenic Cells." Endocrinology 144, no. 5 (May 1, 2003): 2084–91. http://dx.doi.org/10.1210/en.2002-221030.

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We searched expressed sequence tag databases with conserved domains of the short-chain alcohol dehydrogenase superfamily and identified another isoform of 17β-hydroxysteroid dehydrogenase, 17βHSDXI. This enzyme converts 5α-androstane-3α, 17β-diol to androsterone. The substrate has been implicated in supporting gestation and modulating γ-aminobutyric acid receptor activity. 17βHSDXI is colinear with human retinal short-chain dehydrogenase/reductase retSDR2, a protein with no known biological activity (accession no. AAF06939). Of the proteins with known function, 17βHSDXI is most closely related to the retinol-metabolizing enzyme retSDR1, with which it has 30% identity. There is a polymorphic stretch of 15 adenosines in the 5′ untranslated region of the cDNA sequence and a silent polymorphism at C719T. A 17βHSDXI construct with a stretch of 20 adenosines was found to produce significantly more enzyme activity than constructs containing 15 or less adenosines (43% vs. 26%, P < 0.005). The C719T polymorphism is present in 15% of genomic DNA samples. Northern blot analysis showed high levels of 17βHSDXI expression in the pancreas, kidney, liver, lung, adrenal, ovary, and heart. Immunohistochemical staining for 17βHSDXI is strong in steroidogenic cells such as syncytiotrophoblasts, sebaceous gland, Leydig cells, and granulosa cells of the dominant follicle and corpus luteum. In the adrenal 17βHSDXI, staining colocalized with the distribution of 17α-hydroxylase but was stronger in the mid to outer cortex. 17βHSDXI was also found in the fetus and increased after birth. Liver parenchymal cells and epithelium of the endometrium and small intestine also stained. Regulation studies in mouse Y1 cells showed that cAMP down-regulates 17βHSDXI enzymatic activity (40% vs. 32%, P < 0.05) and reduces gene expression to undetectable levels. All-trans-retinoic acid did not affect 17βHSDXI expression or activity, but addition of the retinoid together with cAMP significantly decreased activity over cAMP alone (32% vs. 23%, P < 0.05). Cloning and sequencing of the 17βHSDXI promoter identified the potential nuclear receptor steroidogenic factor-1 half-site TCCAAGGCCGG, and a cluster of three other potential steroidogenic factor-1 half-sites were found in the distal part of intron 1. Collectively, these results suggest a role for 17βHSDXI in androgen metabolism during steroidogenesis and a possible role in nonsteroidogenic tissues including paracrine modulation of 5α-androstane-3α, 17β-diol levels. 17βHSDXI could act by metabolizing compounds that stimulate steroid synthesis and/or by generating metabolites that inhibit it.

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8

Qin, K. "Expression of 17β-hydroxysteroid dehydrogenase type 5 in human ovary: a pilot study." Journal of the Society for Gynecologic Investigation 7, no. 1 (February 2000): 61–64. http://dx.doi.org/10.1016/s1071-5576(99)00067-2.

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9

Penning, Trevor M., Michael E. Burczynski, Joseph M. Jez, Hseuh-Kung Lin, Haiching Ma, Margaret Moore, Kapila Ratnam, and Nisha Palackal. "Structure-function aspects and inhibitor design of type 5 17β-hydroxysteroid dehydrogenase (AKR1C3)." Molecular and Cellular Endocrinology 171, no. 1-2 (January 2001): 137–49. http://dx.doi.org/10.1016/s0303-7207(00)00426-3.

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10

Steckelbroeck, Stephan, Matthias Watzka, Birgit Stoffel-Wagner, Volkmar H. J. Hans, Lioba Redel, Hans Clusmann, Christian E. Elger, Frank Bidlingmaier, and Dietrich Klingmüller. "Expression of the 17β-hydroxysteroid dehydrogenase type 5 mRNA in the human brain." Molecular and Cellular Endocrinology 171, no. 1-2 (January 2001): 165–68. http://dx.doi.org/10.1016/s0303-7207(00)00432-9.

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11

Qin, Ke-nan, and Robert L. Rosenfield. "Expression of 17β-Hydroxysteroid Dehydrogenase Type 5 in Human Ovary: A Pilot Study." Journal of the Society for Gynecologic Investigation 7, no. 1 (January 2000): 61–64. http://dx.doi.org/10.1177/107155760000700109.

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12

Zang, Tianzhu, Kshitij Verma, Mo Chen, Yi Jin, Paul C. Trippier, and Trevor M. Penning. "Screening baccharin analogs as selective inhibitors against type 5 17β-hydroxysteroid dehydrogenase (AKR1C3)." Chemico-Biological Interactions 234 (June 2015): 339–48. http://dx.doi.org/10.1016/j.cbi.2014.12.015.

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13

Fung, K.-M., E. N. S. Samara, C. Wong, A. Metwalli, R. Krlin, B. Bane, C. Z. Liu, et al. "Increased expression of type 2 3α-hydroxysteroid dehydrogenase/type 5 17β-hydroxysteroid dehydrogenase (AKR1C3) and its relationship with androgen receptor in prostate carcinoma." Endocrine-Related Cancer 13, no. 1 (March 2006): 169–80. http://dx.doi.org/10.1677/erc.1.01048.

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Type 2 3α-hydroxysteroid dehydrogenase (3α-HSD) is a multi-functional enzyme that possesses 3α-, 17β- and 20α-HSD, as well as prostaglandin (PG) F synthase activities and catalyzes androgen, estrogen, progestin and PG metabolism. Type 2 3α-HSD was cloned from human prostate, is a member of the aldo-keto reductase (AKR) superfamily and was named AKR1C3. In androgen target tissues such as the prostate, AKR1C3 catalyzes the conversion of Δ4-androstene-3,17-dione to testosterone, 5α-dihydrotestosterone to 5α-androstane-3α,17β-diol (3α-diol), and 3α-diol to androsterone. Thus AKR1C3 may regulate the balance of androgens and hence trans-activation of the androgen receptor in these tissues. Tissue distribution studies indicate that AKR1C3 transcripts are highly expressed in human prostate. To measure AKR1C3 protein expression and its distribution in the prostate, we raised a monoclonal antibody specifically recognizing AKR1C3. This antibody allowed us to distinguish AKR1C3 from other AKR1C family members in human tissues. Immunoblot analysis showed that this monoclonal antibody binds to one species of protein in primary cultures of prostate epithelial cells and in LNCaP prostate cancer cells. Immunohistochemistry with this antibody on human prostate detected strong nuclear immunoreactivity in normal stromal and smooth muscle cells, perineurial cells, urothelial (transitional) cells, and endothelial cells. Normal prostate epithelial cells were only faintly immunoreactive or negative. Positive immunoreactivity was demonstrated in primary prostatic adenocarcinoma in 9 of 11 cases. Variable increases in immunoreactivity for AKR1C3 was also demonstrated in non-neoplastic changes in the prostate including chronic inflammation, atrophy and urothelial (transitional) cell metaplasia. We conclude that elevated expression of AKR1C3 is highly associated with prostate carcinoma. Although the biological significance of elevated AKR1C3 in prostatic carcinoma is uncertain, AKR1C3 may be responsible for the trophic effects of androgens and/or PGs on prostatic epithelial cells.

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14

Tchédam Ngatcha, Béatrice, Van Luu-The, and Donald Poirier. "Androsterone 3β-substituted derivatives as inhibitors of type 3 17β-hydroxysteroid dehydrogenase." Bioorganic & Medicinal Chemistry Letters 10, no. 22 (November 2000): 2533–36. http://dx.doi.org/10.1016/s0960-894x(00)00517-5.

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15

Amano, Yasushi, Tomohiko Yamaguchi, Tatsuya Niimi, and Hitoshi Sakashita. "Structures of complexes of type 5 17β-hydroxysteroid dehydrogenase with structurally diverse inhibitors: insights into the conformational changes upon inhibitor binding." Acta Crystallographica Section D Biological Crystallography 71, no. 4 (March 27, 2015): 918–27. http://dx.doi.org/10.1107/s1399004715002175.

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Type 5 17β-hydroxysteroid dehydrogenase (17β-HSD5) is an aldo-keto reductase expressed in the human prostate which catalyzes the conversion of androstenedione to testosterone. Testosterone is converted to 5α-dihydrotestosterone, which is present at high concentrations in patients with castration-resistant prostate cancer (CRPC). Inhibition of 17β-HSD5 is therefore considered to be a promising therapy for treating CRPC. In the present study, crystal structures of complexes of 17β-HSD5 with structurally diverse inhibitors derived from high-throughput screening were determined. In the structures of the complexes, various functional groups, including amide, nitro, pyrazole and hydroxyl groups, form hydrogen bonds to the catalytic residues His117 and Tyr55. In addition, major conformational changes of 17β-HSD5 were observed following the binding of the structurally diverse inhibitors. These results demonstrate interactions between 17β-HSD5 and inhibitors at the atomic level and enable structure-based drug design for anti-CRPC therapy.

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16

Luu-The, Van, Isabelle Dufort, Georges Pelletier, and Fernand Labrie. "Type 5 17β-hydroxysteroid dehydrogenase: its role in the formation of androgens in women." Molecular and Cellular Endocrinology 171, no. 1-2 (January 2001): 77–82. http://dx.doi.org/10.1016/s0303-7207(00)00425-1.

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17

Goodarzi, Mark O., Michelle R. Jones, Heath J. Antoine, Marita Pall, Yii-Der I. Chen, and Ricardo Azziz. "Nonreplication of the Type 5 17β-Hydroxysteroid Dehydrogenase Gene Association with Polycystic Ovary Syndrome." Journal of Clinical Endocrinology & Metabolism 93, no. 1 (January 1, 2008): 300–303. http://dx.doi.org/10.1210/jc.2007-1712.

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18

Nakamura, Yasuhiro, Peter J. Hornsby, Peter Casson, Ryo Morimoto, Fumitoshi Satoh, Yewei Xing, Michael R. Kennedy, Hironobu Sasano, and William E. Rainey. "Type 5 17β-Hydroxysteroid Dehydrogenase (AKR1C3) Contributes to Testosterone Production in the Adrenal Reticularis." Journal of Clinical Endocrinology & Metabolism 94, no. 6 (June 1, 2009): 2192–98. http://dx.doi.org/10.1210/jc.2008-2374.

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19

Blanchard, Pierre-Gilles, and Van Luu-The. "Differential androgen and estrogen substrates specificity in the mouse and primates type 12 17β-hydroxysteroid dehydrogenase." Journal of Endocrinology 194, no. 2 (August 2007): 449–55. http://dx.doi.org/10.1677/joe-07-0144.

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Recently, we have shown that human and monkey type 12 17β-hydroxysteroid dehydrogenases (17β-HSD12) are estrogen-specific enzymes catalyzing the transformation of estrone (E1) into estradiol (E2). To further characterize this novel steroidogenic enzyme in an animal model, we have isolated a cDNA fragment encoding mouse 17β-HSD12 and characterized its enzymatic activity. Using human embryonic kidney cells (HEK)-293 cells stably expressing mouse 17β-HSD12, we found that in contrast with the human and monkey enzymes, which are specific for the transformation of E1 to E2, mouse 17β-HSD12 also catalyzes the transformation of 4-androstenedione into testosterone (T), dehydroepiandroster-one (DHEA) into 5-androstene-3β,17β-diol (5-diol), as well as androsterone into 5α-androstane-3α,17β-diol (3α-diol). Previously, we have shown that the specificity of human and monkey 17β-HSD12s for C18-steroid is due to the presence of a bulky phenylalanine (F) at position 234 creating steric hindrance, preventing the entrance of C19-steroids into the active site. To determine whether the smaller size of the corresponding leucine (L) in the mouse sequence is responsible for the entrance of androgenic substrates, we performed site-directed mutagenesis to substitute Leu 234 for Phe in the mouse enzyme. In agreement with our hypothesis, the mutated enzyme has a highly reduced ability to metabolize androgens. mRNA quantification in several mouse tissues using real-time PCR shows that mouse 17β-HSD12 mRNA is highly expressed in the female clitoral gland, male preputial gland, as well as in retroperitoneal fat and adrenal of both sexes. The differential androgenic/estrogenic substrate specificity of type 12 17β-HSD in the mouse and primates seems to agree with the observation that androgen and estrogen in the mouse are provided almost exclusively by gonads, while in primates an important part of these steroid hormones are produced locally from adrenal precursors.

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20

Provost, Pierre R., Charles H. Blomquist, Chantal Godin, Xiao-Fang Huang, Nicolas Flamand, Van Luu-The, Denis Nadeau, and Yves Tremblay. "Androgen Formation and Metabolism in the Pulmonary Epithelial Cell Line A549: Expression of 17β-Hydroxysteroid Dehydrogenase Type 5 and 3α-Hydroxysteroid Dehydrogenase Type 3*." Endocrinology 141, no. 8 (August 1, 2000): 2786–94. http://dx.doi.org/10.1210/endo.141.8.7589.

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21

Dufort, Isabelle, Patrick Rheault, Xiao-Fang Huang, Penny Soucy, and Van Luu-The. "Characteristics of a Highly Labile Human Type 5 17β-Hydroxysteroid Dehydrogenase1." Endocrinology 140, no. 2 (February 1, 1999): 568–74. http://dx.doi.org/10.1210/endo.140.2.6531.

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22

Tagawa, Noriko, Ryosuke Yuda, Sayaka Kubota, Midori Wakabayashi, Yuko Yamaguchi, Daisuke Kiyonaga, Natsuko Mori, Erika Minamitani, Hiroaki Masuzaki, and Yoshiharu Kobayashi. "17β-Estradiol inhibits 11β-hydroxysteroid dehydrogenase type 1 activity in rodent adipocytes." Journal of Endocrinology 202, no. 1 (April 20, 2009): 131–39. http://dx.doi.org/10.1677/joe-09-0021.

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17β-Estradiol (E2) serves as an anti-obesity steroid; however, the mechanism underlying this effect has not been fully clarified. The effect of E2 on adipocytes opposes that of glucocorticoids, which potentiate adipogenesis and anabolic lipid metabolism. The key to the intracellular activation of glucocorticoid in adipocytes is 11β-hydroxysteroid dehydrogenase type 1 (11β-HSD1), which catalyses the production of active glucocorticoids (cortisol in humans and corticosterone in rodents) from inactive 11-keto steroids (cortisone in humans and 11-dehydrocorticosterone in rodents). Using differentiated 3T3-L1 adipocytes, we showed that E2 inhibited 11β-HSD1 activity. Estrogen receptor (ER) antagonists, ICI-182 780 and tamoxifen, failed to reverse this inhibition. A significant inhibitory effect of E2 on 11β-HSD1 activity was observed within 5–10 min. Furthermore, acetylation or α-epimerization of 17-hydroxy group of E2 attenuated the inhibitory effect on 11β-HSD1. These results indicate that the inhibition of 11β-HSD1 by E2 depends on neither an ER-dependent route, transcriptional pathway nor non-specific fashion. Hexose-6-phosphate dehydrogenase, which provides the cofactor NADPH for full activation of 11β-HSD1, was unaffected by E2. A kinetic study revealed that E2 acted as a non-competitive inhibitor of 11β-HSD1. The inhibitory effect of E2 on 11β-HSD1 was reproduced in adipocytes isolated from rat mesenteric fat depots. This is the first demonstration that E2 inhibits 11β-HSD1, thereby providing a novel insight into the anti-obesity mechanism of estrogen.

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23

Quinkler, Marcus, Binayak Sinha, Jeremy W. Tomlinson, Iwona J. Bujalska, Paul M. Stewart, and Wiebke Arlt. "Androgen generation in adipose tissue in women with simple obesity – a site-specific role for 17β-hydroxysteroid dehydrogenase type 5." Journal of Endocrinology 183, no. 2 (November 2004): 331–42. http://dx.doi.org/10.1677/joe.1.05762.

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Women with polycystic ovary syndrome (PCOS) have high circulating androgens, thought to originate from ovaries and adrenals, and frequently suffer from the metabolic syndrome including obesity. However, serum androgens are positively associated with body mass index (BMI) not only in PCOS, but also in simple obesity, suggesting androgen synthesis within adipose tissue. Thus we investigated androgen generation in human adipose tissue, including expression of 17β-hydroxysteroid dehydrogenase (17β-HSD) isozymes, important regulators of sex steroid metabolism. Paired omental and subcutaneous fat biopsies were obtained from 27 healthy women undergoing elective abdominal surgery (age range 30–50 years; BMI 19.7–39.2 kg/m2). Enzymatic activity assays in preadipocyte proliferation cultures revealed effcient conversion of androstenedione to testosterone in both subcutaneous and omental fat. RT-PCR of whole fat and preadipocytes of subcutaneous and omental origin showed expression of 17β-HSD types 4 and 5, but no relevant expression of 17β-HSD types 1, 2, or 3. Microarray analysis confirmed this expression pattern (17β-HSD5>17β-HSD4) and suggested a higher expression of 17β-HSD5 in subcutaneous fat. Accordingly, quantitative real-time RT-PCR showed significantly higher expression of 17β-HSD5 in subcutaneous compared with omental fat (P<0.05). 17β-HSD5 expression in subcutaneous, but not omental, whole fat correlated significantly with BMI (r=0.51, P<0.05). In keeping with these findings, 17β-HSD5 expression in subcutaneous fat biopsies from six women taking part in a weight loss study decreased significantly with weight loss (P<0.05). A role for 17β-HSD5 in adipocyte differentiation was further supported by the observed increase in 17β-HSD5 expression upon differentiation of stromal preadipocytes to mature adipocytes (n=5; P<0.005), which again was higher in cells of subcutaneous origin. Functional activity of 17β-HSD5 also significantly increased with differentiation, revealing a net gain in androgen activation (androstenedione to testosterone) in subcutaneous cultures, contrasting with a net gain in androgen inactivation (testosterone to androstenedione) in omental cultures. Thus, human adipose tissue is capable of active androgen synthesis catalysed by 17β-HSD5, and increased expression in obesity may contribute to circulating androgen excess.

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24

Qiu, Wei, Ming Zhou, Fernand Labrie, and Sheng-Xiang Lin. "Crystal Structures of the Multispecific 17β-Hydroxysteroid Dehydrogenase Type 5: Critical Androgen Regulation in Human Peripheral Tissues." Molecular Endocrinology 18, no. 7 (July 1, 2004): 1798–807. http://dx.doi.org/10.1210/me.2004-0032.

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Abstract Human type 5 17β-hydroxysteroid dehydrogenase (17β-HSD5;AKR1C3) plays a major role in the metabolism of androgens in peripheral tissues. In prostate basal cells, this enzyme is involved in the transformation of dehydroepiandrosterone into dihydrotestosterone, the most potent androgen. It is thus a potential target for prostate cancer therapy because it is understood that the testosterone formation by this enzyme is an important factor, particularly in patients who have undergone surgical or medical castration. Here we report the first structure of a human type 5 17β-HSD in two ternary complexes, in which we found that the androstenedione molecule has a different binding position from that of testosterone. The two testosterone-binding orientations in the substrate-binding site demonstrate the structural basis of the alternative binding and multispecificity of the enzyme. Phe306 and Trp227 are the key residues involved in ligand recognition as well as product release. A safety belt in the cofactor-binding site enhances nicotinamide adenine dinucleotide phosphate binding and accounts for its high affinity as demonstrated by kinetic studies. These structures have provided a dynamic view of the enzyme reaction converting androstenedione to testosterone as well as valuable information for the development of potent enzyme inhibitors.

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25

Penning, Trevor M. "AKR1C3 (type 5 17β-hydroxysteroid dehydrogenase/prostaglandin F synthase): Roles in malignancy and endocrine disorders." Molecular and Cellular Endocrinology 489 (June 2019): 82–91. http://dx.doi.org/10.1016/j.mce.2018.07.002.

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26

Zhou, Ming, Wei Qiu, Ho-Jin Chang, Anne Gangloff, and Sheng-Xiang Lin. "Purification, crystallization and preliminary X-ray diffraction results of human 17β-hydroxysteroid dehydrogenase type 5." Acta Crystallographica Section D Biological Crystallography 58, no. 6 (May 29, 2002): 1048–50. http://dx.doi.org/10.1107/s0907444902005255.

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27

Gazvoda, Martin, Nataša Beranič, Samo Turk, Bojan Burja, Marijan Kočevar, Tea Lanišnik Rižner, Stanislav Gobec, and Slovenko Polanc. "2,3-Diarylpropenoic acids as selective non-steroidal inhibitors of type-5 17β-hydroxysteroid dehydrogenase (AKR1C3)." European Journal of Medicinal Chemistry 62 (April 2013): 89–97. http://dx.doi.org/10.1016/j.ejmech.2012.12.045.

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28

Blouin, Karine, Christian Richard, Chantal Bélanger, Pierre Dupont, Marleen Daris, Philippe Laberge, Van Luu-The, and André Tchernof. "Local Androgen Inactivation in Abdominal Visceral Adipose Tissue." Journal of Clinical Endocrinology & Metabolism 88, no. 12 (December 1, 2003): 5944–50. http://dx.doi.org/10.1210/jc.2003-030535.

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Abstract We examined the expression and activity of two enzymes from the aldoketoreductase (AKR) family 1C, namely type 5 17β-hydroxysteroid dehydrogenase (17β-HSD-5, AKR1C3) and type 3 3α-hydroxysteroid dehydrogenase (3α-HSD-3, AKR1C2) in female sc and omental adipose tissue and in preadipocyte primary cultures. 17β-HSD-5 preferentially synthesizes testosterone from the inactive adrenal precursor androstenedione, whereas 3α-HSD-3 inactivates dihydrotestosterone. mRNAs of both enzymes were detected in adipose tissue from the omental and sc compartments. Real-time PCR quantification indicated a 3-fold higher 3α-HSD-3 expression compared with 17β-HSD-5, and the expression of both enzymes tended to be higher in the sc vs. the omental depot. Accordingly, dose-response and time-course experiments performed in preadipocyte primary cultures indicated that 3α-HSD activity was higher than 17β-HSD activity (13-fold maximum velocity difference). We measured 3α-HSD activity in omental and sc adipose tissue samples of 32 women for whom body composition and body fat distribution were evaluated by dual-energy x-ray absorptiometry and CT, respectively. We found that androgen inactivation in omental adipose tissue through 3α-HSD activity was significantly higher in women with elevated vs. low visceral adipose tissue accumulation (1.7-fold difference; P < 0.05). Moreover, omental adipose tissue 3α-HSD activity was positively and significantly associated with CT-measured visceral adipose tissue (r = 0.43; P < 0.02) and omental adipocyte diameter (r = 0.42; P < 0.02). These results indicate that local androgen inactivation is a predominant reaction in female abdominal adipose tissue, with the greatest conversion rates observed in the presence of abdominal visceral obesity. Increased androgen inactivation in omental adipose tissue of abdominally obese women may impact locally on the regulation of adipocyte metabolism.

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29

El-Alfy, Mohamed, Van Luu-The, Xiao-Fang Huang, Louise Berger, Fernand Labrie, and Georges Pelletier. "Localization of Type 5 17β-Hydroxysteroid Dehydrogenase, 3β-Hydroxysteroid Dehydrogenase, and Androgen Receptor in the Human Prostate by in Situ Hybridization and Immunocytochemistry." Endocrinology 140, no. 3 (March 1, 1999): 1481–91. http://dx.doi.org/10.1210/endo.140.3.6585.

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30

Cho, Moon-Kyun. "Decreased Expression of Type 5 17β-Hydroxysteroid Dehydrogenase (AKR1C3) Protein Identified in Human Diabetic Skin Tissue." Annals of Dermatology 25, no. 4 (2013): 423. http://dx.doi.org/10.5021/ad.2013.25.4.423.

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31

Ishikura, Shuhei, Kengo Matsumoto, Masaharu Sanai, Kenji Horie, Toshiyuki Matsunaga, Kazuo Tajima, Ossama El-Kabbani, and Akira Hara. "Molecular Cloning of a Novel Type of Rat Cytoplasmic 17β-Hydroxysteroid Dehydrogenase Distinct from the Type 5 Isozyme." Journal of Biochemistry 139, no. 6 (June 1, 2006): 1053–63. http://dx.doi.org/10.1093/jb/mvj109.

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32

Lin, Hsueh-Kung, Stephan Steckelbroeck, Kar-Ming Fung, Amy N. Jones, and Trevor M. Penning. "Characterization of a monoclonal antibody for human aldo-keto reductase AKR1C3 (type 2 3α-hydroxysteroid dehydrogenase/type 5 17β-hydroxysteroid dehydrogenase); immunohistochemical detection in breast and prostate." Steroids 69, no. 13-14 (December 2004): 795–801. http://dx.doi.org/10.1016/j.steroids.2004.09.014.

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33

RANELLETTI, FRANCO O., MAURO PIANTELLI, ARNALDO CARBONE, ALESSANDRO RINELLI, GIOVANNI SCAMBIA, PIERLUIGI BENEDETTI PANICI, and SALVATORE MANCUSO. "Type II Estrogen-Binding Sites and 17β-Hydroxysteroid Dehydrogenase Activity in Human Peripheral Blood Mononuclear Cells*." Journal of Clinical Endocrinology & Metabolism 67, no. 5 (November 1988): 888–92. http://dx.doi.org/10.1210/jcem-67-5-888.

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34

Chang, Yi-Hsun, Yuan-Liang Wang, Jain-Yu Lin, Lea-Yea Chuang, and Chi-Ching Hwang. "Expression, Purification, and Characterization of a Human Recombinant 17β-Hydroxysteroid Dehydrogenase Type 1 in Escherichia coli." Molecular Biotechnology 44, no. 2 (November 14, 2009): 133–39. http://dx.doi.org/10.1007/s12033-009-9221-5.

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Yang, Sijun, Zongjuan Fang, Bilgin Gurates, Mitsutoshi Tamura, Josephine Miller, Karen Ferrer, and Serdar E. Bulun. "Stromal PRs Mediate Induction of 17β-Hydroxysteroid Dehydrogenase Type 2 Expression in Human Endometrial Epithelium: A Paracrine Mechanism for Inactivation Of E2." Molecular Endocrinology 15, no. 12 (December 1, 2001): 2093–105. http://dx.doi.org/10.1210/mend.15.12.0742.

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Abstract Progesterone stimulates the expression of 17β-hydroxysteroid dehydrogenase (HSD) type 2, which catalyzes the conversion of the potent estrogen, E2, to an inactive form, estrone, in epithelial cells of human endometrial tissue. Various effects of progesterone on uterine epithelium have recently been shown to be mediated by stromal PRs in mice. We describe herein a critical paracrine mechanism whereby progesterone induction of 17β-HSD type 2 enzyme activity, transcript levels, and promoter activity in human endometrial epithelial cells are mediated primarily by PR in endometrial stromal cells. Medium conditioned with progestin-pretreated human endometrial stromal cells robustly increased 17β-HSD type 2 enzyme activity (2-fold) and mRNA levels (13.2-fold) in Ishikawa malignant endometrial epithelial cells. In contrast, direct progestin treatment of Ishikawa epithelial cells gave rise to much smaller increases in enzyme activity (1.2-fold) and mRNA levels (4-fold). These results suggest that progesterone- dependent paracrine factors arising from stromal cells are primarily responsible for the induction of epithelial 17β-HSD type 2 expression in the endometrium. We transfected serial deletion mutants of the −1,244 bp 5′-flanking region of the 17β-HSD type 2 gene into Ishikawa cells. No progesterone response elements could be identified upstream of the 17β-HSD type 2 promoter. Stromal PR-dependent induction of the 17β-HSD type 2 promoter was mediated by a critical regulatory region mapped to the −200/−100 bp sequence. Direct treatment of Ishikawa cells with progestin gave rise to a maximal increase in the activity of −200 bp/Luciferase construct only by 1.2-fold, whereas medium conditioned by progestin-pretreated endometrial stromal cells increased promoter activity up to 2.4-fold in a time- and concentration-dependent manner. The stimulatory effect of medium conditioned by progestin-pretreated stromal cells was enhanced strikingly by increasing stromal cell PR levels with the addition of estrogen. This epithelial-stromal interaction was specific for endometrial epithelial cells, since 17β-HSD type 2 could not be induced in malignant breast epithelial cells by media conditioned with progestin-treated breast or endometrial stromal cells. In conclusion, progesterone regulates the conversion of biologically active E2 to estrone by inducing the 17β-HSD type 2 enzyme in human endometrial epithelium primarily via PR in stromal cells, which secrete factors that induce transcription mediated primarily by the −200/−100 bp 5′-regulatory region of the 17β-HSD type 2 promoter.

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Endo, Satoshi, Toshiyuki Matsunaga, Ayano Kanamori, Yoko Otsuji, Hiroko Nagai, Krithika Sundaram, Ossama El-Kabbani, Naoki Toyooka, Shozo Ohta, and Akira Hara. "Selective Inhibition of Human Type-5 17β-Hydroxysteroid Dehydrogenase (AKR1C3) by Baccharin, a Component of Brazilian Propolis." Journal of Natural Products 75, no. 4 (April 16, 2012): 716–21. http://dx.doi.org/10.1021/np201002x.

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Pelletier, G., V. Luu-The, S. Li, and F. Labrie. "Localization of type 5 17β-hydroxysteroid dehydrogenase mRNA in mouse tissues as studied by in situ hybridization." Cell and Tissue Research 320, no. 3 (April 22, 2005): 393–98. http://dx.doi.org/10.1007/s00441-005-1105-9.

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38

Poirier, Donald, Jenny Roy, and René Maltais. "A Targeted-Covalent Inhibitor of 17β-HSD1 Blocks Two Estrogen-Biosynthesis Pathways: In Vitro (Metabolism) and In Vivo (Xenograft) Studies in T-47D Breast Cancer Models." Cancers 13, no. 8 (April 13, 2021): 1841. http://dx.doi.org/10.3390/cancers13081841.

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17β-Hydroxysteroid dehydrogenase type 1 (17β-HSD1) plays an important role in estrogen-dependent breast tumor growth. In addition to being involved in the production of estradiol (E2), the most potent estrogen in women, 17β-HSD1 is also responsible for the production of 5-androsten-3β,17β-diol (5-diol), a weaker estrogen than E2, but whose importance increases after menopause. 17β-HSD1 is therefore a target of choice for the treatment of estrogen-dependent diseases such as breast cancer and endometriosis. After we developed the first targeted-covalent (irreversible) and non-estrogenic inhibitor of 17β-HSD1, a molecule named PBRM, our goal was to demonstrate its therapeutic potential. Enzymatic assays demonstrated that estrone (E1) and dehydroepiandrosterone (DHEA) were transformed into E2 and 5-diol in T-47D human breast cancer cells, and that PBRM was able to block these transformations. Thereafter, we tested PBRM in a mouse tumor model (cell-derived T-47D xenografts). After treatment of ovariectomized (OVX) mice receiving E1 or DHEA, PBRM given orally was able to reduce the tumor growth at the control (OVX) level without any observed toxic effects. Thanks to its irreversible type of inhibition, PBRM retained its anti-tumor growth effect, even after reducing its frequency of administration to only once a week, a clear advantage over reversible inhibitors.

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Lee, C. M. H., F. R. Tekpetey, D. T. Armstrong, and M. W. Khalil. "Conversion of 5(10)-oestrene-3β,17β-diol to 19-nor-4-ene-3-ketosteroids by luteal cells in vitro: possible involvement of the 3β-hydroxysteroid dehydrogenase/isomerase." Journal of Endocrinology 129, no. 2 (May 1991): 233–43. http://dx.doi.org/10.1677/joe.0.1290233.

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ABSTRACT We have previously suggested that in porcine granulosa cells, a putative intermediate, 5(10)-oestrene-3,17-dione is involved in 4-oestrene-3,17-dione (19-norandrostenedione; 19-norA) and 4-oestren-17β-ol-3-one (19-nortestosterone: 19-norT) formation from C19 aromatizable androgens. In this study, luteal cells prepared from porcine, bovine and rat corpora lutea by centrifugal elutriation were used as a source of 3β-hydroxysteroid dehydrogenase/isomerase in order to investigate the role of this enzyme in the biosynthesis of 19-norsteroids. Small porcine luteal cells made mainly 19-norT and large porcine luteal cells 19-norA from 5(10)-oestrene-3β,17β-diol, the reduced product of the putative intermediate 5(10)-oestrene-3,17-dione. However, neither small nor large cells metabolized androstenedione to 19-norsteroids. Serum and serum plus LH significantly stimulated formation of both 19-norA and 19-norT from 5(10)-oestrene-3β,17β-diol, compared with controls. Inhibitors of the 3β-hydroxysteroid dehydrogenase/isomerase (trilostane and cyanoketone) significantly reduced formation of 19-norT in small porcine luteal cells and 19-norA in large porcine luteal cells, although they were effective at different concentrations in each cell type. In parallel incubations, formation of [4-14C]androstenedione from added [4-14C]dehydroepiandrosterone was also inhibited by cyanoketone in both small and large porcine luteal cells in a dose-dependent manner; however, trilostane (up to 100 μmol/l) did not inhibit androstenedione formation in large porcine luteal cells. In addition, the decrease in progesterone synthesis induced by trilostane and cyanoketone (100 μmol/l each) was accompanied by a parallel accumulation of pregnenolone in both cell types. These results suggest that 3β-hydroxysteroid dehydrogenase/isomerase, or a closely related enzyme, present in small and large porcine luteal cells can convert added 5(10)-3β-hydroxysteroids into 19-nor-4(5)-3-kestosteroids in vitro. In the porcine ovarian follicle, therefore, formation of 19-norA from androstenedione can be envisaged as a two-step enzymatic process: 19-demethylation of androstenedione to produce the putative intermediate 5(10)-oestrene-3,17-dione, and subsequent isomerization to 19-norA. In contrast to granulosa cells, porcine luteal cells synthesized 19-norA or 19-norT only when provided with the appropriate substrate. Unfractionated rat luteal cells also metabolized 5(10)-oestrene-3β,17β-diol to a mixture of 19-norA and 19-norT; conversion was inhibited by trilostane. In addition, small bovine luteal cells synthesized mainly 19-norT and formation was also inhibited by trilostane and cyanoketone. In addition to 19-norA, an unknown metabolite, formed in low amounts by large porcine luteal cells, appears to be related to another steroid which accumulated at high inhibitor concentrations; it may represent 5(10)-oestrene-3,17-dione postulated as a putative intermediate formed during 19-norsteroid biosynthesis. Journal of Endocrinology (1991) 129, 233–243

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40

Kikuchi, Aya, Kentaro Enjo, Takashi Furutani, Hidenori Azami, Tatsuya Nimi, Sadao Kuromitsu, and Yoshiteru Kamiyma. "ASP9521, a novel, selective, orally bioavailable AKR1C3 (type 5, 17ß-hydroxysteroid dehydrogenase) inhibitor: In vitro and in vivo characterization." Journal of Clinical Oncology 31, no. 15_suppl (May 20, 2013): 5046. http://dx.doi.org/10.1200/jco.2013.31.15_suppl.5046.

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5046 Background: Aldo–keto reductase 1C3 (AKR1C3), also known as type 5, 17β-hydroxysteroid dehydrogenase, is reported to be highly expressed in human normal prostate and prostate cancer (PC) and the expression increases along with increasing malignancy or grade of PC. Since AKR1C3 converts the adrenal androgen, androstenedione (AD) into testosterone (T), combination with a GnRH analogue and AKR1C3 inhibitor would be expected to provide total androgen blockade in the treatment of castration-resistant prostate cancer (CRPC). We obtained a lead compound having a non-steroidal scaffold by high throughput screening (HTS) approaches for targeting enzyme activity of AKR1C3. After optimization of the lead compound, we found ASP9521 as a potent, selective, and orally bioavailable AKR1C3 inhibitor. Methods: The inhibitory effect of ASP9521 on enzymatic conversion from AD to T by AKR1C3 was evaluated in vitro, and in CWR22R xenograft models. Effect of PSA production and proliferation on LNCaP cells stably expressing AKR1C3 was examined. Pharmacokinetics in various animals were also investigated. Results: ASP9521 showed potent inhibitory effect on enzymatic conversion from AD to T by both human AKR1C3 and cynomolgus monkey homologues in a concentration-dependent manner, with IC50 values of 11 and 49 nmol/L, respectively ASP9521 suppressed both AD-dependent PSA production and cell proliferation in LNCaP cells exogenously expressing AKR1C3 in vitro. The bioavailability of ASP9521after oral administration of 1mg/kg were 30% and 78% in rat and dog, respectively. Furthermore, ASP9521 single oral administration of 3 mg/kg suppressed AD-induced intratumoral T production in CWR22R xenografted castrate nude mice, and this inhibitory effect was maintained for 24 h. In addition, ASP9521 was rapidly eliminated from plasma after oral administration while its intratumoral concentration remained high in tumors expressing AKR1C3. Conclusions: These preclinical in vitro and in vivo data are consistent with a potent inhibition of 17β-hydroxysteroid dehydrogenase. The results suggest that ASP9521 should be investigated further to elucidate its role as treatment for PC.

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Nakamura, Yasuhiro, Takashi Suzuki, Masao Nakabayashi, Mareyuki Endoh, Kazuhiro Sakamoto, Yoshiki Mikami, Takuya Moriya, et al. "In situ androgen producing enzymes in human prostate cancer." Endocrine-Related Cancer 12, no. 1 (March 2005): 101–7. http://dx.doi.org/10.1677/erc.1.00914.

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Androgens have been proposed to be actively produced in situ in human prostate cancer. These locally produced androgens have also been considered to play important roles in the pathogenesis and development of prostate cancer. Therefore, it is important to examine the status of this in situ androgen metabolism and/or synthesis in detail in order to improve the clinical response to hormonal therapy in patients diagnosed with prostate cancer. Several studies have previously demonstrated the expression of androgen-producing enzymes such as 5α-reductase types 1 and 2, and 17β-hydroxysteroid dehydrogenase type 5 (17β-HSD5), in human prostate carcinoma cells. However, their biological significance has remained largely unknown. In this study, we evaluated the immunoreactivities of these steroidogenic enzymes in human prostate cancer obtained from surgery (n=70), and correlated the findings with clinicopathological features of the patients. 17β-HSD5 immunoreactivity was detected in 54 cases (77%), 5α-reductase type 1 in 51 cases (73%) and 5α-reductase type 2 in 39 cases (56%). 5α-reductase type 2 immunoreactivity was significantly correlated with that of androgen receptor (AR), and 17β-HSD5 positive cases were significantly associated with clinical stage (TNM stage pT3 vs pT2). These data all suggest that androgen-producing enzymes, such as 5α-reductase type 1 and type 2, and 17β-HSD5 are expressed in a majority of prostate cancers, and are involved in the local production and actions of androgens in prostate cancers.

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42

Jakob, Franz, Dorothee Homann, and Jerzy Adamski. "Expression and regulation of aromatase and 17β-hydroxysteroid dehydrogenase type 4 in human THP 1 leukemia cells." Journal of Steroid Biochemistry and Molecular Biology 55, no. 5-6 (December 1995): 555–63. http://dx.doi.org/10.1016/0960-0760(95)00206-5.

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Simard, Marc, Julie Plante, Mélanie Boucher, Pierre R. Provost, and Yves Tremblay. "Type 2 and 5 17β-hydroxysteroid dehydrogenases and androgen receptor in human fetal lungs." Molecular and Cellular Endocrinology 319, no. 1-2 (May 5, 2010): 79–87. http://dx.doi.org/10.1016/j.mce.2009.12.007.

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Li, Y., V. Isomaa, A. Pulkka, R. Herva, H. Peltoketo, and P. Vihko. "Expression of 3β-hydroxysteroid dehydrogenase type 1, P450 aromatase, and 17β-hydroxysteroid dehydrogenase types 1, 2, 5 and 7 mRNAs in human early and mid-gestation placentas." Placenta 26, no. 5 (May 2005): 387–92. http://dx.doi.org/10.1016/j.placenta.2004.07.008.

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Rotinen, Mirja, Jon Celay, Marta M. Alonso, Aranzazu Arrazola, Ignacio Encio, and Joaquin Villar. "Estradiol induces type 8 17β-hydroxysteroid dehydrogenase expression: crosstalk between estrogen receptor α and C/EBPβ." Journal of Endocrinology 200, no. 1 (October 13, 2008): 85–92. http://dx.doi.org/10.1677/joe-08-0134.

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Hydroxysteroid (17-beta) dehydrogenase (HSD17B) are the enzymes responsible for the reversible interconversion of 17-hydroxy and 17-keto steroids. The human and mouse type 8 17β-HSD (HSD17B8) selectively catalyze the conversion ofestradiol (E2) to estrone (E1). We previously described thatHSD17B8 is transcriptionally regulated by C/EBPβ, andthat C/EBPβ is bound to CCAAT boxes located at −5 and −46 of the transcription start site in basal conditions in HepG2 cells. Furthermore, ectopic expression of C/EBPβ transactivated the HSD17B8 promoter activity. Here, we show that HSD17B8 expression is up-regulated in response toE2 in the estrogen receptor α (ERα) positive MCF-7 cells. Results showed that this induction is mediated by ERα because i) E2 did not induce HSD17B8 expression in ERαnegative HepG2 cells, ii) ectopic expression of ERα restored E2-induced HSD17B8 expression, and iii) this induction wasblocked by the anti-ER ICI 182 780. Additional experiments showed that no estrogen response element was necessary for this regulation. However, the CCAAT boxes located at the HSD17B8 proximal promoter were required for E2-induced transcription. Furthermore, co-immunoprecipitation studies revealed tethering of ERαtoC/EBPβ inresponse to E2 in cells expressing ERα. Additionally, chromatin immunoprecipitation assays demonstrated that, in response to E2, ERα is recruited to the CCAAT boxes in which C/EBPβ is already bound. Taken together, our results reveal that ERα is involved in the transcriptional regulation ofHSD17B8gene in response to E2 through its interaction with C/EBPβ.

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Qin, Kenan, David A. Ehrmann, Nancy Cox, Samuel Refetoff, and Robert L. Rosenfield. "Identification of a Functional Polymorphism of the Human Type 5 17β-Hydroxysteroid Dehydrogenase Gene Associated with Polycystic Ovary Syndrome." Journal of Clinical Endocrinology & Metabolism 91, no. 1 (January 2006): 270–76. http://dx.doi.org/10.1210/jc.2005-2012.

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Schuster, Daniela, Dorota Kowalik, Johannes Kirchmair, Christian Laggner, Patrick Markt, Christel Aebischer-Gumy, Fabian Ströhle, et al. "Identification of chemically diverse, novel inhibitors of 17β-hydroxysteroid dehydrogenase type 3 and 5 by pharmacophore-based virtual screening." Journal of Steroid Biochemistry and Molecular Biology 125, no. 1-2 (May 2011): 148–61. http://dx.doi.org/10.1016/j.jsbmb.2011.01.016.

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Adeniji, Adegoke O., Barry M. Twenter, Michael C. Byrns, Yi Jin, Jeffrey D. Winkler, and Trevor M. Penning. "Discovery of substituted 3-(phenylamino)benzoic acids as potent and selective inhibitors of type 5 17β-hydroxysteroid dehydrogenase (AKR1C3)." Bioorganic & Medicinal Chemistry Letters 21, no. 5 (March 2011): 1464–68. http://dx.doi.org/10.1016/j.bmcl.2011.01.010.

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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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Dufort, Isabelle, Fernand Labrie, and Van Luu-The. "Human Types 1 and 3 3α-Hydroxysteroid Dehydrogenases: Differential Lability and Tissue Distribution1." Journal of Clinical Endocrinology & Metabolism 86, no. 2 (February 1, 2001): 841–46. http://dx.doi.org/10.1210/jcem.86.2.7216.

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3α-Hydroxysteroid dehydrogenases (3α-HSDs) catalyze the conversion of 3-ketosteroids to 3α-hydroxy compounds. The best known 3α-HSD activity is the transformation of the most potent natural androgen, dihydrotestosterone, into 5α-androstan-3α,17β-diol (3α-diol), a compound having much lower activity. Previous reports show that 3α-HSDs are involved in the metabolism of glucocorticoids, progestins, prostaglandins, bile acid precursors, and xenobiotics. 3α-HSDs could, thus, play a crucial role in the control of a series of active steroid levels in target tissues. In the human, type 1 3α-HSD was first identified as human chlordecone reductase. Recently, we have isolated and characterized type 3 3α-HSD that shares 81.7% identity with human type 1 3α-HSD. The transfection of vectors expressing types 1 and 3 3α-HSD in transformed human embryonic kidney (HEK-293) cells indicates that both enzymes efficiently catalyze the transformation of dihydrotestosterone into 3α-diol in intact cells. However, when the cells are broken, the activity of type 3 3α-HSD is rapidly lost, whereas the type 1 3α-HSD activity remains stable. We have previously found that human type 5 17β-HSD which possesses 84% and 86% identity with types 1 and 3 3α-HSD, respectively, is also labile, whereas rodent enzymes such as mouse type 5 17β-HSD and rat 3α-HSD are stable after homogenization of the cells. The variable stability of different enzymatic activities in broken cell preparations renders the comparison of different enzymes difficult. RNA expression analysis indicates that human type 1 3α-HSD is expressed exclusively in the liver, whereas type 3 is more widely expressed and is found in the liver, adrenal, testis, brain, prostate, and HaCaT keratinocytes. Based on enzymatic characteristics and sequence homology, it is suggested that type 1 3α-HSD is an ortholog of rat 3α-HSD while type 3 3α-HSD, which must have diverged recently, seems unique to human and is probably more involved in intracrine activity.

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