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Integrated view on 17beta-hydroxysteroid dehydrogenases
Abstract
17beta-Hydroxysteroid dehydrogenases (17beta-HSDs) are important enzymes in steroid metabolism. Long known members of the protein family seemed to be well characterised concerning their role in the regulation of the biological potency of steroid hormones, but today more and more evidence points to pivotal contributions of these enzymes in a variety of other metabolic pathways. Therefore, studies on 17beta-HSDs develop towards metabolomic survey. Latest research results give new insights into the complex metabolic interconnectivity of the 17beta-HSDs. In this paper metabolic activities of 17beta-HSDs will be compared, their interplay with endogenous substrates summarised, and interlacing pathways depicted. Strategies on deciphering the physiological role of 17beta-HSDs and the genetic predisposition for associated diseases will be presented.
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“Mutations in CYP11B2 selectively impair aldosterone synthesis, causing hyponatremia and hyperkalemia with normal cortisol production (39,90).”
From Congenital Adrenal Hyperplasia—Current Insights in Pathophysiology, Diagnostics, and Management (2022) · cites this paper as [90]
In the citing paper
“Generally, these enzymes are multi-functional and often have overlapping substrate specificities and expression patterns, allowing for redundant enzymes to cover in case of deficiency of another enzyme [107,114].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [114]
In the citing paper
“To date, 14 human enzymes with 17β-HSD/oxoreductase activities have been identified [105,106,113].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [106]
In the citing paper
“The majority of 5α/β-3α-metabolites of testosterone and DHT, which contain a 17β-hydroxy, are converted to 17-keto steroids by the action of the oxidative 17β-HSDs, HSD17B2 and HSD17B4 [106].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [106]
Citations
Cites
ABAD Directly Links Aß to Mitochondrial Toxicity in Alzheimer's Disease
Lustbader, J. W., Cirilli, M., Lin, C., Xu, H. W., Takuma, K., Wang, N., Caspersen, C., Chen, X., Pollak, S., Chaney, M., et al. (2004) · Science · doi:10.1126/science.1091230 · Cited by 1,303
PENNING, T. M., BURCZYNSKI, M. E., JEZ, J. M., HUNG, C.-F., LIN, H.-K., MA, H., MOORE, M., PALACKAL, N., & RATNAM, K. (2000) · Biochemical Journal · doi:10.1042/bj3510067 · Cited by 649
Short-chain dehydrogenases/reductases (SDR): the 2002 update
Oppermann, U. C. T., Filling, C., Hult, M., Shafqat, N., Wu, X., Lindh, M., Shafqat, J., Nordling, E., Kallberg, Y., Persson, B., et al. (2003) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00164-3 · Cited by 633
Male pseudohermaphroditism caused by mutations of testicular 17β-hydroxysteroid dehydrogenase 3
Geissler, W. M., Davis, D. L., Wu, L., Bradshaw, K. D., Patel, S., Mendonca, B. B., Elliston, K. O., Wilson, J. D., Russell, D. W., & Andersson, S. (1994) · Nature Genetics · doi:10.1038/ng0594-34 · Cited by 570
Wu, L., Einstein, M., Geissler, W. M., Chan, H. K., Elliston, K. O., & Andersson, S. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31480-7 · Cited by 437
The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative
Persson, B., Kallberg, Y., Bray, J. E., Bruford, E. A., Dellaporta, S. L., Favia, A. D., Duarte, R. G., Jörnvall, H., Kavanagh, K. L., Kedishvili, N. Y., et al. (2008) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2008.10.040 · Cited by 397
Du Yan, S., Fu, J., Soto, C., Chen, X., Zhu, H., Al-Mohanna, F., Collison, K., Zhu, A., Stern, E., Saido, T., et al. (1997) · Nature · doi:10.1038/39522 · Cited by 379
Endometriosis: The pathophysiology as an estrogen-dependent disease
Kitawaki, J., Kado, N., Ishihara, H., Koshiba, H., Kitaoka, Y., & Honjo, H. (2002) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(02)00260-1 · Cited by 370
Polymorphisms Associated With Circulating Sex Hormone Levels in Postmenopausal Women
Dunning, A. M., Dowsett, M., Healey, C. S., Tee, L. J., Luben, R., Folkerd, E. J., Novik, K. L., Kelemen, L., Ogata, S., Pharoah, P. D. P., et al. (2004) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djh167 · Cited by 346
Fujimoto, Y., Itabe, H., Sakai, J., Makita, M., Noda, J., Mori, M., Higashi, Y., Kojima, S., & Takano, T. (2003) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2003.10.018 · Cited by 331
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Research works printed but not linked: 2
- Lenski, 2007, The reduced expression of the HADH2 protein causes X-linked mental retardation, choreoathetosis, and abnormal behavior, Am. J. Hum. Genet., 80, 372, 10.1086/511527 · DOI
- Nagasaki, S., Suzuki, T., Miki, Y., Akahira, J., Kitada, K., Ishida, T., Handa, H., Ohuchi, N., Sasano, H., in press. 17β-hydroxysteroid dehydrogenase type12 in human breast carcinoma: a prognostic factor via potential regulation of fatty acids synthesis. Cancer Res.
Cited by
Sorted by citations
Items 101–200 of 226
Zhang, Y., Wang, Q., Ji, Y., Zhang, Q., Wu, H., Xie, J., & Zhao, J. (2014) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2014.04.027 · Cited by 20
17β-Hydroxysteroid dehydrogenases and neurosteroid metabolism in the central nervous system
He, X., Dobkin, C., & Yang, S. (2018) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2018.10.002 · Cited by 20
Molecular Mechanism Study on Stereo-Selectivity of α or β Hydroxysteroid Dehydrogenases
Gao, M., Nie, K., Qin, M., Xu, H.-J., Wang, F., & Liu, L. (2021) · Crystals · doi:10.3390/cryst11030224 · Cited by 22
“Up to now, over 14 different subtypes of 17β–HSDHs (17β–HSD1–14) have been identified, most of them belong to the SDR superfamily except 17β–HSD5, which is a member of the AKR superfamily [54,55].”
BackgroundMeier, M., Tokarz, J., Haller, F., Mindnich, R., & Adamski, J. (2008) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2008.10.036 · Cited by 19
Zhou, J., Gao, Y.-F., Li, L., Zhai, H.-N., Tan, S., & Cai, Z. (2011) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-011-0811-8 · Cited by 20
“a Rossmann-fold, consisting of a central b-sheet flanked by a-helices [11].”
BackgroundSpermatogenesis and regulatory factors in the wall lizard Podarcis sicula
Rosati, L., Agnese, M., Lorenzo, M. D., Barra, T., Valiante, S., & Prisco, M. (2020) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2020.113579 · Cited by 19
Tu, X., Kuang, Z., Gong, X., Shi, Y., Yu, L., Shi, H., Wang, J., & Sun, Z. (2015) · PLoS ONE · doi:10.1371/journal.pone.0141800 · Cited by 20
“expressed in the ovaries of pregnant animals [36].”
BackgroundExpression of steroidogenesis-related genes in murine male germ cells
Culty, M., Liu, Y., Manku, G., Chan, W., & Papadopoulos, V. (2015) · Steroids · doi:10.1016/j.steroids.2015.08.011 · Cited by 18
“HSD17B12, which shares 40% sequence homology with HSD17B3, has been shown to reduce E1 to E2 in cell lines, but its main function is thought to be its role in the synthesis of long chain fatty acids [51,52].”
BackgroundInfluentialDjigoué, G. B., Kenmogne, L. C., Roy, J., Maltais, R., & Poirier, D. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.07.049 · Cited by 18
Shammas, C., Neocleous, V., Toumba, M., Costi, C., Phedonos, A., Efstathiou, E., Kyriakou, A., Phylactou, L. A., & Skordis, N. (2012) · Genetic Testing and Molecular Biomarkers · doi:10.1089/gtmb.2011.0381 · Cited by 18
“There are at least 14 known isoenzymes of 17 b -HSD that play a role in the final stages of all androgen and estrogen synthesis (Labrie et al. , 1997; Wu et al. , 2007; Kowalik et al. , 2009; Moeller and Adamski, 2009).”
Transcript level of AKR1C3 is down-regulated in gastric cancer
Frycz, B. A., Murawa, D., Borejsza‐Wysocki, M., Wichtowski, M., Spychała, A., Marciniak, R., Murawa, P., Drews, M., & Jagodziński, P. P. (2015) · Biochemistry and Cell Biology · doi:10.1139/bcb-2015-0096 · Cited by 19
Expression of 17β-hydroxysteroid dehydrogenase type 1 in gastric cancer
Frycz, B. A., Murawa, D., Borejsza‐Wysocki, M., Marciniak, R., Murawa, P., Drews, M., & Jagodziński, P. P. (2013) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2013.06.012 · Cited by 18
“The two isoforms, HSD17B1 and B7, reduce E1 to E2, whereas the opposite reaction is catalysed by types 2, 4, 8 and 10 [23].”
BackgroundIjiri, S., Shibata, Y., Takezawa, N., Kazeto, Y., Takatsuka, N., Kato, E., Hagihara, S., Ozaki, Y., Adachi, S., Yamauchi, K., et al. (2016) · Endocrinology · doi:10.1210/en.2016-1349 · Cited by 17
Maltais, R., Trottier, A., Barbeau, X., Lagüe, P., Perreault, M., Thériault, J.-F., Lin, S., & Poirier, D. (2015) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2015.10.020 · Cited by 16
“This enzyme transforms the steroid estrone (E1) into E2, the most potent estrogen in women, but also transforms dehydroepiandrosterone (DHEA) into 5-androstene-3b,17b-diol (5-diol), a less potent estrogen found in large concentration in post-menopausal women [9,10].”
Herman, B. E., Szabó, J., Bacsa, I., Woelfling, J., Schneider, G., Bálint, M., Hetényi, C., Mernyák, E., & Szécsi, M. (2016) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2016.1204610 · Cited by 16
“In this work, we determined the in vitro inhibitory potencies on human placental 17b-HSD1 of the 3-hydroxy and the 3-ether derivatives of 13a- and 13b-estrones (1, 2) and D-secoestrones (3–6) (Figure 1) in the presence of NADPH or NADH.”
BackgroundNyuji, M., Hongo, Y., Kazeto, Y., & Yoneda, M. (2023) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2023.114423 · Cited by 14
Trottier, A., Maltais, R., Ayan, D. P., Barbeau, X., Roy, J., Perreault, M., Poulin, R., Lagüe, P., & Poirier, D. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.08.004 · Cited by 15
Haller, F., Momán, E., Hartmann, R. W., Adamski, J., & Mindnich, R. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.04.002 · Cited by 15
Type 10 17β-hydroxysteroid dehydrogenase expression is regulated by C/EBPβ in HepG2 cells
Rotinen, M., Villar, J., Celay, J., & Encı́o, I. (2010) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.07.003 · Cited by 15
The Adrenal Cortex and Its Disorders
Miller, W. L., Flück, C. E., Breault, D. T., & Feldman, B. J. (2021) · Elsevier eBooks · doi:10.1016/b978-0-323-62520-3.00014-2 · Cited by 14
Formation of Δ1 and Δ6 testosterone metabolites by human hepatocytes
Fabregat, A., Marcos, J., Ventura, R., Casals, G., Jiménez, W., Reichenbach, V., Segura, J., & Pozo, Ó. J. (2014) · Steroids · doi:10.1016/j.steroids.2014.12.006 · Cited by 14
Analogues of Natural Chalcones as Efficient Inhibitors of AKR1C3
Möller, G., Temml, V., Cala, A., Gruet, O., Richomme, P., Séraphin, D., Viault, G., Kraus, L., Huber‐Cantonati, P., Schopfhauser, E., et al. (2022) · Metabolites · doi:10.3390/metabo12020099 · Cited by 16
“HSD17B2 catalyses the oxidation of oestradiol to estrone and testosterone to ∆4-androstene-3,17-dione and has its role in eliminating active steroid hormones [2].”
BackgroundInfluentialNeocleous, V., Sismani, C., Shammas, C., Efstathiou, E., Alexandrou, A., Ioannides, M., Argyrou, M., Patsalis, P. C., Phylactou, L. A., & Skordis, N. (2012) · Gene · doi:10.1016/j.gene.2012.03.031 · Cited by 14
“There are at least 14 known isoenzymes of 17β-HSD that play a role in the final stages of all androgen and oestrogen synthesis (Kowalik et al., 2009; Labrie et al., 1997; Moeller and Adamski, 2009; Wu et al., 2007).”
BackgroundKulmány, Á. E., Herman, B. E., Zupkó, I., Sinreih, M., Rižner, T. L., Savić, M. P., Oklješa, A. M., Nikolić, A. R., Nagy, V., Ocsovszki, I., et al. (2021) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2021.105997 · Cited by 13
Abbas, N. A. T., & Hassan, H. A. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.108801 · Cited by 13
Maltais, R., Trottier, A., Delhomme, A., Barbeau, X., Lagüe, P., & Poirier, D. (2015) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2015.01.059 · Cited by 13
Kraynak, M., Flowers, M. T., Shapiro, R. A., Kapoor, A., Levine, J. E., & Abbott, D. H. (2017) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00058.2017 · Cited by 13
Ribeiro, I. P., Esteves, L., Anjo, S. I., MARQUES, F., Barroso, L., Manadas, B. J., Carreira, I. M., & Melo, J. B. (2020) · Cancer Genomics & Proteomics · doi:10.21873/cgp.20186 · Cited by 13
Hendrickson, R. C., Cicinnati, V. R., Albers, A. E., Dworacki, G., Gambotto, A. A., Pagliano, O., Tüting, T., Mayordomo, J. I., Visús, C., Appella, E., et al. (2009) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-009-0730-7 · Cited by 13
“It has now been determined that Hsd17b isoforms are members of the short chain dehydrogenase/reductase (SDR) superfamily and function in the synthesis of long-chain fatty acids, in particular arachidonic acid, the precursor of steroids and prostaglandins [ 42 , 43].”
BackgroundWang, S., Yang, H., Fu, Y., Teng, X., Wang, C., & Xu, W. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/7982344 · Cited by 19
“This was the fi rst proven enzyme that exhibits dehydrogenase activity with not only 3-hydroxyacyl-CoA derivates of fatty acids but also steroids [124, 125].”
Dileo, E., Saba, F., Parasiliti‐Caprino, M., Rosso, C., & Bugianesi, E. (2025) · Nutrients · doi:10.3390/nu17030477 · Cited by 13
“…particularly in the regulation of the biological effects of steroid hormones, but these enzymes are also involved in the regulation of fatty acid metabolic pathways, affecting several bioactive lipid species (e.g., leukotriene B4), that have been implicated in lipid-mediated inflammation [13].”
Cassetta, A., Krastanova, I. B., Kristan, K., Brunskole, M., Lamba, D., Rižner, T. L., & Stojan, J. (2011) · Biochemical Journal · doi:10.1042/bj20110567 · Cited by 12
Xu, K., Wetzel, M., Hartmann, R. W., & Marchais‐Oberwinkler, S. (2011) · Letters in Drug Design & Discovery · doi:10.2174/157018011795514230 · Cited by 12
Androgen-metabolizing enzymes: A structural perspective
Manenda, M. S., Hamel, J., Masselot--Joubert, L., Picard, M.-È., & Shi, R. (2016) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2016.02.021 · Cited by 11
Wu, C.-H., Yang, J.-G., Chang, Y., Hsu, C., & Kuo, P. (2013) · Taiwanese Journal of Obstetrics and Gynecology · doi:10.1016/j.tjog.2013.10.006 · Cited by 11
Roy, J., Fournier, M.-A., Maltais, R., Kenmogne, L. C., & Poirier, D. (2014) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2013.12.019 · Cited by 12
Substrate multispecificity among 20β-hydroxysteroid dehydrogenase type 2 members
Tokarz, J., Lintelmann, J., Möller, G., & Adamski, J. (2020) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2020.110822 · Cited by 11
Shen, Z., Saloniemi, T., Rönnblad, A., Järvensivu, P., Pakarinen, P., & Poutanen, M. (2009) · Endocrinology · doi:10.1210/en.2009-0670 · Cited by 10
Yang, Q., Li, L., Wang, B., Zhu, L., & Tan, J. (2020) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-020-03473-w · Cited by 10
Yatung, S., & Trivedi, A. K. (2024) · Journal of Neuroendocrinology · doi:10.1111/jne.13478 · Cited by 10
“37 – 39 Later, 17 α hydroxy pregnenolone is converted to 17 β OH-progesterone by Cyp21 and is further converted to cortisol by Cyp11b and to cortisone by Hsd11b2.”
Grimbly, C., Caluseriu, O., Metcalfe, P., Jetha, M. M., & Rosolowsky, E. T. (2016) · International Journal of Pediatric Endocrinology · doi:10.1186/s13633-016-0030-x · Cited by 10
“There are at least 12 isoforms of 17βHSD present in organs including the liver, brain, and skin [6, 7].”
BackgroundCortés‐Benítez, F., Roy, J., Perreault, M., Maltais, R., & Poirier, D. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00624 · Cited by 10
Rotinen, M., Villar, J., & Encı́o, I. (2012) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-012-0155-1 · Cited by 10
Jo, J. L., Hwang, J. H., Kwon, S. G., Park, D. H., Kim, T. W., Kang, D. G., Yu, G. E., Kim, I. S., Ha, J. G., & Kim, C. W. (2016) · Genetics and Molecular Research · doi:10.4238/gmr15048970 · Cited by 10
Yan, X., He, B., Hu, L., Gao, J., Chen, S., & Jiang, G. (2018) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2018.02.165 · Cited by 9
The Effects of Neuroactive Steroids on Myelin in Health and Disease
Kalakh, S., & Mouihate, A. (2024) · Medical Principles and Practice · doi:10.1159/000537794 · Cited by 8
“The enzyme 17 β -hydroxysteroid dehydrogenase (17 β -HSD) mediates the conversion of DHEA into ADIOL [99].”
BackgroundFaber-Hammond, J. J., Samanta, M. P., Whitchurch, E. A., Manning, D. P., Sisneros, J. A., & Coffin, A. B. (2015) · PLoS ONE · doi:10.1371/journal.pone.0142814 · Cited by 9
Tsujimoto, T., Takaichi, M., Kishimoto, M., Noto, H., Yamamoto‐Honda, R., Takahashi, Y., Kajio, H., Noda, M., Endo, H., Gomibuchi, H., et al. (2010) · The American Journal of the Medical Sciences · doi:10.1097/maj.0b013e3181f54e59 · Cited by 9
Bérubé, M., Delagoutte, F., & Poirier, D. (2010) · Molecules · doi:10.3390/molecules15031590 · Cited by 9
“This very important steroidogenic enzyme catalyzes the last step in the biosynthesis of estradiol (E2), the most potent estrogen [2–4].”
BackgroundThériault, J.-F., & Lin, S. (2018) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2018.09.012 · Cited by 9
Recent advances in the development of 17beta-hydroxysteroid dehydrogenase inhibitors
Poirier, D. (2024) · Steroids · doi:10.1016/j.steroids.2024.109529 · Cited by 12
Liu, M., Ding, H., Jin, C., Wang, M., Li, P., Bao, Z., Wáng, B., & Hu, J. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25042180 · Cited by 9
“Although Hsd17b family genes, except for Hsd17b5 , which belongs to the AKR family, are part of the SDR superfamily, their amino acid similarity is relatively low, typically only 15% to 20% in vertebrates [25].”
BackgroundTranscription start sites and epigenetic analysis of the HSD17B10 proximal promoter
Yang, S., Dobkin, C., He, X., & Brown, W. T. (2013) · BMC Biochemistry · doi:10.1186/1471-2091-14-17 · Cited by 8
“So far fourteen different types of hydroxysteroid (17β) dehydrogenases have been identified in mammalian cells [23].”
BackgroundRotinen, M., Villar, J., Celay, J., Serrano-Mendioroz, I., Notario, V., & Encı́o, I. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.03.015 · Cited by 9
“17β-Hydroxysteroid dehydrogenases (HSD17Bs) are the enzymes responsible for reduction or oxidation of sex hormones, fatty acids and bile acids in vivo (Moeller and Adamski 2009).”
BackgroundSynthesis and characterization of targeted 17β-hydroxysteroid dehydrogenase type 7 inhibitors
Sancéau, J., Maltais, R., Zhou, M., Lin, S., & Poirier, D. (2024) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2024.106544 · Cited by 7
HCC in metabolic syndrome: current concepts and future directions
Zampaglione, L., Ferrari, J., Pedica, F., & Goossens, N. (2021) · Hepatoma Research · doi:10.20517/2394-5079.2021.22 · Cited by 7
Mungamuri, S. K., Gupta, Y. K., Rao, P. N., & Ravishankar, B. (2023) · Gene Expression · doi:10.14218/ge.2022.00014 · Cited by 6
Severe Undervirilisation in a 46,XY Case Due to a Novel Mutation in HSD17B3 Gene
Alikaşifoğlu, A., Vurallı, D., Hiort, O., Gonc, N. E., Özön, A., & Kandemir, N. (2015) · Journal of Clinical Research in Pediatric Endocrinology · doi:10.4274/jcrpe.2069 · Cited by 7
“The 17β-HSD3 enzyme family includes at least 14 isoenzymes identified thus far and these isoenzymes contribute to reproductive organ development by playing a role in the final steps of androgen and estrogen syntheses (2).”
BackgroundThe mouse as a model to investigate sex steroid metabolism in the normal and pathological prostate
McNamara, K. M., Handelsman, D. J., & Simanainen, U. (2011) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2011.10.009 · Cited by 7
Crystal structure of human 17beta-HSD type 1 in ternary complex with PBRM and NADP+
Li, T., & Lin, S. X. (2018) · Worldwide Protein Data Bank · doi:10.2210/pdb6cge/pdb · Cited by 7
Three types of 17β-hydroxysteroid dehydrogenases involved in Japanese eel ovarian steroidogenesis
Suzuki, H., Ito, R., Ozaki, Y., & Kazeto, Y. (2025) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2025.114697 · Cited by 6
Felicia, M., & Cavallo, L. (2012) · InTech eBooks · doi:10.5772/27190 · Cited by 6
van Son, M., Agarwal, R., Kent, M., Grove, H., Grindflek, E. H., & Lien, S. (2017) · Animal Genetics · doi:10.1111/age.12615 · Cited by 6
Revathy, V. S. (2018) · Asian Fisheries Science · doi:10.33997/j.afs.2018.31.04.004 · Cited by 6
Wang, C.-T., Li, C., Wu, W., Huang, C., Li, C., Li, W., Chan, T., Liang, P., Hsing, C., & Liao, K. (2016) · Journal of Cancer · doi:10.7150/jca.16777 · Cited by 6
“These processes involve NAD+/NADH or NADP+/NADPH-dependent biological reactions [2].”
BackgroundHerman, B. E., Kiss, A., Woelfling, J., Mernyák, E., Szécsi, M., & Schneider, G. (2019) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2019.1634064 · Cited by 5
“one (15) Compound 11 (435mg, 1mmol) was dissolved in acetone (10ml) and Jones reagent (1ml) was added while cooling with ice.”
MethodSinreih, M., Gjorgoska, M., Möller, G., Adamski, J., & Rižner, T. L. (2023) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2023.04.015 · Cited by 5
Gunawan, A., Listyarini, K., Furqon, A., Jakaria, J., Sumantri, C., Akter, S., & Uddin, M. J. (2019) · Gene Reports · doi:10.1016/j.genrep.2019.100370 · Cited by 5
Çiftçi, N., Kayaş, L., Çamtosun, E., & Akıncı, A. (2020) · Journal of Clinical Research in Pediatric Endocrinology · doi:10.4274/jcrpe.galenos.2020.2020.0249 · Cited by 5
“biologically active form testosterone (T) (1).”
Mitochondrial RNase P Complex in Animals: Mitochondrial tRNA Processing and Links to Disease
Saoji, M. M., & Cox, R. T. (2018) · Nucleic acids and molecular biology · doi:10.1007/978-3-319-78190-7_3 · Cited by 5
Tabęcka-Łonczyńska, A., Koszła, O., & Sołek, P. (2024) · Chemosphere · doi:10.1016/j.chemosphere.2024.142802 · Cited by 4
Giraldo‐Deck, L. M., Loveland, J. L., Goymann, W., Lank, D. B., & Küpper, C. (2024) · Hormones and Behavior · doi:10.1016/j.yhbeh.2024.105645 · Cited by 6
“Conversely, for androstenedione a precursor of testosterone and less potent androgen (Moeller and Adamski, 2009), Satellites and Faeders have higher levels than In-dependents (Küpper et al., 2016; Loveland et al., 2022, Loveland et al., 2021a).”
BackgroundMolecular Marker–Assisted Selective Breeding of Largemouth Bass
Junjie, B., & Li, S. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816473-0.00005-0 · Cited by 4
Poirier, D., Maltais, R., Rousseau, J. A., Roy, J., Phoenix, S., Cortés‐Benítez, F., & Lecomte, R. (2022) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2022.106145 · Cited by 4
Colinas, N., Montero‐Pau, J., Carmona, M. J., Sabatino, R., Cesare, A. D., Eckert, E. M., & García-Roger, E. M. (2023) · Hydrobiologia · doi:10.1007/s10750-023-05316-1 · Cited by 4
“Since edh encodes for 17 -β- dehydrogenase 12 enzyme, which is required to catalyse the interconversion of estrogenic hormones estrone and 17-β -estradiol (Mind-nich et al., 2004; Moeller & Adamski, 2009), the low expression of the gene would be expected to result in a reduced level of estradiol.”
Tabęcka-Łonczyńska, A., Kaczka, P., & Kaleniuk, E. (2023) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2023.106398 · Cited by 4
Ouellet, É., Ayan, D. P., & Poirier, D. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.06.110 · Cited by 4
Nashev, L. G., Atanasov, A. G., Baker, M. E., & Odermatt, A. (2013) · International Journal of Cell Biology · doi:10.1155/2013/769536 · Cited by 4
“Hindawi Publishing Corporation International Journal of Cell Biology Volume 2013, Article ID 769536, 8 pages http://dx.doi.org/10.1155/2013/769536”
BackgroundInfluentialSOME ASPECTS OF STEROID REGULATION IN TELEOSTS
Львович, Р. Н. (2018) · Proceedings of the Karelian Research Centre of the Russian Academy of Sciences · doi:10.17076/eb777 · Cited by 4
Penning, T. M., & Adamski, J. (2011) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2011.04.011 · Cited by 4
The steroid hormone ADIOL promotes learning by reducing neural kynurenic acid levelsPreprint
Lemieux, G. A., Yoo, S., Lin, L., Vohra, M., & Ashrafi, K. (2023) · Genes & Development · doi:10.1101/gad.350745.123 · Cited by 5
Female Adipose Tissue Sex Steroid Biosynthesis
Hetemäki, N., Mikkola, T. S., & Savolainen-Peltonen, H. M. (2025) · Seminars in Reproductive Medicine · doi:10.1055/s-0045-1811952 · Cited by 5
Iibuchi, R., Shimozuru, M., Kamine, A., Nio‐Kobayashi, J., Iwanaga, T., & Tsubota, T. (2010) · Journal of Reproduction and Development · doi:10.1262/jrd.09-188n · Cited by 3
“The 17βHSD family controls the last step in the formation of androgens and estrogens, and at least 14 isoenzymes are known in vertebrates [23].”
BackgroundIdentification of a First Enzymatic Activator of a 17β-Hydroxysteroid Dehydrogenase
Trottier, A., Maltais, R., & Poirier, D. (2014) · ACS Chemical Biology · doi:10.1021/cb500109e · Cited by 3
Giraldo‐Deck, L. M., Loveland, J. L., Goymann, W., Lank, D. B., & Küpper, C. (2022) · doi:10.22541/au.166913241.14402024/v1 · Cited by 3
Tokarz, J., Schmitt, S. M., Möller, G., Brändli, A. W., & Adamski, J. (2021) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2021.105874 · Cited by 2
Boutin, S., Roy, J., Maltais, R., & Poirier, D. (2019) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2019.126783 · Cited by 2
Kolodkina, A. A., Калинченко, Н. Ю., Nizhnik, A. N., Nokel', M. A., & Tiulpakov, A. N. (2011) · Problems of Endocrinology · doi:10.14341/probl201157325-30 · Cited by 2
Farhane, S., Fournier, M.-A., & Poirier, D. (2013) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2013.05.002 · Cited by 2
Heinosalo, T., Saarinen, N., Biehl, A., Rytkönen, K. T., Villa, P., Juhila, J., Koskimies, P., Laiho, A., Hämäläinen, E. K., Kajantie, E., et al. (2024) · Biology of Reproduction · doi:10.1093/biolre/ioae078 · Cited by 1
Identification of Hydroxysteroid Dehydrogenase Type 1 As a Potential Bladder Tumor Marker
Albadawy, A., Alqudaimi, M., Cui, H., Yan, X., Sun, J., & Shi, P. (2024) · ̒Ulūm va funūn-i bastah/bandī · doi:10.61186/ibj.4068 · Cited by 1
“These processes involve biological reactions that rely on either NAD + /NADH or NADP + /NADPH [5] .”
BackgroundRasal, K. D., Davu, S., Asgolkar, P., Shinde, S., Kumar, P. V., Dhere, S., Acharya, A., Kumar, R., Sonwane, A., Brahmane, M. P., et al. (2024) · Gene Reports · doi:10.1016/j.genrep.2024.102018 · Cited by 1
Breakdown and clearance of steroids
Honour, J. W. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-818124-9.00001-2 · Cited by 1
Single cell resolution of neurosteroidogenesis in the murine brain: intermediary biosynthesis
Koganti, P. P., & Selvaraj, V. (2025) · Journal of Endocrinology · doi:10.1530/joe-24-0333 · Cited by 1
Carruba, G. (2012) · Springer eBooks · doi:10.1007/978-1-4471-2864-9_30 · Cited by 1
Nishimoto, M., Toyoshima, M., Shiga, N., Utsunomiya, H., Suzuki, F., Nagase, S., Nishigori, H., Suzuki, T., Sasano, H., Ito, K., et al. (2016) · Open Journal of Endocrine and Metabolic Diseases · doi:10.4236/ojemd.2016.69025 · Cited by 1
“There are two subtypes of 17β-HSD: type 1 catalyzes E1 to E2, and type 2 preferentially catalyzes the oxidation of E2 to E1 [3] [4] [14].”
BackgroundKarkola, S. (2009) · Työväentutkimus Vuosikirja · Cited by 1
Molecular profiling of human endometrium and endometriosis
Huhtinen, K. (2010) · UTUPub (University of Turku) · Cited by 1
Todenhöfer, T., Schwentner, C., & Stenzl, A. (2012) · European Urology · doi:10.1016/j.eururo.2011.12.052 · Cited by 1
“Variants of these enzymes have been linked to a broad spectrum of diseases, including sexual disorders, breast cancer, and polycystic kidney disease, and have been shown to correlate with sex hormone levels [6].”
BackgroundWetzel, M. (2011) · Publications of the UdS (Saarland University) · doi:10.22028/d291-22814
Metadata
- Authors
- Moeller, G., & Adamski, J.
- Affiliations
- Helmholtz Munich (DE)
- ORCID
- Adamski, Jerzy
- Venue
- Molecular and Cellular Endocrinology
- Publisher
- Elsevier BV
- Published
- 2009-03
- Volume
- 301
- Issue
- 1-2
- Pages
- 7-19
- ISSN
- 0303-7207 (ISSN-L)
- OpenAlex
- W2048714965
- Cited by
- 214
- References
- 176
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 12 · 2023: 8 · 2022: 6 · 2021: 8 · 2020: 11 · 2019: 8 · 2018: 17 · 2017: 12 · 2016: 14 · 2015: 12 · 2014: 11 · 2013: 16 · 2012: 11
- FWCI
- 1.52
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Molecular and Cellular Endocrinology (publishedVersion)
- PubMed (publishedVersion)
- Site cant be reached (submittedVersion)
- Topics
- Physical Sciences › Chemistry › Organic Chemistry › Steroid Chemistry and Biochemistry
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adrenal Hormones and Disorders
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Hormonal Regulation and Hypertension
- Keywords
- 17β-hydroxysteroid dehydrogenase, steroid metabolism, steroid hormone regulation, metabolomics, endogenous substrates, genetic susceptibility, disease
- MeSH terms
- Animals, Disease, Humans, Polymorphism, Genetic, 17-Hydroxysteroid Dehydrogenases, Crystallography, X-Ray, Models, Animal
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