AKR1C3 (type 5 17β-hydroxysteroid dehydrogenase/prostaglandin F synthase): Roles in malignancy and endocrine disorders

Penning, Trevor M.

doi:10.1016/j.mce.2018.07.002

Cited by 120Aldose Reductase and TaurineProstate Cancer Treatment and ResearchEstrogen and related hormone effects

AKR1C3 (type 5 17β-hydroxysteroid dehydrogenase/prostaglandin F synthase): Roles in malignancy and endocrine disorders

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Penning, Trevor M.·2019·Molecular and Cellular Endocrinology

DOI 10.1016/j.mce.2018.07.002PMC PMC6422768

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Abstract

Aldo-Keto-Reductase 1C3 (type 5 17β-hydroxysteroid dehydrogenase (HSD)/prostaglandin (PG) F 2α synthase) is the only 17β-HSD that is not a short-chain dehydrogenase/reductase. By acting as a 17-ketosteroid reductase, AKR1C3 produces potent androgens in peripheral tissues which activate the androgen receptor (AR) or act as substrates for aromatase. AKR1C3 is implicated in the production of androgens in castration-resistant prostate cancer (CRPC) and polycystic ovarian syndrome; and is implicated in the production of aromatase substrates in breast cancer. By acting as an 11-ketoprostaglandin reductase, AKR1C3 generates 11β-PGF 2α to activate the FP receptor and deprives peroxisome proliferator activator receptorγ of its putative PGJ 2 ligands. These growth stimulatory signals implicate AKR1C3 in non-hormonal dependent malignancies e.g. acute myeloid leukemia (AML). AKR1C3 moonlights by acting as a co-activator of the AR and stabilizes ubiquitin ligases. AKR1C3 inhibitors have been used clinically for CRPC and AML and can be used to probe its pluripotency.

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Other prostaglandin synthases in the same family as PTGES3 have been implicated in the production of androgens.
“other prostaglandin synthases in the same family as PTGES3 have been implicated in the production of androgens48,49.”
From Genome-scale CRISPR screens identify PTGES3 as a direct modulator of androgen receptor function in advanced prostate cancer (2025) · cites this paper as [48]
The Prostaglandin biosynthesis section identifies AKR1C3 as a prostaglandin F synthase, and the Steroid biosynthesis section says it converts androgen precursors to testosterone and dihydrotestosterone. The paper does not identify AKR1C3 as being in the same family as PTGES3, so that part of the claim is unsupported. (LLM, conf=0.85)
Experimental — accuracy not yet measured
PTGES3 protein is reported to have several protein functions and to be localized to both the cytosol and nucleus.
“PTGES3 protein is reported to have several protein functions and to be localized to both the cytosol and nucleus41–49 (Fig. 3f).”
From Genome-scale CRISPR screens identify PTGES3 as a direct modulator of androgen receptor function in advanced prostate cancer (2025) · cites this paper as [48]
The Introduction and Prostaglandin biosynthesis sections describe functions of AKR1C3, not PTGES3. Searches for PTGES3 and its alternative names found no passage in our copy addressing its functions or localization in the cytosol and nucleus. Page numbers were not available in the indexed passages. (LLM, conf=0.76)
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Abiraterone and Increased Survival in Metastatic Prostate Cancer
de Bono, J. S., Logothetis, C. J., Molina, A., Fizazi, K., North, S., Chu, L., Chi, K. N., Jones, R. J., Goodman, O. B., Saad, F., et al. (2011) · New England Journal of Medicine · doi:10.1056/nejmoa1014618 · Cited by 4,407 · see citing works
A prostaglandin J2 metabolite binds peroxisome proliferator-activated receptor γ and promotes adipocyte differentiation
Kliewer, S. A., Lenhard, J. M., Willson, T. M., Patel, I., Morris, D. C., & Lehmann, J. M. (1995) · Cell · doi:10.1016/0092-8674(95)90194-9 · Cited by 2,028 · see citing works
9-cis retinoic acid is a high affinity ligand for the retinoid X receptor
Heyman, R. A., Mangelsdorf, D. J., Dyck, J. A., Stein, R. B., Eichele, G., Evans, R. M., & Thaller, C. (1992) · Cell · doi:10.1016/0092-8674(92)90479-v · Cited by 1,780 · cited 7× · see citing works
“As 9-cis-retinoic acid is the major ligand for RXR (Heyman et al., 1992; Levin et al., 1992), the conversion of 9cis-retinal to 9-cis-retinol mediated by AKR1B15 would deprive RXR of its 9-cis-retinoic acid ligand.”
BackgroundInfluential
9-Cis retinoic acid stereoisomer binds and activates the nuclear receptor RXRα
Levin, A. A., Sturzenbecker, L. J., Kazmer, S., Bosakowski, T., Huselton, C. A., Allenby, G., Speck, J., ratzeisen, C., Rosenberger, M., Lovey, A. J., et al. (1992) · Nature · doi:10.1038/355359a0 · Cited by 1,221 · see citing works
Increased Expression of Genes Converting Adrenal Androgens to Testosterone in Androgen-Independent Prostate Cancer
Stanbrough, M., Bubley, G. J., Ross, K., Golub, T. R., Rubin, M. A., Penning, T. M., Febbo, P. G., & Balk, S. P. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4000 · Cited by 1,082 · see citing works
Self-citation
Antitumour activity of MDV3100 in castration-resistant prostate cancer: a phase 1–2 study
Scher, H. I., Beer, T. M., Higano, C. S., Anand, A., Taplin, M., Efstathiou, E., Rathkopf, D. E., Shelkey, J., Yu, E. Y., Alumkal, J. J., et al. (2010) · The Lancet · doi:10.1016/s0140-6736(10)60172-9 · Cited by 1,063 · see citing works
Phase I Clinical Trial of a Selective Inhibitor of CYP17, Abiraterone Acetate, Confirms That Castration-Resistant Prostate Cancer Commonly Remains Hormone Driven
Attard, G., Reid, A. H. M., Yap, T. A., Raynaud, F., Dowsett, M., Settatree, S., Barrett, M., Parker, C., Martins, V., Folkerd, E., et al. (2008) · Journal of Clinical Oncology · doi:10.1200/jco.2007.15.9749 · Cited by 903 · see citing works
Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease
Tebay, L. E., Robertson, H., Durant, S. T., Vitale, S. R., Penning, T. M., Dinkova-Kostova, A. T., & Hayes, J. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.021 · Cited by 837 · see citing works
Self-citation
Human 3α-hydroxysteroid dehydrogenase isoforms (AKR1C1–AKR1C4) of the aldo–keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones
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:10.1042/0264-6021:3510067 · Cited by 649 · see citing works
Self-citation
Human 3α-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones
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 · see citing works
Self-citation
Comparative anatomy of the aldo–keto reductase superfamily
Jez, J. M., BENNETT, M. J., Schlegel, B. P., Lewis, M., & Penning, T. M. (1997) · Biochemical Journal · doi:10.1042/bj3260625 · Cited by 603 · see citing works
Self-citation
Phase II Multicenter Study of Abiraterone Acetate Plus Prednisone Therapy in Patients With Docetaxel-Treated Castration-Resistant Prostate Cancer
Danila, D. C., Morris, M. J., de Bono, J. S., Ryan, C. J., Denmeade, S. R., Smith, M. R., Taplin, M.-E., Bubley, G. J., Kheoh, T., Haqq, C., et al. (2010) · Journal of Clinical Oncology · doi:10.1200/jco.2009.25.9259 · Cited by 410 · see citing works
Interaction of the peroxisome-proliferator-activated receptor and retinoid X receptor.
Gearing, K. L., Göttlicher, M., Teboul, M., Widmark, E., & Gustafsson, J.-Α. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.4.1440 · Cited by 395 · see citing works
Aldo-Keto Reductases and Bioactivation/Detoxication
Jin, Y., & Penning, T. M. (2006) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105337 · Cited by 386 · see citing works
Self-citation
The backdoor pathway to dihydrotestosterone
Auchus, R. J. (2004) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2004.09.004 · Cited by 347 · see citing works
Dihydrotestosterone synthesis bypasses testosterone to drive castration-resistant prostate cancer
Chang, K.-H., Li, R., Papari-Zareei, M., Watumull, L., Zhao, Y. D., Auchus, R. J., & Sharifi, N. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107898108 · Cited by 346 · see citing works
Biosynthesis of 15-deoxy-Δ12,14-PGJ2 and the ligation of PPARγ
Bell, L. C., Ide, T., Lawson, J. A., McNamara, P., Reilly, M. P., & FitzGerald, G. A. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18012 · Cited by 341 · see citing works
Aberrant Expression of the Transcription Factors Snail and Slug Alters the Response to Genotoxic Stress
Kajita, M., McClinic, K. N., & Wade, P. A. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.17.7559-7566.2004 · Cited by 334 · see citing works
Biosynthesis of 15-deoxy-Δ12,14-PGJ2 and the ligation of PPARγ
Bell-Parikh, L. C., Ide, T., Lawson, J. A., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200318012 · Cited by 302 · see citing works
Prostaglandins Promote and Block Adipogenesis through Opposing Effects on Peroxisome Proliferator-activated Receptor γ
Reginato, M. J., Krakow, S. L., Bailey, S. T., & Lazar, M. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.4.1855 · Cited by 279 · see citing works
Epigenetic regulation of Keap1-Nrf2 signaling
Guo, Y., Yu, S., Zhang, C., & Kong, A. T. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.013 · Cited by 261 · see citing works
Intracrine Androgens and AKR1C3 Activation Confer Resistance to Enzalutamide in Prostate Cancer
Liu, C., Lou, W., Zhu, Y., Yang, J. C., Nadiminty, N., Gaikwad, N. W., Evans, C. P., & Gao, A. C. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-3080 · Cited by 245 · see citing works
α,β-Unsaturated Ketone Is a Core Moiety of Natural Ligands for Covalent Binding to Peroxisome Proliferator-activated Receptor γ
Shiraki, T., Kamiya, N., Shiki, S., Kodama, T. S., Kakizuka, A., & Jingami, H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500901200 · Cited by 218 · see citing works
17β-Hydroxysteroid dehydrogenases (17β-HSDs) as therapeutic targets: Protein structures, functions, and recent progress in inhibitor development
Marchais-Oberwinkler, S., Henn, C., Möller, G., Klein, T., Negri, M., Oster, A., Spadaro, A., Werth, R., Wetzel, M., Xu, K., et al. (2011) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.12.013 · Cited by 216 · see citing works
AKR1C3-mediated adipose androgen generation drives lipotoxicity in women with polycystic ovary syndrome
O’Reilly, M. W., Kempegowda, P., Walsh, M., Taylor, A. E., Manolopoulos, K. N., Allwood, J. W., Semple, R. K., Hebenstreit, D., Dunn, W. B., Tomlinson, J. W., et al. (2017) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2017-00947 · Cited by 215 · see citing works
Distinct Patterns of Dysregulated Expression of Enzymes Involved in Androgen Synthesis and Metabolism in Metastatic Prostate Cancer Tumors
Mitsiades, N., Sung, C. C., Schultz, N. D., Danila, D. C., He, B., Eedunuri, V. K., Fleisher, M., Sander, C., Sawyers, C. L., & Scher, H. I. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-1335 · Cited by 196 · see citing works
Expression and Characterization of Recombinant Type 2 3α-Hydroxysteroid Dehydrogenase (HSD) from Human Prostate: Demonstration of Bifunctional 3α/17β-HSD Activity and Cellular Distribution
Lin, H.-K., Jez, J. M., Schlegel, B. P., Peehl, D. M., Pachter, J. A., & Penning, T. M. (1997) · Molecular Endocrinology · doi:10.1210/mend.11.13.0026 · Cited by 194 · cited 6× · see citing works
“Examination of these data showed that AKR1C1 preferentially functions as a 20- ketosteroid reductase inactivating progesterone; AKR1C2 preferentially functions as a 3- ketosteroid reductase inactivating dihydrotestosterone (DHT) and AKR1C3 preferentially functions as a 17-ketosteroid reductase converting: 4-androstene…”
BackgroundInfluentialSelf-citation
Evidence of limited contributions for intratumoral steroidogenesis in prostate cancer
Hofland, J., van Weerden, W. M., Dits, N. F. J., Steenbergen, J., van Leenders, G. J. L. H., Jenster, G., Schröder, F. H., & de Jong, F. H. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-2092 · Cited by 176 · see citing works
Identification of a Principal mRNA Species for Human 3 -Hydroxysteroid Dehydrogenase Isoform (AKR1C3) That Exhibits High Prostaglandin D2 11-Ketoreductase Activity
Matsuura, K., Shiraishi, H., Hara, A., Sato, K., Deyashiki, Y., Ninomiya, M., & Sakai, S. (1998) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a022211 · Cited by 172 · see citing works
Human aldose reductase and human small intestine aldose reductase are efficient retinal reductases: consequences for retinoid metabolism
Crosas, B., Hyndman, D., Gallego, O., Martras, S., Parés, X., Flynn, T. G., & Farrés, J. (2003) · Biochemical Journal · doi:10.1042/bj20021818 · Cited by 163 · see citing works
The aldo-keto reductase AKR1C3 is a novel suppressor of cell differentiation that provides a plausible target for the non-cyclooxygenase-dependent antineoplastic actions of nonsteroidal anti-inflammatory drugs.
Desmond, J. C., Mountford, J. C., Drayson, M. T., Walker, E. A., Hewison, M., Ride, J. P., Luong, Q. T., Hayden, R. E., Vanin, E. F., & Bunce, C. M. (2003) · PubMed · Cited by 150 · see citing works
An indomethacin analogue, N-(4-chlorobenzoyl)-melatonin, is a selective inhibitor of aldo-keto reductase 1C3 (type 2 3α-HSD, type 5 17β-HSD, and prostaglandin F synthase), a potential target for the treatment of hormone dependent and hormone independent malignancies
Byrns, M. C., Steckelbroeck, S., & Penning, T. M. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.09.008 · Cited by 145 · see citing works
Self-citation
Inhibitors of type 5 17β-hydroxysteroid dehydrogenase (AKR1C3): Overview and structural insights
Byrns, M. C., Jin, Y., & Penning, T. M. (2010) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.11.004 · Cited by 144 · see citing works
Self-citation
Mutagenesis of 3α-Hydroxysteroid Dehydrogenase Reveals a “Push−Pull” Mechanism for Proton Transfer in Aldo−Keto Reductases
Schlegel, B. P., Jez, J. M., & Penning, T. M. (1998) · Biochemistry · doi:10.1021/bi9723055 · Cited by 139 · see citing works
Self-citation
MAPK- Kinases as Nucleo-Cytoplasmic Shuttles for PPARγ
Burgermeister, E., & Seger, R. (2007) · Cell Cycle · doi:10.4161/cc.6.13.4453 · Cited by 138 · see citing works
Expression and Characterization of Four Recombinant Human Dihydrodiol Dehydrogenase Isoforms: Oxidation of trans-7,8-Dihydroxy-7,8-dihydrobenzo[a]pyrene to the Activated o-Quinone Metabolite Benzo[a]pyrene-7,8-dione,
Burczynski, M. E., Harvey, R. G., & Penning, T. M. (1998) · Biochemistry · doi:10.1021/bi972725u · Cited by 134 · see citing works
Self-citation
Human type 3 3α-hydroxysteroid dehydrogenase (aldo-keto reductase 1C2) and androgen metabolism in prostate cells
Rižner, T. L., Lin, H. K., Peehl, D. M., Steckelbroeck, S., Bauman, D. R., & Penning, T. M. (2003) · Endocrinology · doi:10.1210/en.2002-0032 · Cited by 132 · see citing works
Self-citation
cDNA cloning, expression and characterization of human prostaglandin F synthase1
Suzuki-Yamamoto, T., Nishizawa, M., Fukui, M., Okuda‐Ashitaka, E., Nakajima, T., Ito, S., & Watanabe, K. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01551-3 · Cited by 131 · see citing works
Comparative functional analysis of human medium-chain dehydrogenases, short-chain dehydrogenases/reductases and aldo-keto reductases with retinoids.
Gallego, O., Belyaeva, O., Porté, S., Ruiz, F., Stetsenko, A., Shabrova, E., Kostereva, N., Farrés, J., Parés, X., & Kedishvili, N. (2006) · Biochemical Journal · doi:10.1042/bj20051988 · Cited by 130 · see citing works
Type 5 17β-hydroxysteroid dehydrogenase (AKR1C3) contributes to testosterone production in the adrenal reticularis
Nakamura, Y., Hornsby, P. J., Casson, P., Morimoto, R., Satoh, F., Xing, Y., Kennedy, M. R., Sasano, H., & Rainey, W. E. (2009) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2008-2374 · Cited by 129 · see citing works
Increased expression of type 2 3α-hydroxysteroid dehydrogenase/type 5 17β-hydroxysteroid dehydrogenase (AKR1C3) and its relationship with androgen receptor in prostate carcinoma
Fung, K.-M., Samara, E. N. S., Wong, C., Metwalli, A., Krlin, R., Bane, B., Liu, C. Z., Yang, J. T., Pitha, J. V., Culkin, D. J., et al. (2006) · Endocrine Related Cancer · doi:10.1677/erc.1.01048 · Cited by 129 · see citing works
Self-citation
Inhibition of AKR1C3 Activation Overcomes Resistance to Abiraterone in Advanced Prostate Cancer
Liu, C., Armstrong, C. M., Lou, W., Lombard, A. P., Evans, C. P., & Gao, A. C. (2016) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-16-0186 · Cited by 124 · see citing works
Steroidogenic Enzyme AKR1C3 Is a Novel Androgen Receptor-Selective Coactivator that Promotes Prostate Cancer Growth
Yepuru, M., Wu, Z., Kulkarni, A. L., Yin, F., Barrett, C. M., Kim, J.-H., Steiner, M. S., Miller, D. D., Dalton, J. T., & Narayanan, R. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-1151 · Cited by 122 · see citing works
Drug resistant MCF-7 cells exhibit epithelial-mesenchymal transition gene expression pattern
İşeri, Ö. D., Kars, M. D., Arpacı, F., Atalay, C., Pak, I., & Gündüz, U. (2010) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2010.10.004 · Cited by 121 · see citing works
Aldo–keto reductase 1C3 expression in MCF-7 cells reveals roles in steroid hormone and prostaglandin metabolism that may explain its over-expression in breast cancer
Byrns, M. C., Duan, L., Lee, S. H., Blair, I. A., & Penning, T. M. (2010) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2009.12.009 · Cited by 116 · see citing works
Self-citation
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
Lin, H., Steckelbroeck, S., Fung, K.-M. A., Jones, A. N., & Penning, T. M. (2004) · Steroids · doi:10.1016/j.steroids.2004.09.014 · Cited by 111 · see citing works
Self-citation
Crystal Structure of Human Prostaglandin F Synthase (AKR1C3),
Komoto, J., Yamada, T., Watanabe, K., & Takusagawa, F. (2004) · Biochemistry · doi:10.1021/bi036046x · Cited by 109 · see citing works
The human short-chain dehydrogenase/reductase (SDR) superfamily: A bioinformatics summary
Bray, J. E., Marsden, B. D., & Oppermann, U. C. T. (2008) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2008.10.058 · Cited by 107 · see citing works
Development of Potent and Selective Indomethacin Analogues for the Inhibition of AKR1C3 (Type 5 17β-Hydroxysteroid Dehydrogenase/Prostaglandin F Synthase) in Castrate-Resistant Prostate Cancer
Liedtke, A. J., Adeniji, A. O., Chen, M., Byrns, M. C., Jin, Y., Christianson, D. W., Marnett, L. J., & Penning, T. M. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm3017656 · Cited by 106 · see citing works
Self-citation
Aldo-Keto Reductase (AKR) 1C3 inhibitors: a patent review
Penning, T. M. (2017) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2017.1379503 · Cited by 96 · see citing works
Self-citation
Expression, Localization, and Signaling of Prostaglandin F2αReceptor in Human Endometrial Adenocarcinoma: Regulation of Proliferation by Activation of the Epidermal Growth Factor Receptor and Mitogen-Activated Protein Kinase Signaling Pathways
Sales, K. J., Milne, S. A., Williams, A. R. W., Anderson, R. A., & Jabbour, H. N. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2003-031434 · Cited by 91 · see citing works
Aldo-keto Reductase Family 1 Member C3 (AKR1C3) Is a Biomarker and Therapeutic Target for Castration-Resistant Prostate Cancer
Hamid, A. R. A. H., Pfeiffer, M. J., Verhaegh, G. W. C. T., Schaafsma, E., Brandt, A. M., Sweep, F. C. G. J., Sedelaar, J. P. M., & Schalken, J. A. (2012) · Molecular Medicine · doi:10.2119/molmed.2012.00296 · Cited by 87 · see citing works
Lack of functional and expression homology between human and mouse aldo-keto reductase 1C enzymes: implications for modelling human cancers
Veliça, P., Davies, N., Rocha, P. P., Schrewe, H., Ride, J. P., & Bunce, C. M. (2009) · Molecular Cancer · doi:10.1186/1476-4598-8-121 · Cited by 80 · see citing works
Crystal Structures of the Multispecific 17β-Hydroxysteroid Dehydrogenase Type 5: Critical Androgen Regulation in Human Peripheral Tissues
Qiu, W., Zhou, M., Labrie, F., & Lin, S. (2004) · Molecular Endocrinology · doi:10.1210/me.2004-0032 · Cited by 76 · see citing works
Combined Bezafibrate and Medroxyprogesterone Acetate: Potential Novel Therapy for Acute Myeloid Leukaemia
Khanim, F. L., Hayden, R. E., Birtwistle, J., Lodi, A., Tiziani, S., Davies, N., Ride, J. P., Viant, M. R., Günther, U. L., Mountford, J. C., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0008147 · Cited by 74 · see citing works
17β-Hydroxysteroid Dehydrogenase 14 Affects Estradiol Levels in Breast Cancer Cells and Is a Prognostic Marker in Estrogen Receptor–Positive Breast Cancer
Jansson, A., Gunnarsson, C., Cohen, M., Sivik, T., & Stål, O. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-1448 · Cited by 73 · see citing works
ERG/AKR1C3/AR Constitutes a Feed-Forward Loop for AR Signaling in Prostate Cancer Cells
Powell, K., Semaan, L., Conley‐LaComb, M. K., Asangani, I. A., Wu, Y.-M., Ginsburg, K., Williams, J. L., Squire, J. A., Maddipati, K. R., Cher, M. L., et al. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-2352 · Cited by 70 · see citing works
Safety, tolerability and anti-tumour activity of the androgen biosynthesis inhibitor ASP9521 in patients with metastatic castration-resistant prostate cancer: multi-centre phase I/II study
Loriot, Y., Fizazi, K. S., Jones, R. J., den Brande, J. V., Molife, R., Omlin, A. G., James, N. D., Baskin-Bey, E. S., Heeringa, M. J., Baron, B., et al. (2014) · Investigational New Drugs · doi:10.1007/s10637-014-0101-x · Cited by 65 · see citing works
Crystal structures of AKR1C3 containing an N-(aryl)amino-benzoate inhibitor and a bifunctional AKR1C3 inhibitor and androgen receptor antagonist. Therapeutic leads for castrate resistant prostate cancer
Chen, M., Adeniji, A. O., Twenter, B. M., Winkler, J. D., Christianson, D. W., & Penning, T. M. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.03.085 · Cited by 65 · see citing works
Self-citation
In vitro and in vivo characterisation of ASP9521: a novel, selective, orally bioavailable inhibitor of 17β-hydroxysteroid dehydrogenase type 5 (17βHSD5; AKR1C3)
Kikuchi, A., Furutani, T., Azami, H., Watanabe, K., Niimi, T., Kamiyama, Y., Kuromitsu, S., Baskin-Bey, E. S., Heeringa, M. J., Ouatas, T., et al. (2014) · Investigational New Drugs · doi:10.1007/s10637-014-0130-5 · Cited by 63 · see citing works
Castration Induces Up-Regulation of Intratumoral Androgen Biosynthesis and Androgen Receptor Expression in an Orthotopic VCaP Human Prostate Cancer Xenograft Model
Knuuttila, M., Yatkin, E., Kallio, J., Savolainen, S., Laajala, T. D., Aittokallio, T. A., Oksala, R., Häkkinen, M. R., Keski‐Rahkonen, P., Auriola, S. O. K., et al. (2014) · American Journal Of Pathology · doi:10.1016/j.ajpath.2014.04.010 · Cited by 62 · see citing works
Effect of insulin on AKR1C3 expression in female adipose tissue: in-vivo and in-vitro study of adipose androgen generation in polycystic ovary syndrome
O’Reilly, M., Gathercole, L., Capper, F., Arlt, W., & Tomlinson, J. (2015) · The Lancet · doi:10.1016/s0140-6736(15)60331-2 · Cited by 62 · see citing works
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Yi, J., Nguyen, M. M., Wang, D., Pascal, L. E., Guo, W., Xu, Y., Ai, J., Fm, D., Masoodi, K. Z., Yu, X., et al. (2017) · Oncogene · doi:10.1038/onc.2017.371 · Cited by 61 · see citing works
Multiple steps determine the overall rate of the reduction of 5α-dihydrotestosterone catalyzed by human type 3 3α-hydroxysteroid dehydrogenase: implications for the elimination of androgens
Jin, Y., & Penning, T. M. (2006) · Biochemistry · doi:10.1021/bi060591r · Cited by 60 · see citing works
Self-citation
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Byrns, M. C., Mindnich, R., Duan, L., & Penning, T. M. (2012) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2011.12.012 · Cited by 60 · see citing works
Self-citation
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Cooper, W. C., Jin, Y., & Penning, T. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703414200 · Cited by 58 · see citing works
Self-citation
Deoxycorticosterone inactivation by AKR1C3 in human mineralocorticoid target tissues
Sharma, K. K., Lindqvist, A., Zhou, X. J., Auchus, R. J., Penning, T. M., & Andersson, S. (2006) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2005.10.024 · Cited by 57 · see citing works
Self-citation
Positional conservation and amino acids shape the correct diagnosis and population frequencies of benign and damaging personal amino acid mutationsPreprint
Kumar, S., Suleski, M., Markov, G. J., Lawrence, S., Marco, A. D., & Filipski, A. J. (2009) · Genome Research · doi:10.1101/gr.091991.109 · Cited by 56 · see citing works
The molecular biology of androgenic 17β-hydroxysteroid dehydrogenases
Andersson, S., Geissler, W. M., Patel, S., & Wu, L. (1995) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/0960-0760(95)00039-3 · Cited by 54 · see citing works
AKR1C3 overexpression may serve as a promising biomarker for prostate cancer progression
Tian, Y., Zhao, L., Zhang, H., Liu, X., Zhao, L., Zhao, X., Li, Y., & Li, J. (2014) · Diagnostic Pathology · doi:10.1186/1746-1596-9-42 · Cited by 54 · see citing works
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Komoto, J., Yamada, T., Watanabe, K., Woodward, D. F., & Takusagawa, F. (2006) · Biochemistry · doi:10.1021/bi051861t · Cited by 53 · see citing works
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Kim, S., Yao, J., Suyama, K., Qian, X., Qian, B., Bandyopadhyay, S., Loudig, O. D., Leon-Rodriguez, C. D., Zhou, Z. N., Segall, J. E., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-2591 · Cited by 51 · see citing works
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Kim, H., Kim, J., Meng, Z., Wang, L. H., Liu, F., Conrads, T. P., Burke, T. R., Veenstra, T. D., & Farrar, W. L. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3043 · Cited by 50 · see citing works
Human Estrogenic 17β-Hydroxysteroid Dehydrogenase: Predominance of Estrone Reduction and Its Induction by NADPH
Jin, J.-Z., & Lin, S. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0704 · Cited by 50 · see citing works
Canonical Androstenedione Reduction Is the Predominant Source of Signaling Androgens in Hormone-Refractory Prostate Cancer
Fankhauser, M., Tan, Y., Macintyre, G., Haviv, I., Hong, M. K. H., Nguyen, A., Pedersen, J. S., Costello, A. J., Hovens, C. M., & Corcoran, N. M. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-3483 · Cited by 48 · see citing works
The endometrial cancer cell lines Ishikawa and HEC-1A, and the control cell line HIEEC, differ in expression of estrogen biosynthetic and metabolic genes, and in androstenedione and estrone-sulfate metabolism
Hevir, N., & Rižner, T. L. (2014) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2014.11.015 · Cited by 47 · see citing works
In situ production of sex steroids in human breast carcinoma
Suzuki, T., Miki, Y., Moriya, T., Akahira, J., Hirakawa, H., Ohuchi, N., & Sasano, H. (2007) · Medical Molecular Morphology · doi:10.1007/s00795-007-0365-8 · Cited by 43 · see citing works
Altered expression of genes involved in progesterone biosynthesis, metabolism and action in endometrial cancer
Sinreih, M., Hevir, N., & Rižner, T. L. (2012) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2012.11.012 · Cited by 38 · see citing works
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Sinreih, M., Anko, M., Hevir, N., Kocbek, V., & Rižner, T. L. (2014) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2014.11.009 · Cited by 37 · see citing works
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Penning, T. M., Chen, M., & Jin, Y. (2014) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2014.12.003 · Cited by 34 · see citing works
Self-citation
Prostaglandin 15d-PGJ2 Inhibits Androgen Receptor Signaling in Prostate Cancer Cells
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Expression of the 17β-hydroxysteroid dehydrogenase type 5 mRNA in the human brain
Steckelbroeck, S., Watzka, M., Stoffel‐Wagner, B., Hans, V., Redel, L., Clusmann, H., Elger, C. E., BIDLINGMAIER, F., & Klingmüller, D. (2001) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(00)00432-9 · Cited by 33 · see citing works
Molecular Markers in Sex Hormone Pathway Genes Associated with the Efficacy of Androgen-Deprivation Therapy for Prostate Cancer
Yu, C.-C., Huang, S.-P., Lee, Y.-C., Huang, C., Liu, C.-C., Hour, T., Huang, C.-N., You, B.-J., Chang, T.-Y., Huang, C.-H., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054627 · Cited by 31 · see citing works
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Platt, A., Xia, Z., Liu, Y., Chen, G., & Lazarus, P. J. (2016) · Pharmacogenetics and Genomics · doi:10.1097/fpc.0000000000000226 · Cited by 31 · see citing works
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Karunasinghe, N., Zhu, Y., Han, D. Y., Lange, K., Zhu, S., Wang, A., Ellett, S., Masters, J., Goudie, M., Keogh, J., et al. (2016) · BMC Urology · doi:10.1186/s12894-016-0164-4 · Cited by 30 · see citing works
Substrate Specificity, Inhibitor Selectivity and Structure-Function Relationships of Aldo-Keto Reductase 1B15: A Novel Human Retinaldehyde Reductase
Giménez-Dejoz, J., Kolář, M. H., Ruiz, F. X., Crespo, I., Cousido-Siah, A., PODJARNY, A. D., Barski, O. A., Fanfrlík, J., Parés, X., Farrés, J., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0134506 · Cited by 29 · see citing works
Association analysis between the polymorphisms of HSD17B5 and HSD17B6 and risk of polycystic ovary syndrome in Chinese population
Ju, R., Wu, W., Fei, J., Qin, Y., Tang, Q., Wu, D., Xia, Y., Wu, J., & Wang, X. (2014) · European Journal of Endocrinology · doi:10.1530/eje-14-0615 · Cited by 27 · see citing works
Structure and activity of the murine type 5 17β-hydroxysteroid dehydrogenase gene
Rheault, P., Charbonneau, A., & Luu-The, V. (1999) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(99)00106-2 · Cited by 25 · see citing works
Genome-Wide Analysis of Human Disease Alleles Reveals That Their Locations Are Correlated in Paralogous Proteins
Yandell, M. D., Moore, B., Salas, F., Mungall, C., MacBride, A. R., White, C., & Reese, M. G. (2008) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000218 · Cited by 25 · see citing works
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Söderhäll, C., Körberg, I. B., Thai, H. T. T., Cao, J., Chen, Y., Zhang, X., Zu, S., van der Zanden, L. F. M., van Rooij, I. A. L. M., Frisén, L., et al. (2014) · European Journal of Human Genetics · doi:10.1038/ejhg.2014.129 · Cited by 22 · see citing works
Knockdown of AKR1C3 exposes a potential epigenetic susceptibility in prostate cancer cells
Doig, C. L., Battaglia, S., Khanim, F. L., Bunce, C. M., & Campbell, M. J. (2015) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2015.09.037 · Cited by 21 · see citing works
15-Deoxy-Δ12,14-prostaglandin J2 induces growth inhibition, cell cycle arrest and apoptosis in human endometrial cancer cell lines
Li, H., & Narahara, H. (2013) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2013.1268 · Cited by 13 · see citing works
Progestin effects on expression of AKR1C1–AKR1C3, SRD5A1 and PGR in the Z-12 endometriotic epithelial cell line
Beranič, N., & Rižner, T. L. (2012) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2012.10.028 · Cited by 12 · see citing works
Positive biopsy (bx) rates for prostate cancer (PCA) based on prostate specific antigen (PSA) grouping in a large cancer screening trial: Prostate, Lung, Colorectal, and Ovarian Cancer Screening Trial (PLCO).
Reding, D. J., McCarty, C. A., Riley, T. L., Hickey, T., & Hocking, W. G. (2010) · Journal of Clinical Oncology · doi:10.1200/jco.2010.28.15_suppl.4563 · Cited by 9 · see citing works
Generation of human endometrial knockout cell lines with the CRISPR/Cas9 system confirms the prostaglandin F2 synthase activity of aldo-ketoreductase 1B1
Lacroix‐Pepin, N., Chapdelaine, P., Rodriguez, Y., Tremblay, J. P., & Fortier, M. A. (2014) · Molecular Human Reproduction · doi:10.1093/molehr/gau023 · Cited by 9 · see citing works
Functional Significance May Underlie the Taxonomic Utility of Single Amino Acid Substitutions in Conserved Proteins
Tyler, K. M., Wagner, G. K., Wu, Q., & Huber, K. T. (2010) · Journal of Molecular Evolution · doi:10.1007/s00239-010-9338-y · Cited by 8 · see citing works
A Single Nucleotide Variant in the Promoter Region of 17β-HSD Type 5 Gene Influences External Genitalia Virilization in Females with 21-Hydroxylase Deficiency
Kaupert, L. C., Gomes, L. G., Brito, V. N., de Lemos‐Marini, S. H. V., de Mello, M. P., Longui, C. A., Kochi, C., de Castro, M., Guerra‐Júnior, G., Mendonca, B. B., et al. (2016) · Hormone Research in Paediatrics · doi:10.1159/000445684 · Cited by 7 · see citing works

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Rizal A, Hamid AH, Pfeiffer MI, Verhaegh GW, Schaafsma E, Brandt A, Sweep FC, Sedelaar PM, Schalken JA, 2012 Aldo-keto reductase 1 member C3 (AKR1C3) is a biomarker and therapeutic target for castration-resistant prostate cancer. Mol. Med. 18, 1449– 1455. PMC3563708 23196782

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Detlefsen, A. J., Mesaros, C., Duan, L., & Penning, T. M. (2023) · Cancer Research Communications · doi:10.1158/2767-9764.crc-23-0235 · Cited by 14 · see citing works
Self-citation
Structure-guided optimization of 3-hydroxybenzoisoxazole derivatives as inhibitors of Aldo-keto reductase 1C3 (AKR1C3) to target prostate cancer
Pippione, A. C., Kovachka, S., Vigato, C., Bertarini, L., Mannella, I., Sainas, S., Rolando, B., Denasio, E., Piercy-Mycock, H., Romalho, L., et al. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116193 · Cited by 13 · see citing works
Microproteomics and Immunohistochemistry Reveal Differences in Aldo‐Keto Reductase Family 1 Member C3 in Tissue Specimens of Ulcerative Colitis and Crohn's Disease
Arafah, K., Kriegsmann, M., Renner, M., Lasitschka, F., Fresnais, M., Kriegsmann, K., von Winterfeld, M., Goeppert, B. F., Kriegsmann, J., Casadonte, R., et al. (2020) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201900110 · Cited by 13 · see citing works
Identification of Featured Metabolism-Related Genes in Patients with Acute Myocardial Infarction
Xie, H., Zhao, E., & Zhang, Y. (2020) · Disease Markers · doi:10.1155/2020/8880004 · Cited by 12 · see citing works
Androgen and Estrogen β Receptor Expression Enhances Efficacy of Antihormonal Treatments in Triple-Negative Breast Cancer Cell Lines
Crespo, B., Illera, J. C., Silván, G., Lopez-Plaza, P., de la Muela, M. H., Yagüe, M. D. L. P., del Arco, C. D., Illera, M. J., & Cáceres, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031471 · Cited by 11 · see citing works
Potential biomarkers of acute myocardial infarction based on co‑expression network analysis
Hu, Z., Liu, R., Hu, H., Ding, X., Ji, Y., Li, G., Wang, Y., Xie, S., Liu, X., & Ding, Z. (2021) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2021.11085 · Cited by 11 · see citing works
Characterization of the major single nucleotide polymorphic variants of aldo-keto reductase 1C3 (type 5 17β-hydroxysteroid dehydrogenase)
Detlefsen, A. J., Wangtrakuldee, P., & Penning, T. M. (2022) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2022.106121 · Cited by 12 · see citing works
Self-citation
Genome-scale CRISPR screens identify PTGES3 as a direct modulator of androgen receptor function in advanced prostate cancer
Li, H., Melnyk, J. E., Fu, B. X. H., Shrestha, R., Zhang, M., Sjöström, M., Feng, S., Anderson, J. A., Han, W., Chesner, L. N., et al. (2025) · Nature Genetics · doi:10.1038/s41588-025-02388-8 · Cited by 10 · see citing works
“PTGES3 is also reported to be a cytosolic prostaglandin synthase that converts Prostaglandin H2 (PGH2) to Prostaglandin E2 (PGE2) 47 ; of note, other prostaglandin synthases in the same family as PTGES3 have been implicated in the production of androgens 48,49 .”
Aldo-keto reductase family 1 member C3 (AKR1C3) gene polymorphism (rs12529) is associated with breast cancer in Bangladeshi population: A case-control study and computational investigation
Shaon, M. A., Ansari, F., Mahmud, Z., Tamanna, S., Ibrahim, M. N. B., Alam, N. F., Hossain, M. N., & Howlader, M. Z. H. (2025) · PLoS ONE · doi:10.1371/journal.pone.0318079 · Cited by 11 · see citing works
Small molecules as products of evolution
Markov, G. V., & Laudet, V. (2022) · Current Biology · doi:10.1016/j.cub.2021.12.038 · Cited by 10 · see citing works
Quantitative Systems Toxicology Identifies Independent Mechanisms for Hepatotoxicity and Bilirubin Elevations Due to AKR1C3 Inhibitor BAY1128688
Battista, C., Shoda, L. K. M., Watkins, P. B., Groettrup‐Wolfers, E., Rottmann, A., Raschke, M., & Generaux, G. T. (2023) · Clinical Pharmacology & Therapeutics · doi:10.1002/cpt.3010 · Cited by 10 · see citing works
Inhibitory Interplay of SULT2B1b Sulfotransferase with AKR1C3 Aldo-keto Reductase in Prostate Cancer
Park, S.-G., Song, C.-S., Lin, C.-L., Jiang, S., Osmulski, P. A., Wang, C., Marck, B. T., Matsumoto, A. M., Morrissey, C. M., Gaczynska, M. E., et al. (2020) · Endocrinology · doi:10.1210/endocr/bqz042 · Cited by 10 · see citing works
Canonical and Noncanonical Androgen Metabolism and Activity
Storbeck, K., & Mostaghel, E. A. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-32656-2_11 · Cited by 10 · see citing works
Influence of Indomethacin on Steroid Metabolism: Endocrine Disruption and Confounding Effects in Urinary Steroid Profiling of Anti-Doping Analyses
Stoll, A., Iannone, M., Gregorio, G. D., Molaioni, F., de la Torre, X., Botrè, F., & Parr, M. K. (2020) · Metabolites · doi:10.3390/metabo10110463 · Cited by 10 · see citing works
Aberrant epigenetic regulation of estrogen and progesterone signaling at the level of endometrial/endometriotic tissue in the pathomechanism of endometriosis
Szukiewicz, D. (2022) · Vitamins and hormones · doi:10.1016/bs.vh.2022.11.005 · Cited by 10 · see citing works
A Mansonone Derivative Coupled with Monoclonal Antibody 4D5-Modified Chitosan Inhibit AKR1C3 to Treat Castration-Resistant Prostate Cancer
Zhou, M., Wang, X., Xia, J., Cheng, Y., Xiao, L., Yu, B., Tang, J., Huang, Y., Xiang, Q., & Huang, S. (2020) · International Journal of Nanomedicine · doi:10.2147/ijn.s241324 · Cited by 9 · see citing works
Network Pharmacological Study of the Active Ingredient of Panax Notoginseng Saponins for the Treatment of Lung Cancer by Inhibiting AKR1C3
Wei, Y.-Z., Yang, M.-Z., & Yuan, W. (2023) · Letters in Drug Design & Discovery · doi:10.2174/1570180820666230914104206 · Cited by 8 · see citing works
The third generation AKR1C3-activated prodrug, ACHM-025, eradicates disease in preclinical models of aggressive T-cell acute lymphoblastic leukemia
Toscan, C. E., McCalmont, H., Ashoorzadeh, A., Lin, X., Fu, Z., Doculara, L., Kosasih, H. J., Cadiz, R., Zhou, A., Williams, S., et al. (2024) · Blood Cancer Journal · doi:10.1038/s41408-024-01180-x · Cited by 8 · see citing works
Recent advances in the development of 17beta-hydroxysteroid dehydrogenase inhibitors
Poirier, D. (2024) · Steroids · doi:10.1016/j.steroids.2024.109529 · Cited by 12 · see citing works
Ferroptosis-related gene signature predicts prognosis in kidney renal papillary cell carcinoma
Yin, H., Mei, L., Liang, S., Wei, M., Huang, C., Qin, F., Nong, J., Zeng, X., Nong, C., & Qin, H. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.988867 · Cited by 8 · see citing works
Dynamics of HSD17B3 expression in human fetal testis: implications for the role of Sertoli cells in fetal testosterone biosynthesis
Planinić, A., Marić, T., Himelreich-Perić, M., Ježek, D., & Bojanac, A. K. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1429292 · Cited by 8 · see citing works
Human AKR1C3 binds agonists of GPR84 and participates in an expanded polyamine pathway
Dudkina, N., Park, H. B., Song, D., Jain, A., Khan, S. A., Flavell, R. A., Johnson, C. H., Palm, N. W., & Crawford, J. M. (2024) · Cell chemical biology · doi:10.1016/j.chembiol.2024.07.011 · Cited by 7 · see citing works
A novel AKR1C3 specific prodrug AST-3424 and its combination therapy in hepatocellular carcinoma
Chen, X., Zhang, Y., Zheng, X., & Qin, S. (2023) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2023.03.004 · Cited by 7 · see citing works
In Silico Analysis to Identify Molecular Targets for Chemicals of Concern: The Case Study of Flocoumafen, an Anticoagulant Pesticide
Coronado‐Posada, N., Mercado‐Camargo, J., & Olivero‐Verbel, J. (2021) · Environmental Toxicology and Chemistry · doi:10.1002/etc.5042 · Cited by 7 · see citing works
Protocadherin 19 Clustering Epilepsy and Neurosteroids: Opportunities for Intervention
de Nys, R., Kumar, R., & Gécz, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22189769 · Cited by 7 · see citing works
AI Based Discovery of a New AKR1C3 Inhibitor for Anticancer Applications.
Pippione, A. C., Vigato, C., Tucciarello, C., Hussain, S., Salladini, E., Truong, H. H., Henriksen, N. M., Vanzetti, G., Giordano, G., Zonari, D., et al. (2024) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.4c00150 · Cited by 7 · see citing works
AKR1C3 mediates gastric cancer cell invasion and metastasis via the AKT and JNK/p-NF-κB signaling pathways
Lin, L., Xiao, X., Guo, X., Zhong, C., Zhuang, M., Xu, J., Wang, Y., & Chen, F. (2024) · Scientific Reports · doi:10.1038/s41598-024-82039-w · Cited by 7 · see citing works
Entinostat overcomes cisplatin resistance in bladder cancer by promoting H3K18la-mediated DHRS2 expression and nuclear translocation to suppress the AKR1C3-androgen axis
Xu, G., Zheng, M., Wu, Z., Xie, T., Li, Y., Hu, G., Fang, S., Zhang, J., Diao, W., Zhao, W., et al. (2025) · Drug Resistance Updates · doi:10.1016/j.drup.2025.101343 · Cited by 6 · see citing works
Emerging small-molecule AKR1C3 inhibitors development for cancer therapy: Progress from 2021 to 2025
Gao, H.-N., Wu, X.-S., Pan, Z.-J., Liu, H.-M., Chen, K.-Q., Teng, M.-X., Zhao, J.-T., Zhou, J., You, Q.-D., & Zhang, C. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.118490 · Cited by 7 · see citing works
Establishment of Ferroptosis-Related Key Gene Signature and Its Validation in Compression-Induced Intervertebral Disc Degeneration Rats
Guo, J., Yang, Y.-L., Niu, J., Luo, Z., Shi, Q., & Yang, H. (2023) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2023/9020236 · Cited by 6 · see citing works
Mechanisms of action of Zishen Yutai pills in treating premature ovarian failure determined by integrating UHPLC-Q-TOF-MS and network pharmacology analysis
Dang, L., Zhang, C., Su, B., Ning, N., Huang, Q., Zhou, S., Wu, M., Ma, W., Wang, M., Cui, P., et al. (2022) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-022-03763-2 · Cited by 6 · see citing works
Proteomic analysis of tear film in canine diabetic patients with and without retinopathy
Winiarczyk, D., Winiarczyk, M., Balicki, I., Szadkowski, M., Michalak, K., Winiarczyk, S., & Adaszek, Ł. (2022) · Journal of Veterinary Research · doi:10.2478/jvetres-2022-0053 · Cited by 6 · see citing works
Deconstructing Intratumoral Heterogeneity through Multiomic and Multiscale Analysis of Serial Sections
Schupp, P. G., Shelton, S. J., Brody, D. J., Eliscu, R., Johnson, B., Mazor, T., Kelley, K. W., Potts, M. B., McDermott, M. W., Huang, E. J., et al. (2024) · Cancers · doi:10.3390/cancers16132429 · Cited by 5 · see citing works
Influence of aldo–keto reductase 1C3 polymorphisms in early-onset female psoriasis patients
Nojiri, Y., Nakamura, M., Magara, T., Yamamoto, A., Ikumi, K., Nakamura, R. M., Nishida, E., Haarmann‐Stemmann, T., & Morita, A. (2023) · Scientific Reports · doi:10.1038/s41598-023-30464-8 · Cited by 5 · see citing works
Transitional cell metaplasia of the uterine cervix: A histopathological and immunohistochemical analysis suggesting a possible role of androgenic conversion during urothelial-like differentiation in peri/postmenopausal women
Yoo, S. H., Kim, K.-R., & Park, J. Y. (2021) · Annals of Diagnostic Pathology · doi:10.1016/j.anndiagpath.2021.151839 · Cited by 5 · see citing works
Prostanoid Signaling in Cancers: Expression and Regulation Patterns of Enzymes and Receptors
Ershov, P. V., Yablokov, E. O., Kaluzhskiy, L. A., Mezentsev, Y. V., & Ivanov, A. S. (2022) · Biology · doi:10.3390/biology11040590 · Cited by 5 · see citing works
Intracrine androgen biosynthesis and drug resistance
Penning, T. M., Asangani, I. A., Sprenger, C. C. T., & Plymate, S. R. (2020) · Cancer Drug Resistance · doi:10.20517/cdr.2020.60 · Cited by 6 · see citing works
Self-citation
Identification of Pyroptosis-Related Molecular Subtypes and Diagnostic Model development in Major Depressive Disorder
Feng, L., Yuan, J., Li, L., & Tang, J. (2024) · Molecular Biotechnology · doi:10.1007/s12033-024-01252-0 · Cited by 4 · see citing works
In silico prediction of deleterious single nucleotide polymorphism in human AKR1C3 gene and identification of potent inhibitors using molecular docking approach
Aloyuni, S. (2021) · Journal of King Saud University - Science · doi:10.1016/j.jksus.2021.101514 · Cited by 4 · see citing works
Computational modeling studies reveal the origin of the binding preference of 3‐(3,4‐di hydroisoquinolin‐2( 1H )‐ylsulfonyl)benzoic acids for AKR1C3 over its isoforms
Kong, X., Xing, E., Wu, S., Zhuang, T., Li, P., Li, C., & Cheng, X. (2022) · Protein Science · doi:10.1002/pro.4499 · Cited by 4 · see citing works
Reversible downregulation of MYC in a spheroid model of metastatic epithelial ovarian cancer
Buensuceso, A. V., Borrelli, M. J., Valdés, Y. R., & Shepherd, T. G. (2024) · Cancer Gene Therapy · doi:10.1038/s41417-024-00850-z · Cited by 4 · see citing works
Downregulation of Dihydrotestosterone and Estradiol Levels by HEXIM1
Mozar, F. S., Sharma, V., Gorityala, S., Albert, J. M., Xu, Y., & Montano, M. M. (2021) · Endocrinology · doi:10.1210/endocr/bqab236 · Cited by 4 · see citing works
Localized high-risk prostate cancer harbors an androgen receptor low subpopulation susceptible to HER2 inhibitionPreprint
Wilkinson, S. C., Ku, A. T., Lis, R. T., King, I. M., Low, D., Trostel, S. Y., Bright, J. R., Terrigino, N. T., Baj, A., Fenimore, J. M., et al. (2024) · medRxiv · doi:10.1101/2024.02.09.24302395 · Cited by 4 · see citing works
Discovery of Highly Selective AKR1C3 Inhibitors to Overcome EGFR C797S-Mediated Osimertinib Resistance in Non-Small Cell Lung Cancer
Guo, C., Wang, X., Guan, Q., Zhong, S., Zhang, L., Liu, Y., Han, B., Shao, J., Liu, Z., Chen, Y., et al. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c03655 · Cited by 3 · see citing works
Androgen metabolism in prostate cancer: recent advances
Sharifi, N. (2026) · Endocrinology · doi:10.1210/endocr/bqag021 · Cited by 3 · see citing works
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Kang, N., Liu, S., Li, X. Q., Luo, R., Chen, W.-T., Ran, C., Wang, P., & Yang, J. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c03834 · Cited by 3 · see citing works
Aldo-Keto reductase 1C3 reduces myocardial cell damage after acute myocardial infarction by activating the Kelch-like ECH-associated protein 1-nuclear factor erythroid 2-related factor 2-antioxidant response element pathway to inhibit ferroptosis
Wang, M. I. A. O., & Yun-Zhao, H. U. (2024) · 老年心脏病学杂志：英文版 · doi:10.26599/1671-5411.2024.09.001 · Cited by 3 · see citing works
AKR1C3 protects cardiomyocytes against hypoxia-induced cell apoptosis through the Nrf-2/NF-κB pathway
Zhang, W., Tian, W., Xia, X., Tian, H., & Sun, T. (2024) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2024230 · Cited by 3 · see citing works
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Meng, T., Jung, D. T., Cai, X., Lu, Z., Yu, J., Qi, T., Meng, F., Ruan, M., & Duan, J. (2024) · Biopharmaceutics & Drug Disposition · doi:10.1002/bdd.2385 · Cited by 2 · see citing works
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Sun, Z., Qin, Y., & Zhang, X. (2025) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1490745 · Cited by 3 · see citing works
Ferroptosis induction, androgen biosynthesis disruption and prostate cancer suppression by androgen and vitamin D combination
Park, B., Khadka, S., Ahn, J., Vaquiz, J., Igbekoyi, O., Song, C. S., & Chatterjee, B. (2025) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2025.130828 · Cited by 2 · see citing works
In silico study of novel alpha tocopheroids as effective inhibitors of aldo-keto reductase 1c3 (AKR1C3) enzyme
Basu, T., & Upadhyay, A. K. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2241543 · Cited by 1 · see citing works
Cancer-Associated fibroblasts regulate the development of cholangiocarcinoma through IL-6/STAT3/AKR1C3 signaling axis
Huang, T.-C., Feng, W.-D., Fang, G.-X., Zhang, Q.-H., Wei, G.-Y., Li, C.-Z., Wang, J.-M., & Liu, J.-F. (2026) · Scientific Reports · doi:10.1038/s41598-026-37583-y · Cited by 1 · see citing works
Single-cell and spatial transcriptomics reveal an arachidonic acid–related cellular atlas in lung adenocarcinoma
Sun, C., Zhang, Y., Pan, Y., 夏贵喜, Yang, G., Huang, C., Li, J., & Ma, P. (2026) · Inflammation Research · doi:10.1007/s00011-026-02251-4 · Cited by 1 · see citing works
Characterization of a highly specific monoclonal antibody against human aldo-keto reductase AKR1C3
Liu, J., He, P., Lin, L., Zhao, Y., Deng, W., Ding, H., Li, Q., & Wang, Z. (2019) · Steroids · doi:10.1016/j.steroids.2019.01.001 · Cited by 1 · see citing works
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Pandey, D. K., Bharti, M., Rana, A., Prabhakaran, S., & Chauhan, R. (2024) · Letters in Organic Chemistry · doi:10.2174/0115701786275607231228094526 · Cited by 1 · see citing works
Steroids Static Postural Balance Changes After Exercise Intervention Correlate with Steroidome in Elderly Female
Kornatovská, Z., Hill, M., Jandová, D., Krejčí, M., & Zwierzchowska, A. (2025) · Metabolites · doi:10.3390/metabo15040239 · Cited by 1 · see citing works
Mechanisms of Action of Zishen Yutai pills in Treating Premature Ovarian Failure Determined by Integrating UHPLC-Q-TOF-MS and Network Pharmacology AnalysisPreprint
Dang, L., Zhang, C., Su, B., Na, N., Huang, Q., Zhou, S., Wu, M., Ma, W., Wang, M., Cui, P., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1176592/v1
Docking is not enough: 17-trifluoromethylphenyl trinor PGF2α is only a very weak ligand of neurokinin-1 receptor
Matalińska, J., & Lipiński, P. F. J. (2022) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2022.104849
Comprehensive clinical analysis of AKR1 expression profiles in the diagnosis of human colorectal cancerPreprint
Li, H., Duan, L., Li, S., He, R., Li, Z., Liao, X., Luo, D., & Zheng, L. (2023) · Research Square · doi:10.21203/rs.3.rs-2526991/v1
Research Progress of AR Gene Family in Prostate Cancer Therapy
Khan, M. (2024) · annals of urologic oncology · doi:10.32948/auo.2024.10.13
A Prognostic Survival Model Based on Endocrine-Related Gene Expression in Acute Myelogenous Leukemia
Lv, W., Wang, Y., Hu, F., Huang, H.-Y., Cui, Y., Song, Y., Chen, L., Wu, B., & Liang, Y. (2025) · Acta Haematologica · doi:10.1159/000543272
The Relationship between AKR1C3 and Diseases
袁, 大. (2025) · Hans Journal of Medicinal Chemistry · doi:10.12677/hjmce.2025.131008

Inhibitors of type 5 17β-hydroxysteroid dehydrogenase (AKR1C3): Overview and structural insights
Byrns, M. C., Jin, Y., & Penning, T. M. (2010) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.11.004 · Cited by 144 · see citing works
Self-citation
Aldo-keto reductase (AKR) 1C3 as an androgen receptor coactivator.
Narayanan, R., Yepuru, M., Wu, Z., Barrett, C. M., Kim, J., Penning, T. M., Steiner, M. S., Miller, D. D., & Dalton, J. T. (2013) · Journal of Clinical Oncology · doi:10.1200/jco.2013.31.6_suppl.100 · Cited by 2 · see citing works
Self-citation
Type 5 17β-hydroxysteroid dehydrogenase/prostaglandin F synthase (AKR1C3): Role in breast cancer and inhibition by non-steroidal anti-inflammatory drug analogs
Byrns, M. C., & Penning, T. M. (2008) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2008.10.024 · Cited by 82 · see citing works
Self-citation
Aldo-keto reductase (AKR) 1C3: Role in prostate disease and the development of specific inhibitors
Penning, T. M., Steckelbroeck, S., Bauman, D. R., Miller, M. W., Jin, Y., Peehl, D. M., Fung, K.-M. A., & Lin, H.-K. (2006) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2005.12.009 · Cited by 125 · see citing works
Self-citation
11-Oxygenated androgen precursors are the preferred substrates for aldo-keto reductase 1C3 (AKR1C3): implications for castration resistant prostate cancer
Barnard, M., Quanson, J. L., Mostaghel, E., Pretorius, E., Snoep, J. L., & Storbeck, K.-H. (2018) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2018.06.013 · Cited by 72 · see citing works

Authors: Penning, T. M.
Affiliations: University of Pennsylvania (US)
Corresponding author: Penning, Trevor M.
ORCID: Penning, Trevor M.
Venue: Molecular and Cellular Endocrinology
Publisher: Elsevier BV
Published: 2019-06
Volume: 489
Pages: 82-91
ISSN: 0303-7207 (ISSN-L)
DOI: 10.1016/j.mce.2018.07.002
PMC: PMC6422768
OpenAlex: W2890789239
Cited by: 117
References: 99
Citations by year: 2026: 18 · 2025: 13 · 2024: 20 · 2023: 14 · 2022: 20 · 2021: 17 · 2020: 11 · 2019: 4
FWCI: 0.90
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Molecular and Cellular Endocrinology (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health (P30-ES013508, R01-CA90744)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Aldose Reductase and Taurine
Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Prostate Cancer Treatment and Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
Keywords: AKR1C3, 17β-hydroxysteroid dehydrogenase type 5, androgen production, castration-resistant prostate cancer, polycystic ovary syndrome, breast cancer, prostaglandin F2alpha, FP receptor, PPARγ, acute myeloid leukemia, AKR1C3 inhibitors, moonlighting enzymes
MeSH terms: Aldo-Keto Reductase Family 1 Member C3, Endocrine System Diseases, Endocrine Gland Neoplasms, Enzyme Inhibitors, Humans, Steroids, Epigenesis, Genetic

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AKR1C3 (type 5 17β-hydroxysteroid dehydrogenase/prostaglandin F synthase): Roles in malignancy and endocrine disorders

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