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, Michael C.; Duan, Ling; Lee, Seon Hwa; Blair, Ian A.; Penning, Trevor M.

doi:10.1016/j.jsbmb.2009.12.009

Cited by 123Aldose Reductase and TaurineEstrogen and related hormone effectsSteroid Chemistry and Biochemistry

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

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Byrns, Michael C., Duan, Ling, Lee, Seon Hwa, Blair, Ian A., Penning, Trevor M.·2010·The Journal of Steroid Biochemistry and Molecular Biology

DOI 10.1016/j.jsbmb.2009.12.009PMC PMC2819162

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Abstract

Aldo-keto reductase (AKR) 1C3 (type 5 17beta-hydroxysteroid dehydrogenase and prostaglandin F synthase), may stimulate proliferation via steroid hormone and prostaglandin (PG) metabolism in the breast. Purified recombinant AKR1C3 reduces PGD(2) to 9alpha,11beta-PGF(2), Delta(4)-androstenedione to testosterone, progesterone to 20alpha-hydroxyprogesterone, and to a lesser extent, estrone to 17beta-estradiol. We established MCF-7 cells that stably express AKR1C3 (MCF-7-AKR1C3 cells) to model its over-expression in breast cancer. AKR1C3 expression increased steroid conversion by MCF-7 cells, leading to a pro-estrogenic state. Unexpectedly, estrone was reduced fastest by MCF-7-AKR1C3 cells when compared to other substrates at 0.1muM. MCF-7-AKR1C3 cells proliferated three times faster than parental cells in response to estrone and 17beta-estradiol. AKR1C3 therefore represents a potential target for attenuating estrogen receptor alpha induced proliferation. MCF-7-AKR1C3 cells also reduced PGD(2), limiting its dehydration to form PGJ(2) products. The AKR1C3 product was confirmed as 9alpha,11beta-PGF(2) and quantified with a stereospecific stable isotope dilution liquid chromatography-mass spectrometry method. This method will allow the examination of the role of AKR1C3 in endogenous prostaglandin formation in response to inflammatory stimuli. Expression of AKR1C3 reduced the anti-proliferative effects of PGD(2) on MCF-7 cells, suggesting that AKR1C3 limits peroxisome proliferator activated receptor gamma (PPARgamma) signaling by reducing formation of 15-deoxy-Delta(12,14)-PGJ(2) (15dPGJ(2)).

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In MCF-7 cells stably transfected with AKR1C3, the enzyme converts 0.1 μM estrone to 17β-estradiol faster than it converts Δ4-androstene-3,17-dione to testosterone or progesterone to 20α-hydroxy-pregn-4-ene-3-one.
“In MCF-7 cells stably transfected with AKR1C3 it was found that the enzyme converts 0.1 μM estrone to 17β-estradiol faster than it catalyzes either the conversion of Δ4-androstene-3,17-dione to testosterone or the conversion of progesterone to 20α-hydroxy-pregn-4-ene-3-one”
From Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism (2014) · cites this paper as [37]

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Aldo-keto reductase 1C3—Assessment as a new target for the treatment of endometriosis
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Elevated Expression of AKR1C3 Increases Resistance of Cancer Cells to Ionizing Radiation via Modulation of Oxidative Stress
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Selective Inhibition of Human Type-5 17β-Hydroxysteroid Dehydrogenase (AKR1C3) by Baccharin, a Component of Brazilian Propolis
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Enzymes of the AKR1B and AKR1C Subfamilies and Uterine Diseases
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Aldo–keto reductases AKR1C1, AKR1C2 and AKR1C3 may enhance progesterone metabolism in ovarian endometriosis
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Modification of cysteine residues by cyclopentenone prostaglandins: Interplay with redox regulation of protein function
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In vitro inhibition of AKR1Cs by sulphonylureas and the structural basis
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Role of hydroxysteroid (17beta) dehydrogenase type 1 in reproductive tissues and hormone-dependent diseases
Heinosalo, T., Saarinen, N., & POUTANEN, M. H. (2018) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2018.08.004 · Cited by 40 · see citing works
PTHrP stimulates prostate cancer cell growth and upregulates aldo–keto reductase 1C3
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Aldo-Keto Reductase 1C3 Is Expressed in Differentiated Human Epidermis, Affects Keratinocyte Differentiation, and Is Upregulated in Atopic Dermatitis
Mantel, A., Carpenter-Mendini, A. B., VanBuskirk, J., Benedetto, A. D., Beck, L. A., & Pentland, A. P. (2011) · Journal of Investigative Dermatology · doi:10.1038/jid.2011.412 · Cited by 40 · see citing works
Retinaldehyde is a substrate for human aldo–keto reductases of the 1C subfamily
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11β-Prostaglandin F2α, a bioactive metabolite catalyzed by AKR1C3, stimulates prostaglandin F receptor and induces slug expression in breast cancer
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Pyrithione-based ruthenium complexes as inhibitors of aldo–keto reductase 1C enzymes and anticancer agents
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Promiscuity and diversity in 3-ketosteroid reductases
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The Significance of the Sulfatase Pathway for Local Estrogen Formation in Endometrial Cancer
Sinreih, M., Knific, T., Anko, M., Hevir, N., Vouk, K., Jerin, A., Frković Grazio, S., & Rižner, T. L. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00368 · Cited by 33 · see citing works
AKR1C3 in carcinomas: from multifaceted roles to therapeutic strategies
Li, M., Zhang, L., Yu, J., Wang, X., Cheng, L., Ma, Z., Chen, X., Wang, L., & Goh, B. C. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1378292 · Cited by 33 · see citing works
The Activity of SN33638, an Inhibitor of AKR1C3, on Testosterone and 17β-Estradiol Production and Function in Castration-Resistant Prostate Cancer and ER-Positive Breast Cancer
Yin, Y. D., Fu, M., Brooke, D. G., Heinrich, D. M., Denny, W. A., & Jamieson, S. M. F. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00159 · Cited by 33 · see citing works
Isoquinoline alkaloids as a novel type of AKR1C3 inhibitors
Zemanová, L., Hofman, J., Chlebek, J., Havrankova, J., Kosanova, K., Skarka, A., Hošťálková, A., Plucha, T., Cahlíková, L., & Wsól, V. (2014) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2014.04.005 · Cited by 32 · see citing works
Aldo-keto reductase family 1 member C3 (AKR1C3) is expressed in adenocarcinoma and squamous cell carcinoma but not small cell carcinoma.
Miller, V. L., Lin, H.-K., Murugan, P., Fan, M. D., Penning, T. M., Brame, L. S., Yang, Q., & Fung, K.-M. A. (2012) · Europe PMC (PubMed Central) · Cited by 32 · see citing works
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Selective Inhibitors of Aldo-Keto Reductases AKR1C1 and AKR1C3 Discovered by Virtual Screening of a Fragment Library
Brožič, P., Turk, S., Adeniji, A. O., Konc, J., Janežič, D., Penning, T. M., Rižner, T. L., & Gobec, S. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300841n · Cited by 30 · see citing works
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Synthesis of non-prenyl analogues of baccharin as selective and potent inhibitors for aldo-keto reductase 1C3
Endo, S., Hu, D., Matsunaga, T., Otsuji, Y., El-Kabbani, O. A. L., Kandeel, M. K., Ikari, A., Hara, A., Kitade, Y., & Toyooka, N. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2014.08.007 · Cited by 29 · see citing works
Simvastatin in combination with meclofenamic acid inhibits the proliferation and migration of human prostate cancer PC‑3 cells via an AKR1C3 mechanism
Sekine, Y., Nakayama, H., Miyazawa, Y., Kato, H., Furuya, Y., Arai, S., Koike, H., Matsui, H., Shibata, Y., Ito, K., et al. (2017) · Oncology Letters · doi:10.3892/ol.2017.7721 · Cited by 28 · see citing works
AKR1C3 Is Associated with Better Survival of Patients with Endometrial Carcinomas
Hojnik, M., Šuster, N. K., Smrkolj, Š., Grazio, S. F., Verdenik, I., & Rižner, T. L. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9124105 · Cited by 26 · see citing works
Overview of human 20 alpha-hydroxysteroid dehydrogenase (AKR1C1): Functions, regulation, and structural insights of inhibitors
Chu, X., He, S., Liu, Y., Liu, Y., Feng, F., Guo, Q., Zhao, L., & Sun, H. (2021) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2021.109746 · Cited by 26 · see citing works
Aldo-keto reductases: Role in cancer development and theranostics
Nagini, S., Kallamadi, P. R., Tanagala, K. K. K., & Reddy, G. B. (2024) · Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics · doi:10.32604/or.2024.049918 · Cited by 25 · see citing works
Aldo-keto reductase (AKR) superfamily website and database: An update
Huacachino, A. A., Joo, J., Narayanan, N., Tehim, A., Himes, B. E., & Penning, T. M. (2024) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2024.111111 · Cited by 25 · see citing works
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AKR1C3 Overexpression Mediates Methotrexate Resistance in Choriocarcinoma Cells
Zhao, J., Xiang, Y., Xiao, C., Guo, P., Wang, D., Liu, Y., & Shen, Y. (2014) · International Journal of Medical Sciences · doi:10.7150/ijms.9239 · Cited by 25 · see citing works
Role of Aldo–Keto Reductase Enzymes in Mediating the Timing of Parturition
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Alterations in estrogen signalling pathways upon acquisition of anthracycline resistance in breast tumor cells
Chewchuk, S., Guo, B., & Parissenti, A. M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0172244 · Cited by 22 · see citing works
Significance of aldo-keto reductase 1C3 and ATP-binding cassette transporter B1 in gain of irinotecan resistance in colon cancer cells
Matsunaga, T., Okumura, N., Saito, H., Morikawa, Y., Suenami, K., Hisamatsu, A., Endo, S., & Ikari, A. (2020) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2020.109295 · Cited by 22 · see citing works
Development of Biaryl-Containing Aldo-Keto Reductase 1C3 (AKR1C3) Inhibitors for Reversing AKR1C3-Mediated Drug Resistance in Cancer Treatment
He, S., Chu, X., Wu, Y., Jiang, J., Fang, P., Chen, Y., Liu, Y., Qiu, Z., Xiao, Y., Li, Z., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00213 · Cited by 21 · 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
The roles of AKR1C1 and AKR1C2 in ethyl-3,4-dihydroxybenzoate induced esophageal squamous cell carcinoma cell death
Li, W., Hou, G., Zhou, D., Lou, X., Xu, Y., Liu, S., & Zhao, X. (2016) · Oncotarget · doi:10.18632/oncotarget.7775 · Cited by 21 · see citing works
Buparlisib is a novel inhibitor of daunorubicin reduction mediated by aldo-keto reductase 1C3
Büküm, N., Novotná, E., Morell, A., Hofman, J., & Wsól, V. (2019) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2019.01.026 · Cited by 20 · see citing works
Aldo‐keto reductase 1 C 3 is overexpressed in skin squamous cell carcinoma ( SCC ) and affects SCC growth via prostaglandin metabolism
Mantel, A., Carpenter-Mendini, A. B., VanBuskirk, J., & Pentland, A. P. (2014) · Experimental Dermatology · doi:10.1111/exd.12468 · Cited by 19 · see citing works
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 · see citing works
Bruton’s Tyrosine Kinase Inhibitors Ibrutinib and Acalabrutinib Counteract Anthracycline Resistance in Cancer Cells Expressing AKR1C3
Morell, A., Čermáková, L., Novotná, E., Laštovičková, L., Haddad, M., Haddad, A., Portillo, R., & Wsól, V. (2020) · Cancers · doi:10.3390/cancers12123731 · Cited by 17 · see citing works
The role of aldo‐keto reductase 1 C 3 ( AKR 1 C 3)‐mediated prostaglandin D 2 ( PGD 2) metabolism in keloids
Mantel, A., Newsome, A., Thekkudan, T., Frazier, R., & Katdare, M. (2015) · Experimental Dermatology · doi:10.1111/exd.12854 · Cited by 16 · see citing works
Dehydroepiandrosterone (DHEA)-SO 4 Depot and Castration-Resistant Prostate Cancer
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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 15 · see citing works
Transition from androgenic to neurosteroidal action of 5α-androstane-3α, 17β-diol through the type A γ-aminobutyric acid receptor in prostate cancer progression
Xia, D., Lai, D. V., Wu, W., Webb, Z. D., Yang, Q., Zhao, L., Yu, Z., Thorpe, J. E., Disch, B. C., Ihnat, M. A., et al. (2017) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2017.11.006 · Cited by 15 · see citing works
Molecular docking, 3D-QSAR and simulation studies for identifying pharmacophoric features of indole derivatives as 17β-hydroxysteroid dehydrogenase type 5 (17β-HSD5) inhibitors
Kulkarni, S., Singh, Y., Biharee, A., Bhatia, N., Monga, V., & Thareja, S. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2175265 · Cited by 14 · see citing works
Deletion of Alox15 improves kidney dysfunction and inhibits fibrosis by increased PGD2 in the kidney
Takahashi, N., Kikuchi, H., Usui, A., Furusho, T., Fujimaru, T., Fujiki, T., Yanagi, T., Matsuura, Y., Asano, K., Yamamoto, K., et al. (2021) · Clinical and Experimental Nephrology · doi:10.1007/s10157-021-02021-y · Cited by 14 · see citing works
Genetic variation in the eicosanoid pathway is associated with non-small-cell lung cancer (NSCLC) survival
Sausville, L. N., Jones, C. C., Aldrich, M. C., Blot, W. J., Pozzi, A., & Williams, S. M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0180471 · Cited by 12 · see citing works
Type 5 17-hydroxysteroid dehydrogenase/prostaglandin F synthase (AKR1C3) inhibition and potential anti-proliferative activity of cholest-4-ene-3,6-dione in MCF-7 breast cancer cells
Sali, V. K., Mani, S., Meenaloshani, G., Ilavarasi, A. V., & Vasanthi, H. R. (2020) · Steroids · doi:10.1016/j.steroids.2020.108638 · Cited by 12 · 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
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Isocitrate dehydrogenase 2 inhibitor enasidenib synergizes daunorubicin cytotoxicity by targeting aldo-keto reductase 1C3 and ATP-binding cassette transporters
Morell, A., Budagaga, Y., Vagiannis, D., Zhang, Y. X., Laštovičková, L., Novotná, E., Haddad, A., Haddad, M., Portillo, R., Hofman, J., et al. (2022) · Archives of Toxicology · doi:10.1007/s00204-022-03359-2 · Cited by 12 · see citing works
Identification of genes associated with castration-resistant prostate cancer by gene expression profile analysis
Huang, C., Li, F. X., Pan, S., Xu, C., Dai, J. Q., & Zhao, X. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.7488 · Cited by 12 · see citing works
The role of 17βHSDs in breast tissue and breast cancers
McNamara, K. M., & Sasano, H. (2018) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2018.10.019 · Cited by 12 · see citing works
Discovery of Highly Potent AKR1C3 Inhibitors Treating Sorafenib-Resistant Hepatocellular Carcinoma
Xing, S., Jiang, J., Chu, X., Wang, X., Wang, Z., Li, X., Lv, B., Guo, C., He, S., Wang, L., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c03035 · Cited by 11 · see citing works
2,3-Diarylpropenoic acids as selective non-steroidal inhibitors of type-5 17β-hydroxysteroid dehydrogenase (AKR1C3)
Gazvoda, M., Beranič, N., Turk, S., Burja, B., Kočevar, M., Rižner, T. L., Gobec, S., & Polanc, S. (2013) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2012.12.045 · Cited by 11 · see citing works
Instability of C154Y variant of aldo-keto reductase 1C3
Endo, S., Takada, S., Honda, R. P., Müller, K., Weishaupt, J. H., Andersen, P. M., Ludolph, A. C., Kamatari, Y. O., Matsunaga, T., Kuwata, K., et al. (2016) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2016.12.018 · Cited by 11 · see citing works
The beneficial androgenic action of steroidal aromatase inactivators in estrogen-dependent breast cancer after failure of nonsteroidal drugs
Gao, L., Bao, Z., Deng, H., Li, X., Li, J., Rong, Z., Yang, Y., Liu, L., Nie, D., Wang, G., et al. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1724-9 · Cited by 11 · see citing works
New enzymatic assay for the AKR1C enzymes
Beranič, N., Štefane, B., Brus, B., Gobec, S., & Rižner, T. L. (2012) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2012.12.003 · Cited by 10 · see citing works
Tolrestat acts atypically as a competitive inhibitor of the thermostable aldo‐keto reductase Tm1743 from Thermotoga maritima
Zhang, C., Min, Z., Liu, X., Wang, C., Wang, Z., Shen, J., Tang, W., Zhang, X., Liu, D., & Xu, X. (2019) · FEBS Letters · doi:10.1002/1873-3468.13630 · Cited by 10 · see citing works
Development of new steroid-based hydrazide and (thio)semicarbazone compounds with anticancer properties
Janković, Ð. D., Šestić, T. L., Bekić, S. S., Savić, M. P., Ćelić, A. S., Scholda, J., Kopp, F. B., Marinović, M. A., Petri, E. T., & Ajduković, J. J. (2024) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2024.106545 · Cited by 9 · see citing works
Selective inhibition of aldo-keto reductase 1C3: a novel mechanism involved in midostaurin and daunorubicin synergism
Morell, A., Novotná, E., Milan, J., Danielisová, P., Büküm, N., & Wsól, V. (2020) · Archives of Toxicology · doi:10.1007/s00204-020-02884-2 · Cited by 9 · see citing works
Pregnane X receptor (PXR) deficiency promotes hepatocarcinogenesis via induction of Akr1c18 expression and prostaglandin F2α (PGF2α) levels
Shi, T., Fan, Q., Liu, S., & Zhang, S. (2024) · Biochemical Pharmacology · doi:10.1016/j.bcp.2024.116309 · Cited by 8 · see citing works
Bruton’s Tyrosine Kinase Inhibitor Zanubrutinib Effectively Modulates Cancer Resistance by Inhibiting Anthracycline Metabolism and Efflux
Čermáková, L., Hofman, J., Laštovičková, L., Havlíčková, L., Špringrová, I., Novotná, E., & Wsól, V. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14101994 · Cited by 8 · see citing works
Modulated Expression of Genes Encoding Estrogen Metabolizing Enzymes by G1-Phase Cyclin-Dependent Kinases 6 and 4 in Human Breast Cancer Cells
Jia, Y., Domenico, J. M., Swasey, C. H., Wang, M., Gelfand, E. W., & Lucas, J. J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0097448 · Cited by 8 · see citing works
9,10-Phenanthrenequinone Induces Monocytic Differentiation of U937 Cells through Regulating Expression of Aldo-Keto Reductase 1C3
Matsunaga, T., Hosogai, M., Arakaki, M., Endo, S., El-Kabbani, O. A. L., & Hara, A. (2012) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b12-00237 · Cited by 7 · see citing works
Design and Evaluation of NSAID Derivatives as AKR1C3 Inhibitors for Breast Cancer Treatment through Computer-Aided Drug Design and In Vitro Analysis
Fonseca-Benítez, A. V., Acosta‐Guzmán, P., Sánchez, J. E., Alarcón, Z., Jiménez, R. A., & Guevara‐Pulido, J. O. (2024) · Molecules · doi:10.3390/molecules29081802 · Cited by 6 · see citing works
Discovery of highly potent AKR1Cs pan-inhibitors as chemotherapeutic potentiators to restore breast cancer drug resistance
Xing, S., Liu, Y., Xie, H., Guo, C., Wang, X., Lv, B., Li, X., Shao, J., Guo, Q., Feng, F., et al. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117413 · Cited by 5 · see citing works
Deciphering 17-β-hydroxysteroid dehydrogenase 4: from molecular insights to cancer therapeutics
Liao, M.-B., Lau, A. T. Y., & Xu, Y. (2025) · Cancer Cell International · doi:10.1186/s12935-025-03885-w · 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
The Aldo-Keto Reductase Superfamily
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Analysis of Expression and Regulation of AKR1C2 in HPV-Positive and -Negative Oropharyngeal Squamous Cell Carcinoma
Ziogas, M., Siefer, O. G., Wuerdemann, N., Balaji, H., Gross, E., Drebber, U., Klußmann, J. P., & Huebbers, C. U. (2024) · Cancers · doi:10.3390/cancers16172976 · Cited by 3 · see citing works
Embryo-derived human chorionic gonadotropin promotes human decidualization through activating epithelial prostaglandin F2α secretion
Jin, D.-D., He, Y., Ran, F., Hong-yuan, Y., Yan, G., & Yang, Z. (2025) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2025.112581 · Cited by 3 · see citing works
Genetic association study of preterm birth and gestational age in a population-based case-control study in Peru
Juvinao-Quintero, D. L., Sánchez, S. E., Workalemahu, T., Pinto, N., Liang, L., Williams, M. A., & Gelaye, B. (2024) · Journal of Neonatal-Perinatal Medicine · doi:10.3233/npm-230228 · Cited by 3 · see citing works
Catalytic characteristics of AKR1C1-AKR1C4 and AKR1C9 on oxymesterone
Hu, H., Li, S., Zhang, C., Li, L., Yang, J., Wu, Q., Ou, L., You, J., Sun, A., Wieland, F. H., et al. (2024) · Molecular Catalysis · doi:10.1016/j.mcat.2024.114256 · Cited by 2 · see citing works
Environmental Lead Promotes Breast Cancer Migration and Invasion via the AKR1C3–NF-κB–MMP Axis
Liu, J., Ding, Y., Qiao, L., Meng, R., Shi, S., Zhang, Y., Liu, Y., Liu, S., Liu, Y., He, X., et al. (2026) · Biomedicines · doi:10.3390/biomedicines14020286 · Cited by 2 · see citing works
Identification of Anti‐Cancer Agents Targeting Aldo‐Keto Reductase (AKR) 1C3 Protein by Pharmacophore Modeling, Virtual Screening and Molecular Docking
Khalilullah, H. (2021) · ChemistrySelect · doi:10.1002/slct.202103151 · Cited by 2 · see citing works
Phthalate-treated endometrial cancer cell lines show increased AKR1C1 expression
Song, J.-Y., & Cho, H. (2014) · Molecular & Cellular Toxicology · doi:10.1007/s13273-014-0042-7 · Cited by 2 · see citing works
Identification of significantly mutated subnetworks in the breast cancer genome
Ajwad, R., Domaratzki, M., Liu, Q., Feizi, N., & Hu, P. (2021) · Scientific Reports · doi:10.1038/s41598-020-80204-5 · 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

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
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Rapid kinetics of tyrosyl radical formation and heme redox state changes in prostaglandin H synthase-1 and -2
Tsai, A., Wu, G., Palmer, G., Bambai, B., Koehn, J. A., Marshall, P. J., & Kulmacz, R. J. (1999) · Prostaglandins & Other Lipid Mediators · doi:10.1016/s0090-6980(99)90355-6
Steroid hormone transforming aldo–keto reductases and cancer
Penning, T. M., & Byrns, M. C. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.03700.x · Cited by 181 · 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
AKR1C3 (type 5 17β-hydroxysteroid dehydrogenase/prostaglandin F synthase): Roles in malignancy and endocrine disorders
Penning, T. M. (2019) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2018.07.002 · Cited by 117 · see citing works
Self-citation

Authors: Byrns, M. C., Duan, L., Lee, S. H., Blair, I. A., & Penning, T. M.
Affiliations: University of Pennsylvania (US)
Corresponding author: Penning, Trevor M.
ORCID: Lee, Seon Hwa
Blair, Ian A.
Penning, Trevor M.
Venue: The Journal of Steroid Biochemistry and Molecular Biology
Publisher: Elsevier BV
Published: 2010-02
Volume: 118
Issue: 3
Pages: 177-187
ISSN: 0960-0760 (ISSN-L)
DOI: 10.1016/j.jsbmb.2009.12.009
PMC: PMC2819162
OpenAlex: W1984703484
Cited by: 116
References: 45
Citations by year: 2026: 9 · 2025: 6 · 2024: 11 · 2023: 4 · 2022: 4 · 2021: 6 · 2020: 8 · 2019: 5 · 2018: 5 · 2017: 7 · 2016: 5 · 2015: 7 · 2014: 14 · 2013: 5 · 2012: 11
FWCI: 2.97
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: The Journal of Steroid Biochemistry and Molecular Biology (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: Japan Society for the Promotion of Science (22590130)
National Cancer Institute (R01CA090744)
National Institute of Diabetes and Digestive and Kidney Diseases (T32DK007314)
National Institute of Environmental Health Sciences (U01ES016004, P30ES013508)
Eunice Kennedy Shriver National Institute of Child Health and Human Development (T32HD007305)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Aldose Reductase and Taurine
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Steroid Chemistry and Biochemistry
Keywords: AKR1C3, MCF-7 cells, breast cancer, steroid hormone metabolism, prostaglandin metabolism, prostaglandin F2alpha, estrogen metabolism, estrone, estradiol, cell proliferation, estrogen receptor alpha, PPARγ signaling
MeSH terms: Aldo-Keto Reductase Family 1 Member C3, Androstenedione, Androsterone, Breast Neoplasms, 20-alpha-Dihydroprogesterone, Estradiol, Estrone, Etiocholanolone, Female, Humans, Hydroxyprostaglandin Dehydrogenases, Ketosteroids, Kinetics, Progesterone, Prostaglandins, Recombinant Proteins, Gonadal Steroid Hormones, Dihydrotestosterone, Testosterone, Transfection, 3-Hydroxysteroid Dehydrogenases, Prostaglandin D2, Dinoprost, Up-Regulation, Gene Expression Regulation, Neoplastic, 5-alpha-Dihydroprogesterone, Cell Line, Tumor, Cell Proliferation, Biocatalysis

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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

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