The emerging roles of histone demethylases in cancers.

Cancers Complex therapy strategies Histone demethylases Inhibitors

Journal

Cancer metastasis reviews
ISSN: 1573-7233
Titre abrégé: Cancer Metastasis Rev
Pays: Netherlands
ID NLM: 8605731

Informations de publication

Date de publication:
16 Jan 2024
Historique:
received: 26 04 2022
accepted: 05 12 2023
medline: 16 1 2024
pubmed: 16 1 2024
entrez: 16 1 2024
Statut: aheadofprint

Résumé

Modulation of histone methylation status is regarded as an important mechanism of epigenetic regulation and has substantial clinical potential for the therapy of diseases, including cancer and other disorders. The present study aimed to provide a comprehensive introduction to the enzymology of histone demethylases, as well as their cancerous roles, molecular mechanisms, therapeutic possibilities, and challenges for targeting them, in order to advance drug design for clinical therapy and highlight new insight into the mechanisms of these enzymes in cancer. A series of clinical trials have been performed to explore potential roles of histone demethylases in several cancer types. Numerous targeted inhibitors associated with immunotherapy, chemotherapy, radiotherapy, and targeted therapy have been used to exert anticancer functions. Future studies should evaluate the dynamic transformation of histone demethylases leading to carcinogenesis and explore individual therapy.

Identifiants

pubmed: 38227150
doi: 10.1007/s10555-023-10160-9
pii: 10.1007/s10555-023-10160-9
doi:

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Chongqing Municipal Public Health Bureau, Chongqing People's Municipal Government
ID : 2018QNXM041
Organisme : Chongqing Basic and Frontier Research Project
ID : cstc2018jcyjAX0645
Organisme : National Natural Science Foundation of China
ID : 81902302

Informations de copyright

© 2024. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.

Références

Huang, J., Sengupta, R., Espejo, A. B., Lee, M. G., Dorsey, J. A., Richter, M., Opravil, S., Shiekhattar, R., Bedford, M. T., Jenuwein, T., et al. (2007). p53 is regulated by the lysine demethylase LSD1. Nature, 449(7158), 105–108.
pubmed: 17805299 doi: 10.1038/nature06092
Wang, J., Hevi, S., Kurash, J. K., Lei, H., Gay, F., Bajko, J., Su, H., Sun, W., Chang, H., Xu, G., et al. (2009). The lysine demethylase LSD1 (KDM1) is required for maintenance of global DNA methylation. Nature Genetics, 41(1), 125–129.
pubmed: 19098913 doi: 10.1038/ng.268
Kontaki, H., & Talianidis, I. (2010). Lysine methylation regulates E2F1-induced cell death. Molecular Cell, 39(1), 152–160.
pubmed: 20603083 doi: 10.1016/j.molcel.2010.06.006
Lu, T., Jackson, M. W., Wang, B., Yang, M., Chance, M. R., Miyagi, M., Gudkov, A. V., & Stark, G. R. (2010). Regulation of NF-kappaB by NSD1/FBXL11-dependent reversible lysine methylation of p65. Proceedings of the National Academy of Sciences of the United States of America, 107(1), 46–51.
pubmed: 20080798 doi: 10.1073/pnas.0912493107
Chopra, A., Willmore, W. G., & Biggar, K. K. (2022). Insights into a cancer-target demethylase: substrate prediction through systematic specificity analysis for KDM3A. Biomolecules, 12(5), 641.
pubmed: 35625569 pmcid: 9139010 doi: 10.3390/biom12050641
Baba, A., Ohtake, F., Okuno, Y., Yokota, K., Okada, M., Imai, Y., Ni, M., Meyer, C. A., Igarashi, K., Kanno, J., et al. (2011). PKA-dependent regulation of the histone lysine demethylase complex PHF2-ARID5B. Nature Cell Biology, 13(6), 668–675.
pubmed: 21532585 doi: 10.1038/ncb2228
Feng, T., Yamamoto, A., Wilkins, S. E., Sokolova, E., Yates, L. A., Munzel, M., Singh, P., Hopkinson, R. J., Fischer, R., Cockman, M. E., et al. (2014). Optimal translational termination requires C4 lysyl hydroxylation of eRF1. Molecular Cell, 53(4), 645–654.
pubmed: 24486019 pmcid: 3991326 doi: 10.1016/j.molcel.2013.12.028
Shen, J., Xiang, X., Chen, L., Wang, H., Wu, L., Sun, Y., Ma, L., Gu, X., Liu, H., Wang, L., et al. (2017). JMJD5 cleaves monomethylated histone H3 N-tail under DNA damaging stress. EMBO Reports, 18(12), 2131–2143.
pubmed: 28982940 pmcid: 5709736 doi: 10.15252/embr.201743892
Liu, H., Wang, C., Lee, S., Ning, F., Wang, Y., Zhang, Q., Chen, Z., Zang, J., Nix, J., Dai, S., et al. (2018). Specific recognition of arginine methylated histone tails by JMJD5 and JMJD7. Science and Reports, 8(1), 3275.
doi: 10.1038/s41598-018-21432-8
Webby, C. J., Wolf, A., Gromak, N., Dreger, M., Kramer, H., Kessler, B., Nielsen, M. L., Schmitz, C., Butler, D. S., Yates, J. R., 3rd., et al. (2009). Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing. Science, 325(5936), 90–93.
pubmed: 19574390 doi: 10.1126/science.1175865
Mantri, M., Krojer, T., Bagg, E. A., Webby, C. A., Butler, D. S., Kochan, G., Kavanagh, K. L., Oppermann, U., McDonough, M. A., & Schofield, C. J. (2010). Crystal Structure of the 2-Oxoglutarate- and Fe(II)-Dependent Lysyl Hydroxylase JMJD6. Journal of Molecular Biology, 401(2), 211–222.
pubmed: 20684070 doi: 10.1016/j.jmb.2010.05.054
Sterling, J., Menezes, S. V., Abbassi, R. H., & Munoz, L. (2020). Histone lysine demethylases and their functions in cancer. International Journal of Cancer, 148(10), 2375–2388.
pubmed: 33128779 doi: 10.1002/ijc.33375
Hojfeldt, J. W., Agger, K., & Helin, K. (2013). Histone lysine demethylases as targets for anticancer therapy. Nature Reviews. Drug Discovery, 12(12), 917–930.
pubmed: 24232376 doi: 10.1038/nrd4154
Sarah, L., & Fujimori, D. (2023). Recent developments in catalysis and inhibition of the Jumonji histone demethylases. Current opinion in structural biology, 83, 102707.
pubmed: 37832177 pmcid: 10769511 doi: 10.1016/j.sbi.2023.102707
Dorna, D., Grabowska, A., & Paluszczak, J. (2023). Natural products modulating epigenetic mechanisms by affecting histone methylation/demethylation: Targeting cancer cells. British Journal of Pharmacology. https://doi.org/10.1111/bph.16237
doi: 10.1111/bph.16237 pubmed: 37700551
Young, D., Guha, C., & Sidoli, S. (2023). The role of histone H3 lysine demethylases in glioblastoma. Cancer and Metastasis Reviews, 42(2), 445–454.
pubmed: 37286866 doi: 10.1007/s10555-023-10114-1
Wu, C. Y., Hsieh, C. Y., Huang, K. E., Chang, C., & Kang, H. Y. (2012). Cryptotanshinone down-regulates androgen receptor signaling by modulating lysine-specific demethylase 1 function. International Journal of Cancer, 131(6), 1423–1434.
pubmed: 22052438 doi: 10.1002/ijc.27343
Gao, S., Chen, S., Han, D., Wang, Z., Li, M., Han, W., Besschetnova, A., Liu, M., Zhou, F., Barrett, D., et al. (2020). Chromatin binding of FOXA1 is promoted by LSD1-mediated demethylation in prostate cancer. Nature Genetics, 52(10), 1011–1017.
pubmed: 32868907 pmcid: 7541538 doi: 10.1038/s41588-020-0681-7
Regufe da Mota, S., Bailey, S., Strivens, R. A., Hayden, A. L., Douglas, L. R., Duriez, P. J., Borrello, M. T., Benelkebir, H., Ganesan, A., Packham, G., et al. (2018). LSD1 inhibition attenuates androgen receptor V7 splice variant activation in castration resistant prostate cancer models. Cancer Cell International, 18, 71.
pubmed: 29760584 pmcid: 5941811 doi: 10.1186/s12935-018-0568-1
Sehrawat, A., Gao, L., Wang, Y., Bankhead, A., 3rd., McWeeney, S. K., King, C. J., Schwartzman, J., Urrutia, J., Bisson, W. H., Coleman, D. J., et al. (2018). LSD1 activates a lethal prostate cancer gene network independently of its demethylase function. Proceedings of the National Academy of Sciences of the United States of America, 115(18), E4179–E4188.
pubmed: 29581250 pmcid: 5939079
Wang, Z., Gao, S., Han, D., Han, W., Li, M., & Cai, C. (2019). LSD1 activates PI3K/AKT signaling through regulating p85 expression in prostate cancer cells. Frontiers in Oncology, 9, 721.
pubmed: 31428587 pmcid: 6688199 doi: 10.3389/fonc.2019.00721
Gupta, S., Weston, A., Bearrs, J., Thode, T., Neiss, A., Soldi, R., & Sharma, S. (2016). Reversible lysine-specific demethylase 1 antagonist HCI-2509 inhibits growth and decreases c-MYC in castration- and docetaxel-resistant prostate cancer cells. Prostate Cancer and Prostatic Diseases, 19(4), 349–357.
pubmed: 27349498 pmcid: 5133270 doi: 10.1038/pcan.2016.21
Coleman, D. J., Sampson, D. A., Sehrawat, A., Kumaraswamy, A., Sun, D., Wang, Y., Schwartzman, J., Urrutia, J., Lee, A. R., Coleman, I. M., et al. (2020). Alternative splicing of LSD1+8a in neuroendocrine prostate cancer is mediated by SRRM4. Neoplasia, 22(6), 253–262.
pubmed: 32403054 pmcid: 7218227 doi: 10.1016/j.neo.2020.04.002
Cai, C., He, H. H., Chen, S., Coleman, I., Wang, H., Fang, Z., Nelson, P. S., Liu, X. S., Brown, M., & Balk, S. P. (2011). Androgen receptor gene expression in prostate cancer is directly suppressed by the androgen receptor through recruitment of lysine-specific demethylase 1. Cancer Cell, 20(4), 457–471.
pubmed: 22014572 pmcid: 3225024 doi: 10.1016/j.ccr.2011.09.001
Cortez, V., Mann, M., Tekmal, S., Suzuki, T., Miyata, N., Rodriguez-Aguayo, C., Lopez-Berestein, G., Sood, A. K., & Vadlamudi, R. K. (2012). Targeting the PELP1-KDM1 axis as a potential therapeutic strategy for breast cancer. Breast Cancer Research, 14(4), R108.
pubmed: 22812534 pmcid: 3680946 doi: 10.1186/bcr3229
Bennani-Baiti, I. M. (2012). Integration of ERalpha-PELP1-HER2 signaling by LSD1 (KDM1A/AOF2) offers combinatorial therapeutic opportunities to circumventing hormone resistance in breast cancer. Breast Cancer Research, 14(5), 112.
pubmed: 22992372 pmcid: 4053100 doi: 10.1186/bcr3249
Lim, S., Janzer, A., Becker, A., Zimmer, A., Schule, R., Buettner, R., & Kirfel, J. (2010). Lysine-specific demethylase 1 (LSD1) is highly expressed in ER-negative breast cancers and a biomarker predicting aggressive biology. Carcinogenesis, 31(3), 512–520.
pubmed: 20042638 doi: 10.1093/carcin/bgp324
Pollock, J. A., Larrea, M. D., Jasper, J. S., McDonnell, D. P., & McCafferty, D. G. (2012). Lysine-specific histone demethylase 1 inhibitors control breast cancer proliferation in ERalpha-dependent and -independent manners. ACS Chemical Biology, 7(7), 1221–1231.
pubmed: 22533360 pmcid: 3582702 doi: 10.1021/cb300108c
Kim, J., Park, U. H., Moon, M., Um, S. J., & Kim, E. J. (2013). Negative regulation of ERalpha by a novel protein CAC1 through association with histone demethylase LSD1. FEBS Letters, 587(1), 17–22.
pubmed: 23178685 doi: 10.1016/j.febslet.2012.10.054
Grimaldi, P., Pucci, M., Di Siena, S., Di Giacomo, D., Pirazzi, V., Geremia, R., & Maccarrone, M. (2012). The faah gene is the first direct target of estrogen in the testis: Role of histone demethylase LSD1. Cellular and Molecular Life Sciences, 69(24), 4177–4190.
pubmed: 22802127 doi: 10.1007/s00018-012-1074-6
Cao, C., Vasilatos, S. N., Bhargava, R., Fine, J. L., Oesterreich, S., Davidson, N. E., & Huang, Y. (2017). Functional interaction of histone deacetylase 5 (HDAC5) and lysine-specific demethylase 1 (LSD1) promotes breast cancer progression. Oncogene, 36(1), 133–145.
pubmed: 27212032 doi: 10.1038/onc.2016.186
Vasilatos, S. N., Katz, T. A., Oesterreich, S., Wan, Y., Davidson, N. E., & Huang, Y. (2013). Crosstalk between lysine-specific demethylase 1 (LSD1) and histone deacetylases mediates antineoplastic efficacy of HDAC inhibitors in human breast cancer cells. Carcinogenesis, 34(6), 1196–1207.
pubmed: 23354309 pmcid: 3670252 doi: 10.1093/carcin/bgt033
Zhou, M., Venkata, P. P., Viswanadhapalli, S., Palacios, B., Alejo, S., Chen, Y., He, Y., Pratap, U. P., Liu, J., Zou, Y., et al. (2021). KDM1A inhibition is effective in reducing stemness and treating triple negative breast cancer. Breast Cancer Research and Treatment, 185(2), 343–357.
pubmed: 33057995 doi: 10.1007/s10549-020-05963-1
Hu, X., Xiang, D., Xie, Y., Tao, L., Zhang, Y., Jin, Y., Pinello, L., Wan, Y., Yuan, G. C., & Li, Z. (2019). LSD1 suppresses invasion, migration and metastasis of luminal breast cancer cells via activation of GATA3 and repression of TRIM37 expression. Oncogene, 38(44), 7017–7034.
pubmed: 31409898 pmcid: 6823153 doi: 10.1038/s41388-019-0923-2
Wang, Y., Zhang, H., Chen, Y., Sun, Y., Yang, F., Yu, W., Liang, J., Sun, L., Yang, X., Shi, L., et al. (2009). LSD1 is a subunit of the NuRD complex and targets the metastasis programs in breast cancer. Cell, 138(4), 660–672.
pubmed: 19703393 doi: 10.1016/j.cell.2009.05.050
Malagraba, G., Yarmohammadi, M., Javed, A., Barcelo, C., & Rubio-Tomas, T. (2022). The Role of LSD1 and LSD2 in Cancers of the Gastrointestinal System: An Update. Biomolecules, 12(3), 462.
pubmed: 35327654 pmcid: 8946813 doi: 10.3390/biom12030462
Magerl, C., Ellinger, J., Braunschweig, T., Kremmer, E., Koch, L. K., Holler, T., Buttner, R., Luscher, B., & Gutgemann, I. (2010). H3K4 dimethylation in hepatocellular carcinoma is rare compared with other hepatobiliary and gastrointestinal carcinomas and correlates with expression of the methylase Ash2 and the demethylase LSD1. Human Pathology, 41(2), 181–189.
pubmed: 19896696 doi: 10.1016/j.humpath.2009.08.007
Xu, T. P., Wang, W. Y., Ma, P., Shuai, Y., Zhao, K., Wang, Y. F., Li, W., Xia, R., Chen, W. M., Zhang, E. B., et al. (2018). Upregulation of the long noncoding RNA FOXD2-AS1 promotes carcinogenesis by epigenetically silencing EphB3 through EZH2 and LSD1, and predicts poor prognosis in gastric cancer. Oncogene, 37(36), 5020–5036.
pubmed: 29789713 doi: 10.1038/s41388-018-0308-y
Sun, M., Nie, F., Wang, Y., Zhang, Z., Hou, J., He, D., Xie, M., Xu, L., De, W., Wang, Z., et al. (2016). LncRNA HOXA11-AS promotes proliferation and invasion of gastric cancer by scaffolding the chromatin modification factors PRC2, LSD1, and DNMT1. Cancer Research, 76(21), 6299–6310.
pubmed: 27651312 doi: 10.1158/0008-5472.CAN-16-0356
Ding, J., Xie, M., Lian, Y., Zhu, Y., Peng, P., Wang, J., Wang, L., & Wang, K. (2017). Long noncoding RNA HOXA-AS2 represses P21 and KLF2 expression transcription by binding with EZH2, LSD1 in colorectal cancer. Oncogenesis, 6(1), e288.
pubmed: 28112720 pmcid: 5294247 doi: 10.1038/oncsis.2016.84
Wang, Y., Sun, L., Luo, Y., & He, S. (2019). Knockdown of KDM1B inhibits cell proliferation and induces apoptosis of pancreatic cancer cells. Pathology, Research and Practice, 215(5), 1054–1060.
pubmed: 30846414 doi: 10.1016/j.prp.2019.02.014
Cai, S., Wang, J., Zeng, W., Cheng, X., Liu, L., & Li, W. (2020). Lysine-specific histone demethylase 1B (LSD2/KDM1B) represses p53 expression to promote proliferation and inhibit apoptosis in colorectal cancer through LSD2-mediated H3K4me2 demethylation. Aging (Albany NY), 12(14), 14990–15001.
pubmed: 32726297 doi: 10.18632/aging.103558
Huang, Y., Yin, Y., & Sun, M. (2018). Targeting LSD2 in breast cancer. Aging (Albany NY), 10(1), 11–12.
pubmed: 29356682 doi: 10.18632/aging.101371
Chen, J. Y., Luo, C. W., Lai, Y. S., Wu, C. C., & Hung, W. C. (2017). Lysine demethylase KDM2A inhibits TET2 to promote DNA methylation and silencing of tumor suppressor genes in breast cancer. Oncogenesis, 6(8), e369.
pubmed: 28785073 pmcid: 5608919 doi: 10.1038/oncsis.2017.71
Zhao, Y., Chen, X., Jiang, J., Wan, X., Wang, Y., & Xu, P. (2020). Epigallocatechin gallate reverses gastric cancer by regulating the long noncoding RNA LINC00511/miR-29b/KDM2A axis. Biochimica et Biophysica Acta, Molecular Basis of Disease, 1866(10), 165856.
pubmed: 32512188 doi: 10.1016/j.bbadis.2020.165856
Kong, Y., Zou, S., Yang, F., Xu, X., Bu, W., Jia, J., & Liu, Z. (2016). RUNX3-mediated up-regulation of miR-29b suppresses the proliferation and migration of gastric cancer cells by targeting KDM2A. Cancer Letters, 381(1), 138–148.
pubmed: 27497248 doi: 10.1016/j.canlet.2016.07.038
Suzuki, T., Minehata, K., Akagi, K., Jenkins, N. A., & Copeland, N. G. (2006). Tumor suppressor gene identification using retroviral insertional mutagenesis in Blm-deficient mice. EMBO Journal, 25(14), 3422–3431.
pubmed: 16858412 pmcid: 1523184 doi: 10.1038/sj.emboj.7601215
Pfau, R., Tzatsos, A., Kampranis, S. C., Serebrennikova, O. B., Bear, S. E., & Tsichlis, P. N. (2008). Members of a family of JmjC domain-containing oncoproteins immortalize embryonic fibroblasts via a JmjC domain-dependent process. Proceedings of the National Academy of Sciences of the United States of America, 105(6), 1907–1912.
pubmed: 18250326 pmcid: 2538857 doi: 10.1073/pnas.0711865105
Frescas, D., Guardavaccaro, D., Bassermann, F., Koyama-Nasu, R., & Pagano, M. (2007). JHDM1B/FBXL10 is a nucleolar protein that represses transcription of ribosomal RNA genes. Nature, 450(7167), 309–313.
pubmed: 17994099 doi: 10.1038/nature06255
Frescas, D., Guardavaccaro, D., Kuchay, S. M., Kato, H., Poleshko, A., Basrur, V., Elenitoba-Johnson, K. S., Katz, R. A., & Pagano, M. (2008). KDM2A represses transcription of centromeric satellite repeats and maintains the heterochromatic state. Cell Cycle, 7(22), 3539–3547.
pubmed: 19001877 doi: 10.4161/cc.7.22.7062
Pedersen, M. T., & Helin, K. (2010). Histone demethylases in development and disease. Trends in Cell Biology, 20(11), 662–671.
pubmed: 20863703 doi: 10.1016/j.tcb.2010.08.011
Ueda, T., Nagamachi, A., Takubo, K., Yamasaki, N., Matsui, H., Kanai, A., Nakata, Y., Ikeda, K., Konuma, T., Oda, H., et al. (2015). Fbxl10 overexpression in murine hematopoietic stem cells induces leukemia involving metabolic activation and upregulation of Nsg2. Blood, 125(22), 3437–3446.
pubmed: 25872778 pmcid: 4447860 doi: 10.1182/blood-2014-03-562694
He, J., Nguyen, A. T., & Zhang, Y. (2011). KDM2b/JHDM1b, an H3K36me2-specific demethylase, is required for initiation and maintenance of acute myeloid leukemia. Blood, 117(14), 3869–3880.
pubmed: 21310926 pmcid: 3083299 doi: 10.1182/blood-2010-10-312736
Zhao, X., Wang, X., Li, Q., Chen, W., Zhang, N., Kong, Y., Lv, J., Cao, L., Lin, D., Xu, G., et al. (2018). FBXL10 contributes to the development of diffuse large B-cell lymphoma by epigenetically enhancing ERK1/2 signaling pathway. Cell Death & Disease, 9(2), 46.
doi: 10.1038/s41419-017-0066-8
Tzatsos, A., Paskaleva, P., Lymperi, S., Contino, G., Stoykova, S., Chen, Z., Wong, K. K., & Bardeesy, N. (2011). Lysine-specific demethylase 2B (KDM2B)-let-7-enhancer of zester homolog 2 (EZH2) pathway regulates cell cycle progression and senescence in primary cells. Journal of Biological Chemistry, 286(38), 33061–33069.
pubmed: 21757686 pmcid: 3190920 doi: 10.1074/jbc.M111.257667
Yan, M., Yang, X., Shen, R., Wu, C., Wang, H., Ye, Q., Yang, P., Zhang, L., Chen, M., Wan, B., et al. (2018). miR-146b promotes cell proliferation and increases chemosensitivity, but attenuates cell migration and invasion via FBXL10 in ovarian cancer. Cell Death & Disease, 9(11), 1123.
doi: 10.1038/s41419-018-1093-9
Koyama-Nasu, R., David, G., & Tanese, N. (2007). The F-box protein Fbl10 is a novel transcriptional repressor of c-Jun. Nature Cell Biology, 9(9), 1074–1080.
pubmed: 17704768 doi: 10.1038/ncb1628
Polytarchou, C., Pfau, R., Hatziapostolou, M., & Tsichlis, P. N. (2008). The JmjC domain histone demethylase Ndy1 regulates redox homeostasis and protects cells from oxidative stress. Molecular and Cellular Biology, 28(24), 7451–7464.
pubmed: 18838535 pmcid: 2593427 doi: 10.1128/MCB.00688-08
Han, X. R., Zha, Z., Yuan, H. X., Feng, X., Xia, Y. K., Lei, Q. Y., Guan, K. L., & Xiong, Y. (2016). KDM2B/FBXL10 targets c-Fos for ubiquitylation and degradation in response to mitogenic stimulation. Oncogene, 35(32), 4179–4190.
pubmed: 26725323 pmcid: 4931990 doi: 10.1038/onc.2015.482
Beyer, S., Kristensen, M. M., Jensen, K. S., Johansen, J. V., & Staller, P. (2008). The histone demethylases JMJD1A and JMJD2B are transcriptional targets of hypoxia-inducible factor HIF. Journal of Biological Chemistry, 283(52), 36542–36552.
pubmed: 18984585 pmcid: 2662309 doi: 10.1074/jbc.M804578200
Krieg, A. J., Rankin, E. B., Chan, D., Razorenova, O., Fernandez, S., & Giaccia, A. J. (2010). Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1 alpha enhances hypoxic gene expression and tumor growth. Molecular and Cellular Biology, 30(1), 344–353.
pubmed: 19858293 doi: 10.1128/MCB.00444-09
Pollard, P. J., Loenarz, C., Mole, D. R., McDonough, M. A., Gleadle, J. M., Schofield, C. J., & Ratcliffe, P. J. (2008). Regulation of Jumonji-domain-containing histone demethylases by hypoxia-inducible factor (HIF)-1alpha. The Biochemical Journal, 416(3), 387–394.
pubmed: 18713068 doi: 10.1042/BJ20081238
Wan, W., Peng, K., Li, M., Qin, L., Tong, Z., Yan, J., Shen, B., & Yu, C. (2017). Histone demethylase JMJD1A promotes urinary bladder cancer progression by enhancing glycolysis through coactivation of hypoxia inducible factor 1alpha. Oncogene, 36(27), 3868–3877.
pubmed: 28263974 doi: 10.1038/onc.2017.13
Mimura, I., Nangaku, M., Kanki, Y., Tsutsumi, S., Inoue, T., Kohro, T., Yamamoto, S., Fujita, T., Shimamura, T., Suehiro, J., et al. (2012). Dynamic change of chromatin conformation in response to hypoxia enhances the expression of GLUT3 (SLC2A3) by cooperative interaction of hypoxia-inducible factor 1 and KDM3A. Molecular and Cellular Biology, 32(15), 3018–3032.
pubmed: 22645302 pmcid: 3434521 doi: 10.1128/MCB.06643-11
Yamane, K., Toumazou, C., Tsukada, Y., Erdjument-Bromage, H., Tempst, P., Wong, J., & Zhang, Y. (2006). JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor. Cell, 125(3), 483–495.
pubmed: 16603237 doi: 10.1016/j.cell.2006.03.027
Xu, S., Fan, L., Jeon, H. Y., Zhang, F., Cui, X., Mickle, M. B., Peng, G., Hussain, A., Fazli, L., Gleave, M. E., et al. (2020). p300-mediated acetylation of histone demethylase JMJD1A prevents its degradation by ubiquitin ligase STUB1 and enhances its activity in prostate cancer. Cancer Research, 80(15), 3074–3087.
pubmed: 32522824 pmcid: 7415556 doi: 10.1158/0008-5472.CAN-20-0233
Fan, L., Zhang, F., Xu, S., Cui, X., Hussain, A., Fazli, L., Gleave, M., Dong, X., & Qi, J. (2018). Histone demethylase JMJD1A promotes alternative splicing of AR variant 7 (AR-V7) in prostate cancer cells. Proc Natl Acad Sci U S A, 115(20), E4584–E4593.
pubmed: 29712835 pmcid: 5960326 doi: 10.1073/pnas.1802415115
Tang, D. E., Dai, Y., Fan, L. L., Geng, X. Y., Fu, D. X., Jiang, H. W., & Xu, S. H. (2020). Histone demethylase JMJD1A promotes tumor progression via activating snail in prostate cancer. Molecular Cancer Research, 18(5), 698–708.
pubmed: 32019811 doi: 10.1158/1541-7786.MCR-19-0889
Fan, L., Xu, S., Zhang, F., Cui, X., Fazli, L., Gleave, M., Clark, D. J., Yang, A., Hussain, A., Rassool, F., et al. (2020). Histone demethylase JMJD1A promotes expression of DNA repair factors and radio-resistance of prostate cancer cells. Cell Death & Disease, 11(4), 214.
doi: 10.1038/s41419-020-2405-4
Kim, J. Y., Kim, K. B., Eom, G. H., Choe, N., Kee, H. J., Son, H. J., Oh, S. T., Kim, D. W., Pak, J. H., Baek, H. J., et al. (2012). KDM3B is the H3K9 demethylase involved in transcriptional activation of lmo2 in leukemia. Molecular and Cellular Biology, 32(14), 2917–2933.
pubmed: 22615488 pmcid: 3416203 doi: 10.1128/MCB.00133-12
Nakamura, S., Tan, L., Nagata, Y., Takemura, T., Asahina, A., Yokota, D., Yagyu, T., Shibata, K., Fujisawa, S., & Ohnishi, K. (2013). JmjC-domain containing histone demethylase 1B-mediated p15(Ink4b) suppression promotes the proliferation of leukemic progenitor cells through modulation of cell cycle progression in acute myeloid leukemia. Molecular Carcinogenesis, 52(1), 57–69.
pubmed: 22086844 doi: 10.1002/mc.20878
Hu, Z., Gomes, I., Horrigan, S. K., Kravarusic, J., Mar, B., Arbieva, Z., Chyna, B., Fulton, N., Edassery, S., Raza, A., et al. (2001). A novel nuclear protein, 5qNCA (LOC51780) is a candidate for the myeloid leukemia tumor suppressor gene on chromosome 5 band q31. Oncogene, 20(47), 6946–6954.
pubmed: 11687974 doi: 10.1038/sj.onc.1204850
Sui, Y., Gu, R., & Janknecht, R. (2021). Crucial functions of the JMJD1/KDM3 epigenetic regulators in cancer. Molecular Cancer Research, 19(1), 3–13.
pubmed: 32605929 doi: 10.1158/1541-7786.MCR-20-0404
Saavedra, F., Gurard-Levin, Z. A., Rojas-Villalobos, C., Vassias, I., Quatrini, R., Almouzni, G., & Loyola, A. (2020). JMJD1B, a novel player in histone H3 and H4 processing to ensure genome stability. Epigenetics & Chromatin, 13(1), 6.
doi: 10.1186/s13072-020-00331-1
Peeken, J. C., Jutzi, J. S., Wehrle, J., Koellerer, C., Staehle, H. F., Becker, H., Schoenwandt, E., Seeger, T. S., Schanne, D. H., Gothwal, M., et al. (2018). Epigenetic regulation of NFE2 overexpression in myeloproliferative neoplasms. Blood, 131(18), 2065–2073.
pubmed: 29519804 pmcid: 5934799 doi: 10.1182/blood-2017-10-810622
Izaguirre-Carbonell, J., Christiansen, L., Burns, R., Schmitz, J., Li, C., Mokry, R. L., Bluemn, T., Zheng, Y., Shen, J., Carlson, K. S., et al. (2019). Critical role of Jumonji domain of JMJD1C in MLL-rearranged leukemia. Blood Advances, 3(9), 1499–1511.
pubmed: 31076406 pmcid: 6517669 doi: 10.1182/bloodadvances.2018026054
Zhu, N., Chen, M., Eng, R., DeJong, J., Sinha, A. U., Rahnamay, N. F., Koche, R., Al-Shahrour, F., Minehart, J. C., Chen, C. W., et al. (2016). MLL-AF9- and HOXA9-mediated acute myeloid leukemia stem cell self-renewal requires JMJD1C. The Journal of Clinical Investigation, 126(3), 997–1011.
pubmed: 26878175 pmcid: 4767347 doi: 10.1172/JCI82978
Lynch, J. R., Salik, B., Connerty, P., Vick, B., Leung, H., Pijning, A., Jeremias, I., Spiekermann, K., Trahair, T., Liu, T., et al. (2019). JMJD1C-mediated metabolic dysregulation contributes to HOXA9-dependent leukemogenesis. Leukemia, 33(6), 1400–1410.
pubmed: 30622285 doi: 10.1038/s41375-018-0354-z
Chen, M., Zhu, N., Liu, X., Laurent, B., Tang, Z., Eng, R., Shi, Y., Armstrong, S. A., & Roeder, R. G. (2015). JMJD1C is required for the survival of acute myeloid leukemia by functioning as a coactivator for key transcription factors. Genes & Development, 29(20), 2123–2139.
doi: 10.1101/gad.267278.115
Schimek, V., Bjorn, N., Pelle, L., Svedberg, A., & Green, H. (2021). JMJD1C knockdown affects myeloid cell lines proliferation, viability, and gemcitabine/carboplatin-sensitivity. Pharmacogenetics and Genomics, 31(3), 60–67.
pubmed: 33075016 doi: 10.1097/FPC.0000000000000422
Xu, X., Wang, L., Hu, L., Dirks, W. G., Zhao, Y., Wei, Z., Chen, D., Li, Z., Wang, Z., Han, Y., et al. (2020). Small molecular modulators of JMJD1C preferentially inhibit growth of leukemia cells. International Journal of Cancer, 146(2), 400–412.
pubmed: 31271662 doi: 10.1002/ijc.32552
Black, J. C., Allen, A., Van Rechem, C., Forbes, E., Longworth, M., Tschop, K., Rinehart, C., Quiton, J., Walsh, R., Smallwood, A., et al. (2010). Conserved antagonism between JMJD2A/KDM4A and HP1gamma during cell cycle progression. Molecular Cell, 40(5), 736–748.
pubmed: 21145482 doi: 10.1016/j.molcel.2010.11.008
Kim, T. D., Shin, S., Berry, W. L., Oh, S., & Janknecht, R. (2012). The JMJD2A demethylase regulates apoptosis and proliferation in colon cancer cells. Journal of Cellular Biochemistry, 113(4), 1368–1376.
pubmed: 22134899 doi: 10.1002/jcb.24009
Gray, S. G., Iglesias, A. H., Lizcano, F., Villanueva, R., Camelo, S., Jingu, H., Teh, B. T., Koibuchi, N., Chin, W. W., Kokkotou, E., et al. (2005). Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein. Journal of Biological Chemistry, 280(31), 28507–28518.
pubmed: 15927959 doi: 10.1074/jbc.M413687200
Li, B. X., Zhang, M. C., Luo, C. L., Yang, P., Li, H., Xu, H. M., Xu, H. F., Shen, Y. W., Xue, A. M., & Zhao, Z. Q. (2011). Effects of RNA interference-mediated gene silencing of JMJD2A on human breast cancer cell line MDA-MB-231 in vitro. Journal of Experimental & Clinical Cancer Research, 30, 90.
doi: 10.1186/1756-9966-30-90
Berry, W. L., Shin, S., Lightfoot, S. A., & Janknecht, R. (2012). Oncogenic features of the JMJD2A histone demethylase in breast cancer. International Journal of Oncology, 41(5), 1701–1706.
pubmed: 22948256 doi: 10.3892/ijo.2012.1618
Zhang, J., Li, Q., Zhang, S., Xu, Q., & Wang, T. (2016). Lgr4 promotes prostate tumorigenesis through the Jmjd2a/AR signaling pathway. Experimental Cell Research, 349(1), 77–84.
pubmed: 27743893 doi: 10.1016/j.yexcr.2016.09.023
Cui, S. Z., Lei, Z. Y., Guan, T. P., Fan, L. L., Li, Y. Q., Geng, X. Y., Fu, D. X., Jiang, H. W., & Xu, S. H. (2020). Targeting USP1-dependent KDM4A protein stability as a potential prostate cancer therapy. Cancer Science, 111(5), 1567–1581.
pubmed: 32133742 pmcid: 7226285 doi: 10.1111/cas.14375
Kim, J. G., Yi, J. M., Park, S. J., Kim, J. S., Son, T. G., Yang, K., Yoo, M. A., & Heo, K. (2012). Histone demethylase JMJD2B-mediated cell proliferation regulated by hypoxia and radiation in gastric cancer cell. Biochimica et Biophysica Acta, 1819(11–12), 1200–1207.
pubmed: 23046878 doi: 10.1016/j.bbagrm.2012.10.001
Fu, L., Chen, L., Yang, J., Ye, T., Chen, Y., & Fang, J. (2012). HIF-1alpha-induced histone demethylase JMJD2B contributes to the malignant phenotype of colorectal cancer cells via an epigenetic mechanism. Carcinogenesis, 33(9), 1664–1673.
pubmed: 22745382 doi: 10.1093/carcin/bgs217
Yang, J., Jubb, A. M., Pike, L., Buffa, F. M., Turley, H., Baban, D., Leek, R., Gatter, K. C., Ragoussis, J., & Harris, A. L. (2010). The histone demethylase JMJD2B is regulated by estrogen receptor alpha and hypoxia, and is a key mediator of estrogen induced growth. Cancer Research, 70(16), 6456–6466.
pubmed: 20682797 pmcid: 4261152 doi: 10.1158/0008-5472.CAN-10-0413
Shi, L., Sun, L., Li, Q., Liang, J., Yu, W., Yi, X., Yang, X., Li, Y., Han, X., Zhang, Y., et al. (2011). Histone demethylase JMJD2B coordinates H3K4/H3K9 methylation and promotes hormonally responsive breast carcinogenesis. Proceedings of the National Academy of Sciences of the United States of America, 108(18), 7541–7546.
pubmed: 21502505 pmcid: 3088624 doi: 10.1073/pnas.1017374108
Kawazu, M., Saso, K., Tong, K. I., McQuire, T., Goto, K., Son, D. O., Wakeham, A., Miyagishi, M., Mak, T. W., & Okada, H. (2011). Histone demethylase JMJD2B functions as a co-factor of estrogen receptor in breast cancer proliferation and mammary gland development. PLoS ONE, 6(3), e17830.
pubmed: 21445275 pmcid: 3060874 doi: 10.1371/journal.pone.0017830
Hui, Z., Yiling, C., Wenting, Y., XuQun, H., ChuanYi, Z., & Hui, L. (2015). miR-491-5p functions as a tumor suppressor by targeting JMJD2B in ERalpha-positive breast cancer. FEBS Letters, 589(7), 812–821.
pubmed: 25725194 doi: 10.1016/j.febslet.2015.02.014
Castellini, L., Moon, E. J., Razorenova, O. V., Krieg, A. J., von Eyben, R., & Giaccia, A. J. (2017). KDM4B/JMJD2B is a p53 target gene that modulates the amplitude of p53 response after DNA damage. Nucleic Acids Research, 45(7), 3674–3692.
pubmed: 28073943 pmcid: 5397198
Zheng, H., Chen, L., Pledger, W. J., Fang, J., & Chen, J. (2013). p53 promotes repair of heterochromatin DNA by regulating JMJD2b and SUV39H1 expression. Oncogene, 33(6), 734–744.
pubmed: 23376847 pmcid: 3912226 doi: 10.1038/onc.2013.6
Duan, L., Perez, R. E., Lai, X., Chen, L., & Maki, C. G. (2019). The histone demethylase JMJD2B is critical for p53-mediated autophagy and survival in Nutlin-treated cancer cells. Journal of Biological Chemistry, 294(23), 9186–9197.
pubmed: 31036564 pmcid: 6556578 doi: 10.1074/jbc.RA118.007122
Liu, L., Yu, T., Jin, Y., Mai, W., Zhou, J., & Zhao, C. (2021). MicroRNA-15a carried by mesenchymal stem cell-derived extracellular vesicles inhibits the immune evasion of colorectal cancer cells by regulating the KDM4B/HOXC4/PD-L1 Axis. Frontiers in Cell and Developmental Biology, 9, 629893.
pubmed: 33732698 pmcid: 7959841 doi: 10.3389/fcell.2021.629893
Tang, D. E., Dai, Y., He, J. X., Lin, L. W., Leng, Q. X., Geng, X. Y., Fu, D. X., Jiang, H. W., & Xu, S. H. (2020). Targeting the KDM4B-AR-c-Myc axis promotes sensitivity to androgen receptor-targeted therapy in advanced prostate cancer. The Journal of Pathology, 252(2), 101–113.
pubmed: 32617978 doi: 10.1002/path.5495
Duan, L., Chen, Z., Lu, J., Liang, Y., Wang, M., Roggero, C. M., Zhang, Q. J., Gao, J., Fang, Y., Cao, J., et al. (2019). Histone lysine demethylase KDM4B regulates the alternative splicing of the androgen receptor in response to androgen deprivation. Nucleic Acids Research, 47(22), 11623–11636.
pubmed: 31647098 pmcid: 7145715
Sha, J., Han, Q., Chi, C., Zhu, Y., Pan, J., Dong, B., Huang, Y., Xia, W., & Xue, W. (2020). Upregulated KDM4B promotes prostate cancer cell proliferation by activating autophagy. Journal of Cellular Physiology, 235(3), 2129–2138.
pubmed: 31468537 doi: 10.1002/jcp.29117
Margareto, J., Leis, O., Larrarte, E., Pomposo, I. C., Garibi, J. M., & Lafuente, J. V. (2009). DNA copy number variation and gene expression analyses reveal the implication of specific oncogenes and genes in GBM. Cancer Investigation, 27(5), 541–548.
pubmed: 19219654 doi: 10.1080/07357900802563044
Ehrbrecht, A., Muller, U., Wolter, M., Hoischen, A., Koch, A., Radlwimmer, B., Actor, B., Mincheva, A., Pietsch, T., Lichter, P., et al. (2006). Comprehensive genomic analysis of desmoplastic medulloblastomas: Identification of novel amplified genes and separate evaluation of the different histological components. The Journal of Pathology, 208(4), 554–563.
pubmed: 16400626 doi: 10.1002/path.1925
Italiano, A., Attias, R., Aurias, A., Perot, G., Burel-Vandenbos, F., Otto, J., Venissac, N., & Pedeutour, F. (2006). Molecular cytogenetic characterization of a metastatic lung sarcomatoid carcinoma: 9p23 neocentromere and 9p23-p24 amplification including JAK2 and JMJD2C. Cancer Genetics and Cytogenetics, 167(2), 122–130.
pubmed: 16737911 doi: 10.1016/j.cancergencyto.2006.01.004
Helias, C., Struski, S., Gervais, C., Leymarie, V., Mauvieux, L., Herbrecht, R., & Lessard, M. (2008). Polycythemia vera transforming to acute myeloid leukemia and complex abnormalities including 9p homogeneously staining region with amplification of MLLT3, JMJD2C, JAK2, and SMARCA2. Cancer Genetics and Cytogenetics, 180(1), 51–55.
pubmed: 18068534 doi: 10.1016/j.cancergencyto.2007.09.010
Nacheva, E. P., Brazma, D., Virgili, A., Howard-Reeves, J., Chanalaris, A., Gancheva, K., Apostolova, M., Valganon, M., Mazzullo, H., & Grace, C. (2010). Deletions of immunoglobulin heavy chain and T cell receptor gene regions are uniquely associated with lymphoid blast transformation of chronic myeloid leukemia. BMC Genomics, 11, 41.
pubmed: 20082691 pmcid: 2822760 doi: 10.1186/1471-2164-11-41
Vinatzer, U., Gollinger, M., Mullauer, L., Raderer, M., Chott, A., & Streubel, B. (2008). Mucosa-associated lymphoid tissue lymphoma: Novel translocations including rearrangements of ODZ2, JMJD2C, and CNN3. Clinical Cancer Research, 14(20), 6426–6431.
pubmed: 18927281 doi: 10.1158/1078-0432.CCR-08-0702
Liu, G., Bollig-Fischer, A., Kreike, B., van de Vijver, M. J., Abrams, J., Ethier, S. P., & Yang, Z. Q. (2009). Genomic amplification and oncogenic properties of the GASC1 histone demethylase gene in breast cancer. Oncogene, 28(50), 4491–4500.
pubmed: 19784073 pmcid: 2795798 doi: 10.1038/onc.2009.297
Berdel, B., Nieminen, K., Soini, Y., Tengstrom, M., Malinen, M., Kosma, V. M., Palvimo, J., & Mannermaa, A. (2012). Histone demethylase GASC1—A potential prognostic and predictive marker in invasive breast cancer. BMC Cancer, 12(1), 516.
pubmed: 23148692 pmcid: 3547738 doi: 10.1186/1471-2407-12-516
Han, W., Jung, E. M., Cho, J., Lee, J. W., Hwang, K. T., Yang, S. J., Kang, J. J., Bae, J. Y., Jeon, Y. K., Park, I. A., et al. (2008). DNA copy number alterations and expression of relevant genes in triple-negative breast cancer. Genes, Chromosomes & Cancer, 47(6), 490–499.
doi: 10.1002/gcc.20550
Wu, J., Liu, S., Liu, G., Dombkowski, A., Abrams, J., Martin-Trevino, R., Wicha, M. S., Ethier, S. P., & Yang, Z. Q. (2012). Identification and functional analysis of 9p24 amplified genes in human breast cancer. Oncogene, 31(3), 333–341.
pubmed: 21666724 doi: 10.1038/onc.2011.227
Rui, L., Emre, N. C., Kruhlak, M. J., Chung, H. J., Steidl, C., Slack, G., Wright, G. W., Lenz, G., Ngo, V. N., Shaffer, A. L., et al. (2010). Cooperative epigenetic modulation by cancer amplicon genes. Cancer Cell, 18(6), 590–605.
pubmed: 21156283 pmcid: 3049192 doi: 10.1016/j.ccr.2010.11.013
Peng, K., Zhuo, M., Li, M., Chen, Q., Mo, P., & Yu, C. (2020). Histone demethylase JMJD2D activates HIF1 signaling pathway via multiple mechanisms to promote colorectal cancer glycolysis and progression. Oncogene, 39(47), 7076–7091.
pubmed: 32989255 doi: 10.1038/s41388-020-01483-w
Deng, Y., Li, M., Zhuo, M., Guo, P., Chen, Q., Mo, P., Li, W., & Yu, C. (2021). Histone demethylase JMJD2D promotes the self-renewal of liver cancer stem-like cells by enhancing EpCAM and Sox9 expression. Journal of Biological Chemistry, 296, 100121.
Yang, G. J., Zhu, M. H., Lu, X. J., Liu, Y. J., Lu, J. F., Leung, C. H., Ma, D. L., & Chen, J. (2021). The emerging role of KDM5A in human cancer. Journal of Hematology & Oncology, 14(1), 30.
doi: 10.1186/s13045-021-01041-1
Yang, G. J., Wu, J., Miao, L., Zhu, M. H., Zhou, Q. J., Lu, X. J., Lu, J. F., Leung, C. H., Ma, D. L., & Chen, J. (2021). Pharmacological inhibition of KDM5A for cancer treatment. European Journal of Medicinal Chemistry, 226, 113855.
pubmed: 34555614 doi: 10.1016/j.ejmech.2021.113855
Wang, G. G., Song, J., Wang, Z., Dormann, H. L., Casadio, F., Li, H., Luo, J. L., Patel, D. J., & Allis, C. D. (2009). Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger. Nature, 459(7248), 847–851.
pubmed: 19430464 pmcid: 2697266 doi: 10.1038/nature08036
Zeng, J., Ge, Z., Wang, L., Li, Q., Wang, N., Bjorkholm, M., Jia, J., & Xu, D. (2010). The histone demethylase RBP2 Is overexpressed in gastric cancer and its inhibition triggers senescence of cancer cells. Gastroenterology, 138(3), 981–992.
pubmed: 19850045 doi: 10.1053/j.gastro.2009.10.004
Peng, D., Lin, B., Xie, M., Zhang, P., Guo, Q., Li, Q., Gu, Q., Yang, S., & Sen, L. (2021). Histone demethylase KDM5A promotes tumorigenesis of osteosarcoma tumor. Cell Death Discov, 7(1), 9.
pubmed: 33436536 pmcid: 7803953 doi: 10.1038/s41420-020-00396-7
Cardin, S., Bilodeau, M., Roussy, M., Aubert, L., Milan, T., Jouan, L., Rouette, A., Laramee, L., Gendron, P., Duchaine, J., et al. (2019). Human models of NUP98-KDM5A megakaryocytic leukemia in mice contribute to uncovering new biomarkers and therapeutic vulnerabilities. Blood Advances, 3(21), 3307–3321.
pubmed: 31698461 pmcid: 6855103 doi: 10.1182/bloodadvances.2019030981
van Zutven, L. J., Onen, E., Velthuizen, S. C., van Drunen, E., von Bergh, A. R., van den Heuvel-Eibrink, M. M., Veronese, A., Mecucci, C., Negrini, M., de Greef, G. E., et al. (2006). Identification of NUP98 abnormalities in acute leukemia: JARID1A (12p13) as a new partner gene. Genes, Chromosomes & Cancer, 45(5), 437–446.
doi: 10.1002/gcc.20308
Xia, X., Lemieux, M. E., Li, W., Carroll, J. S., Brown, M., Liu, X. S., & Kung, A. L. (2009). Integrative analysis of HIF binding and transactivation reveals its role in maintaining histone methylation homeostasis. Proceedings of the National Academy of Sciences of the United States of America, 106(11), 4260–4265.
pubmed: 19255431 pmcid: 2657396 doi: 10.1073/pnas.0810067106
Ma, Y. S., Wu, T. M., Qian, B., Liu, Y. S., Ding, H., Fan, M. M., Liu, J. B., Yu, F., Wang, H. M., Shi, Y., et al. (2021). KDM5A silencing transcriptionally suppresses the FXYD3-PI3K/AKT axis to inhibit angiogenesis in hepatocellular cancer via miR-433 up-regulation. Journal of Cellular and Molecular Medicine, 25(8), 4040–4052.
pubmed: 33621431 pmcid: 8051710 doi: 10.1111/jcmm.16371
Zhou, X., Sun, H., Chen, H., Zavadil, J., Kluz, T., Arita, A., & Costa, M. (2010). Hypoxia induces trimethylated H3 lysine 4 by inhibition of JARID1A demethylase. Cancer Research, 70(10), 4214–4221.
pubmed: 20406991 pmcid: 3007597 doi: 10.1158/0008-5472.CAN-09-2942
Xhabija, B., & Kidder, B. L. (2019). KDM5B is a master regulator of the H3K4-methylome in stem cells, development and cancer. Seminars in Cancer Biology, 57, 79–85.
pubmed: 30448242 doi: 10.1016/j.semcancer.2018.11.001
Xiang, Y., Zhu, Z., Han, G., Ye, X., Xu, B., Peng, Z., Ma, Y., Yu, Y., Lin, H., Chen, A. P., et al. (2007). JARID1B is a histone H3 lysine 4 demethylase up-regulated in prostate cancer. Proceedings of the National Academy of Sciences of the United States of America, 104(49), 19226–19231.
pubmed: 18048344 pmcid: 2148272 doi: 10.1073/pnas.0700735104
Barrett, A., Santangelo, S., Tan, K., Catchpole, S., Roberts, K., Spencer-Dene, B., Hall, D., Scibetta, A., Burchell, J., Verdin, E., et al. (2007). Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases. International Journal of Cancer, 121(2), 265–275.
pubmed: 17373667 doi: 10.1002/ijc.22673
Li, G., Kanagasabai, T., Lu, W., Zou, M. R., Zhang, S. M., Celada, S. I., Izban, M. G., Liu, Q., Lu, T., Ballard, B. R., et al. (2020). KDM5B is essential for the hyperactivation of PI3K/AKT signaling in prostate tumorigenesis. Cancer Research, 80(21), 4633–4643.
pubmed: 32868382 pmcid: 8034842 doi: 10.1158/0008-5472.CAN-20-0505
Mitra, D., Das, P. M., Huynh, F. C., & Jones, F. E. (2011). Jumonji/ARID1 B (JARID1B) protein promotes breast tumor cell cycle progression through epigenetic repression of microRNA let-7e. Journal of Biological Chemistry, 286(47), 40531–40535.
pubmed: 21969366 pmcid: 3220509 doi: 10.1074/jbc.M111.304865
Catchpole, S., Spencer-Dene, B., Hall, D., Santangelo, S., Rosewell, I., Guenatri, M., Beatson, R., Scibetta, A. G., Burchell, J. M., & Taylor-Papadimitriou, J. (2011). PLU-1/JARID1B/KDM5B is required for embryonic survival and contributes to cell proliferation in the mammary gland and in ER+ breast cancer cells. International Journal of Oncology, 38(5), 1267–1277.
pubmed: 21369698
Wang, J., Wu, X., & Shan, L. (2018). JARID1B modulates breast cancer cell apoptosis by regulating p53 expression. International Journal of Clinical and Experimental Pathology, 11(9), 4529–4536.
pubmed: 31949850 pmcid: 6962977
Scibetta, A. G., Santangelo, S., Coleman, J., Hall, D., Chaplin, T., Copier, J., Catchpole, S., Burchell, J., & Taylor-Papadimitriou, J. (2007). Functional analysis of the transcription repressor PLU-1/JARID1B. Molecular and Cellular Biology, 27(20), 7220–7235.
pubmed: 17709396 pmcid: 2168894 doi: 10.1128/MCB.00274-07
Yamane, K., Tateishi, K., Klose, R. J., Fang, J., Fabrizio, L. A., Erdjument-Bromage, H., Taylor-Papadimitriou, J., Tempst, P., & Zhang, Y. (2007). PLU-1 is an H3K4 demethylase involved in transcriptional repression and breast cancer cell proliferation. Molecular Cell, 25(6), 801–812.
pubmed: 17363312 doi: 10.1016/j.molcel.2007.03.001
Nisio, E. D., Licursi, V., Mannironi, C., Buglioni, V., Paiardini, A., Robusti, G., Noberini, R., Bonaldi, T., & Negri, R. (2023). A truncated and catalytically inactive isoform of KDM5B histone demethylase accumulates in breast cancer cells and regulates H3K4 trimethylation and gene expression. Cancer Gene Therapy, 30, 822–832.
pubmed: 36697763 pmcid: 10281864 doi: 10.1038/s41417-022-00584-w
Zhang, Z. G., Zhang, H. S., Sun, H. L., Liu, H. Y., Liu, M. Y., & Zhou, Z. (2019). KDM5B promotes breast cancer cell proliferation and migration via AMPK-mediated lipid metabolism reprogramming. Experimental Cell Research, 379(2), 182–190.
pubmed: 30978340 doi: 10.1016/j.yexcr.2019.04.006
Li, Q., Shi, L., Gui, B., Yu, W., Wang, J., Zhang, D., Han, X., Yao, Z., & Shang, Y. (2011). Binding of the JmjC demethylase JARID1B to LSD1/NuRD suppresses angiogenesis and metastasis in breast cancer cells by repressing chemokine CCL14. Cancer Research, 71(21), 6899–6908.
pubmed: 21937684 doi: 10.1158/0008-5472.CAN-11-1523
Roesch, A., Fukunaga-Kalabis, M., Schmidt, E. C., Zabierowski, S. E., Brafford, P. A., Vultur, A., Basu, D., Gimotty, P., Vogt, T., & Herlyn, M. (2010). A temporarily distinct subpopulation of slow-cycling melanoma cells is required for continuous tumor growth. Cell, 141(4), 583–594.
pubmed: 20478252 pmcid: 2882693 doi: 10.1016/j.cell.2010.04.020
Vogel, F. C. E., Bordag, N., Zugner, E., Trajkovic-Arsic, M., Chauvistre, H., Shannan, B., Varaljai, R., Horn, S., Magnes, C., Thomas Siveke, J., et al. (2019). Targeting the H3K4 demethylase KDM5B reprograms the metabolome and phenotype of melanoma cells. Journal of Investigative Dermatology, 139(12), 2506–2516.
pubmed: 31229500 doi: 10.1016/j.jid.2019.06.124
Liu, X., Zhang, S. M., McGeary, M. K., Krykbaeva, I., Lai, L., Jansen, D. J., Kales, S. C., Simeonov, A., Hall, M. D., Kelly, D. P., et al. (2019). KDM5B promotes drug resistance by regulating melanoma-propagating cell subpopulations. Molecular Cancer Therapeutics, 18(3), 706–717.
pubmed: 30523048 doi: 10.1158/1535-7163.MCT-18-0395
Hayami, S., Yoshimatsu, M., Veerakumarasivam, A., Unoki, M., Iwai, Y., Tsunoda, T., Field, H. I., Kelly, J. D., Neal, D. E., Yamaue, H., et al. (2010). Overexpression of the JmjC histone demethylase KDM5B in human carcinogenesis: Involvement in the proliferation of cancer cells through the E2F/RB pathway. Molecular Cancer, 9, 59.
pubmed: 20226085 pmcid: 2848192 doi: 10.1186/1476-4598-9-59
Nijwening, J. H., Geutjes, E. J., Bernards, R., & Beijersbergen, R. L. (2011). The histone demethylase Jarid1b (Kdm5b) is a novel component of the Rb pathway and associates with E2f-target genes in MEFs during senescence. PLoS ONE, 6(9), e25235.
pubmed: 21980403 pmcid: 3181323 doi: 10.1371/journal.pone.0025235
Benevolenskaya, E. V., Murray, H. L., Branton, P., Young, R. A., & Kaelin, W. G., Jr. (2005). Binding of pRB to the PHD protein RBP2 promotes cellular differentiation. Molecular Cell, 18(6), 623–635.
pubmed: 15949438 doi: 10.1016/j.molcel.2005.05.012
Huang, Y., Zou, Y., Zheng, R., & Ma, X. (2019). MiR-137 inhibits cell proliferation in acute lymphoblastic leukemia by targeting JARID1B. European Journal of Haematology, 103(3), 215–224.
pubmed: 31206203 doi: 10.1111/ejh.13276
Guo, J. C., Liu, Z., Yang, Y. J., Guo, M., Zhang, J. Q., & Zheng, J. F. (2021). KDM5B promotes self-renewal of hepatocellular carcinoma cells through the microRNA-448-mediated YTHDF3/ITGA6 axis. Journal of Cellular and Molecular Medicine, 25(13), 5949–5962.
pubmed: 33829656 pmcid: 8256355 doi: 10.1111/jcmm.16342
McBrayer, S. K., Olenchock, B. A., DiNatale, G. J., Shi, D. D., Khanal, J., Jennings, R. B., Novak, J. S., Oser, M. G., Robbins, A. K., Modiste, R., et al. (2018). Autochthonous tumors driven by Rb1 loss have an ongoing requirement for the RBP2 histone demethylase. Proceedings of the National Academy of Sciences of the United States of America, 115(16), E3741–E3748.
pubmed: 29610306 pmcid: 5910822
Pu, Y., Xiang, J., & Zhang, J. (2020). KDM5B-mediated microRNA-448 up-regulation restrains papillary thyroid cancer cell progression and slows down tumor growth via TGIF1 repression. Life Sciences, 250, 117519.
pubmed: 32147429 doi: 10.1016/j.lfs.2020.117519
Zhou, Y., An, Q., Guo, R. X., Qiao, Y. H., Li, L. X., Zhang, X. Y., & Zhao, X. L. (2017). miR424-5p functions as an anti-oncogene in cervical cancer cell growth by targeting KDM5B via the Notch signaling pathway. Life Sciences, 171, 9–15.
pubmed: 28082020 doi: 10.1016/j.lfs.2017.01.006
Xu, L. M., Yu, H., Yuan, Y. J., Zhang, J., Ma, Y., Cao, X. C., Wang, J., Zhao, L. J., & Wang, P. (2020). overcoming of radioresistance in non-small cell lung cancer by microRNA-320a through HIF1alpha-suppression mediated methylation of PTEN. Frontiers in Cell and Developmental Biology, 8, 553733.
pubmed: 33304897 pmcid: 7693713 doi: 10.3389/fcell.2020.553733
Dalgliesh, G. L., Furge, K., Greenman, C., Chen, L., Bignell, G., Butler, A., Davies, H., Edkins, S., Hardy, C., Latimer, C., et al. (2010). Systematic sequencing of renal carcinoma reveals inactivation of histone modifying genes. Nature, 463(7279), 360–363.
pubmed: 20054297 pmcid: 2820242 doi: 10.1038/nature08672
Liao, L., Liu, Z. Z., Langbein, L., Cai, W., Cho, E. A., Na, J., Niu, X., Jiang, W., Zhong, Z., Cai, W. L., et al. (2018). Multiple tumor suppressors regulate a HIF-dependent negative feedback loop via ISGF3 in human clear cell renal cancer. Elife, 7, e37925.
pubmed: 30355451 pmcid: 6234029 doi: 10.7554/eLife.37925
Niu, X., Zhang, T., Liao, L., Zhou, L., Lindner, D. J., Zhou, M., Rini, B., Yan, Q., & Yang, H. (2012). The von Hippel-Lindau tumor suppressor protein regulates gene expression and tumor growth through histone demethylase JARID1C. Oncogene, 31(6), 776–786.
pubmed: 21725364 doi: 10.1038/onc.2011.266
Gao, X., Jegede, O., Gray, C., Catalano, P. J., Novak, J., Kwiatkowski, D. J., McKay, R. R., George, D. J., Choueiri, T. K., McDermott, D. F., et al. (2018). Comprehensive genomic profiling of metastatic tumors in a phase 2 biomarker study of everolimus in advanced renal cell carcinoma. Clinical Genitourinary Cancer, 16(5), 341–348.
pubmed: 29754934 pmcid: 6175670 doi: 10.1016/j.clgc.2018.04.001
Perinchery, G., Sasaki, M., Angan, A., Kumar, V., Carroll, P., & Dahiya, R. (2000). Deletion of Y-chromosome specific genes in human prostate cancer. Journal of Urology, 163(4), 1339–1342.
pubmed: 10737540 doi: 10.1016/S0022-5347(05)67774-9
Gupta, S., Halabi, S., Kemeny, G., Anand, M., Giannakakou, P., Nanus, D. M., George, D. J., Gregory, S. G., & Armstrong, A. J. (2021). Circulating tumor cell genomic evolution and hormone therapy outcomes in men with metastatic castration-resistant prostate cancer. Molecular Cancer Research, 19(6), 1040–1050.
pubmed: 33771885 doi: 10.1158/1541-7786.MCR-20-0975
Li, N., Dhar, S. S., Chen, T. Y., Kan, P. Y., Wei, Y., Kim, J. H., Chan, C. H., Lin, H. K., Hung, M. C., & Lee, M. G. (2016). JARID1D Is a suppressor and prognostic marker of prostate cancer invasion and metastasis. Cancer Research, 76(4), 831–843.
pubmed: 26747897 pmcid: 4755879 doi: 10.1158/0008-5472.CAN-15-0906
Komura, K., Jeong, S. H., Hinohara, K., Qu, F., Wang, X., Hiraki, M., Azuma, H., Lee, G. S., Kantoff, P. W., & Sweeney, C. J. (2016). Resistance to docetaxel in prostate cancer is associated with androgen receptor activation and loss of KDM5D expression. Proceedings of the National Academy of Sciences of the United States of America, 113(22), 6259–6264.
pubmed: 27185910 pmcid: 4896695 doi: 10.1073/pnas.1600420113
Komura, K., Yoshikawa, Y., Shimamura, T., Chakraborty, G., Gerke, T. A., Hinohara, K., Chadalavada, K., Jeong, S. H., Armenia, J., Du, S. Y., et al. (2018). ATR inhibition controls aggressive prostate tumors deficient in Y-linked histone demethylase KDM5D. The Journal of Clinical Investigation, 128(7), 2979–2995.
pubmed: 29863497 pmcid: 6025984 doi: 10.1172/JCI96769
Hurst, C. D., Alder, O., Platt, F. M., Droop, A., Stead, L. F., Burns, J. E., Burghel, G. J., Jain, S., Klimczak, L. J., Lindsay, H., et al. (2017). Genomic subtypes of non-invasive bladder cancer with distinct metabolic Profile and female gender bias in KDM6A mutation frequency. Cancer Cell, 32(5), 701–715.
pubmed: 29136510 pmcid: 5774674 doi: 10.1016/j.ccell.2017.08.005
Kaneko, S., & Li, X. (2018). X chromosome protects against bladder cancer in females via a KDM6A-dependent epigenetic mechanism. Science Advances, 4(6), eaar5598.
pubmed: 29928692 pmcid: 6007159 doi: 10.1126/sciadv.aar5598
Kim, G. J., Kim, D. H., Min, K. W., Chae, S. W., Kim, S. H., Son, B. K., Moon, K. M., & Kim, Y. H. (2020). Expression of UTX indicates poor prognosis in patients with luminal breast cancer and is associated with MMP-11 expression. Applied Immunohistochemistry & Molecular Morphology, 28(7), 544–550.
doi: 10.1097/PAI.0000000000000795
Benedetti, R., Dell’Aversana, C., De Marchi, T., Rotili, D., Liu, N. Q., Novakovic, B., Boccella, S., Di Maro, S., Cosconati, S., Baldi, A., et al. (2019). Inhibition of histone demethylases LSD1 and UTX regulates ERalpha signaling in breast cancer. Cancers (Basel), 11(12), 2027.
pubmed: 31888209 doi: 10.3390/cancers11122027
Lu, H., Xie, Y., Tran, L., Lan, J., Yang, Y., Murugan, N. L., Wang, R., Wang, Y. J., & Semenza, G. L. (2020). Chemotherapy-induced S100A10 recruits KDM6A to facilitate OCT4-mediated breast cancer stemness. The Journal of Clinical Investigation, 130(9), 4607–4623.
pubmed: 32427586 pmcid: 7456215 doi: 10.1172/JCI138577
Nickerson, M. L., Dancik, G. M., Im, K. M., Edwards, M. G., Turan, S., Brown, J., Ruiz-Rodriguez, C., Owens, C., Costello, J. C., Guo, G., et al. (2014). Concurrent alterations in TERT, KDM6A, and the BRCA pathway in bladder cancer. Clinical Cancer Research, 20(18), 4935–4948.
pubmed: 25225064 pmcid: 4166537 doi: 10.1158/1078-0432.CCR-14-0330
Gui, Y., Guo, G., Huang, Y., Hu, X., Tang, A., Gao, S., Wu, R., Chen, C., Li, X., Zhou, L., et al. (2011). Frequent mutations of chromatin remodeling genes in transitional cell carcinoma of the bladder. Nature Genetics, 43(9), 875–878.
pubmed: 21822268 pmcid: 5373841 doi: 10.1038/ng.907
Ler, L. D., Ghosh, S., Chai, X., Thike, A. A., Heng, H. L., Siew, E. Y., Dey, S., Koh, L. K., Lim, J. Q., Lim, W. K., et al. (2017). Loss of tumor suppressor KDM6A amplifies PRC2-regulated transcriptional repression in bladder cancer and can be targeted through inhibition of EZH2. Science Translational Medicine, 9(378), eaai8312.
pubmed: 28228601 doi: 10.1126/scitranslmed.aai8312
Kobatake, K., Ikeda, K. I., Nakata, Y., Yamasaki, N., Ueda, T., Kanai, A., Sentani, K., Sera, Y., Hayashi, T., Koizumi, M., et al. (2020). Kdm6a deficiency activates inflammatory pathways, promotes M2 macrophage polarization, and causes bladder cancer in cooperation with p53 dysfunction. Clinical Cancer Research, 26(8), 2065–2079.
pubmed: 32047002 doi: 10.1158/1078-0432.CCR-19-2230
Barrows, D., Feng, L., Carroll, T. S., & Allis, C. D. (2020). Loss of UTX/KDM6A and the activation of FGFR3 converge to regulate differentiation gene-expression programs in bladder cancer. Proceedings of the National Academy of Sciences of the United States of America, 117(41), 25732–25741.
pubmed: 32989154 pmcid: 7568298 doi: 10.1073/pnas.2008017117
Andricovich, J., Perkail, S., Kai, Y., Casasanta, N., Peng, W., & Tzatsos, A. (2018). Loss of KDM6A activates super-enhancers to induce gender-specific squamous-like pancreatic cancer and confers sensitivity to BET inhibitors. Cancer Cell, 33(3), 512–526.
pubmed: 29533787 pmcid: 5854186 doi: 10.1016/j.ccell.2018.02.003
Watanabe, S., Shimada, S., Akiyama, Y., Ishikawa, Y., Ogura, T., Ogawa, K., Ono, H., Mitsunori, Y., Ban, D., Kudo, A., et al. (2019). Loss of KDM6A characterizes a poor prognostic subtype of human pancreatic cancer and potentiates HDAC inhibitor lethality. International Journal of Cancer, 145(1), 192–205.
pubmed: 30556125 doi: 10.1002/ijc.32072
Kalisz, M., Bernardo, E., Beucher, A., Maestro, M. A., Del Pozo, N., Millan, I., Haeberle, L., Schlensog, M., Safi, S. A., Knoefel, W. T., et al. (2020). HNF1A recruits KDM6A to activate differentiated acinar cell programs that suppress pancreatic cancer. EMBO Journal, 39(9), e102808.
pubmed: 32154941 pmcid: 7196917 doi: 10.15252/embj.2019102808
Barthel, S., Schneider, G., & Saur, D. (2020). Blocking the road to de-differentiation: HNF1A/KDM6A complex safeguards epithelial integrity in pancreatic cancer. EMBO Journal, 39(9), e104759.
pubmed: 32236961 pmcid: 7196913 doi: 10.15252/embj.2020104759
Kim, J. H., Sharma, A., Dhar, S. S., Lee, S. H., Gu, B., Chan, C. H., Lin, H. K., & Lee, M. G. (2014). UTX and MLL4 coordinately regulate transcriptional programs for cell proliferation and invasiveness in breast cancer cells. Cancer Research, 74(6), 1705–1717.
pubmed: 24491801 pmcid: 3962500 doi: 10.1158/0008-5472.CAN-13-1896
Hinz, S., Weikert, S., Magheli, A., Hoffmann, M., Engers, R., Miller, K., & Kempkensteffen, C. (2009). Expression profile of the polycomb group protein enhancer of Zeste homologue 2 and its prognostic relevance in renal cell carcinoma. Journal of Urology, 182(6), 2920–2925.
pubmed: 19846140 doi: 10.1016/j.juro.2009.08.014
Kato, H., Asamitsu, K., Sun, W., Kitajima, S., Yoshizawa-Sugata, N., Okamoto, T., Masai, H., & Poellinger, L. (2020). Cancer-derived UTX TPR mutations G137V and D336G impair interaction with MLL3/4 complexes and affect UTX subcellular localization. Oncogene, 39(16), 3322–3335.
pubmed: 32071397 doi: 10.1038/s41388-020-1218-3
Zha, L., Cao, Q., Cui, X., Li, F., Liang, H., Xue, B., & Shi, H. (2016). Epigenetic regulation of E-cadherin expression by the histone demethylase UTX in colon cancer cells. Medical Oncology, 33(3), 21.
pubmed: 26819089 doi: 10.1007/s12032-016-0734-z
Tang, X., Cai, W., Cheng, J., Lu, P., Ma, S., Chen, C., Chen, Y., Sun, Y., Wang, C., Hu, P., et al. (2019). The histone H3 lysine-27 demethylase UTX plays a critical role in colorectal cancer cell proliferation. Cancer Cell International, 19, 144.
pubmed: 31139021 pmcid: 6530047 doi: 10.1186/s12935-019-0841-y
Chen, X., Yang, Z., Feng, J., Duan, T., Pan, T., Yan, L., Jin, T., Xiang, Y., Zhang, M., Chen, P., et al. (2021). Combination of lysine-specific demethylase 6A (KDM6A) and mismatch repair (MMR) status is a potential prognostic factor in colorectal cancer. Cancer Medicine, 10(1), 317–324.
pubmed: 33174323 doi: 10.1002/cam4.3602
Terashima, M., Ishimura, A., Wanna-Udom, S., & Suzuki, T. (2017). Epigenetic regulation of epithelial-mesenchymal transition by KDM6A histone demethylase in lung cancer cells. Biochemical and Biophysical Research Communications, 490(4), 1407–1413.
pubmed: 28698146 doi: 10.1016/j.bbrc.2017.07.048
Mar, B. G., Bullinger, L., Basu, E., Schlis, K., Silverman, L. B., Dohner, K., & Armstrong, S. A. (2012). Sequencing histone-modifying enzymes identifies UTX mutations in acute lymphoblastic leukemia. Leukemia, 26(8), 1881–1883.
pubmed: 22377896 pmcid: 4701195 doi: 10.1038/leu.2012.56
Wang, J. K., Tsai, M. C., Poulin, G., Adler, A. S., Chen, S., Liu, H., Shi, Y., & Chang, H. Y. (2010). The histone demethylase UTX enables RB-dependent cell fate control. Genes & Development, 24(4), 327–332.
doi: 10.1101/gad.1882610
Tsai, M. C., Wang, J. K., & Chang, H. Y. (2010). Tumor suppression by the histone demethylase UTX. Cell Cycle, 9(11), 2043–2044.
pubmed: 20505331 doi: 10.4161/cc.9.11.11845
Terashima, M., Ishimura, A., Yoshida, M., Suzuki, Y., Sugano, S., & Suzuki, T. (2010). The tumor suppressor Rb and its related Rbl2 genes are regulated by Utx histone demethylase. Biochemical and Biophysical Research Communications, 399(2), 238–244.
pubmed: 20650264 doi: 10.1016/j.bbrc.2010.07.061
Agger, K., Cloos, P. A., Rudkjaer, L., Williams, K., Andersen, G., Christensen, J., & Helin, K. (2009). The H3K27me3 demethylase JMJD3 contributes to the activation of the INK4A-ARF locus in response to oncogene- and stress-induced senescence. Genes & Development, 23(10), 1171–1176.
doi: 10.1101/gad.510809
Barradas, M., Anderton, E., Acosta, J. C., Li, S., Banito, A., Rodriguez-Niedenfuhr, M., Maertens, G., Banck, M., Zhou, M. M., Walsh, M. J., et al. (2009). Histone demethylase JMJD3 contributes to epigenetic control of INK4a/ARF by oncogenic RAS. Genes & Development, 23(10), 1177–1182.
doi: 10.1101/gad.511109
Martinelli, P., Bonetti, P., Sironi, C., Pruneri, G., Fumagalli, C., Raviele, P. R., Volorio, S., Pileri, S., Chiarle, R., McDuff, F. K., et al. (2011). The lymphoma-associated NPM-ALK oncogene elicits a p16INK4a/pRb-dependent tumor-suppressive pathway. Blood, 117(24), 6617–6626.
pubmed: 21518927 doi: 10.1182/blood-2010-08-301135
Lin, T. Y., Cheng, Y. C., Yang, H. C., Lin, W. C., Wang, C. C., Lai, P. L., & Shieh, S. Y. (2012). Loss of the candidate tumor suppressor BTG3 triggers acute cellular senescence via the ERK-JMJD3-p16(INK4a) signaling axis. Oncogene, 31(27), 3287–3297.
pubmed: 22020331 doi: 10.1038/onc.2011.491
Ene, C. I., Edwards, L., Riddick, G., Baysan, M., Woolard, K., Kotliarova, S., Lai, C., Belova, G., Cam, M., Walling, J., et al. (2012). Histone demethylase Jumonji D3 (JMJD3) as a tumor suppressor by regulating p53 protein nuclear stabilization. PLoS ONE, 7(12), e51407.
pubmed: 23236496 pmcid: 3517524 doi: 10.1371/journal.pone.0051407
Pereira, F., Barbachano, A., Silva, J., Bonilla, F., Campbell, M. J., Munoz, A., & Larriba, M. J. (2011). KDM6B/JMJD3 histone demethylase is induced by vitamin D and modulates its effects in colon cancer cells. Human Molecular Genetics, 20(23), 4655–4665.
pubmed: 21890490 doi: 10.1093/hmg/ddr399
Yang, J., Wang, X., Huang, B., Liu, R., Xiong, H., Ye, F., Zeng, C., Fu, X., & Li, L. (2021). An IFN-gamma/STAT1/JMJD3 axis induces ZEB1 expression and promotes aggressiveness in lung adenocarcinoma. Molecular Cancer Research, 19(7), 1234–1246.
pubmed: 33771881 doi: 10.1158/1541-7786.MCR-20-0948
Lee, S. H., Kim, O., Kim, H. J., Hwangbo, C., & Lee, J. H. (2021). Epigenetic regulation of TGF-beta-induced EMT by JMJD3/KDM6B histone H3K27 demethylase. Oncogenesis, 10(2), 17.
pubmed: 33637682 pmcid: 7910473 doi: 10.1038/s41389-021-00307-0
Tricarico, R., Nicolas, E., Hall, M. J., & Golemis, E. A. (2020). X- and Y-linked chromatin-modifying genes as regulators of sex-specific cancer incidence and prognosis. Clinical Cancer Research, 26(21), 5567–5578.
pubmed: 32732223 pmcid: 7642178 doi: 10.1158/1078-0432.CCR-20-1741
Ahn, J., Kim, K. H., Park, S., Ahn, Y. H., Kim, H. Y., Yoon, H., Lee, J. H., Bang, D., & Lee, D. H. (2016). Target sequencing and CRISPR/Cas editing reveal simultaneous loss of UTX and UTY in urothelial bladder cancer. Oncotarget, 7(39), 63252–63260.
pubmed: 27533081 pmcid: 5325361 doi: 10.18632/oncotarget.11207
Laaser, I., Theis, F. J., de Angelis, M. H., Kolb, H. J., & Adamski, J. (2011). Huge splicing frequency in human Y chromosomal UTY gene. OMICS: A Journal of Integrative Biology, 15(3), 141–154.
pubmed: 21329462 doi: 10.1089/omi.2010.0107
Dutta, A., Le Magnen, C., Mitrofanova, A., Ouyang, X., Califano, A., & Abate-Shen, C. (2016). Identification of an NKX3.1-G9a-UTY transcriptional regulatory network that controls prostate differentiation. Science, 352(6293), 1576–1580.
pubmed: 27339988 pmcid: 5507586 doi: 10.1126/science.aad9512
Ivanov, R., Hol, S., Aarts, T., Hagenbeek, A., Slager, E. H., & Ebeling, S. (2005). UTY-specific TCR-transfer generates potential graft-versus-leukaemia effector T cells. British Journal of Haematology, 129(3), 392–402.
pubmed: 15842664 doi: 10.1111/j.1365-2141.2005.05461.x
Bund, D., Buhmann, R., Gokmen, F., Zorn, J., Kolb, H. J., & Schmetzer Helga, M. (2012). Minor-histocompatibility-antigen UTY as target for graft-versus-leukemia and graft-versus-haematopoiesis in the canine-model. Scandinavian Journal of Immunology, 77(1), 39–53.
doi: 10.1111/sji.12011
Lee, K. H., Hong, S., Kang, M., Jeong, C. W., Ku, J. H., Kim, H. H., & Kwak, C. (2018). Histone demethylase KDM7A controls androgen receptor activity and tumor growth in prostate cancer. International Journal of Cancer, 143(11), 2849–2861.
pubmed: 30183076 doi: 10.1002/ijc.31843
Lee, K. H., Kim, B. C., Jeong, S. H., Jeong, C. W., Ku, J. H., Kim, H. H., & Kwak, C. (2020). Histone demethylase kdm7a regulates androgen receptor activity, and its chemical inhibitor TC-E 5002 overcomes cisplatin-resistance in bladder cancer cells. International journal of molecular sciences, 21(16), 5658.
pubmed: 32781788 pmcid: 7460860 doi: 10.3390/ijms21165658
Meng, Z., Liu, Y., Wang, J., Fan, H., Fang, H., Li, S., Yuan, L., Liu, C., Peng, Y., Zhao, W., et al. (2020). Histone demethylase KDM7A is required for stem cell maintenance and apoptosis inhibition in breast cancer. Journal of Cellular Physiology, 235(2), 932–943.
pubmed: 31236965 doi: 10.1002/jcp.29008
Li, W., Yang, X., Shi, C., & Zhou, Z. (2020). Hsa_circ_002178 Promotes the growth and migration of breast cancer cells and maintains cancer stem-like cell properties through regulating miR-1258/KDM7A Axis. Cell Transplantation, 29, 963689720960174.
pubmed: 32951449 doi: 10.1177/0963689720960174
Liu, Q., Borcherding, N., Shao, P., Cao, H., Zhang, W., & Qi, H. H. (2019). Identification of novel TGF-beta regulated genes with pro-migratory roles. Biochimica et Biophysica Acta, Molecular Basis of Disease, 1865(12), 165537.
pubmed: 31449970 doi: 10.1016/j.bbadis.2019.165537
Bjorkman, M., Ostling, P., Harma, V., Virtanen, J., Mpindi, J. P., Rantala, J., Mirtti, T., Vesterinen, T., Lundin, M., Sankila, A., et al. (2011). Systematic knockdown of epigenetic enzymes identifies a novel histone demethylase PHF8 overexpressed in prostate cancer with an impact on cell proliferation, migration and invasion. Oncogene, 31(29), 3444–3456.
pubmed: 22120715 doi: 10.1038/onc.2011.512
Qin, J., Liu, X., Laffin, B., Chen, X., Choy, G., Jeter, C. R., Calhoun-Davis, T., Li, H., Palapattu, G. S., Pang, S., et al. (2012). The PSA(-/lo) prostate cancer cell population harbors self-renewing long-term tumor-propagating cells that resist castration. Cell Stem Cell, 10(5), 556–569.
pubmed: 22560078 pmcid: 3348510 doi: 10.1016/j.stem.2012.03.009
Qiu, J., Shi, G., Jia, Y., Li, J., Wu, M., Dong, S., & Wong, J. (2010). The X-linked mental retardation gene PHF8 is a histone demethylase involved in neuronal differentiation. Cell Research, 20(8), 908–918.
pubmed: 20548336 doi: 10.1038/cr.2010.81
Liu, Q., Pang, J., Wang, L. A., Huang, Z., Xu, J., Yang, X., Xie, Q., Huang, Y., Tang, T., Tong, D., et al. (2021). Histone demethylase PHF8 drives neuroendocrine prostate cancer progression by epigenetically upregulating FOXA2. The Journal of Pathology, 253(1), 106–118.
pubmed: 33009820 doi: 10.1002/path.5557
Tong, D., Liu, Q., Liu, G., Yuan, W., Wang, L., Guo, Y., Lan, W., Zhang, D., Dong, S., Wang, Y., et al. (2016). The HIF/PHF8/AR axis promotes prostate cancer progression. Oncogenesis, 5(12), e283.
pubmed: 27991916 pmcid: 5177772 doi: 10.1038/oncsis.2016.74
Maina, P. K., Shao, P., Jia, X., Liu, Q., Umesalma, S., Marin, M., Long, D., Jr., Concepcion-Roman, S., & Qi, H. H. (2017). Histone demethylase PHF8 regulates hypoxia signaling through HIF1alpha and H3K4me3. Biochimica et Biophysica Acta, Gene Regulatory Mechanisms, 1860(9), 1002–1012.
pubmed: 28734980 doi: 10.1016/j.bbagrm.2017.07.005
Maina, P. K., Shao, P., Liu, Q., Fazli, L., Tyler, S., Nasir, M., Dong, X., & Qi, H. H. (2016). c-MYC drives histone demethylase PHF8 during neuroendocrine differentiation and in castration-resistant prostate cancer. Oncotarget, 7(46), 75585–75602.
pubmed: 27689328 pmcid: 5342763 doi: 10.18632/oncotarget.12310
Liu, Q., Borcherding, N. C., Shao, P., Maina, P. K., Zhang, W., & Qi, H. H. (2020). Contribution of synergism between PHF8 and HER2 signalling to breast cancer development and drug resistance. eBioMedicine, 51, 102612.
pubmed: 31923801 pmcid: 7000350 doi: 10.1016/j.ebiom.2019.102612
Shao, P., Liu, Q., Maina, P. K., Cui, J., Bair, T. B., Li, T., Umesalma, S., Zhang, W., & Qi, H. H. (2017). Histone demethylase PHF8 promotes epithelial to mesenchymal transition and breast tumorigenesis. Nucleic Acids Research, 45(4), 1687–1702.
pubmed: 27899639 doi: 10.1093/nar/gkw1093
Wang, Q., Ma, S., Song, N., Li, X., Liu, L., Yang, S., Ding, X., Shan, L., Zhou, X., Su, D., et al. (2016). Stabilization of histone demethylase PHF8 by USP7 promotes breast carcinogenesis. The Journal of Clinical Investigation, 126(6), 2205–2220.
pubmed: 27183383 pmcid: 4887182 doi: 10.1172/JCI85747
Ye, H., Yang, Q., Qi, S., & Li, H. (2019). PHF8 Plays an oncogene function in hepatocellular carcinoma formation. Oncology Research, 27(5), 613–621.
pubmed: 30764899 pmcid: 7848440 doi: 10.3727/096504018X15410353669149
Zhou, W., Gong, L., Wu, Q., Xing, C., Wei, B., Chen, T., Zhou, Y., Yin, S., Jiang, B., Xie, H., et al. (2018). PHF8 upregulation contributes to autophagic degradation of E-cadherin, epithelial-mesenchymal transition and metastasis in hepatocellular carcinoma. Journal of Experimental & Clinical Cancer Research, 37(1), 215.
doi: 10.1186/s13046-018-0890-4
Sinha, S., Singh, R. K., Alam, N., Roy, A., Roychoudhury, S., & Panda, C. K. (2008). Alterations in candidate genes PHF2, FANCC, PTCH1 and XPA at chromosomal 9q22.3 region: pathological significance in early- and late-onset breast carcinoma. Mol Cancer, 7, 84.
pubmed: 18990233 pmcid: 2633285 doi: 10.1186/1476-4598-7-84
Ghosh, A., Ghosh, S., Maiti, G. P., Mukherjee, S., Mukherjee, N., Chakraborty, J., Roy, A., Roychoudhury, S., & Panda, C. K. (2011). Association of FANCC and PTCH1 with the development of early dysplastic lesions of the head and neck. Annals of surgical oncology, 19, 528–538.
doi: 10.1245/s10434-011-1991-x
Lee, K. H., Park, J. W., Sung, H. S., Choi, Y. J., Kim, W. H., Lee, H. S., Chung, H. J., Shin, H. W., Cho, C. H., Kim, T. Y., et al. (2015). PHF2 histone demethylase acts as a tumor suppressor in association with p53 in cancer. Oncogene, 34(22), 2897–2909.
pubmed: 25043306 doi: 10.1038/onc.2014.219
Fu, Y., Liu, M., Li, F., Qian, L., Zhang, P., Lv, F., Cheng, W., & Hou, R. (2019). MiR-221 promotes hepatocellular carcinoma cells migration via targeting PHF2. BioMed Research International, 2019, 4371405.
pubmed: 31214616 pmcid: 6535842 doi: 10.1155/2019/4371405
Liu, Y., Chen, T., Guo, M., Li, Y., Zhang, Q., Tan, G., Yu, L., & Tan, Y. (2021). FOXA2-interacting FOXP2 prevents epithelial-mesenchymal transition of breast cancer cells by stimulating E-cadherin and PHF2 transcription. Frontiers in Oncology, 11, 605025.
pubmed: 33718155 pmcid: 7947682 doi: 10.3389/fonc.2021.605025
McCann, T. S., Parrish, J. K., Hsieh, J., Sechler, M., Sobral, L. M., Self, C., Jones, K. L., Goodspeed, A., Costello, J. C., & Jedlicka, P. (2020). KDM5A and PHF2 positively control expression of pro-metastatic genes repressed by EWS/Fli1, and promote growth and metastatic properties in Ewing sarcoma. Oncotarget, 11(43), 3818–3831.
pubmed: 33196691 pmcid: 7597412 doi: 10.18632/oncotarget.27737
Zhao, Z., Sun, C., Li, F., Han, J., Li, X., & Song, Z. (2015). Overexpression of histone demethylase JMJD5 promotes metastasis and indicates a poor prognosis in breast cancer. International Journal of Clinical and Experimental Pathology, 8(9), 10325–10334.
pubmed: 26617740 pmcid: 4637555
Yang, C. Y., Tsao, C. H., Hsieh, C. C., Lin, C. K., Lin, C. S., Li, Y. H., Chang, W. C., Cheng, J. C., Lin, G. J., Sytwu, H. K., et al. (2020). Downregulation of Jumonji-C domain-containing protein 5 inhibits proliferation by silibinin in the oral cancer PDTX model. PLoS ONE, 15(7), e0236101.
pubmed: 32678829 pmcid: 7367477 doi: 10.1371/journal.pone.0236101
Yao, Y., Zhou, W. Y., & He, R. X. (2019). Down-regulation of JMJD5 suppresses metastasis and induces apoptosis in oral squamous cell carcinoma by regulating p53/NF-kappaB pathway. Biomedicine & Pharmacotherapy, 109, 1994–2004.
doi: 10.1016/j.biopha.2018.07.144
Hsia, D. A., Tepper, C. G., Pochampalli, M. R., Hsia, E. Y., Izumiya, C., Huerta, S. B., Wright, M. E., Chen, H. W., Kung, H. J., & Izumiya, Y. (2010). KDM8, a H3K36me2 histone demethylase that acts in the cyclin A1 coding region to regulate cancer cell proliferation. Proceedings of the National Academy of Sciences of the United States of America, 107(21), 9671–9676.
pubmed: 20457893 pmcid: 2906833 doi: 10.1073/pnas.1000401107
Zhang, R., Huang, Q., Li, Y., & Song, Y. (2015). JMJD5 is a potential oncogene for colon carcinogenesis. International Journal of Clinical and Experimental Pathology, 8(6), 6482–6489.
pubmed: 26261525 pmcid: 4525859
Huang, X., Zhang, S., Qi, H., Wang, Z., Chen, H. W., Shao, J., & Shen, J. (2015). JMJD5 interacts with p53 and negatively regulates p53 function in control of cell cycle and proliferation. Biochim Biophys Acta, 1853(10 Pt A), 2286–2295.
pubmed: 26025680 doi: 10.1016/j.bbamcr.2015.05.026
Wu, J., He, Z., Yang, X. M., Li, K. L., Wang, D. L., & Sun, F. L. (2017). RCCD1 depletion attenuates TGF-beta-induced EMT and cell migration by stabilizing cytoskeletal microtubules in NSCLC cells. Cancer Letters, 400, 18–29.
pubmed: 28455245 doi: 10.1016/j.canlet.2017.04.021
Wang, H. J., Hsieh, Y. J., Cheng, W. C., Lin, C. P., Lin, Y. S., Yang, S. F., Chen, C. C., Izumiya, Y., Yu, J. S., Kung, H. J., et al. (2014). JMJD5 regulates PKM2 nuclear translocation and reprograms HIF-1alpha-mediated glucose metabolism. Proceedings of the National Academy of Sciences of the United States of America, 111(1), 279–284.
pubmed: 24344305 doi: 10.1073/pnas.1311249111
Wang, H. J., Pochampalli, M., Wang, L. Y., Zou, J. X., Li, P. S., Hsu, S. C., Wang, B. J., Huang, S. H., Yang, P., Yang, J. C., et al. (2019). KDM8/JMJD5 as a dual coactivator of AR and PKM2 integrates AR/EZH2 network and tumor metabolism in CRPC. Oncogene, 38(1), 17–32.
pubmed: 30072740 doi: 10.1038/s41388-018-0414-x
Wang, Z., Wang, C., Huang, X., Shen, Y., Shen, J., & Ying, K. (2012). Differential proteome profiling of pleural effusions from lung cancer and benign inflammatory disease patients. Biochimica et Biophysica Acta, 1824(4), 692–700.
pubmed: 22326748 doi: 10.1016/j.bbapap.2012.01.016
Vangimalla, S. S., Ganesan, M., Kharbanda, K. K., & Osna, N. A. (2017). Bifunctional enzyme JMJD6 contributes to multiple disease pathogenesis: New twist on the old story. Biomolecules, 7(2), 41.
pubmed: 28587176 pmcid: 5485730 doi: 10.3390/biom7020041
Hong, X., Zang, J., White, J., Wang, C., Pan, C. H., Zhao, R., Murphy, R. C., Dai, S., Henson, P., Kappler, J. W., et al. (2010). Interaction of JMJD6 with single-stranded RNA. Proc Natl Acad Sci U S A, 107(33), 14568–14572.
pubmed: 20679243 pmcid: 2930430 doi: 10.1073/pnas.1008832107
Heim, A., Grimm, C., Muller, U., Haussler, S., Mackeen, M. M., Merl, J., Hauck, S. M., Kessler, B. M., Schofield, C. J., Wolf, A., et al. (2014). Jumonji domain containing protein 6 (Jmjd6) modulates splicing and specifically interacts with arginine-serine-rich (RS) domains of SR- and SR-like proteins. Nucleic Acids Research, 42(12), 7833–7850.
pubmed: 24914048 pmcid: 4081092 doi: 10.1093/nar/gku488
Tong, D. (2021). The role of JMJD6/U2AF65/AR-V7 axis in castration-resistant prostate cancer progression. Cancer Cell International, 21(1), 45.
pubmed: 33430885 pmcid: 7802141 doi: 10.1186/s12935-020-01739-1
Paschalis, A., Welti, J., Neeb, A. J., Yuan, W., Figueiredo, I., Pereira, R., Ferreira, A., Riisnaes, R., Rodrigues, D. N., Jimenez-Vacas, J. M., et al. (2021). JMJD6 is a druggable oxygenase that regulates AR-V7 expression in prostate cancer. Cancer Research, 81(4), 1087–1100.
pubmed: 33822745 pmcid: 8025710 doi: 10.1158/0008-5472.CAN-20-1807
Lee, Y. F., Miller, L. D., Chan, X. B., Black, M. A., Pang, B., Ong, C. W., Salto-Tellez, M., Liu, E. T., & Desai, K. V. (2012). JMJD6 is a driver of cellular proliferation and motility and a marker of poor prognosis in breast cancer. Breast Cancer Research, 14(3), R85.
pubmed: 22621393 pmcid: 3446348 doi: 10.1186/bcr3200
Rahman, S., Sowa, M. E., Ottinger, M., Smith, J. A., Shi, Y., Harper, J. W., & Howley, P. M. (2011). The Brd4 extraterminal domain confers transcription activation independent of pTEFb by recruiting multiple proteins, including NSD3. Molecular and Cellular Biology, 31(13), 2641–2652.
pubmed: 21555454 pmcid: 3133372 doi: 10.1128/MCB.01341-10
Ormandy, C. J., Musgrove, E. A., Hui, R., Daly, R. J., & Sutherland, R. L. (2003). Cyclin D1, EMS1 and 11q13 amplification in breast cancer. Breast Cancer Research and Treatment, 78(3), 323–335.
pubmed: 12755491 doi: 10.1023/A:1023033708204
Song, Y. Q., Yang, G. J., Ma, D. L., Wang, W. H., & Leung, C. H. (2023). The role and prospect of lysine-specific demethylases in cancer chemoresistance. Medicinal Research Reviews, 43(5), 1438–1469.
pubmed: 37012609 doi: 10.1002/med.21955
Wirawan, A., Tajima, K., Takahashi, F., Mitsuishi, Y., Winardi, W., Hidayat, M., Hayakawa, D., Matsumoto, N., Izumi, K., Asao, T., et al. (2022). A novel therapeutic strategy targeting the mesenchymal phenotype of malignant pleural mesothelioma by suppressing LSD1. Molecular Cancer Research, 20(1), 127–138.
pubmed: 34593606 doi: 10.1158/1541-7786.MCR-21-0230
Verigos, J., Karakaidos, P., Kordias, D., Papoudou-Bai, A., Evangelou, Z., Harissis, H. V., Klinakis, A., & Magklara, A. (2019). The histone demethylase LSD1/KappaDM1A mediates chemoresistance in breast cancer via regulation of a stem cell program. Cancers (Basel), 11(10), 1585.
pubmed: 31627418 doi: 10.3390/cancers11101585
Peng, W., Zhang, H., Tan, S., Li, Y., Zhou, Y., Wang, L., Liu, C., Li, Q., Cen, X., Yang, S., et al. (2020). Synergistic antitumor effect of 5-fluorouracil with the novel LSD1 inhibitor ZY0511 in colorectal cancer. Therapeutic Advances in Medical Oncology, 12, 1758835920937428.
pubmed: 32754230 pmcid: 7378962 doi: 10.1177/1758835920937428
Li, Y., Tao, L., Zuo, Z., Zhou, Y., Qian, X., Lin, Y., Jie, H., Liu, C., Li, Z., Zhang, H., et al. (2019). ZY0511, a novel, potent and selective LSD1 inhibitor, exhibits anticancer activity against solid tumors via the DDIT4/mTOR pathway. Cancer Letters, 454, 179–190.
pubmed: 30978443 doi: 10.1016/j.canlet.2019.03.052
Augert, A., Eastwood, E., Ibrahim, A. H., Wu, N., Grunblatt, E., Basom, R., Liggitt, D., Eaton, K. D., Martins, R., Poirier, J. T., et al. (2019). Targeting NOTCH activation in small cell lung cancer through LSD1 inhibition. Science Signaling, 12(567), eaau2922.
pubmed: 30723171 pmcid: 6530478 doi: 10.1126/scisignal.aau2922
Ekstrom, T. L., Pathoulas, N. M., Huehls, A. M., Kanakkanthara, A., & Karnitz, L. M. (2021). VLX600 disrupts homologous recombination and synergizes with PARP inhibitors and cisplatin by inhibiting histone lysine demethylases. Molecular Cancer Therapeutics, 20(9), 1561–1571.
pubmed: 34224364 pmcid: 8419117 doi: 10.1158/1535-7163.MCT-20-1099
Bayo, J., Tran, T. A., Wang, L., Pena-Llopis, S., Das, A. K., & Martinez, E. D. (2018). Jumonji inhibitors overcome radioresistance in cancer through changes in H3K4 methylation at double-strand breaks. Cell Reports, 25(4), 1040–1050.
pubmed: 30355483 doi: 10.1016/j.celrep.2018.09.081
Macedo-Silva, C., Miranda-Goncalves, V., Lameirinhas, A., Lencart, J., Pereira, A., Lobo, J., Guimaraes, R., Martins, A. T., Henrique, R., Bravo, I., et al. (2020). JmjC-KDMs KDM3A and KDM6B modulate radioresistance under hypoxic conditions in esophageal squamous cell carcinoma. Cell Death & Disease, 11(12), 1068.
doi: 10.1038/s41419-020-03279-y
Wu, L. W., Zhou, D. M., Zhang, Z. Y., Zhang, J. K., Zhu, H. J., Lin, N. M., & Zhang, C. (2019). Suppression of LSD1 enhances the cytotoxic and apoptotic effects of regorafenib in hepatocellular carcinoma cells. Biochemical and Biophysical Research Communications, 512(4), 852–858.
pubmed: 30929918 doi: 10.1016/j.bbrc.2019.03.154
Jostes, S., Nettersheim, D., & Schorle, H. (2019). Epigenetic drugs and their molecular targets in testicular germ cell tumours. Nature Reviews. Urology, 16(4), 245–259.
pubmed: 30765888 doi: 10.1038/s41585-019-0154-x
Li, Z., Qin, T., Zhao, X., Zhang, X., Zhao, T., Yang, N., Miao, J., Ma, J., & Zhang, Z. (2021). Discovery of quinazoline derivatives as a novel class of potent and in vivo efficacious LSD1 inhibitors by drug repurposing. European Journal of Medicinal Chemistry, 225, 113778.
pubmed: 34416665 doi: 10.1016/j.ejmech.2021.113778
Zheng, Y., Ma, Y., Cao, H., Yan, L., Gu, Y., Ren, X., Jiao, X., Wan, S., & Shao, F. (2021). Identification of fenoldopam as a novel LSD1 inhibitor to abrogate the proliferation of renal cell carcinoma using drug repurposing strategy. Bioorganic Chemistry, 108, 104561.
pubmed: 33349457 doi: 10.1016/j.bioorg.2020.104561
Li, Z. R., Suo, F. Z., Hu, B., Guo, Y. J., Fu, D. J., Yu, B., Zheng, Y. C., & Liu, H. M. (2019). Identification of osimertinib (AZD9291) as a lysine specific demethylase 1 inhibitor. Bioorganic Chemistry, 84, 164–169.
pubmed: 30502627 doi: 10.1016/j.bioorg.2018.11.018
Kleszcz, R., Skalski, M., Krajka-Kuzniak, V., & Paluszczak, J. (2021). The inhibitors of KDM4 and KDM6 histone lysine demethylases enhance the anti-growth effects of erlotinib and HS-173 in head and neck cancer cells. European Journal of Pharmaceutical Sciences, 166, 105961.
pubmed: 34363938 doi: 10.1016/j.ejps.2021.105961
Milzman, J., Sheng, W., & Levy, D. (2021). Modeling LSD1-Mediated Tumor Stagnation. Bulletin of Mathematical Biology, 83(2), 15.
pubmed: 33433736 doi: 10.1007/s11538-020-00842-8
Soldi, R., Ghosh Halder, T., Weston, A., Thode, T., Drenner, K., Lewis, R., Kaadige, M. R., Srivastava, S., Daniel Ampanattu, S., Rodriguez Del Villar, R., et al. (2020). The novel reversible LSD1 inhibitor SP-2577 promotes anti-tumor immunity in SWItch/Sucrose-NonFermentable (SWI/SNF) complex mutated ovarian cancer. PLoS ONE, 15(7), e0235705.
pubmed: 32649682 pmcid: 7351179 doi: 10.1371/journal.pone.0235705
Carter, D. M., Specker, E., Malecki, P. H., Przygodda, J., Dudaniec, K., Weiss, M. S., Heinemann, U., Nazare, M., & Gohlke, U. (2021). Enhanced properties of a benzimidazole benzylpyrazole lysine demethylase inhibitor: Mechanism-of-action, binding site analysis, and activity in cellular models of prostate cancer. Journal of Medicinal Chemistry, 64(19), 14266–14282.
pubmed: 34555281 doi: 10.1021/acs.jmedchem.1c00693
Kanouni, T., Severin, C., Cho, R. W., Yuen, N. Y., Xu, J., Shi, L., Lai, C., Del Rosario, J. R., Stansfield, R. K., Lawton, L. N., et al. (2020). Discovery of CC-90011: A potent and selective reversible inhibitor of lysine specific demethylase 1 (LSD1). Journal of Medicinal Chemistry, 63(23), 14522–14529.
pubmed: 33034194 doi: 10.1021/acs.jmedchem.0c00978
Hollebecque, A., Salvagni, S., Plummer, R., Isambert, N., Niccoli, P., Capdevila, J., Curigliano, G., Moreno, V., Martin-Romano, P., Baudin, E., et al. (2021). Phase I study of lysine-specific demethylase 1 inhibitor, CC-90011, in patients with advanced solid tumors and relapsed/refractory non-Hodgkin lymphoma. Clinical Cancer Research, 27(2), 438–446.
pubmed: 33046517 doi: 10.1158/1078-0432.CCR-20-2380
Tayari, M. M., Santos, H. G. D., Kwon, D., Bradley, T. J., Thomassen, A., Chen, C., Dinh, Y., Perez, A., Zelent, A., Morey, L., et al. (2021). Clinical responsiveness to all-trans retinoic acid is potentiated by LSD1 inhibition and associated with a quiescent transcriptome in myeloid malignancies. Clinical Cancer Research, 27(7), 1893–1903.
pubmed: 33495312 pmcid: 8026558 doi: 10.1158/1078-0432.CCR-20-4054
Salamero, O., Montesinos, P., Willekens, C., Perez-Simon, J. A., Pigneux, A., Recher, C., Popat, R., Carpio, C., Molinero, C., Mascaro, C., et al. (2020). The LSD1 Inhibitor Iadademstat is active in acute myeloid leukemia. Cancer Discovery, 10(12), OF4.
doi: 10.1158/2159-8290.CD-RW2020-155
Kurmasheva, R. T., Erickson, S. W., Han, R., Teicher, B. A., Smith, M. A., Roth, M., Gorlick, R., & Houghton, P. J. (2021). In vivo evaluation of the lysine-specific demethylase (KDM1A/LSD1) inhibitor SP-2577 (Seclidemstat) against pediatric sarcoma preclinical models: A report from the Pediatric Preclinical Testing Consortium (PPTC). Pediatric Blood & Cancer, 68(11), e29304.
doi: 10.1002/pbc.29304
Johnston, G., Ramsey, H. E., Liu, Q., Wang, J., Stengel, K. R., Sampathi, S., Acharya, P., Arrate, M., Stubbs, M. C., Burn, T., et al. (2020). Nascent transcript and single-cell RNA-seq analysis defines the mechanism of action of the LSD1 inhibitor INCB059872 in myeloid leukemia. Gene, 752, 144758.
pubmed: 32422235 pmcid: 7401316 doi: 10.1016/j.gene.2020.144758
Salamero, O., Montesinos, P., Willekens, C., Perez-Simon, J. A., Pigneux, A., Recher, C., Popat, R., Carpio, C., Molinero, C., Mascaro, C., et al. (2020). First-in-human phase I study of Iadademstat (ORY-1001): A first-in-class lysine-specific histone demethylase 1A inhibitor, in relapsed or refractory acute myeloid leukemia. Journal of Clinical Oncology, 38(36), 4260–4273.
pubmed: 33052756 pmcid: 7768337 doi: 10.1200/JCO.19.03250
Yang, G. J., Wang, W., Mok, S. W. F., Wu, C., Law, B. Y. K., Miao, X. M., Wu, K. J., Zhong, H. J., Wong, C. Y., Wong, V. K. W., et al. (2018). Selective inhibition of lysine-specific demethylase 5A (KDM5A) Using a Rhodium(III) complex for triple-negative breast cancer therapy. Angewandte Chemie (International ed. in English), 57(40), 13091–13095.
pubmed: 29968419 doi: 10.1002/anie.201807305
Shin, S., & Janknecht, R. (2007). Activation of androgen receptor by histone demethylases JMJD2A and JMJD2D. Biochemical and Biophysical Research Communications, 359(3), 742–746.
pubmed: 17555712 doi: 10.1016/j.bbrc.2007.05.179
Kim, T. D., Oh, S., Shin, S., & Janknecht, R. (2012). Regulation of tumor suppressor p53 and HCT116 cell physiology by histone demethylase JMJD2D/KDM4D. PLoS ONE, 7(4), e34618.
pubmed: 22514644 pmcid: 3326058 doi: 10.1371/journal.pone.0034618
Yang, G. J., Zhu, M. H., Lu, X. J., Liu, Y. J., Lu, J. F., Leung, C. H., Ma, D. L., & Chen, J. (2021). The emerging role of KDM5A in human cancer. Journal of hematology & oncology, 14(1), 1–18.
doi: 10.1186/s13045-021-01041-1
Dai, B., Huang, H., Guan, F., Zhu, G. T., Xiao, Z. Y., Mao, B. B., Su, H. Y., & Hu, Z. Q. (2018). Histone demethylase KDM5A inhibits glioma cells migration and invasion by down regulating ZEB1. Biomedicine & Pharmacotherapy, 99, 72–80.
doi: 10.1016/j.biopha.2018.01.020
Sase, H., Nakanishi, Y., Aida, S., Horiguchi-Takei, K., Akiyama, N., Fujii, T., Sakata, K., Mio, T., Aoki, M., & Ishii, N. (2018). Acquired JHDM1D-BRAF fusion confers resistance to FGFR inhibition in FGFR2-amplified gastric cancer. Molecular Cancer Therapeutics, 17(10), 2217–2225.
pubmed: 30045926 doi: 10.1158/1535-7163.MCT-17-1022
Cheng, Y., Wang, Y., Li, J., Chang, I., & Wang, C. Y. (2017). A novel read-through transcript JMJD7-PLA2G4B regulates head and neck squamous cell carcinoma cell proliferation and survival. Oncotarget, 8(2), 1972–1982.
pubmed: 28030848 doi: 10.18632/oncotarget.14081
Bodmer, D., Schepens, M., Eleveld, M. J., & Schoenmakers, E. F. (2003). Geurts van Kessel A: Disruption of a novel gene, DIRC3, and expression of DIRC3-HSPBAP1 fusion transcripts in a case of familial renal cell cancer and t(2;3)(q35;q21). Genes, Chromosomes & Cancer, 38(2), 107–116.
doi: 10.1002/gcc.10243
Chang, S., Yim, S., & Park, H. (2019). The cancer driver genes IDH1/2, JARID1C/ KDM5C, and UTX/ KDM6A: Crosstalk between histone demethylation and hypoxic reprogramming in cancer metabolism. Experimental & Molecular Medicine, 51(6), 1–17.
doi: 10.1038/s12276-019-0230-6
Rondinelli, B., Schwerer, H., Antonini, E., Gaviraghi, M., Lupi, A., Frenquelli, M., Cittaro, D., Segalla, S., Lemaitre, J. M., & Tonon, G. (2015). H3K4me3 demethylation by the histone demethylase KDM5C/JARID1C promotes DNA replication origin firing. Nucleic Acids Research, 43(5), 2560–2574.
pubmed: 25712104 pmcid: 4357704 doi: 10.1093/nar/gkv090
Wang, N., Ma, T., & Yu, B. (2023). Targeting epigenetic regulators to overcome drug resistance in cancers. Signal Transduction and Targeted Therapy, 8(1), 69.
pubmed: 36797239 pmcid: 9935618 doi: 10.1038/s41392-023-01341-7
Petty, W. J., & Paz-Ares, L. (2023). Emerging strategies for the treatment of small cell lung cancer: A review. Jama Oncology, 9(3), 419–429.
pubmed: 36520421 doi: 10.1001/jamaoncol.2022.5631

Auteurs

Dali Tong (D)

Department of Urological Surgery, Daping Hospital, Army Medical University (Third Military Medical University), Chongqing, 400042, People's Republic of China. tongdali1985@163.com.

Ying Tang (Y)

Chongqing Key Laboratory of Translational Research for Cancer Metastasis and Individualized Treatment, Chongqing University Cancer Hospital, Chongqing, China. tangyingvip@163.com.

Peng Zhong (P)

Department of Pathology, Daping Hospital, Army Medical University (Third Military Medical University), Chongqing, 400042, People's Republic of China. zhongpeng19861001@163.com.

Classifications MeSH