Hypoxia-inducible KDM3A addiction in multiple myeloma

Röllig, 2015, Multiple myeloma, Lancet, 385, 2197, 10.1016/S0140-6736(14)60493-1 Easwaran, 2014, Cancer epigenetics: tumor heterogeneity, plasticity of stem-like states, and drug resistance, Mol Cell, 54, 716, 10.1016/j.molcel.2014.05.015 Kawano, 2015, Targeting the bone marrow microenvironment in multiple myeloma, Immunol Rev, 263, 160, 10.1111/imr.12233 Kikuchi, 2015, Phosphorylation-mediated EZH2 inactivation promotes drug resistance in multiple myeloma, J Clin Invest, 125, 4375, 10.1172/JCI80325 Umezu, 2014, Exosomal miR-135b shed from hypoxic multiple myeloma cells enhances angiogenesis by targeting factor-inhibiting HIF-1, Blood, 124, 3748, 10.1182/blood-2014-05-576116 Azab, 2012, Hypoxia promotes dissemination of multiple myeloma through acquisition of epithelial to mesenchymal transition-like features, Blood, 119, 5782, 10.1182/blood-2011-09-380410 Kawano, 2013, Hypoxia reduces CD138 expression and induces an immature and stem cell-like transcriptional program in myeloma cells, Int J Oncol, 43, 1809, 10.3892/ijo.2013.2134 Maiso, 2015, Metabolic signature identifies novel targets for drug resistance in multiple myeloma, Cancer Res, 75, 2071, 10.1158/0008-5472.CAN-14-3400 Ikeda, 2017, Hypoxia-inducible microRNA-210 regulates the DIMT1-IRF4 oncogenic axis in multiple myeloma, Cancer Sci, 108, 641, 10.1111/cas.13183 Carmeliet, 1998, Role of HIF-1alpha in hypoxia-mediated apoptosis, cell proliferation and tumour angiogenesis, Nature, 394, 485, 10.1038/28867 Gardner, 2001, Hypoxia inhibits G1/S transition through regulation of p27 expression, J Biol Chem, 276, 7919, 10.1074/jbc.M010189200 Goda, 2003, Hypoxia-inducible factor 1alpha is essential for cell cycle arrest during hypoxia, Mol Cell Biol, 23, 359, 10.1128/MCB.23.1.359-369.2003 Kim, 2004, BH3-only protein Noxa is a mediator of hypoxic cell death induced by hypoxia-inducible factor 1alpha, J Exp Med, 199, 113, 10.1084/jem.20030613 Storti, 2013, Hypoxia-inducible factor (HIF)-1α suppression in myeloma cells blocks tumoral growth in vivo inhibiting angiogenesis and bone destruction, Leukemia, 27, 1697, 10.1038/leu.2013.24 Martin, 2011, The emerging role of hypoxia, HIF-1 and HIF-2 in multiple myeloma, Leukemia, 25, 1533, 10.1038/leu.2011.122 Shaffer, 2008, IRF4 addiction in multiple myeloma, Nature, 454, 226, 10.1038/nature07064 Nakano, 2012, Up-regulation of hexokinaseII in myeloma cells: targeting myeloma cells with 3-bromopyruvate, J Bioenerg Biomembr, 44, 31, 10.1007/s10863-012-9412-9 Osawa, 2011, Increased expression of histone demethylase JHDM1D under nutrient starvation suppresses tumor growth via down-regulating angiogenesis, Proc Natl Acad Sci USA, 108, 20725, 10.1073/pnas.1108462109 Osawa, 2013, Inhibition of histone demethylase JMJD1A improves anti-angiogenic therapy and reduces tumor-associated macrophages, Cancer Res, 73, 3019, 10.1158/0008-5472.CAN-12-3231 Osawa, 2013, Targeting cancer cells resistant to hypoxia and nutrient starvation to improve anti-angiogeneic therapy, Cell Cycle, 12, 2519, 10.4161/cc.25729 Wellmann, 2008, Hypoxia upregulates the histone demethylase JMJD1A via HIF-1, Biochem Biophys Res Commun, 372, 892, 10.1016/j.bbrc.2008.05.150 Beyer, 2008, The histone demethylases JMJD1A and JMJD2B are transcriptional targets of hypoxia-inducible factor HIF, J Biol Chem, 283, 36542, 10.1074/jbc.M804578200 Pollard, 2008, Regulation of Jumonji-domain-containing histone demethylases by hypoxia-inducible factor (HIF)-1alpha, Biochem J, 416, 387, 10.1042/BJ20081238 Krieg, 2010, Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1 alpha enhances hypoxic gene expression and tumor growth, Mol Cell Biol, 30, 344, 10.1128/MCB.00444-09 Mattioli, 2005, Gene expression profiling of plasma cell dyscrasias reveals molecular patterns associated with distinct IGH translocations in multiple myeloma, Oncogene, 24, 2461, 10.1038/sj.onc.1208447 Chng, 2007, Molecular dissection of hyperdiploid multiple myeloma by gene expression profiling, Cancer Res, 67, 2982, 10.1158/0008-5472.CAN-06-4046 Uemura, 2010, Jumonji domain containing 1A is a novel prognostic marker for colorectal cancer: in vivo identification from hypoxic tumor cells, Clin Cancer Res, 16, 4636, 10.1158/1078-0432.CCR-10-0407 Wade, 2015, The histone demethylase enzyme KDM3A is a key estrogen receptor regulator in breast cancer, Nucleic Acids Res, 43, 196, 10.1093/nar/gku1298 Ohguchi, 2016, The KDM3A-KLF2-IRF4 axis maintains myeloma cell survival, Nat Commun, 7, 10258, 10.1038/ncomms10258 Cho, 2014, MALAT1 long non-coding RNA is overexpressed in multiple myeloma and may serve as a marker to predict disease progression, BMC Cancer, 14, 809, 10.1186/1471-2407-14-809 Handa, 2017, Long non-coding RNA MALAT1 is an inducible stress response gene associated with extramedullary spread and poor prognosis of multiple myeloma, Br J Haematol, 179, 449, 10.1111/bjh.14882 Ronchetti, 2016, Distinct lncRNA transcriptional fingerprints characterize progressive stages of multiple myeloma, Oncotarget, 7, 14814, 10.18632/oncotarget.7442 Tee, 2014, The histone demethylase JMJD1A induces cell migration and invasion by up-regulating the expression of the long noncoding RNA MALAT1, Oncotarget, 5, 1793, 10.18632/oncotarget.1785 Barski, 2007, High-resolution profiling of histone methylations in the human genome, Cell, 129, 823, 10.1016/j.cell.2007.05.009 Cho, 2012, The JmjC domain-containing histone demethylase KDM3A is a positive regulator of the G1/S transition in cancer cells via transcriptional regulation of the HOXA1 gene, Int J Cancer, 131, E179, 10.1002/ijc.26501 Ji, 2003, MALAT-1, a novel noncoding RNA, and thymosin beta4 predict metastasis and survival in early-stage non-small cell lung cancer, Oncogene, 22, 8031, 10.1038/sj.onc.1206928 Yoshimoto, 2016, MALAT1 long non-coding RNA in cancer, Biochim Biophys Acta, 1859, 192, 10.1016/j.bbagrm.2015.09.012 Yang, 2015, Elevated JMJD1A is a novel predictor for prognosis and a potential therapeutic target for gastric cancer, Int J Clin Exp Pathol, 8, 11092 Luo, 2016, The lncRNA MALAT1, acting through HIF-1α stabilization, enhances arsenite-induced glycolysis in human hepatic L-02 cells, Biochim Biophys Acta, 1862, 1685, 10.1016/j.bbadis.2016.06.004 Zeng, 2002, RNA interference in human cells is restricted to the cytoplasm, RNA, 8, 855, 10.1017/S1355838202020071 Leung-Hagesteijn, 2013, Xbp1s-negative tumor B cells and pre-plasmablasts mediate therapeutic proteasome inhibitor resistance in multiple myeloma, Cancer Cell, 24, 289, 10.1016/j.ccr.2013.08.009 Lu, 2014, The myeloma drug lenalidomide promotes the cereblon-dependent destruction of Ikaros proteins, Science, 343, 305, 10.1126/science.1244917 Krönke, 2014, Lenalidomide causes selective degradation of IKZF1 and IKZF3 in multiple myeloma cells, Science, 343, 301, 10.1126/science.1244851 Gandhi, 2014, Immunomodulatory agents lenalidomide and pomalidomide co-stimulate T cells by inducing degradation of T cell repressors Ikaros and Aiolos via modulation of the E3 ubiquitin ligase complex CRL4(CRBN.), Br J Haematol, 164, 811, 10.1111/bjh.12708 Bjorklund, 2015, Rate of CRL4(CRBN) substrate Ikaros and Aiolos degradation underlies differential activity of lenalidomide and pomalidomide in multiple myeloma cells by regulation of c-Myc and IRF4, Blood Cancer J, 5, e354, 10.1038/bcj.2015.66 Hu, 2013, Synergistic induction of apoptosis in multiple myeloma cells by bortezomib and hypoxia-activated prodrug TH-302, in vivo and in vitro, Mol Cancer Ther, 12, 1763, 10.1158/1535-7163.MCT-13-0123