References
- Anastasiou, D., Poulogiannis, G., Asara, J.M., Boxer, M.B., Jiang, J.K., Shen, M., Bellinger, G., Sasaki, A.T., Locasale, J.W., Auld, D.S., et al. (2011). Inhibition of pyruvate kinase M2 by reactive oxygen species contributes to cellular antioxidant responses. Science 334, 1278-1283. https://doi.org/10.1126/science.1211485
- Azoitei, N., Becher, A., Steinestel, K., Rouhi, A., Diepold, K., Genze, F., Simmet, T., and Seufferlein, T. (2016). PKM2 promotes tumor angiogenesis by regulating HIF-1alpha through NF-kappaB activation. Mol. Cancer 15, 3.
- Barbie, T.U., Alexe, G., Aref, A.R., Li, S., Zhu, Z., Zhang, X., Imamura, Y., Thai, T.C., Huang, Y., Bowden, M., et al. (2014). Targeting an IKBKE cytokine network impairs triple-negative breast cancer growth. J. Clin. Invest. 124, 5411-5423. https://doi.org/10.1172/JCI75661
- Bianchini, G., Balko, J.M., Mayer, I.A., Sanders, M.E., and Gianni, L. (2016). Triple-negative breast cancer: challenges and opportunities of a heterogeneous disease. Nat. Rev. Clin. Oncol. 13, 674-690. https://doi.org/10.1038/nrclinonc.2016.66
- Bonotto, M., Gerratana, L., Poletto, E., Driol, P., Giangreco, M., Russo, S., Minisini, A.M., Andreetta, C., Mansutti, M., Pisa, F.E., et al. (2014). Measures of outcome in metastatic breast cancer: insights from a real-world scenario. Oncologist 19, 608-615. https://doi.org/10.1634/theoncologist.2014-0002
- Chaneton, B. and Gottlieb, E. (2012). Rocking cell metabolism: revised functions of the key glycolytic regulator PKM2 in cancer. Trends Biochem. Sci. 37, 309-316. https://doi.org/10.1016/j.tibs.2012.04.003
- Chang, B., Sokhn, J., James, E., and Abu-Khalaf, M. (2014). Prolonged progression-free survival in a patient with triple-negative breast cancer metastatic to the liver after chemotherapy and local radiation therapy. Clin. Breast Cancer 14, e61-e64. https://doi.org/10.1016/j.clbc.2013.11.007
- Chiavarina, B., Whitaker-Menezes, D., Martinez-Outschoorn, U.E., Witkiewicz, A.K., Birbe, R., Howell, A., Pestell, R.G., Smith, J., Daniel, R., Sotgia, F., et al. (2011). Pyruvate kinase expression (PKM1 and PKM2) in cancer-associated fibroblasts drives stromal nutrient production and tumor growth. Cancer Biol. Ther. 12, 1101-1113. https://doi.org/10.4161/cbt.12.12.18703
- Christofk, H.R., Vander Heiden, M.G., Harris, M.H., Ramanathan, A., Gerszten, R.E., Wei, R., Fleming, M.D., Schreiber, S.L., and Cantley, L.C. (2008). The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth. Nature 452, 230-233. https://doi.org/10.1038/nature06734
- Dang, C.V. (2012). Links between metabolism and cancer. Genes Dev. 26, 877-890. https://doi.org/10.1101/gad.189365.112
- DeBerardinis, R.J., Lum, J.J., Hatzivassiliou, G., and Thompson, C.B. (2008). The biology of cancer: metabolic reprogramming fuels cell growth and proliferation. Cell Metab. 7, 11-20. https://doi.org/10.1016/j.cmet.2007.10.002
- Fantin, V.R., St-Pierre, J., and Leder, P. (2006). Attenuation of LDH-A expression uncovers a link between glycolysis, mitochondrial physiology, and tumor maintenance. Cancer Cell 9, 425-434. https://doi.org/10.1016/j.ccr.2006.04.023
- Gao, X., Wang, H., Yang, J.J., Liu, X., and Liu, Z.R. (2012). Pyruvate kinase M2 regulates gene transcription by acting as a protein kinase. Mol. Cell 45, 598-609. https://doi.org/10.1016/j.molcel.2012.01.001
- Han, D., Wei, W., Chen, X., Zhang, Y., Wang, Y., Zhang, J., Wang, X., Yu, T., Hu, Q., Liu, N., et al. (2015). NF-kappaB/RelA-PKM2 mediates inhibition of glycolysis by fenofibrate in glioblastoma cells. Oncotarget 6, 26119-26128. https://doi.org/10.18632/oncotarget.4444
- Harris, I., McCracken, S., and Mak, T.W. (2012). PKM2: a gatekeeper between growth and survival. Cell Res. 22, 447-449. https://doi.org/10.1038/cr.2011.203
- Hayden, M.S. and Ghosh, S. (2008). Shared principles in NF-kappaB signaling. Cell 132, 344-362. https://doi.org/10.1016/j.cell.2008.01.020
-
House, C.D., Grajales, V., Ozaki, M., Jordan, E., Wubneh, H., Kimble, D.C., James, J.M., Kim, M.K., and Annunziata, C.M. (2018).
$IKK_\varepsilon$ cooperates with either MEK or non-canonical NF-kB driving growth of triple-negative breast cancer cells in different contexts. BMC Cancer 18, 595. https://doi.org/10.1186/s12885-018-4507-2 - Israel, A. (2010). The IKK complex, a central regulator of NF-kappaB activation. Cold Spring Harb. Perspect. Biol. 2, a000158. https://doi.org/10.1101/cshperspect.a000158
- Ito-Kureha, T., Koshikawa, N., Yamamoto, M., Semba, K., Yamaguchi, N., Yamamoto, T., Seiki, M., and Inoue, J. (2015). Tropomodulin 1 expression driven by NF-kappaB enhances breast cancer growth. Cancer Res. 75, 62-72. https://doi.org/10.1158/0008-5472.CAN-13-3455
- Kim, D.J., Park, Y.S., Kang, M.G., You, Y.M., Jung, Y., Koo, H., Kim, J.A., Kim, M.J., Hong, S.M., Lee, K.B., et al. (2015). Pyruvate kinase isoenzyme M2 is a therapeutic target of gemcitabine-resistant pancreatic cancer cells. Exp. Cell Res. 336, 119-129. https://doi.org/10.1016/j.yexcr.2015.05.017
- King, A. and Gottlieb, E. (2009). Glucose metabolism and programmed cell death: an evolutionary and mechanistic perspective. Curr. Opin. Cell Biol. 21, 885-893. https://doi.org/10.1016/j.ceb.2009.09.009
- Kroemer, G. and Pouyssegur, J. (2008). Tumor cell metabolism: cancer's Achilles' heel. Cancer Cell 13, 472-482. https://doi.org/10.1016/j.ccr.2008.05.005
- Kuo, W.Y., Hwu, L., Wu, C.Y., Lee, J.S., Chang, C.W., and Liu, R.S. (2017). STAT3/NF-kappaB-regulated lentiviral TK/GCV suicide gene therapy for Cisplatin-resistant triple-negative breast cancer. Theranostics 7, 647-663. https://doi.org/10.7150/thno.16827
- Lebert, J.M., Lester, R., Powell, E., Seal, M., and McCarthy, J. (2018). Advances in the systemic treatment of triple-negative breast cancer. Curr. Oncol. 25(Suppl 1), S142-S150. https://doi.org/10.3747/co.25.3954
- Luo, W., Hu, H., Chang, R., Zhong, J., Knabel, M., O'Meally, R., Cole, R.N., Pandey, A., and Semenza, G.L. (2011). Pyruvate kinase M2 is a PHD3-stimulated coactivator for hypoxia-inducible factor 1. Cell 145, 732-744. https://doi.org/10.1016/j.cell.2011.03.054
- Luo, W. and Semenza, G.L. (2011). Pyruvate kinase M2 regulates glucose metabolism by functioning as a coactivator for hypoxia-inducible factor 1 in cancer cells. Oncotarget 2, 551-556. https://doi.org/10.18632/oncotarget.299
- Lv, L., Li, D., Zhao, D., Lin, R., Chu, Y., Zhang, H., Zha, Z., Liu, Y., Li, Z., Xu, Y., et al. (2011). Acetylation targets the M2 isoform of pyruvate kinase for degradation through chaperone-mediated autophagy and promotes tumor growth. Mol. Cell 42, 719-730. https://doi.org/10.1016/j.molcel.2011.04.025
- Mazurek, S. (2007). Pyruvate kinase type M2: a key regulator within the tumour metabolome and a tool for metabolic profiling of tumours. Ernst Schering Found. Symp. Proc. (4), 99-124.
- Mazurek, S. (2011). Pyruvate kinase type M2: a key regulator of the metabolic budget system in tumor cells. Int. J. Biochem. Cell Biol. 43, 969-980. https://doi.org/10.1016/j.biocel.2010.02.005
- Morita, M., Sato, T., Nomura, M., Sakamoto, Y., Inoue, Y., Tanaka, R., Ito, S., Kurosawa, K., Yamaguchi, K., Sugiura, Y., et al. (2018). PKM1 confers metabolic advantages and promotes cell-autonomous tumor cell growth. Cancer Cell 33, 355-367.e7. https://doi.org/10.1016/j.ccell.2018.02.004
- Nabel, G.J. and Verma, I.M. (1993). Proposed NF-kappa B/I kappa B family nomenclature. Genes Dev. 7, 2063. https://doi.org/10.1101/gad.7.11.2063
- Okazaki, M., Fushida, S., Tsukada, T., Kinoshita, J., Oyama, K., Miyashita, T., Ninomiya, I., Harada, S., and Ohta, T. (2018). The effect of HIF-1alpha and PKM1 expression on acquisition of chemoresistance. Cancer Manag. Res. 10, 1865-1874. https://doi.org/10.2147/CMAR.S166136
- Qiao, Y., He, H., Jonsson, P., Sinha, I., Zhao, C., and Dahlman-Wright, K. (2016). AP-1 is a key regulator of Proinflammatory cytokine TNFalphamediated triple-negative breast cancer progression. J. Biol. Chem. 291, 5068-5079. https://doi.org/10.1074/jbc.M115.702571
- Tennant, D.A., Duran, R.V., Boulahbel, H., and Gottlieb, E. (2009). Metabolic transformation in cancer. Carcinogenesis 30, 1269-1280. https://doi.org/10.1093/carcin/bgp070
- Tennant, D.A., Duran, R.V., and Gottlieb, E. (2010). Targeting metabolic transformation for cancer therapy. Nat. Rev. Cancer 10, 267-277. https://doi.org/10.1038/nrc2817
- Tutt, A., Tovey, H., Cheang, M.C.U., Kernaghan, S., Kilburn, L., Gazinska, P., Owen, J., Abraham, J., Barrett, S., Barrett-Lee, P., et al. (2018). Carboplatin in BRCA1/2-mutated and triple-negative breast cancer BRCAness subgroups: the TNT Trial. Nat. Med. 24, 628-637. https://doi.org/10.1038/s41591-018-0009-7
- Vander Heiden, M.G., Cantley, L.C., and Thompson, C.B. (2009). Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science 324, 1029-1033. https://doi.org/10.1126/science.1160809
- 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. Proc. Natl. Acad. Sci. U. S. A. 111, 279-284. https://doi.org/10.1073/pnas.1311249111
- Wu, X., Zahari, M.S., Ma, B., Liu, R., Renuse, S., Sahasrabuddhe, N.A., Chen, L., Chaerkady, R., Kim, M.S., Zhong, J., et al. (2015). Global phosphotyrosine survey in triple-negative breast cancer reveals activation of multiple tyrosine kinase signaling pathways. Oncotarget 6, 29143-29160. https://doi.org/10.18632/oncotarget.5020
- Yamaguchi, N., Ito, T., Azuma, S., Ito, E., Honma, R., Yanagisawa, Y., Nishikawa, A., Kawamura, M., Imai, J., Watanabe, S., et al. (2009). Constitutive activation of nuclear factor-kappaB is preferentially involved in the proliferation of basal-like subtype breast cancer cell lines. Cancer Sci. 100, 1668-1674. https://doi.org/10.1111/j.1349-7006.2009.01228.x
- Yang, W., Xia, Y., Hawke, D., Li, X., Liang, J., Xing, D., Aldape, K., Hunter, T., Alfred Yung, W.K., and Lu, Z. (2012a). PKM2 phosphorylates histone H3 and promotes gene transcription and tumorigenesis. Cell 150, 685-696. https://doi.org/10.1016/j.cell.2012.07.018
- Yang, W., Zheng, Y., Xia, Y., Ji, H., Chen, X., Guo, F., Lyssiotis, C.A., Aldape, K., Cantley, L.C., and Lu, Z. (2012b). ERK1/2-dependent phosphorylation and nuclear translocation of PKM2 promotes the Warburg effect. Nat. Cell Biol. 14, 1295-1304. https://doi.org/10.1038/ncb2629
- Zhou, Z., Li, M., Zhang, L., Zhao, H., Sahin, O., Chen, J., Zhao, J.J., Songyang, Z., and Yu, D. (2018). Oncogenic kinase-induced PKM2 tyrosine 105 phosphorylation converts nononcogenic PKM2 to a tumor promoter and induces cancer stem-like cells. Cancer Res. 78, 2248-2261. https://doi.org/10.1158/0008-5472.CAN-17-2726
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