References
- Llovet JM, Burroughs A, Bruix J. Hepatocellular carcinoma. Lancet. 2003;362(9399):1907–1917. doi:https://doi.org/10.1016/S0140-6736(03)14964-1
- Chen CJ, Yu MW, Liaw YF. Epidemiological characteristics and risk factors of hepatocellular carcinoma. J Gastroenterol Hepatol. 1997;12(9-10):S294–S308. doi:https://doi.org/10.1111/j.1440-1746.1997.tb00513.x
- Yang T, Zhang J, Lu J-H, Yang L-Q, Yang G-S, Wu M-C, Yu W-F. A new staging system for resectable hepatocellular carcinoma: comparison with six existing staging systems in a large Chinese cohort. J Cancer Res Clin Oncol. 2011;137(5):739–750. doi:https://doi.org/10.1007/s00432-010-0935-3
- Newman DJ, Cragg GM, Snader KM. Natural products as sources of new drugs over the period 1981-2002. J Nat Prod. 2003;66(7):1022–1037. doi:https://doi.org/10.1021/np030096l
- Minh CV, Nhiem NX, Yen HT, Kiem PV, Tai BH, Le Tuan Anh H, Hien TTT, Park S, Kim N, Kim SH, et al. Chemical constituents of Trichosanthes kirilowii and their cytotoxic activities. Arch Pharm Res. 2015;38(8):1443–1448. doi:https://doi.org/10.1007/s12272-014-0490-6
- Iwabuchi M, Kohno-Murase J, Imamura J. Delta 12-oleate desaturase-related enzymes associated with formation of conjugated trans-delta 11, cis-delta 13 double bonds. J Biol Chem. 2003;278(7):4603–10. doi:https://doi.org/10.1074/jbc.M210748200
- Shidoji Y, Ogawa H. Natural occurrence of cancer-preventive geranylgeranoic acid in medicinal herbs. J Lipid Res. 2004;45(6):1092–1103. doi:https://doi.org/10.1194/jlr.M300502-JLR200
- Hikino H, Yoshizawa M, Suzuki Y, Oshima Y, Konno C. Isolation and hypoglycemic activity of trichosans A, B, C, D, and E: glycans of Trichosanthes kirilowii roots. Planta Med. 1989;55(4):349–50. doi:https://doi.org/10.1055/s-2006-962025
- Lo H-Y, Li T-C, Yang T-Y, Li C-C, Chiang J-H, Hsiang C-Y, Ho T-Y. Hypoglycemic effects of Trichosanthes kirilowii and its protein constituent in diabetic mice: the involvement of insulin receptor pathway. BMC Complement Altern Med. 2017;17(1):53 doi:https://doi.org/10.1186/s12906-017-1578-6
- Yu X, Tang L, Wu H, Zhang X, Luo H, Guo R, Xu M, Yang H, Fan J, Wang Z, et al. Trichosanthis Fructus: botany, traditional uses, phytochemistry and pharmacology. J Ethnopharmacol. 2018;224:177–194. doi:https://doi.org/10.1016/j.jep.2018.05.034
- Liu F, Wang B, Wang Z, Yu S. Trichosanthin down-regulates Notch signaling and inhibits proliferation of the nasopharyngeal carcinoma cell line CNE2 in vitro. Fitoterapia. 2012;83(5):838–842. doi:https://doi.org/10.1016/j.fitote.2012.02.011
- Miao J, Jiang Y, Wang D, Zhou J, Fan C, Jiao F, Liu B, Zhang J, Wang Y, Zhang Q, et al. Trichosanthin suppresses the proliferation of glioma cells by inhibiting LGR5 expression and the Wnt/β-catenin signaling pathway . Oncol Rep. 2015;34(6):2845–2852. doi:https://doi.org/10.3892/or.2015.4290
- Premkumar DR, Jane EP, Pollack IF. Cucurbitacin-I inhibits Aurora kinase A, Aurora kinase B and survivin, induces defects in cell cycle progression and promotes ABT-737-induced cell death in a caspase-independent manner in malignant human glioma cells. Cancer Biol Ther. 2015;16(2):233–243. doi:https://doi.org/10.4161/15384047.2014.987548
- Liu P, Xiang Y, Liu X, Zhang T, Yang R, Chen S, Xu L, Yu Q, Zhao H, Zhang L, et al. Cucurbitacin B induces the lysosomal degradation of EGFR and suppresses the CIP2A/PP2A/Akt signaling axis in gefitinib-resistant non-small cell lung cancer. Molecules. 2019;24(3):647. doi:https://doi.org/10.3390/molecules24030647
- Song L, Chang J, Li Z. A serine protease extracted from Trichosanthes kirilowii induces apoptosis via the PI3K/AKT-mediated mitochondrial pathway in human colorectal adenocarcinoma cells. Food Funct. 2016;7(2):843–854. doi:https://doi.org/10.1039/c5fo00760g
- Song L, Xu XB, Li ZY. A serine protease extracted from Trichosanthes kirilowii inhibits epithelial-mesenchymal transition via antagonizing PKM2-mediated STAT3/Snail1 pathway in human colorectal adenocarcinoma cells. J Funct Foods. 2018;40:639–647. doi:https://doi.org/10.1016/j.jff.2017.12.001
- Hsu PP, Sabatini DM. Cancer cell metabolism: Warburg and beyond. Cell. 2008;134(5):703–707. doi:https://doi.org/10.1016/j.cell.2008.08.021
- Kroemer G, Pouyssegur J. Tumor cell metabolism: cancer's Achilles' heel. Cancer Cell. 2008;13(6):472–482. doi:https://doi.org/10.1016/j.ccr.2008.05.005
- Potter M, Newport E, Morten KJ. The Warburg effect: 80 years on. Biochem Soc Trans. 2016;44(5):1499–1505. doi:https://doi.org/10.1042/BST20160094
- Wong N, Ojo D, Yan J, Tang D. PKM2 contributes to cancer metabolism. Cancer Lett. 2015;356(2 Pt A):184–191. doi:https://doi.org/10.1016/j.canlet.2014.01.031
- Jung Y, Jang YJ, Kang MH, Park YS, Oh SJ, Lee DC, Xie Z, Yoo H-S, Park KC, Yeom YI, et al. Metabolic signature genes associated with susceptibility to pyruvate kinase, muscle type 2 gene ablation in cancer cells. Mol Cells. 2013;35(4):335–341. doi:https://doi.org/10.1007/s10059-013-2319-4
- Ogawa H, Nagano H, Konno M, Eguchi H, Koseki JUN, Kawamoto K, Nishida N, Colvin HUGH, Tomokuni A, Tomimaru Y, et al. The combination of the expression of hexokinase 2 and pyruvate kinase M2 is a prognostic marker in patients with pancreatic cancer. Mol Clin Oncol. 2015;3(3):563–571. doi:https://doi.org/10.3892/mco.2015.490
- Mazurek S, Boschek CB, Hugo F, Eigenbrodt E. Pyruvate kinase type M2 and its role in tumor growth and spreading. Semin Cancer Biol. 2005;15(4):300–308. doi:https://doi.org/10.1016/j.semcancer.2005.04.009
- Lu Z. Nonmetabolic functions of pyruvate kinase isoform M2 in controlling cell cycle progression and tumorigenesis. Chin J Cancer. 2012;31(1):5–7. doi:https://doi.org/10.5732/cjc.011.10446
- Yang W, Zheng Y, Xia Y, Ji H, Chen X, Guo F, Lyssiotis CA, Aldape K, Cantley LC, Lu Z, et al. ERK1/2-dependent phosphorylation and nuclear translocation of PKM2 promotes the Warburg effect. Nat Cell Biol. 2012;14(12):1295–1304. doi:https://doi.org/10.1038/ncb2629
- Luo W, Hu H, Chang R, Zhong J, Knabel M, O'Meally R, Cole RN, Pandey A, Semenza GL. Pyruvate kinase M2 is a PHD3-stimulated coactivator for hypoxia-inducible factor 1. Cell. 2011;145(5):732–744. doi:https://doi.org/10.1016/j.cell.2011.03.054
- David CJ, Chen M, Assanah M, Canoll P, Manley JL. HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer. Nature. 2010;463(7279):364–368. doi:https://doi.org/10.1038/nature08697
- Yang P, Li Z, Wang Y, Zhang L, Wu H, Li Z. Secreted pyruvate kinase M2 facilitates cell migration via PI3K/Akt and Wnt/β-catenin pathway in colon cancer cells . Biochem Biophys Res Commun. 2015;459(2):327–332. doi:https://doi.org/10.1016/j.bbrc.2015.02.112
- Song L, Li ZY, Liu WP, Zhao MR. Crosstalk between Wnt/β-catenin and Hedgehog/Gli signaling pathways in colon cancer and implications for therapy . Cancer Biol Ther. 2015;16(1):1–7. doi:https://doi.org/10.4161/15384047.2014.972215
- Chang HY, Chen SY, Wu CH, Lu CC, Yen GC. Glycyrrhizin attenuates the process of epithelial-to-mesenchymal transition by modulating HMGB1 initiated novel signaling pathway in prostate cancer cells. J Agric Food Chem. 2019;67(12):3323–3332. doi:https://doi.org/10.1021/acs.jafc.9b00251
- Mayevsky A. Mitochondrial function and energy metabolism in cancer cells: past overview and future perspectives. Mitochondrion. 2009;9(3):165–179. doi:https://doi.org/10.1016/j.mito.2009.01.009
- Vander Heiden MG, Cantley LC, Thompson CB. Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science. 2009;324(5930):1029–1033. doi:https://doi.org/10.1126/science.1160809
- Fan F-T, Shen C-S, Tao L, Tian C, Liu Z-G, Zhu Z-J, Liu Y-P, Pei C-S, Wu H-Y, Zhang L, et al. PKM2 regulates hepatocellular carcinoma cell epithelial-mesenchymal transition and migration upon EGFR activation. Asian Pac J Cancer Prev. 2014;15(5):1961–1970. doi:https://doi.org/10.7314/apjcp.2014.15.5.1961
- Dong T, Yan Y, Chai H, Chen S, Xiong X, Sun D, Yu Y, Deng L, Cheng F. Pyruvate kinase M2 affects liver cancer cell behavior through up-regulation of HIF-1α and Bcl-xL in culture . Biomed Pharmacother. 2015;69:277–284. doi:https://doi.org/10.1016/j.biopha.2014.12.010
- Chen Y-L, Song J-J, Chen X-C, Xu W, Zhi Q, Liu Y-P, Xu H-Z, Pan J-S, Ren J-L, Guleng B, et al. Mechanisms of pyruvate kinase M2 isoform inhibits cell motility in hepatocellular carcinoma cells. World J Gastroenterol. 2015;21(30):9093–9102.: doi:https://doi.org/10.3748/wjg.v21.i30.9093
- Lee J, Kim HK, Han YM, Kim J. Pyruvate kinase isozyme type M2 (PKM2) interacts and cooperates with Oct-4 in regulating transcription. Int J Biochem Cell Biol. 2008;40(5):1043–1054. doi:https://doi.org/10.1016/j.biocel.2007.11.009
- Yang W, Xia Y, Hawke D, Li X, Liang J, Xing D, Aldape K, Hunter T, Alfred Yung WK, Lu Z, et al. PKM2 phosphorylates histone H3 and promotes gene transcription and tumorigenesis. Cell. 2012;150(4):685–696. doi:https://doi.org/10.1016/j.cell.2012.07.018
- Christofk HR, Vander Heiden MG, Harris MH, Ramanathan A, Gerszten RE, Wei R, Fleming MD, Schreiber SL, Cantley LC. The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth. Nature. 2008;452(7184):230–233. doi:https://doi.org/10.1038/nature06734
- Shiio Y, Donohoe S, Yi EC, Goodlett DR, Aebersold R, Eisenman RN. Quantitative proteomic analysis of Myc oncoprotein function. EMBO J. 2002;21(19):5088–5096. doi:https://doi.org/10.1093/emboj/cdf525
- Schlosser I, Hölzel M, Hoffmann R, Burtscher H, Kohlhuber F, Schuhmacher M, Chapman R, Weidle UH, Eick D. Dissection of transcriptional programmes in response to serum and c-Myc in a human B-cell line. Oncogene. 2005;24(3):520–524. doi:https://doi.org/10.1038/sj.onc.1208198
- Kobayashi M, Honma T, Matsuda Y, Suzuki Y, Narisawa R, Ajioka Y, Asakura H. Nuclear translocation of beta-catenin in colorectal cancer. Br J Cancer. 2000;82(10):1689–1693. doi:https://doi.org/10.1054/bjoc.1999.1112