References
- Rizeq B, Gupta I, Ilesanmi J, AlSafran M, Rahman M, Ouhtit A. The power of phytochemicals combination in cancer chemoprevention. J Cancer. 2020;11(15):4521–4533. doi:https://doi.org/10.7150/jca.34374
- Singh J, Hussain Y, Luqman S, Meena A. Targeting Ca2+ signalling through phytomolecules to combat cancer. Pharmacol Res. 2019;146:104282. doi:https://doi.org/10.1016/j.phrs.2019.104282
- Saghafi T, Taheri RA, Parkkila S, Emameh RZ. Phytochemicals as modulators of long non-coding RNAs and inhibitors of cancer-related carbonic anhydrases. Int J Mol Sci. 2019;20:2939. doi:https://doi.org/10.3390/ijms20122939
- Ranjan A, Ramachandran S, Gupta N, Kaushik I, Wright S, Srivastava S, Das H, Srivastava S, Prasad S, Srivastava SK, et al. Role of phytochemicals in cancer prevention. Int J Mol Sci. 2019;20(20):4981. doi:https://doi.org/10.3390/ijms20204981
- Chen CY, Kao CL, Liu CM. The cancer prevention, anti-inflammatory and anti-oxidation of bioactive phytochemicals targeting the TLR4 signaling pathway. Int J Mol Sci. 2018;19(9):2729. doi:https://doi.org/10.3390/ijms19092729
- Sehrawat A, Roy R, Pore SK, Hahm E-R, Samanta SK, Singh KB, Kim S-H, Singh K, Singh SV. Mitochondrial dysfunction in cancer chemoprevention by phytochemicals from dietary and medicinal plants. Semin Cancer Biol. 2017;47:147–153. doi:https://doi.org/10.1016/j.semcancer.2016.11.009
- Dandawate PR, Subramaniam D, Jensen RA, Anant S. Anant S: Targeting cancer stem cells and signaling pathways by phytochemicals: Novel approach for breast cancer therapy. Semin Cancer Biol. 2016;40–41:192–208. doi:https://doi.org/10.1016/j.semcancer.2016.09.001
- Mao Q-Q, Xu X-Y, Shang A, Gan R-Y, Wu D-T, Atanasov AG, Li H-B. Phytochemicals for the prevention and treatment of gastric cancer: Effects and mechanisms. Int J Mol Sci. 2020;21(2):570. doi:https://doi.org/10.3390/ijms21020570
- Qawoogha SS, Shahiwala A. Identification of potential anticancer phytochemicals against colorectal cancer by structure-based docking studies. J Recept Signal Transduct Res. 2020;40(1):67–76. doi:https://doi.org/10.1080/10799893.2020.1715431
- Fontana F, Raimondi M, Marzagalli M, Domizio AD, Limonta P. Natural compounds in prostate cancer prevention and treatment: Mechanisms of action and molecular targets. Cells. 2020;9(2):460. doi:https://doi.org/10.3390/cells9020460
- Shin HJ, Hwang KA, Choi KC. Antitumor effect of various phytochemicals on diverse types of thyroid cancers. Nutrients. 2019;11(1):125. doi:https://doi.org/10.3390/nu11010125
- Srivastava SK, Arora S, Averett C, Singh S, Singh AP. Modulation of microRNAs by phytochemicals in cancer: underlying mechanisms and translational significance. Biomed Res Int. 2015;2015:848710. doi:https://doi.org/10.1155/2015/848710
- Bong AHL, Monteith GR. Calcium signaling and the therapeutic targeting of cancer cells. Biochim Biophys Acta Mol Cell Res. 2018;1865(11 Pt B):1786–1794. doi:https://doi.org/10.1016/j.bbamcr.2018.05.015
- Stewart TA, Yapa KT, Monteith GR. Altered calcium signaling in cancer cells. Biochim Biophys Acta. 2015;1848(10 Pt B):2502–2511. doi:https://doi.org/10.1016/j.bbamem.2014.08.016
- Azimi I, Roberts-Thomson SJ, Monteith GR. Calcium influx pathways in breast cancer: opportunities for pharmacological intervention. Br J Pharmacol. 2014;171(4):945–960. doi:https://doi.org/10.1111/bph.12486
- Iamshanova O, Pla AF, Prevarskaya N. Molecular mechanisms of tumour invasion: regulation by calcium signals. J Physiol. 2017;595(10):3063–3075. doi:https://doi.org/10.1113/JP272844
- Alharbi A, Parrington J. Endolysosomal Ca2+ signaling in cancer: The role of TPC2, from tumorigenesis to metastasis. Front Cell Dev Biol. 2019;7:302. doi:https://doi.org/10.3389/fcell.2019.00302
- Schwarz EC, Qu B, Hoth M. Calcium, cancer and killing: The role of calcium in killing cancer cells by cytotoxic T lymphocytes and natural killer cells. Biochim Biophys Acta. 2013;1833(7):1603–1611. doi:https://doi.org/10.1016/j.bbamcr.2012.11.016
- Cui C, Merritt R, Fu L, Pan Z. Targeting calcium signaling in cancer therapy. Acta Pharm Sin B. 2017;7(1):3–17. doi:https://doi.org/10.1016/j.apsb.2016.11.001
- Xie R, Xu J, Xiao Y, Wu J, Wan H, Tang B, Liu J, Fan Y, Wang S, Wu Y, et al. Calcium promotes human gastric cancer via a novel coupling of calcium-sensing receptor and TRPV4 channel. Cancer Res. 2017;77(23):6499–6512. doi:https://doi.org/10.1158/0008-5472.CAN-17-0360
- Ando H, Kawaai K, Bonneau B, Mikoshiba K. Remodeling of Ca2+ signaling in cancer: Regulation of inositol 1,4,5-trisphosphate receptors through oncogenes and tumor suppressors. Adv Biol Regul. 2018;68:64–76. doi:https://doi.org/10.1016/j.jbior.2017.12.001
- Yuan Z, Cao A, Liu H, Guo H, Zang Y, Wang Y, Wang Y, Wang H, Yin P, Peng W. Calcium uptake via mitochondrial uniporter contributes to palmitic acid-induced apoptosis in mouse podocytes. J Cell Biochem. 2017;118(9):2809–2818. doi:https://doi.org/10.1002/jcb.25930
- Wang GJ, Guo LY, Wang HX, Yao Y. IP3R and RyR calcium channels are involved in neonatal rat cardiac myocyte hypertrophy induced by tumor necrosis factor-α. Am. J. Transl. Res. 2017;9:343–354.
- Ong HL, Ambudkar IS. The endoplasmic reticulum-plasma membrane junction: A hub for agonist regulation of Ca2+ entry. Cold Spring Harb Perspect Biol. 2020;12(2):a035253. doi:https://doi.org/10.1101/cshperspect.a035253
- Kania E, Roest G, Vervliet T, Parys JB, Bultynck G. IP3 receptor-mediated calcium signaling and its role in autophagy in cancer . Front Oncol. 2017;7:140. doi:https://doi.org/10.3389/fonc.2017.00140
- Samanta K, Douglas S, Parekh AB. Mitochondrial calcium uniporter MCU supports cytoplasmic Ca2+ oscillations, store-operated Ca2+ entry and Ca2+-dependent gene expression in response to receptor stimulation. PLoS One. 2014;9(7):e101188. doi:https://doi.org/10.1371/journal.pone.0101188
- Kerkhofs M, Bittremieux M, Morciano G, Giorgi C, Pinton P, Parys JB, Bultynck G. Emerging molecular mechanisms in chemotherapy: Ca2+ signaling at the mitochondria-associated endoplasmic reticulum membranes. Cell Death Dis. 2018;9(3):334. doi:https://doi.org/10.1038/s41419-017-0179-0
- Shin D-H, Leem D-G, Shin J-S, Kim J-I, Kim K-T, Choi SY, Lee M-H, Choi J-H, Lee K-T. Compound K induced apoptosis via endoplasmic reticulum Ca2+ release through ryanodine receptor in human lung cancer cells. J Ginseng Res. 2018;42(2):165–174. doi:https://doi.org/10.1016/j.jgr.2017.01.015
- Díaz-Vegas AR, Cordova A, Valladares D, Llanos P, Hidalgo C, Gherardi G, De Stefani D, Mammucari C, Rizzuto R, Contreras-Ferrat A, et al. Mitochondrial calcium increase induced by RyR1 and IP3R channel activation after membrane depolarization regulates skeletal muscle metabolism. Front Physiol. 2018;9:791. doi:https://doi.org/10.3389/fphys.2018.00791
- Sampieri A, Santoyo K, Asanov A, Vaca L. Association of the IP3R to STIM1 provides a reduced intraluminal calcium microenvironment, resulting in enhanced store-operated calcium entry. Sci Rep. 2018;8(1):13252. doi:https://doi.org/10.1038/s41598-018-31621-0
- Zhang S, Miao Y, Zheng X, Gong Y, Zhang J, Zou F, Cai C. STIM1 and STIM2 differently regulate endogenous Ca2+ entry and promote TGF-β-induced EMT in breast cancer cells. Biochem Biophys Res Commun. 2017;488(1):74–80. doi:https://doi.org/10.1016/j.bbrc.2017.05.009
- Saint Fleur-Lominy S, Maus M, Vaeth M, Lange I, Zee I, Suh D, Liu C, Wu X, Tikhonova A, Aifantis I, et al. STIM1 and STIM2 Mediate Cancer-Induced Inflammation in T Cell Acute Lymphoblastic Leukemia. Cell Rep. 2018;24(11):3045–3060. doi:https://doi.org/10.1016/j.celrep.2018.08.030
- Dyrda A, Koenig S, Frieden M. STIM1 long and STIM1 gate differently TRPC1 during store-operated calcium entry. Cell Calcium. 2020;86:102134. doi:https://doi.org/10.1016/j.ceca.2019.102134
- Fiorio Pla A, Kondratska K, Prevarskaya N. STIM and ORAI proteins: Crucial roles in hallmarks of cancer. Am J Physiol Cell Physiol. 2016;310(7):C509–C519. doi:https://doi.org/10.1152/ajpcell.00364.2015
- Zhou Y, Gu P, Li J, Li F, Zhu J, Gao P, Zang Y, Wang Y, Shan Y, Yang D, et al. Suppression of STIM1 inhibits the migration and invasion of human prostate cancer cells and is associated with PI3K/Akt signaling inactivation. Oncol Rep. 2017;38(5):2629–2636. doi:https://doi.org/10.3892/or.2017.5961
- Mo PL, Yang SY. The store-operated calcium channels in cancer metastasis: from cell migration, invasion to metastatic colonization. Front Biosci (Landmark Ed). 2018;23:1241–1256. doi:https://doi.org/10.2741/4641
- Chen YJ, Chang CL, Lee WR, Liou J. RASSF4 controls SOCE and ER-PM junctions through regulation of PI(4,5)P. J. Cell Biol. 2017;216(7):2011–2025. doi:https://doi.org/10.1083/jcb.201606047
- Stagno MJ, Zacharopoulou N, Bochem J, Tsapara A, Pelzl L, Al-Maghout T, Kallergi G, Alkahtani S, Alevizopoulos K, Dimas K, et al. Istaroxime inhibits motility and down-regulates orai1 expression, SOCE and FAK phosphorylation in prostate cancer cells. Cell Physiol Biochem. 2017;42(4):1366–1376. doi:https://doi.org/10.1159/000479200
- Ritaine A, Shapovalov G, Prevarskaya N. Metabolic disorders and cancer: Store-operated Ca2+ entry in cancer: Focus on IP3R-mediated Ca2+ release from intracellular stores and its role in migration and invasion. Adv Exp Med Biol. 2017;993:623–637. doi:https://doi.org/10.1007/978-3-319-57732-6_31
- Kanwar N, Carmine-Simmen K, Nair R, Wang C, Moghadas-Jafari S, Blaser H, Tran-Thanh D, Wang D, Wang P, Wang J, et al. Amplification of a calcium channel subunit CACNG4 increases breast cancer metastasis. EBioMedicine. 2020;52:102646: doi:https://doi.org/10.1016/j.ebiom.2020.102646
- Schmitt LI, Leo M, Kleinschnitz C, Hagenacker T. Oxaliplatin modulates the characteristics of voltage-gated calcium channels and action potentials in small dorsal root ganglion neurons of rats. Mol Neurobiol. 2018;55(12):8842–8855. doi:https://doi.org/10.1007/s12035-018-1029-5
- Morrone FB, Gehring MP, Nicoletti NF. Calcium channels and associated receptors in malignant brain tumor therapy. Mol Pharmacol. 2016;90(3):403–409. doi:https://doi.org/10.1124/mol.116.103770
- Valerie NCK, Dziegielewska B, Hosing AS, Augustin E, Gray LS, Brautigan DL, Larner JM, Dziegielewski J. Inhibition of T-type calcium channels disrupts Akt signaling and promotes apoptosis in glioblastoma cells. Biochem Pharmacol. 2013;85(7):888–97. doi:https://doi.org/10.1016/j.bcp.2012.12.017
- Phan NN, Wang C-Y, Chen C-F, Sun Z, Lai M-D, Lin Y-C. Voltage-gated calcium channels: Novel targets for cancer therapy. Oncol Lett. 2017;14(2):2059–2074. doi:https://doi.org/10.3892/ol.2017.6457
- Wang C-Y, Lai M-D, Phan NN, Sun Z, Lin Y-C. Meta-analysis of public microarray datasets reveals voltage-gated calcium gene signatures in clinical cancer patients. PloS One. 2015;10(7):e0125766. doi:https://doi.org/10.1371/journal.pone.0125766
- Graus F, Lang B, Pozo-Rosich P, Saiz A, Casamitjana R, Vincent A. P/Q type calcium-channel antibodies in paraneoplastic cerebellar degeneration with lung cancer. Neurology. 2002;59(5):764–6. doi:https://doi.org/10.1212/wnl.59.5.764
- Hantute-Ghesquier A, Haustrate A, Prevarskaya N, Lehen’kyi V. TRPM family channels in cancer. Pharmaceuticals (Basel). 2018;11(2):58. doi:https://doi.org/10.3390/ph11020058
- Holzer P. Transient receptor potential (TRP) channels as drug targets for diseases of the digestive system. Pharmacol Ther. 2011;131(1):142–170. doi:https://doi.org/10.1016/j.pharmthera.2011.03.006
- Huang Y, Wen LL, Xie JD, Ouyang HD, Chen DT, Zeng W. Antinociceptive effectiveness of the inhibition of NCX reverse-mode action in rodent neuropathic pain model. Mol Pain. 2019;15:1744806919864511. doi:https://doi.org/10.1177/1744806919864511
- Dong H, Shim K-N, Li JMJ, Estrema C, Ornelas TA, Nguyen F, Liu S, Ramamoorthy SL, Ho S, Carethers JM, et al. Molecular mechanisms underlying Ca2+-mediated motility of human pancreatic duct cells. Am J Physiol Cell Physiol. 2010;299(6):C1493–C1503. doi:https://doi.org/10.1152/ajpcell.00242.2010
- Rodrigues T, Estevez GNN, Tersariol ILDS. Na+/Ca2+ exchangers: Unexploited opportunities for cancer therapy? Biochem Pharmacol. 2019;163:357–361. doi:https://doi.org/10.1016/j.bcp.2019.02.032
- Andrikopoulos P, Kieswich J, Harwood SM, Baba A, Matsuda T, Barbeau O, Jones K, Eccles SA, Yaqoob MM. Endothelial angiogenesis and barrier function in response to thrombin require Ca2+ influx through the Na+/Ca2+ exchanger. J Biol Chem. 2015;290(30):18412–18428. doi:https://doi.org/10.1074/jbc.M114.628156
- Andrikopoulos P, Eccles S, Yaqoob M. Coupling between the TRPC3 ion channel and the NCX1 transporter contributed to VEGF-induced ERK1/2 activation and angiogenesis in human primary endothelial cells. Cell Signal. 2017;37:12–30. doi:https://doi.org/10.1016/j.cellsig.2017.05.013
- Varga K, Hollósi A, Pászty K, Hegedűs L, Szakács G, Tímár J, Papp B, Enyedi Á, Padányi R. Expression of calcium pumps is differentially regulated by histone deacetylase inhibitors and estrogen receptor alpha in breast cancer cells. BMC Cancer. 2018;18(1):1029. doi:https://doi.org/10.1186/s12885-018-4945-x
- Dang DK, Makena MR, Llongueras JP, Prasad H, Ko M, Bandral M, Rao R. A Ca2+-ATPase regulates E-cadherin biogenesis and epithelial-mesenchymal transition in breast cancer cells. Mol Cancer Res. 2019;17(8):1735–1747. doi:https://doi.org/10.1158/1541-7786.MCR-19-0070
- Dang D, Rao RJ. Calcium-ATPases: Gene disorders and dysregulation in cancer. Biochim Biophys Acta. 2016;1863(6 Pt B):1344–1350. doi:https://doi.org/10.1016/j.bbamcr.2015.11.016
- Curry M, Roberts-Thomson S, Monteith G. Plasma membrane calcium ATPases and cancer. Biofactors. 2011;37(3):132–138. doi:https://doi.org/10.1002/biof.146
- Ribiczey P, Tordai A, Andrikovics H, Filoteo AG, Penniston JT, Enouf J, Enyedi A, Papp B, Kovács T. Isoform-specific up-regulation of plasma membrane Ca2+ATPase expression during colon and gastric cancer cell differentiation. Cell Calcium. 2007;42(6):590–605. doi:https://doi.org/10.1016/j.ceca.2007.02.003
- Varga K, Pászty K, Padányi R, Hegedűs L, Brouland J-P, Papp B, Enyedi A. Histone deacetylase inhibitor- and PMA-induced upregulation of PMCA4b enhances Ca2+ clearance from MCF-7 breast cancer cells. Cell Calcium. 2014;55(2):78–92. doi:https://doi.org/10.1016/j.ceca.2013.12.003
- Zylińska L, Soszyński M. Plasma membrane Ca2+-ATPase in excitable and nonexcitable cells. Acta Biochim Pol. 2000;47(3):529–39. doi:https://doi.org/10.18388/abp.2000_3976
- Seo J, Kim B, Dhanasekaran D, Tsang B, Song Y. Curcumin induces apoptosis by inhibiting sarco/endoplasmic reticulum Ca2+ ATPase activity in ovarian cancer cells. Cancer Lett. 2016;371(1):30–7. doi:https://doi.org/10.1016/j.canlet.2015.11.021
- Chemaly E, Troncone L, Lebeche D. SERCA control of cell death and survival. Cell Calcium. 2018;69:46–61. doi:https://doi.org/10.1016/j.ceca.2017.07.001
- Yiallouris A, Patrikios I, Johnson EO, Sereti E, Dimas K, De Ford C, Fedosova NU, Graier WF, Sokratous K, Kyriakou K, et al. Annonacin promotes selective cancer cell death via NKA-dependent and SERCA-dependent pathways. Cell Death Dis. 2018;9(7):764. doi:https://doi.org/10.1038/s41419-018-0772-x
- Tosatto A, Sommaggio R, Kummerow C, Bentham RB, Blacker TS, Berecz T, Duchen MR, Rosato A, Bogeski I, Szabadkai G, et al. The mitochondrial calcium uniporter regulates breast cancer progression via HIF-1α. EMBO Mol Med. 2016;8(5):569–585. doi:https://doi.org/10.15252/emmm.201606255
- Marchi S, Corricelli M, Branchini A, Vitto VAM, Missiroli S, Morciano G, Perrone M, Ferrarese M, Giorgi C, Pinotti M, et al. Akt-mediated phosphorylation of MICU1 regulates mitochondrial Ca levels and tumor growth. Embo J. 2019;38(2). doi:https://doi.org/10.15252/embj.201899435
- Hamilton S, Terentyeva R, Kim TY, Bronk P, Clements RT, O-Uchi J, Csordás G, Choi B-R, Terentyev D. Pharmacological modulation of mitochondrial Ca2+ content regulates sarcoplasmic reticulum Ca2+ release via oxidation of the ryanodine receptor by mitochondria-derived reactive oxygen species. Front Physiol. 2018;9:1831. doi:https://doi.org/10.3389/fphys.2018.01831
- Tang S, Wang X, Shen Q, Yang X, Yu C, Cai C, Cai G, Meng X, Zou F. Mitochondrial Ca2+ uniporter is critical for store-operated Ca2+ entry-dependent breast cancer cell migration. Biochem Biophys Res Commun. 2015;458(1):186–193. doi:https://doi.org/10.1016/j.bbrc.2015.01.092
- Liu Y, Jin M, Wang Y, Zhu J, Tan R, Zhao J, Ji X, Jin C, Jia Y, Ren T, et al. MCU-induced mitochondrial calcium uptake promotes mitochondrial biogenesis and colorectal cancer growth. Signal Transduct Target Ther. 2020;5(1):59.
- Chen L, Sun Q, Zhou D, Song W, Yang Q, Ju B, Zhang L, Xie H, Zhou L, Hu Z, et al. HINT2 triggers mitochondrial Ca2+ influx by regulating the mitochondrial Ca uniporter (MCU) complex and enhances gemcitabine apoptotic effect in pancreatic cancer. Cancer Lett. 2017;411:106–116.: doi:https://doi.org/10.1016/j.canlet.2017.09.020
- Chikara S, Nagaprashantha LD, Singhal J, Horne D, Awasthi S, Singhal SS. Oxidative stress and dietary phytochemicals: Role in cancer chemoprevention and treatment. Cancer Lett. 2018;413:122–134. doi:https://doi.org/10.1016/j.canlet.2017.11.002
- Zubair H, Azim S, Ahmad A, Khan M, Patel G, Singh S, Singh A. Cancer chemoprevention by phytochemicals: Nature’s healing touch. Molecules. 2017;22(3):395. doi:https://doi.org/10.3390/molecules22030395
- Abbasi BA, Iqbal J, Ahmad R, Bibi S, Mahmood T, Kanwal S, Bashir S, Gul F, Hameed S. Potential phytochemicals in the prevention and treatment of esophagus cancer: A green therapeutic approach. Pharmacol Rep. 2019;71(4):644–652. doi:https://doi.org/10.1016/j.pharep.2019.03.001
- Kotecha R, Takami A, Espinoza JL. Dietary phytochemicals and cancer chemoprevention: A review of the clinical evidence. Oncotarget. 2016;7(32):52517–52529. doi:https://doi.org/10.18632/oncotarget.9593
- Langner E, Lemieszek MK, Rzeski W. Lycopene, sulforaphane, quercetin, and curcumin applied together show improved antiproliferative potential in colon cancer cells in vitro. J Food Biochem. 2019;43(4):e12802. doi:https://doi.org/10.1111/jfbc.12802
- Jasek K, Kubatka P, Samec M, Liskova A, Smejkal K, Vybohova D, Bugos O, Biskupska-Bodova K, Bielik T, Zubor P, et al. DNA methylation status in cancer disease: Modulations by plant-derived natural compounds and dietary interventions. Biomolecules. 2019;9(7):289. doi:https://doi.org/10.3390/biom9070289
- Parveen A, Subedi L, Kim HW, Khan Z, Zahra Z, Farooqi MQ, Kim SY. Phytochemicals targeting VEGF and VEGF-related multifactors as anticancer therapy. J. Clin. Med. 2019;8.
- Kim S-H, Kim K-Y, Yu S-N, Park S-G, Yu H-S, Seo Y-K, Ahn S-C. Monensin induces PC-3 prostate cancer cell apoptosis via ROS production and Ca2+ homeostasis disruption. Anticancer Res. 2016;36(11):5835–5843. doi:https://doi.org/10.21873/anticanres.11168
- Mohanraj K, Karthikeyan BS, Vivek-Ananth RP, Chand RPB, Aparna SR, Mangalapandi P, Samal A. IMPPAT: A curated database of Indian medicinal plants, phytochemistry and therapeutics. Sci Rep. 2018;8(1):4329. doi:https://doi.org/10.1038/s41598-018-22631-z
- Khamis S, Bibby MC, Brown JE, Cooper PA, Scowen I, Wright CW. Phytochemistry and preliminary biological evaluation of Cyathostemma argenteum, a malaysian plant used traditionally for the treatment of breast cancer. Phytother Res. 2004;18(7):507–510. doi:https://doi.org/10.1002/ptr.1318
- Somsrisa J, Meepowpan P, Krachodnok S, Thaisuchat H, Punyanitya S, Nantasaen N, Pompimon W. Dihydrochalcones with antiinflammatory activity from leaves and twigs of Cyathostemma argenteum. Molecules. 2013;18(6):6898–6907. doi:https://doi.org/10.3390/molecules18066898
- Rachakhom W, Khaw-On P, Pompimon W, Banjerdpongchai R. Dihydrochalcone derivative induces breast cancer cell apoptosis via intrinsic, extrinsic, and ER stress pathways but abolishes EGFR/MAPK pathway. Biomed Res Int. 2019;2019:7298539. doi:https://doi.org/10.1155/2019/7298539
- Qin XX, Xing YF, Zhou ZQ, Yao Y. Dihydrochalcone compounds isolated from crabapple leaves showed anticancer effects on human cancer cell lines. Molecules. 2015;20(12):21193–21203. doi:https://doi.org/10.3390/molecules201219754
- Li Y, Dong C, Xu MJ, Lin WH. New alkylated benzoquinones from mangrove plant Aegiceras corniculatum with anticancer activity. J Asian Nat Prod Res. 2020;22(2):121–130. doi:https://doi.org/10.1080/10286020.2018.1540604
- Ribeiro V, Andrade PB, Valentão P, Pereira D. M: Benzoquinones from Cyperus spp. trigger IRE1α-independent and PERK-dependent ER stress in human stomach cancer cells and are novel proteasome inhibitors. Phytomedicine. 2019;63:153017. doi:https://doi.org/10.1016/j.phymed.2019.153017
- Ma Y-Y, Di Z-M, Cao Q, Xu W-S, Bi S-X, Yu J-S, Shen Y-J, Yu Y-Q, Shen Y-X, Feng L-J, et al. Xanthatin induces glioma cell apoptosis and inhibits tumor growth via activating endoplasmic reticulum stress-dependent CHOP pathway. Acta Pharmacol Sin. 2020;41(3):404–414. doi:https://doi.org/10.1038/s41401-019-0318-5
- Li X-X, Wang D-Q, Sui C-G, Meng F-D, Sun S-L, Zheng J, Jiang Y-H. Oleandrin induces apoptosis via activating endoplasmic reticulum stress in breast cancer cells. Biomed Pharmacother. 2020;124:109852–109852. doi:https://doi.org/10.1016/j.biopha.2020.109852
- Shen K-H, Hung S-H, Yin L-T, Huang C-S, Chao C-H, Liu C-L, Shih Y-W. Acacetin, a flavonoid, inhibits the invasion and migration of human prostate cancer DU145 cells via inactivation of the p38 MAPK signaling pathway. Mol Cell Biochem. 2010;333(1–2):279–291. doi:https://doi.org/10.1007/s11010-009-0229-8
- Kim HR, Park CG, Jung JY. Acacetin (5,7-dihydroxy-4’-methoxyflavone) exhibits in vitro and in vivo anticancer activity through the suppression of NF-κB/Akt signaling in prostate cancer cells. Int J Mol Med. 2014;33(2):317–324. doi:https://doi.org/10.3892/ijmm.2013.1571
- Salimi A, Roudkenar MH, Sadeghi L, Mohseni A, Seydi E, Pirahmadi N, Pourahmad J. Selective anticancer activity of acacetin against chronic lymphocytic leukemia using both in vivo and in vitro methods: Key role of oxidative stress and cancerous mitochondria. Nutr Cancer. 2016;68(8):1404–1416. doi:https://doi.org/10.1080/01635581.2016.1235717
- Prasad N, Sharma JR, Yadav UCS. Induction of growth cessation by acacetin via β-catenin pathway and apoptosis by apoptosis inducing factor activation in colorectal carcinoma cells. Mol Biol Rep. 2020;47(2):987–1001. doi:https://doi.org/10.1007/s11033-019-05191-x
- Shim H-Y, Park J-H, Park H-D, Nah S-Y, Kim DSHL, Han YS. Acacetin-induced apoptosis of human breast cancer MCF-7 cells involves caspase cascade, mitochondria-mediated death signaling and SAPK/JNK1/2-c-Jun activation. Mol Cells. 2007;24(1):95–104.
- Sun F, Li D, Wang C, Peng C, Zheng H, Wang X. Acacetin-induced cell apoptosis in head and neck squamous cell carcinoma cells: Evidence for the role of muscarinic M3 receptor. Phytother Res. 2019;33(5):1551–1561. doi:https://doi.org/10.1002/ptr.6343
- Gao Y, Liu H, Wang H, Hu H, He H, Gu N, Han X, Guo Q, Liu D, Cui S, et al. Baicalin inhibits breast cancer development via inhibiting IĸB kinase activation in vitro and in vivo. Int J Oncol. 2018;53(6):2727–2736.
- Wang Z, Ma L, Su M, Zhou Y, Mao K, Li C, Peng G, Zhou C, Shen B, Dou J, et al. Baicalin induces cellular senescence in human colon cancer cells via upregulation of DEPP and the activation of Ras/Raf/MEK/ERK signaling. Cell Death Dis. 2018;9(2):217: doi:https://doi.org/10.1038/s41419-017-0223-0
- Huang Q, Zhang J, Peng J, Zhang Y, Wang L, Wu J, Ye L, Fang C. Effect of baicalin on proliferation and apoptosis in pancreatic cancer cells. Am J Transl Res. 2019;11(9):5645–5654.
- Zhu Y, Fang J, Wang H, Fei M, Tang T, Liu K, Niu W, Zhou Y. Baicalin suppresses proliferation, migration, and invasion in human glioblastoma cells via Ca2+-dependent pathway. Drug Des Devel Ther. 2018;12:3247–3261. doi:https://doi.org/10.2147/DDDT.S176403
- Lee J-H, Li Y-C, Ip S-W, Hsu S-C, Chang N-W, Tang N-Y, Yu C-S, Chou S-T, Lin S-S, Lino C-C, et al. The role of Ca2+ in baicalein-induced apoptosis in human breast MDA-MB-231 cancer cells through mitochondria- and caspase-3-dependent pathway. Anticancer Res. 2008;28(3A):1701–1711.
- Kyo R, Nakahata N, Sakakibara I, Kubo M, Ohizumi Y. Baicalin and baicalein, constituents of an important medicinal plant, inhibit intracellular Ca2+ elevation by reducing phospholipase C activity in C6 rat glioma cells. J Pharm Pharmacol. 1998;50(10):1179–1182. doi:https://doi.org/10.1111/j.2042-7158.1998.tb03331.x
- Tejada S, Pinya S, Martorell M, Capó X, Tur JA, Pons A, Sureda A. Potential anti-inflammatory effects of hesperidin from the genus citrus. Curr Med Chem. 2018;25(37):4929–4945. doi:https://doi.org/10.2174/0929867324666170718104412
- Wunpathe C, Potue P, Maneesai P, Bunbupha S, Prachaney P, Kukongviriyapan U, Kukongviriyapan V, Pakdeechote P. Hesperidin suppresses renin-angiotensin system mediated NOX2 over-expression and sympathoexcitation in 2K-1C hypertensive rats. Am J Chin Med. 2018;46(4):751–767. doi:https://doi.org/10.1142/S0192415X18500398
- Naz H, Tarique M, Ahamad S, Alajmi MF, Hussain A, Rehman MT, Luqman S, Hassan MI. Hesperidin-CAMKIV interaction and its impact on cell proliferation and apoptosis in the human hepatic carcinoma and neuroblastoma cells. J Cell Biochem. 2019;120(9):15119–15130. doi:https://doi.org/10.1002/jcb.28774
- Xia RM, Xu G, Huang Y, Sheng X, Xu XL, Lu HL. Hesperidin suppresses the migration and invasion of non-small cell lung cancer cells by inhibiting the SDF-1/CXCR-4 pathway. Life Sci. 2018;201:111–120. doi:https://doi.org/10.1016/j.lfs.2018.03.046
- Wang YX, Yu H, Zhang J, Gao J, Ge X, Lou G. Hesperidin inhibits HeLa cell proliferation through apoptosis mediated by endoplasmic reticulum stress pathways and cell cycle arrest. BMC Cancer. 2015;15:682. doi:https://doi.org/10.1186/s12885-015-1706-y
- Khamis AAA, Ali EMM, El-Moneim MAA, Abd-Alhaseeb MM, El-Magd MA, Salim EI. Hesperidin, piperine and bee venom synergistically potentiate the anticancer effect of tamoxifen against breast cancer cells. Biomed Pharmacother. 2018;105:1335–1343. doi:https://doi.org/10.1016/j.biopha.2018.06.105
- Yumnam S, Hong GE, Raha S, Saralamma VVG, Lee HJ, Lee W-S, Kim E-H, Kim GS. Mitochondrial dysfunction and Ca(2+) overload contributes to hesperidin induced paraptosis in hepatoblastoma cells, HepG2. J Cell Physiol. 2016;231(6):1261–1268. doi:https://doi.org/10.1002/jcp.25222
- Huang Y-F, Zhu D-J, Chen X-W, Chen Q-K, Luo Z-T, Liu C-C, Wang G-X, Zhang W-J, Liao N-Z. Curcumin enhances the effects of irinotecan on colorectal cancer cells through the generation of reactive oxygen species and activation of the endoplasmic reticulum stress pathway. Oncotarget. 2017;8(25):40264–40275. doi:https://doi.org/10.18632/oncotarget.16828
- Sala de Oyanguren FJ, Rainey NE, Moustapha A, Saric A, Sureau F, O’Connor J-E, Petit PX. Highlighting curcumin-induced crosstalk between autophagy and apoptosis as supported by its specific subcellular localization. Cells. 2020;9(2):361. doi:https://doi.org/10.3390/cells9020361
- Unlu A, Nayir E, Kalenderoglu MD, Kirca O, Ozdogan M. Curcumin (turmeric) and cancer. J. B.U.On. 2016;21:1050–1060.
- Zhang ZX, Yi PF, Tu CC, Zhan JJ, Jiang LP, Zhang FL. Curcumin inhibits ERK/c-Jun expressions and phosphorylation against endometrial carcinoma. Biomed Res Int. 2019; 2019:8912961.
- Liczbiński P, Michałowicz J, Bukowska B. Molecular mechanism of curcumin action in signaling pathways: Review of the latest research. Phytother Res. 2020;34(8):1992–2005. doi:https://doi.org/10.1002/ptr.6663
- Zhang L, Cheng X, Xu SC, Bao JD, Yu HX. Curcumin induces endoplasmic reticulum stress-associated apoptosis in human papillary thyroid carcinoma BCPAP cells via disruption of intracellular calcium homeostasis. Medicine (Baltimore). 2018;97(24):e11095. doi:https://doi.org/10.1097/MD.0000000000011095
- Xu XD, Chen D, Ye B, Zhong FM, Chen G. Curcumin induces the apoptosis of non-small cell lung cancer cells through a calcium signaling pathway. Int J Mol Med. 2015;35(6):1610–1616. doi:https://doi.org/10.3892/ijmm.2015.2167
- Lagoa R, Marques-da-Sliva D, Diniz M, Daglia M, Bishayee A. Molecular mechanisms linking environmental toxicants to cancer development: Significance for protective interventions with polyphenols. Semin. Cancer Biol. 2020;S1044-579X(20)30035-3.
- Chang J, Zhou Y, Wang Q, Aschner M, Lu RZ. Plant components can reduce methylmercury toxication: A mini-review. Biochim Biophys Acta Gen Subj. 2019;1863(12):129290. doi:https://doi.org/10.1016/j.bbagen.2019.01.012
- Leri M, Scuto M, Ontario ML, Calabrese V, Calabrese EJ, Bucciantini M, Stefani M. Healthy effects of plant polyphenols: Molecular mechanisms. IJMS. 2020;21(4):1250. doi:https://doi.org/10.3390/ijms21041250
- Rauf A, Imran M, Butt MS, Nadeem M, Peters DG, Mubarak MS. Resveratrol as an anti-cancer agent: A review. Crit Rev Food Sci Nutr. 2018;58(9):1428–1447. doi:https://doi.org/10.1080/10408398.2016.1263597
- Sareen D, Darjatmoko SR, Albert DM, Polans AS. Polans AS: Mitochondria, calcium, and calpain are key mediators of resveratrol-induced apoptosis in breast cancer. Mol Pharmacol. 2007;72(6):1466–1475. doi:https://doi.org/10.1124/mol.107.039040
- Ko J-H, Sethi G, Um J-Y, Shanmugam MK, Arfuso F, Kumar AP, Bishayee A, Ahn KS. The role of resveratrol in cancer therapy. Int J Mol Sci. 2017;18(12):2589. doi:https://doi.org/10.3390/ijms18122589
- Peterson JA, Oblad RV, Mecham JC, Kenealey JD. Resveratrol inhibits plasma membrane Ca2+-ATPase inducing an increase in cytoplasmic calcium. Biochem Biophys Rep. 2016;7:253–258. doi:https://doi.org/10.1016/j.bbrep.2016.06.019
- Huang H-C, Lin M-K, Yang H-L, Hseu Y-C, Liaw C-C, Tseng Y-H, Tsuzuki M, Kuo Y-H. Cardenolides and bufadienolide glycosides from Kalanchoe tubiflora and evaluation of cytotoxicity. Planta Med. 2013;79(14):1362–1369. doi:https://doi.org/10.1055/s-0033-1350646
- Hseu Y-C, Cho H-J, Gowrisankar YV, Thiyagarajan V, Chen X-Z, Lin K-Y, Huang H-C, Yang H-L. Kalantuboside B induced apoptosis and cytoprotective autophagy in human melanoma A2058 cells: An in vitro and in vivo study, Free. Free Radic Biol Med. 2019;143:397–411. doi:https://doi.org/10.1016/j.freeradbiomed.2019.08.015
- Ge X, Yannai S, Rennert G, Gruener N, Fares FA. 3,3’-Diindolylmethane induces apoptosis in human cancer cells. Biochem Biophys Res Commun. 1996;228(1):153–158. doi:https://doi.org/10.1006/bbrc.1996.1631
- Ye Y, Fang YF, Xu WR, Wang Q, Zhou JW, Lu RZ. 3,3’-Diindolylmethane induces anti-human gastric cancer cells by the miR-30e-ATG5 modulating autophagy. Biochem Pharmacol. 2016;115:77–84. doi:https://doi.org/10.1016/j.bcp.2016.06.018
- Lanza-Jacoby S, Cheng G. 3,3’-Diindolylmethane enhances apoptosis in docetaxel-treated breast cancer cells by generation of reactive oxygen species. Pharm Biol. 2018;56(1):407–414. doi:https://doi.org/10.1080/13880209.2018.1495747
- Kim SM. Cellular and molecular mechanisms of 3,3’-Diindolylmethane in gastrointestinal cancer. Int J Mol Sci. 2016;17(7):1155. doi:https://doi.org/10.3390/ijms17071155
- Ye Y, Miao SH, Wang Y, Zhou JW, Lu RZ. 3,3’-diindolylmethane potentiates tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis of gastric cancer cells. Oncol Lett. 2015;9(5):2393–2397. doi:https://doi.org/10.3892/ol.2015.3008
- Lee J. 3,3’-Diindolylmethane Inhibits TNF-α- and TGF-β-Induced Epithelial-Mesenchymal Transition in Breast Cancer Cells. Nutr Cancer. 2019;71(6):992–1006. doi:https://doi.org/10.1080/01635581.2019.1577979
- Zhang XB, Sukamporn P, Zhang SQ, Min K-W, Baek SJ. 3,3’-diindolylmethane downregulates cyclin D1 through triggering endoplasmic reticulum stress in colorectal cancer cells. Oncol Rep. 2017;38(1):569–574. doi:https://doi.org/10.3892/or.2017.5693
- Jiang Y, Fang Y, Ye Y, Xu X, Wang B, Gu J, Aschner M, Chen J, Lu R. Anti-cancer effects of 3, 3’-Diindolylmethane on human hepatocellular carcinoma cells is enhanced by calcium ionophore: The role of cytosolic Ca2+ and p38 MAPK. Front Pharmacol. 2019;10:1167. doi:https://doi.org/10.3389/fphar.2019.01167
- Li YW, Sarkar FH. Role of bioresponse 3,3’-Diindolylmethane in the treatment of human prostate cancer: Clinical experience. Med Princ Pract. 2016;25(2):11–7. doi:https://doi.org/10.1159/000439307
- Palomera-Sanchez Z, Watson GW, Wong CP, Beaver LM, Williams DE, Dashwood RH, Ho E. The phytochemical 3,3’-diindolylmethane decreases expression of AR-controlled DNA damage repair genes through repressive chromatin modifications and is associated with DNA damage in prostate cancer cells. J Nutr Biochem. 2017;47:113–119. doi:https://doi.org/10.1016/j.jnutbio.2017.05.005
- Lu Y-C, Chen I-S, Chou C-T, Huang J-K, Chang H-T, Tsai J-Y, Hsu S-S, Liao W-C, Wang J-L, Lin K-L, et al. 3,3’-Diindolylmethane alters Ca2+ homeostasis and viability in MG63 human osteosarcoma cells. Basic Clin Pharmacol Toxicol. 2012;110(4):314–321. doi:https://doi.org/10.1111/j.1742-7843.2011.00816.x
- Ren L, Li Z, Dai C, Zhao D, Wang Y, Ma C, Liu C. Chrysophanol inhibits proliferation and induces apoptosis through NF-κB/cyclin D1 and NF-κB/Bcl-2 signaling cascade in breast cancer cell lines. Mol Med Rep. 2018;17(3):4376–4382. doi:https://doi.org/10.3892/mmr.2018.8443
- Lu C-C, Yang J-S, Huang A-C, Hsia T-C, Chou S-T, Kuo C-L, Lu H-F, Lee T-H, Wood WG, Chung J-G. Chrysophanol induces necrosis through the production of ROS and alteration of ATP levels in J5 human liver cancer cells. Mol Nutr Food Res. 2010;54(7):967–976. doi:https://doi.org/10.1002/mnfr.200900265
- Park S, Lim W, Song G. Chrysophanol selectively represses breast cancer cell growth by inducing reactive oxygen species production and endoplasmic reticulum stress via AKT and mitogen-activated protein kinase signal pathways. Toxicol Appl Pharmacol. 2018;360:201–211. doi:https://doi.org/10.1016/j.taap.2018.10.010
- Lim W, An Y, Yang C, Bazer FW, Song G. Chrysophanol induces cell death and inhibits invasiveness via mitochondrial calcium overload in ovarian cancer cells. J Cell Biochem. 2018;119(12):10216–10227. doi:https://doi.org/10.1002/jcb.27363
- Wang G, Wang P, Yan X, Liu J. Neferine hinders choriocarcinoma cell proliferation, migration and invasion through repression of long noncoding RNA-CHRF. Artif Cells Nanomed Biotechnol. 2019;47(1):4089–4096. doi:https://doi.org/10.1080/21691401.2019.1671429
- Manogaran P, Beeraka NM, Padma VV. The cytoprotective and anti-cancer potential of bisbenzylisoquinoline alkaloids from Nelumbo nucifera . Curr Top Med Chem. 2019;19(32):2940–2957. doi:https://doi.org/10.2174/1568026619666191116160908
- Dasari S, Bakthavachalam V, Chinnapaka S, Venkatesan R, Samy ALPA, Munirathinam G. Neferine, an alkaloid from lotus seed embryo targets HeLa and SiHa cervical cancer cells via pro-oxidant anticancer mechanism. Phytother Res. 2020;34(9):2366–2384. doi:https://doi.org/10.1002/ptr.6687
- Selvi SK, Vinoth A, Varadharajan T, Weng CF, Padma VV. Neferine augments therapeutic efficacy of cisplatin through ROS- mediated non-canonical autophagy in human lung adenocarcinoma (A549 cells). Food Chem Toxicol. 2017;103:28–40. doi:https://doi.org/10.1016/j.fct.2017.02.020
- Ozal SA, Gurlu V, Turkekul K, Guclu H, Erdogan S. Neferine inhibits epidermal growth factor-induced proliferation and migration of retinal pigment epithelial cells through downregulating p38 MAPK and PI3K/AKT signalling. Cutan Ocul Toxicol. 2020;39(2):97–105. doi:https://doi.org/10.1080/15569527.2020.1730882
- Eid W, Abdel-Rehim W. Neferine enhances the antitumor effect of mitomycin-C in hela cells through the activation of p38-MAPK pathway. J Cell Biochem. 2017;118(10):3472–3479. doi:https://doi.org/10.1002/jcb.26006
- Liu Z, Zhang S, Wang T, Shao H, Gao J, Wang Y, Ge Y. Neferine inhibits MDA-MB-231 cells growth and metastasis by regulating miR-374a/FGFR-2. Chem Biol Interact. 2019;309:108716. doi:https://doi.org/10.1016/j.cbi.2019.06.029
- Zhang Q, Li Y, Miao C, Wang Y, Xu Y, Dong R, Zhang Z, Griffin BB, Yuan C, Yan S, et al. Anti-angiogenesis effect of Neferine via regulating autophagy and polarization of tumor-associated macrophages in high-grade serous ovarian carcinoma. Cancer Lett. 2018;432:144–155. doi:https://doi.org/10.1016/j.canlet.2018.05.049
- Poornima P, Weng C, Padma VV. Neferine, an alkaloid from lotus seed embryo, inhibits human lung cancer cell growth by MAPK activation and cell cycle arrest. Biofactors. 2014;40(1):121–131. doi:https://doi.org/10.1002/biof.1115
- Law BYK, Michelangeli F, Qing Y. Neferine induces autophagy-dependent cell death in apoptosis-resistant cancers via ryanodine receptor and Ca-dependent mechanism. Sci. Rep. 2019;9:20034.
- Yoon J-S, Kim H-M, Yadunandam AK, Kim N-H, Jung H-A, Choi J-S, Kim C-Y, Kim G-D. Neferine isolated from Nelumbo nucifera enhances anti-cancer activities in Hep3B cells: Molecular mechanisms of cell cycle arrest, ER stress induced apoptosis and anti-angiogenic response. Phytomedicine. 2013;20(11):1013–1022. doi:https://doi.org/10.1016/j.phymed.2013.03.024
- Singh AN, Baruah MM, Sharma N. Structure based docking studies towards exploring potential anti-androgen activity of selected phytochemicals against prostate cancer. Sci Rep. 2017;7(1):1955. doi:https://doi.org/10.1038/s41598-017-02023-5
- Patergnani S, Danese A, Bouhamida E. Various aspects of calcium signaling in the regulation of apoptosis, autophagy, cell proliferation, and cancer. Int J Mol Sci. 2020;21:8283.