References
- Bray F, Ferlay J, Soerjomataram I, Siegel RL, Torre LA, Jemal A. Global cancer statistics 2018: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries. CA Cancer J Clin 2018;68:394-424. https://doi.org/10.3322/caac.21492
- Sher T, Dy GK, Adjei AA. Small cell lung cancer. Mayo Clin Proc 2008;83:355-67. https://doi.org/10.4065/83.3.355
- Artal Cortes A, Calera Urquizu L, Hernando Cubero J. Adjuvant chemotherapy in non-small cell lung cancer: state-of-the-art. Transl Lung Cancer Res 2015;4:191-7. https://doi.org/10.3978/j.issn.2218-6751.2014.06.01
- Hall A. Rho GTPases and the actin cytoskeleton. Science 1998;279:509-14. https://doi.org/10.1126/science.279.5350.509
- Ridley AJ. Rho GTPases and cell migration. J Cell Sci 2001;114:2713-22. https://doi.org/10.1242/jcs.114.15.2713
- Iden S, Collard JG. Crosstalk between small GTPases and polarity proteins in cell polarization. Nat Rev Mol Cell Biol 2008;9:846-59. https://doi.org/10.1038/nrm2521
- Tomar A, Schlaepfer DD. Focal adhesion kinase: switching between GAPs and GEFs in the regulation of cell motility. Curr Opin Cell Biol 2009;21:676-83. https://doi.org/10.1016/j.ceb.2009.05.006
- Lee BY, Timpson P, Horvath LG, Daly RJ. FAK signaling in human cancer as a target for therapeutics. Pharmacol Ther 2015;146:132-49. https://doi.org/10.1016/j.pharmthera.2014.10.001
- Yeatman TJ. A renaissance for SRC. Nat Rev Cancer 2004;4:470-80. https://doi.org/10.1038/nrc1366
- Zhang S, Yu D. Targeting Src family kinases in anti-cancer therapies: turning promise into triumph. Trends Pharmacol Sci 2012;33:122-8. https://doi.org/10.1016/j.tips.2011.11.002
- Park GB, Kim D. Cigarette smoke-induced EGFR activation promotes epithelial mesenchymal migration of human retinal pigment epithelial cells through regulation of the FAK-mediated Syk/Src pathway. Mol Med Rep 2018;17:3563-74.
- Mitra SK, Schlaepfer DD. Integrin-regulated FAK-Src signaling in normal and cancer cells. Curr Opin Cell Biol 2006;18:516-23. https://doi.org/10.1016/j.ceb.2006.08.011
- Prateep A, Sumkhemthong S, Karnsomwan W, De-Eknamkul W, Chamni S, Chanvorachote P, Chaotham C. Avicequinone B sensitizes anoikis in human lung cancer cells. J Biomed Sci 2018;25:32. https://doi.org/10.1186/s12929-018-0435-3
- Miean KH, Mohamed S. Flavonoid (myricetin, quercetin, kaempferol, luteolin, and apigenin) content of edible tropical plants. J Agric Food Chem 2001;49:3106-12. https://doi.org/10.1021/jf000892m
- Imran M, Rauf A, Abu-Izneid T, Nadeem M, Shariati MA, Khan IA, Imran A, Orhan IE, Rizwan M, Atif M, Gondal TA, Mubarak MS. Luteolin, a flavonoid, as an anticancer agent: a review. Biomed Pharmacother 2019;112:108612. https://doi.org/10.1016/j.biopha.2019.108612
- Lopez-Lazaro M. Distribution and biological activities of the flavonoid luteolin. Mini Rev Med Chem 2009;9:31-59. https://doi.org/10.2174/138955709787001712
- Xu T, Li D, Jiang D. Targeting cell signaling and apoptotic pathways by luteolin: cardioprotective role in rat cardiomyocytes following ischemia/reperfusion. Nutrients 2012;4:2008-19. https://doi.org/10.3390/nu4122008
- Birt DF, Hendrich S, Wang W. Dietary agents in cancer prevention: flavonoids and isoflavonoids. Pharmacol Ther 2001;90:157-77. https://doi.org/10.1016/S0163-7258(01)00137-1
- Martin KR. Targeting apoptosis with dietary bioactive agents. Exp Biol Med (Maywood) 2006;231:117-29. https://doi.org/10.1177/153537020623100201
- 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;58:1428-47. https://doi.org/10.1080/10408398.2016.1263597
-
Chen KC, Chen CY, Lin CR, Yang TY, Chen TH, Wu LC, Wu CC. Luteolin attenuates
$TGF-{\beta}1$ -induced epithelial-mesenchymal transition of lung cancer cells by interfering in the PI3K/Akt-$NF-{\kappa}B$ -Snail pathway. Life Sci 2013;93:924-33. https://doi.org/10.1016/j.lfs.2013.10.004 - Ma L, Peng H, Li K, Zhao R, Li L, Yu Y, Wang X, Han Z. Luteolin exerts an anticancer effect on NCI-H460 human non-small cell lung cancer cells through the induction of Sirt1-mediated apoptosis. Mol Med Rep 2015;12:4196-202. https://doi.org/10.3892/mmr.2015.3956
- Wang Q, Wang H, Jia Y, Ding H, Zhang L, Pan H. Luteolin reduces migration of human glioblastoma cell lines via inhibition of the p-IGF-1R/PI3K/AKT/mTOR signaling pathway. Oncol Lett 2017;14:3545-51. https://doi.org/10.3892/ol.2017.6643
- Sukketsiri W, Sawangjaroen K, Tanasawet S. Anti-apoptotic effects of phyllanthin against alcohol induced liver cell death. Trop J Pharm Res 2016;5:981-8.
- Singkhorn S, Tantisira MH, Tanasawet S, Hutamekalin P, Wongtawatchai T, Sukketsiri W. Induction of keratinocyte migration by ECa 233 is mediated through FAK/Akt, ERK, and p38 MAPK signaling. Phytother Res 2018;32:1397-403. https://doi.org/10.1002/ptr.6075
- Sit ST, Manser E. Rho GTPases and their role in organizing the actin cytoskeleton. J Cell Sci 2011;124:679-83. https://doi.org/10.1242/jcs.064964
- Lin Y, Shi R, Wang X, Shen HM. Luteolin, a flavonoid with potential for cancer prevention and therapy. Curr Cancer Drug Targets 2008;8:634-46. https://doi.org/10.2174/156800908786241050
- Chen P, Zhang JY, Sha BB, Ma YE, Hu T, Ma YC, Sun H, Shi JX, Dong ZM, Li P. Luteolin inhibits cell proliferation and induces cell apoptosis via down-regulation of mitochondrial membrane potential in esophageal carcinoma cells EC1 and KYSE450. Oncotarget 2017;8:27471-80. https://doi.org/10.18632/oncotarget.15832
- Cherng JM, Shieh DE, Chiang W, Chang MY, Chiang LC. Chemopreventive effects of minor dietary constituents in common foods on human cancer cells. Biosci Biotechnol Biochem 2007;71:1500-4. https://doi.org/10.1271/bbb.70008
- Pu Y, Zhang T, Wang J, Mao Z, Duan B, Long Y, Xue F, Liu D, Liu S, Gao Z. Luteolin exerts an anticancer effect on gastric cancer cells through multiple signaling pathways and regulating miRNAs. J Cancer 2018;9:3669-75. https://doi.org/10.7150/jca.27183
- Molina JR, Yang P, Cassivi SD, Schild SE, Adjei AA. Non-small cell lung cancer: epidemiology, risk factors, treatment, and survivorship. Mayo Clin Proc 2008;83:584-94. https://doi.org/10.4065/83.5.584
- Cook MT. Mechanism of metastasis suppression by luteolin in breast cancer. Breast Cancer (Dove Med Press) 2018;10:89-100.
- Carelli S, Zadra G, Vaira V, Falleni M, Bottiglieri L, Nosotti M, Di Giulio AM, Gorio A, Bosari S. Up-regulation of focal adhesion kinase in non-small cell lung cancer. Lung Cancer 2006;53:263-71. https://doi.org/10.1016/j.lungcan.2006.06.001
- Ji HF, Pang D, Fu SB, Jin Y, Yao L, Qi JP, Bai J. Overexpression of focal adhesion kinase correlates with increased lymph node metastasis and poor prognosis in non-small-cell lung cancer. J Cancer Res Clin Oncol 2013;139:429-35. https://doi.org/10.1007/s00432-012-1342-8
- Mazurenko NN, Kogan EA, Zborovskaya IB, Kisseljov FL. Expression of pp60c-src in human small cell and non-small cell lung carcinomas. Eur J Cancer 1992;28:372-7. https://doi.org/10.1016/S0959-8049(05)80056-5
- Bolos V, Gasent JM, Lopez-Tarruella S, Grande E. The dual kinase complex FAK-Src as a promising therapeutic target in cancer. Onco Targets Ther 2010;3:83-97.
- Carragher NO, Frame MC. Focal adhesion and actin dynamics: a place where kinases and proteases meet to promote invasion. Trends Cell Biol 2004;14:241-9. https://doi.org/10.1016/j.tcb.2004.03.011
- Gu MM, Gao D, Yao PA, Yu L, Yang XD, Xing CG, Zhou J, Shang ZF, Li M. p53-inducible gene 3 promotes cell migration and invasion by activating the FAK/Src pathway in lung adenocarcinoma. Cancer Sci 2018;109:3783-93. https://doi.org/10.1111/cas.13818
- Schaller MD, Hildebrand JD, Shannon JD, Fox JW, Vines RR, Parsons JT. Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src. Mol Cell Biol 1994;14:1680-8. https://doi.org/10.1128/MCB.14.3.1680
- Chen M, Chen SC, Pallen CJ. Integrin-induced tyrosine phosphorylation of protein-tyrosine phosphatase-alpha is required for cytoskeletal reorganization and cell migration. J Biol Chem 2006;281:11972-80. https://doi.org/10.1074/jbc.M600561200
- Hsia DA, Mitra SK, Hauck CR, Streblow DN, Nelson JA, Ilic D, Huang S, Li E, Nemerow GR, Leng J, Spencer KS, Cheresh DA, Schlaepfer DD. Differential regulation of cell motility and invasion by FAK. J Cell Biol 2003;160:753-67. https://doi.org/10.1083/jcb.200212114
- Chikara S, Lindsey K, Borowicz P, Christofidou-Solomidou M, Reindl KM. Enterolactone alters FAK-Src signaling and suppresses migration and invasion of lung cancer cell lines. BMC Complement Altern Med 2017;17:30. https://doi.org/10.1186/s12906-016-1512-3
- Sandilands E, Frame MC. Endosomal trafficking of Src tyrosine kinase. Trends Cell Biol 2008;18:322-9. https://doi.org/10.1016/j.tcb.2008.05.004
- Gardel ML, Schneider IC, Aratyn-Schaus Y, Waterman CM. Mechanical integration of actin and adhesion dynamics in cell migration. Annu Rev Cell Dev Biol 2010;26:315-33. https://doi.org/10.1146/annurev.cellbio.011209.122036
- Kim LC, Song L, Haura EB. Src kinases as therapeutic targets for cancer. Nat Rev Clin Oncol 2009;6:587-95. https://doi.org/10.1038/nrclinonc.2009.129
- Summy JM, Gallick GE. Src family kinases in tumor progression and metastasis. Cancer Metastasis Rev 2003;22:337-58. https://doi.org/10.1023/A:1023772912750
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