Page 68 - Read Online

Page 30 of 36 Dave et al. J Cancer Metastasis Treat 2020;6:46 I http://dx.doi.org/10.20517/2394-4722.2020.106

cells. Biochem Biophys Res Commun 2017;482:15-21.
79. Toden S, Tran HM, Tovar-Camargo OA, Okugawa Y, Goel A. Epigallocatechin-3-gallate targets cancer stem-like cells and enhances
5-fluorouracil chemosensitivity in colorectal cancer. Oncotarget 2016;7:16158-71.
80. Jiang P, Xu C, Chen L, et al. EGCG inhibits CSC-like properties through targeting miR-485/CD44 axis in A549-cisplatin resistant cells.
Mol Carcinog 2018;57:1835-44.
81. Sun Y, Liu WZ, Liu T, Feng X, Yang N, Zhou HF. Signaling pathway of MAPK/ERK in cell proliferation, differentiation, migration,
senescence and apoptosis. J Recept Signal Transduct Res 2015;35:600-4.
82. Shirakami Y, Shimizu M. Possible mechanisms of green tea and its constituents against cancer. Molecules 2018;23:2284.
83. Bigelow RL, Cardelli JA. The green tea catechins, (-)-Epigallocatechin-3-gallate (EGCG) and (-)-Epicatechin-3-gallate (ECG), inhibit
HGF/Met signaling in immortalized and tumorigenic breast epithelial cells. Oncogene 2006;25:1922-30.
84. Sah JF, Balasubramanian S, Eckert RL, Rorke EA. Epigallocatechin-3-gallate inhibits epidermal growth factor receptor signaling
pathway. Evidence for direct inhibition of ERK1/2 and AKT kinases. J Biol Chem 2004;279:12755-62.
85. Khan N, Afaq F, Saleem M, Ahmad N, Mukhtar H. Targeting multiple signaling pathways by green tea polyphenol (-)-epigallocatechin-3-
gallate. Cancer Res 2006;66:2500-5.
86. Jiang J, Mo ZC, Yin K, et al. Epigallocatechin-3-gallate prevents TNF-α-induced NF-κB activation thereby upregulating ABCA1 via the
Nrf2/Keap1 pathway in macrophage foam cells. Int J Mol Med 2012;29:946-56.
87. Giakoustidis AE, Giakoustidis DE, Koliakou K, et al. Inhibition of intestinal ischemia/repurfusion induced apoptosis and necrosis via
down-regulation of the NF-kB, c-Jun and caspace-3 expression by epigallocatechin-3-gallate administration. Free Radic Res 2008;42:180-
8.
88. Sen T, Dutta A, Chatterjee A. Epigallocatechin-3-gallate (EGCG) downregulates gelatinase-B (MMP-9) by involvement of FAK/ERK/
NFkappaB and AP-1 in the human breast cancer cell line MDA-MB-231. Anticancer Drugs 2010;21:632-44.
89. Kim HS, Kim MH, Jeong M, et al. EGCG blocks tumor promoter-induced MMP-9 expression via suppression of MAPK and AP-1
activation in human gastric AGS cells. Anticancer Res 2004;24:747-53.
90. Yan Z, Yong-Guang T, Fei-Jun L, Fa-Qing T, Min T, Ya C. Interference effect of epigallocatechin-3-gallate on targets of nuclear factor
kappaB signal transduction pathways activated by EB virus encoded latent membrane protein 1. Int J Biochem Cell Biol 2004;36:1473-
81.
91. Wu Q, Wu W, Fu B, Shi L, Wang X, Kuca K. JNK signaling in cancer cell survival. Med Res Rev 2019;39:2082-104.
92. Yamamoto T, Digumarthi H, Aranbayeva Z, et al. EGCG-targeted p57/KIP2 reduces tumorigenicity of oral carcinoma cells: role of c-Jun
N-terminal kinase. Toxicol Appl Pharmacol 2007;224:318-25.
93. Cao G, Chen M, Song Q, et al. EGCG protects against UVB-induced apoptosis via oxidative stress and the JNK1/c-Jun pathway in
ARPE19 cells. Mol Med Rep 2012;5:54-9.
94. Saeki K, Kobayashi N, Inazawa Y, et al. Oxidation-triggered c-Jun N-terminal kinase (JNK) and p38 mitogen-activated protein (MAP)
kinase pathways for apoptosis in human leukaemic cells stimulated by epigallocatechin-3-gallate (EGCG): a distinct pathway from those
of chemically induced and receptor-mediated apoptosis. Biochem J 2002;368:705-20.
95. Cuadrado A, Nebreda AR. Mechanisms and functions of p38 MAPK signalling. Biochemical Journal 2010;429:403-17.
96. Cerezo-Guisado MI, Zur R, Lorenzo MJ, et al. Implication of Akt, ERK1/2 and alternative p38MAPK signalling pathways in human
colon cancer cell apoptosis induced by green tea EGCG. Food Chem Toxicol 2015;84:125-32.
97. Kim SJ, Jeong HJ, Lee KM, et al. Epigallocatechin-3-gallate suppresses NF-kappaB activation and phosphorylation of p38 MAPK and
JNK in human astrocytoma U373MG cells. J Nutr Biochem 2007;18:587-96.
98. Kang YH, Pezzuto JM. Induction of quinone reductase as a primary screen for natural product anticarcinogens. Methods Enzymol
2004;382:380-414.
99. Fahey JW, Talalay P. Antioxidant functions of sulforaphane: a potent inducer of Phase II detoxication enzymes. Food Chem Toxicol
1999;37:973-9.
100. Lenzi M, Fimognari C, Hrelia P. Sulforaphane as a promising molecule for fighting cancer. Cancer Treat Res 2014;159:207-23.
101. Kuljarachanan T, Fu N, Chiewchan N, Devahastin S, Chen XD. Evolution of important glucosinolates in three common Brassica
vegetables during their processing into vegetable powder and in vitro gastric digestion. Food Funct 2020;11:211-20.
102. Matusheski NV, Swarup R, Juvik JA, Mithen R, Bennett M, Jeffery EH. Epithiospecifier protein from broccoli (Brassica oleracea L. ssp.
italica) inhibits formation of the anticancer agent sulforaphane. J Agric Food Chem 2006;54:2069-76.
103. Matusheski NV, Juvik JA, Jeffery EH. Heating decreases epithiospecifier protein activity and increases sulforaphane formation in
broccoli. Phytochemistry 2004;65:1273-81.
104. Gasper AV, Al-Janobi A, Smith JA, et al. Glutathione S-transferase M1 polymorphism and metabolism of sulforaphane from standard and
high-glucosinolate broccoli. Am J Clin Nutr 2005;82:1283-91.
105. Egner PA, Chen JG, Wang JB, et al. Bioavailability of Sulforaphane from two broccoli sprout beverages: results of a short-term, cross-
over clinical trial in Qidong, China. Cancer Prev Res (Phila) 2011;4:384-95.
106. Houghton CA, Fassett RG, Coombes JS. Sulforaphane: translational research from laboratory bench to clinic. Nutr Rev 2013;71:709-26.
107. Yagishita Y, Fahey JW, Dinkova-Kostova AT, Kensler TW. Broccoli or sulforaphane: is it the source or dose that matters? Molecules
2019;24:3593.
108. Huang C, Wu J, Chen D, Jin J, Wu Y, Chen Z. Effects of sulforaphane in the central nervous system. Eur J Pharmacol 2019;853:153-68.
109. Shawky NM, Shehatou GSG, Suddek GM, Gameil NM. Comparison of the effects of sulforaphane and pioglitazone on insulin resistance
and associated dyslipidemia, hepatosteatosis, and endothelial dysfunction in fructose-fed rats. Environ Toxicol Pharmacol 2019;66:43-54.