Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/69811
標題: The Anti-Cancer Effects of (-)-Epigalocathine-3-Gallate on the Signaling Pathways Associated With Membrane Receptors in MCF-7 Cells
作者: Hsu, Y.C.
Liou, Y.M.
關鍵字: tea polyphenol epigallocatechin-3-gallate
67-kda laminin receptor
beta-catenin
cancer cells
actin cytoskeleton
tumor-suppressor
e-cadherin
expression
tropomyosin
activation
期刊/報告no:: Journal of Cellular Physiology, Volume 226, Issue 10, Page(s) 2721-2730.
摘要: (-)-Epigallocatechin-3-gallate (EGCg) has been implicated in cancer chemo-prevention in studies using many different kinds of cancer cells. The present study measured cell viability, osteopontin (OPN) secretion, fatty acid synthase (FAS) expression, and cytosolic Ca(2+) and verified the anti-cancer activities of EGCg in MCF-7 human breast cancer cells. EGCg-induced apoptosis was evidenced by nuclear condensation, increased protein levels of activated caspase-3, down-regulation of gelsolin and tropomyosin-4 (Tm-4), and up-regulation of tropomyosin-1(Tm-1). By disrupting adherens junction formation, EGCg caused accumulation of extra-nuclear beta-catenin aggregates in the cytosol and alterations of the protein content and mRNA expression of E-cadherin and beta-catenin, but not N-cadherin, in MCF-7 cells. To identify the putative mechanisms underlying the EGCg signaling pathways, EGFP (enhanced green fluorescence protein) was ectopically expressed in MCF-7 cells. This allowed us to monitor the EGCg-induced fluorescence changes associated with the effects of Triton X-100 (to remove plasma membrane) or the addition of laminin, anti-laminin receptor (LR) antibody, epidermal growth factor (EGF), and genistein on the cells. Our results indicated that EGCg acts via the signaling pathways associated with cell membrane to suppress cell proliferation, provoke apoptosis, and disturb cell-cell adhesion in MCF-7 cells. The altered events include the EGFR, LR, FAS, intracellular Ca(2+), OPN secretion, caspace-3, gelsolin, Tm-4, Tm-1, and adherens junction proteins, E-cadherin and beta-catenin. J. Cell. Physiol. 226: 2721-2730, 2011. (C) 2010 Wiley-Liss, Inc.
URI: http://hdl.handle.net/11455/69811
ISSN: 0021-9541
文章連結: http://dx.doi.org/10.1002/jcp.22623
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