Investigation of the effects of ethanol extract of pomegranate juice on the global gene expression in T24 bladder cancer cell by proteomics strategy

• Main Authors: Hsu Li-Ting, 徐麗婷
• Other Authors: 吳定峰
• Format: Others
• Language: zh-TW
• Published: 101
• Online Access: http://ndltd.ncl.edu.tw/handle/68143477187940133691

碩士 === 南台科技大學 === 生物科技系 === 100 === Punica granatum L., also known as pomegranate (punicacease), is a rich source of two types of polyphenolic compounds: anthocyanins and hydrolysable tannis. The pomegranate has numerous therapeutic values, such as anti-hepatotoxicity, anti-lipoperoxidation, antioxidation, anti-infammatory and anti-tumor. Our previous study found that the ethanol extract of pomegranate juice (POME) can induce cell cycle arrest and cell apoptosis via triggering the mitochondrial pathway and endothelium reticulum stress in T24 bladder cancer cell. In this study, we employed the proteomics method to search for the POME-affected genes that might clarify the molecular mechanism underlying T24 cell apoptosis elicited by POME. To achieve the above goal, T24 bladder cancer cells were treated for 36 hours with or without 50 μg/ml POME. A 50 μg/ml treatment was selected because sufficient affected cells that were at the same time still viable could be collected and potentially relevant cellular changes prior to cell death could typically be observed in T24 cells treated after 36 hours with 50 mg/ml POME. Then we underwent two-dimensional gel electrophoreses (2-DE) to acquire the proteomic profiles of POME-treated and naive T24 bladder cancer cells. The proteome maps of treated cancer cells were compared with those of un-treated cell to find the differentially express proteins. The de-regulated protein spots were recorded, which were 2-fold or above in magnitude as observed in at least 5 out of 9 comparisons and statistically significant (P<0.05, student’s t test). Comparative proteomics indicated that 23 dys-regulated proteins were present in POME-incubated T24 cancer cell. These differentially expressed proteins would be identified using tandem mass spectrometry.