Resistance against apoptosis by the cellular prion protein is dependent on its glycosylation status in oral HSC-2 and colon LS 174T cancer cells
Resistance against apoptosis by the cellular prion protein is dependent on its glycosylation status in oral HSC-2 and colon LS 174T cancer cells
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DOI：
10.1016/j.canlet.2011.02.040
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发表时间：
2011-07-01
期刊：
影响因子：
9.7
通讯作者：
Say, Yee-How
中科院分区：
文献类型：
--
作者：
Yap, Yeannie Hui-Yeng;Say, Yee-How
大多数研究都集中在细胞朊蛋白（PrP（c））在神经退行性疾病中的作用，而这种无处不在的蛋白质在神经系统外的功能仍然难以捉摸。因此，在本研究中，分别通过稳定的shRNA敲低和过表达来评估PrP（c）在口腔鳞状细胞癌（HSC-2）和结肠腺癌（LS 174 T）中的抗凋亡特性。MTT测定、Annexin V-FITC/PI和DCFH-DA染色表明，PrP（c）具有抗氧化应激-细胞凋亡的作用，但这种特性在衣霉素的N-糖基化抑制作用下被消除。我们的研究结果表明，抑制过表达PrP（c）的癌细胞中的糖基化可能是一个潜在的治疗靶点。(C)2011爱思唯尔爱尔兰有限公司保留所有权利。
Most studies have focused on the role of the cellular prion protein (PrP(c)) in neurodegenerative diseases, whereas the function of this ubiquitous protein outside the nervous system remains elusive. Therefore, the anti-apoptotic property of PrP(c) in oral squamous cell carcinoma (HSC-2) and colon adenocarcinoma (LS 174T) was evaluated in this study, by stable shRNA knockdown and overexpression, respectively. PrP(c) confers resistance against oxidative stress-apoptosis as indicated by MTT assay, Annexin V-FITC/PI and DCFH-DA staining, but this property is abolished upon N-glycosylation inhibition by tunicamycin. Our results indicate that the inhibition of glycosylation in cancer cells overexpressing PrP(c) could represent a potential therapeutic target. (C) 2011 Elsevier Ireland Ltd. All rights reserved.