38. Jian Shu, Liuyi Dang, Dandan Zhang, Punit Shah, Lijun Chen, Hui Zhang, Shisheng Sun*. Dynamic analysis of proteomic alterations in response to N‐linked glycosylation inhibition in a drug‐resistant ovarian carcinoma cell line. The FEBS journal. 286, 8: 1594-1605.
点击次数:
影响因子:4.392
DOI码:10.1111/febs.14811.
关键字:ER stress; cellular response; glycosylation; proteome; tunicamycin.
摘要:Glycosylation inhibition can improve the efficacy of antitumor drugs and enhance the apoptosis of cancer cells, thus holding great potential for cancer treatment. Inhibition of N-glycosylation induces endoplasmic reticulum (ER) stress and the unfolded protein response (UPR), and eventually triggers ER stress-related apoptosis. Unfortunately, the detailed timeline of these cell responses and protein expression alterations related to N-glycosylation inhibition is not explicit yet, and the pathways involved in different stages of N-glycosylation inhibition still need to be characterized. In this study, the dynamic proteome alterations related to N-glycosylation inhibition were investigated by further analyzing our previously published quantitative proteomics data from tunicamycin (TM)-treated ovarian carcinoma (OVCAR-3) cells. The results revealed that N-glycosylation inhibition not only directly affects the expression of glycosylated proteins but also alters an extended scale of proteins. Functional annotation of these altered proteins demonstrated that proteins related to ER stress start changing within 6 h, followed by UPR within 24 h, and eventually ER stress-related apoptosis is triggered after 48 h, indicating the conversion of cellular response from positive to negative. The dynamic proteome data presented here provide important information for better understanding of the significance of N-glycosylation to cell survival and TM-related cancer treatment.
论文类型:期刊论文
学科门类:理学
一级学科:生物学
文献类型:J
是否译文:否
收录刊物:SCI
上一条:39. Liuyi Dang, Jiechen Shen, Ting Zhao, Fei Zhao, Li Jia, Bojing Zhu, Chen Ma, Danqian Chen, Yingyong Zhao, Shisheng Sun*. Recognition of Bisecting N-Glycans on Intact Glycopeptides by Two Characteristic Ions in Tandem Mass Spectra. Analytical chemistry. 2019, 91(9): 5478-5482.
下一条:37. Shisheng Sun*, Yingwei Hu, Minghui Ao, Punit Shah, Jing Chen, Weiming Yang, Xingwang Jia, Yuan Tian, Stefani Thomas, Hui Zhang*. N-GlycositeAtlas: a database resource for mass spectrometry-based human N-linked glycoprotein and glycosylation site mapping. Clinical Proteomics. 2019, 16 (1): 1-11.