Crosstalk among proteome, acetylome and succinylome in colon cancer HCT116 cell treated with sodium dichloroacetate

• DOI: 10.1038/srep37478
• Publication Date: 2016-11-22T10:26:08Z
• Authors: Danxi Zhu; Lidan Hou; Bin Hu; Hang Zhao; Jie Sun; Jianhua Wang; Xiangjun Meng
• Keywords: Succinylation; Proteome

Protein lysine acetylation and succinylation play important regulatory roles in cells, both of which or each other has a close relationship. Dichloroacetate (DCA), well-known pyruvate dehydrogenase kinase (PDK) inhibitor, the potential to be used as anti-cancer drugs for several tumors including colorectal cancer. However, little is known about mechanism DCA-based cancer therapy by protein posttranslational modifications (PTM) global proteome, acetylome succinylome. Here combinations with stable isotope labeling (SILAC), antibody affinity enrichment high resolution LC-MS/MS analysis were performed human colon HCT116 cells. The quantifiable proteome was annotated using bioinformatics. In total, 4,518 proteins, 1,436 sites, 671 sites quantified, respectively DCA treatment. Among quantified acetylated 158 increased level (quantification ratio >1.5) 145 decreased <0.67). Meanwhile, 179 up-regulated 114 down-regulated succinylated identified. bioinformatics analyses initially showed involved wide range cellular functions upon effects. Notably, protein-protein interaction network demonstrated widespread interactions modulated succinylation. Taken together, this study may shed light on understanding