PROTEOMICS · 2018 · 40 citations · 31 references
Life SciencesBiochemistryMolecular BiologyMolecular OncologyProtein BiochemistryProteomicsCancer ProteomicsKidney CancerPost-translational Modification AnalysisProteomic ProfilingQuantitative ProteomicsRenal Cell CarcinomaCancer Proteome ProfilingGlycolysisProtein Expression ProfilingProteome BioinformaticsProteomic Data AnalysisRenal Cell Carcinoma BiomarkersTumor Proteome ProfilingTumor Proteomics
In light of the increasing incidence of renal cell carcinoma (RCC), its molecular mechanisms have been comprehensively explored in numerous recent studies. However, few studies focus on the influence of multi-factor interactions during the occurrence and development of RCC. This study aims to investigate the quantitative global proteome and the changes in lysine succinylation in related proteins, seeking to facilitate a better understanding of the molecular mechanisms underlying RCC. LC-MS/MS combined with bioinformatics analysis are used to quantitatively detect the perspectives at the global protein level. IP and WB analysis were conducted to further verify the alternations of related proteins and lysine succinylation. A total of 3,217 proteins and 1,238 lysine succinylation sites are quantified in RCC tissues, and 668 differentially expressed proteins and 161 differentially expressed lysine succinylation sites are identified. Besides, expressions of PGK1 and PKM2 at protein and lysine, succinylation levels are significantly altered in RCC tissues. Bioinformatics analysis indicates that the glycolysis pathway is a potential mechanism of RCC progression and lysine succinylation may plays a potential role in energy metabolism. These results can provide a new direction for exploring the molecular mechanism of RCC tumorigenesis.
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