Abstract
BackgroundLysine acetylation is a post-translational modification that regulates a diversity of biological processes, including cancer development.MethodsHere, we performed the quantitative acetylproteomic analysis of three primary cervical cancer tissues and corresponding adjacent normal tissues by using the label-free proteomics approach.ResultsWe identified a total of 928 lysine acetylation sites from 1547 proteins, in which 495 lysine acetylation sites corresponding to 296 proteins were quantified. Further, 41 differentially expressed lysine acetylation sites corresponding to 30 proteins were obtained in cervical cancer tissues compared with adjacent normal tissues (Fold change > 2 and P < 0.05), of which 1 was downregulated, 40 were upregulated. Moreover, 75 lysine acetylation sites corresponding to 58 proteins were specifically detected in cancer tissues or normal adjacent tissues. Motif-X analysis showed that kxxxkxxxk, GkL, AxxEk, kLxE, and kkxxxk are the most enriched motifs with over four-fold increases when compared with the background matches. KEGG analysis showed that proteins identified from differently and specifically expressed peptides may influence key pathways, such as Notch signaling pathway, viral carcinogenesis, RNA transport, and Jak-STAT, which play an important role in tumor progression. Furthermore, the acetylated levels of CREBBP and S100A9 in cervical cancer tissues were confirmed by immunoprecipitation (IP) and Western blot analysis.ConclusionsTaken together, our data provide novel insights into the role of protein lysine acetylation in cervical carcinogenesis.
Highlights
Lysine acetylation is a post-translational modification that regulates a diversity of biological processes, including cancer development
In order to explore the novel lysine acetylation proteins involved in the development of cervical cancer, the present study investigated the differential lysine acetylome profile between primary cervical cancer tissues and corresponding adjacent normal tissues by using a rigorous label-free quantitative mass spectrometry approach
Global profiling of protein lysine acetylation cervical carcinogenesis To investigate the regulatory role of protein lysine acetylation in cervical carcinogenesis, we performed a quantitative, MS-based acetylproteomic analysis of primary cancer tissues and corresponding adjacent normal tissues from three patients with cervical squamous cell carcinoma
Summary
Lysine acetylation is a post-translational modification that regulates a diversity of biological processes, including cancer development. Post-translational modifications, occurring in almost all proteins, regulate a diversity of biological processes by altering the structural, conformational and physicochemical properties of proteins [7]. Recent evidence indicates that lysine acetylation is widespread in almost every compartment of a cell, such as the cytoplasm and mitochondria, and regulates multiple metabolic processes, including citric acid cycle, glycolysis, and fatty acid metabolism [10,11,12]. Aberrant lysine acetylation is associated with cervical cancer development [15]. To the best of our knowledge, there are no reports on large scale analyses of aberrant lysine acetylation in cervical cancer development
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