Profiling amino acid substitution on proteomic scale unveils novel protein regulation in cancer diseases
Zhao, P.; DAI, S.; Lai, S.; Zhou, C.; Yu, W.; Li, N.
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AbstractAmino acid substitutions (AA subs) play an important role in regulating cellular activities, encompassing complex cell signaling and cycling in both normal and cancer cells. Profiling AA subs at a proteomic level has been a challenging issue in the past. In this study, we analyze a large collection of proteomic data originating from 537 patients across five cancer patient cohorts using a novel mass spectrometry data analysis tool, named PIPI3. The pervasive patterns of AA subs are present in essential proteins like exosome-related proteins, actin filament binding proteins, and proteins in glycolysis and gluconeogenesis pathways of cancer cells. The novel identified AA subs are assumed to be caused during the protein synthesis process, which cannot be identified by traditional genome or transcriptome-based methods. Thus, this proteomic scale analysis provides insights into novel regulation mechanisms of AA subs in carcinogenesis, the outcome of which may be applied in cancer diagnosis and interventions.
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