Lysine acetylation-directed high-resolution plasma proteomic landscape of Alzheimer’s disease

Abstract Background Protein lysine acetylation is known to be widely involved in the regulation of various biological processes through extensive physicochemical regulation of each protein function. Methods In order to analyze a system-wide landscape of lysine acetylation on human plasma protein components regarding Alzheimer’s Disease (AD)-related pathogenesis, we performed a global lysine acetylation-directed proteomic analysis of human plasma samples obtained from 20 AD patients and 20 age-matched controls. Results Our large-scale proteomic measurements enabled us to acquire more than 7,600 independent MS/MS spectral data regarding 350 unique lysine acetylation sites not only from already known human plasma proteins but also from novel short open reading frame (ORF)-encoded peptide sequences defined by ribosome profiling technologies. Conclusions This report provides the first lysine acetylation-directed proteomic landscape of AD-related human plasma samples and may contribute to our extensive understanding of biochemical properties regarding human plasma protein components in relation to AD pathogenesis.