A systematic comparison of O-linked β-N-acetylglucosamine (O-GlcNAc) functions between metabolic states has not yet been performed. O-GlcNAcylation is the dynamic and ubiquitous post-translational modification where the intracellular carbohydrate, O-GlcNAc, is appended to serine and threonine hydroxyl moieties. This modification is distinct in its nuclear and cytoplasmic compartmentalization, lack of chain elongation and branching, and rapid cycling. Furthermore, O-GlcNAcylation is involved in a delicate interplay with O-Phosphorylation—an interplay that when perturbed can lead to specific chronic, metabolic pathologies such as cardiovascular disease, diabetes, cancer, and neurodegenerative disorders. Here we describe a bottom-up proteomic approach characterizing distinct and separable disease targets and pathways involved in context-dependent O-GlcNAcylation. This approach processes tandem mass spectrometry data obtained from the immunoprecipitation enrichment of cellular lysates originating from both healthy and chronically diseased—cancer, Alzheimer's disease, and diabetes—cell cultures, identifies unique O-GlcNAcylated proteins involved in specific pathological pathways, and trains machine learning algorithms for increased informatic insight. From this data we hope to aid the development of novel therapeutics for the remediation of these deadly disease states.

Informatic analysis of O-GlcNAc modified proteins in diseases of metabolism

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

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