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Comprehensive Description of the N-Glycoproteome of Mouse Pancreatic β-Cells and Human Islets

Danzer, Carsten, Eckhardt, Katrin, Schmidt, Alexander, Fankhauser, Niklaus, Ribrioux, Sebastien, Wollscheid, Bernd, Müller, Lukas, Schiess, Ralph, Züllig, Richard, Lehmann, Roger, Spinas, Giatgen, Aebersold, Rudolf, Krek, Wilhelm
Journal of Proteome Research 2012 v.11 no.3 pp. 1598-1608
G-protein coupled receptors, biomarkers, diabetes, drugs, glucose, glycoproteins, homeostasis, humans, insulin secretion, islets of Langerhans, mice, protein kinases, proteinases, proteome, proteomics, surface proteins
Cell surface N-glycoproteins provide a key interface of cells to their environment and therapeutic entry points for drug and biomarker discovery. Their comprehensive description denotes therefore a formidable challenge. The β-cells of the pancreas play a crucial role in blood glucose homeostasis, and disruption of their function contributes to diabetes. By combining cell surface and whole cell capturing technologies with high-throughput quantitative proteomic analysis, we report on the identification of a total of 956 unique N-glycoproteins from mouse MIN6 β-cells and human islets. Three-hundred-forty-nine of these proteins encompass potential surface N-glycoproteins and include orphan G-protein-coupled receptors, novel proteases, receptor protein kinases, and phosphatases. Interestingly, stimulation of MIN6 β-cells with glucose and the hormone GLP1, known stimulators of insulin secretion, causes significant changes in surface N-glycoproteome expression. Taken together, this β-cell N-glycoproteome resource provides a comprehensive view on the composition of β-cell surface proteins and expands the scope of signaling systems potentially involved in mediating responses of β-cells to various forms of (patho)physiologic stress and the extent of dynamic remodeling of surface N-glycoprotein expression associated with metabolic and hormonal stimulation. Moreover, it provides a foundation for the development of diabetes medicines that target or are derived from the β-cell surface N-glycoproteome.