Journal
JOURNAL OF PROTEOME RESEARCH
Volume 11, Issue 3, Pages 1598-1608Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr2007895
Keywords
beta-cells; islets; surface N-glycoproteins; proteomics; diabetes
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Funding
- JDRF [26-2008-633]
- Hoffmann La Roche Ltd., Basel
- CC-SPMD
- SystemsX.ch
- Swiss National Science Foundation (SNF) [31000-10767]
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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 beta-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 beta-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 beta-cells with glucose and the hormone GLP1, known stimulators of insulin secretion, causes significant changes in surface N-glycoproteome expression. Taken together, this beta-cell N-glycoproteome resource provides a comprehensive view on the composition of beta-cell surface proteins and expands the scope of signaling systems potentially involved in mediating responses of beta-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 beta-cell surface N-glycoproteome.
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