Comprehensive description of the N-glycoproteome of mouse pancreatic ß-cells and human islets.
J Proteome Res
; 11(3): 1598-608, 2012 Mar 02.
Article
em En
| MEDLINE
| ID: mdl-22148984
ABSTRACT
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 ß-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 ß-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 ß-cells with glucose and the hormone GLP1, known stimulators of insulin secretion, causes significant changes in surface N-glycoproteome expression. Taken together, this ß-cell N-glycoproteome resource provides a comprehensive view on the composition of ß-cell surface proteins and expands the scope of signaling systems potentially involved in mediating responses of ß-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 ß-cell surface N-glycoproteome.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Glicoproteínas de Membrana
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Ilhotas Pancreáticas
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Proteoma
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Células Secretoras de Insulina
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Peptídeo 1 Semelhante ao Glucagon
Limite:
Adult
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Aged
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Animals
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Humans
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article