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Unveiling the metabolic fate of monosaccharides in cell membranes with glycomic and glycoproteomic analyses

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Abstract

Cell membrane protein glycosylation is dependent on the metabolic state of the cell as well as exogenous nutrients available. Although the metabolism and interconversion of monosaccharides have been well-studied, their incorporation into cell surface glycans and their corresponding glycoproteins remains relatively unknown. In this study, we developed a method to investigate quantitatively the incorporation pathways of dietary saccharides into specific glycans and glycoproteins on the cell membrane by treating intestinal Caco-2 and hepatic KKU-M213 cells with 13C-labeled monosaccharides and characterizing the resulting cell surface glycans and glycopeptides by LC-MS/MS. Time-course studies using uniformly labeled glucose revealed that the rate of incorporation was both glycan-specific and protein-dependent. Comparative studies using different dietary saccharides and multiple cell lines revealed the variance of monosaccharide utilization and interconversion in different tissues and organisms. The robust isotope-labeling and glycan profiling methods can provide a useful tool for differentiating glycosylation pathways and enhance the understanding of how dietary sugar intake affects health.

Graphical abstract: Unveiling the metabolic fate of monosaccharides in cell membranes with glycomic and glycoproteomic analyses

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Publication details

The article was received on 04 Apr 2019, accepted on 10 Jun 2019 and first published on 11 Jun 2019


Article type: Edge Article
DOI: 10.1039/C9SC01653H
Chem. Sci., 2019, Advance Article
  • Open access: Creative Commons BY license
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    Unveiling the metabolic fate of monosaccharides in cell membranes with glycomic and glycoproteomic analyses

    G. Xu, M. Wong, Q. Li, D. Park, Z. Cheng and C. B. Lebrilla, Chem. Sci., 2019, Advance Article , DOI: 10.1039/C9SC01653H

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