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- W2516316171 abstract "Surface glycoproteins regulate nearly every extracellular event and they are dynamic for cells to adapt to the ever-changing extracellular environment. These glycoproteins contain a wealth of information on cellular development and disease states, and have significant biomedical implications. Systematic investigation of surface glycoproteins will result in a better understanding of surface protein functions, cellular activities and the molecular mechanisms of disease. However, it is extraordinarily challenging to specifically and globally analyze surface glycoproteins. Here we designed the first method to systematically analyze surface glycoprotein dynamics and measure their half-lives by integrating pulse-chase labeling, selective enrichment of surface glycoproteins, and multiplexed proteomics. The current results clearly demonstrated that surface glycoproteins with catalytic activities were more stable than those with binding and receptor activities. Glycosylation sites located outside of any domain had a notably longer median half-life than those within domains, which strongly suggests that glycans within domains regulate protein interactions with other molecules while those outside of domains mainly play a role in protecting the protein from degradation. This method can be extensively applied to biological and biomedical research." @default.
- W2516316171 created "2016-09-16" @default.
- W2516316171 creator A5019829909 @default.
- W2516316171 creator A5049862161 @default.
- W2516316171 date "2017-01-01" @default.
- W2516316171 modified "2023-10-13" @default.
- W2516316171 title "Quantitative investigation of human cell surface N-glycoprotein dynamics" @default.
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- W2516316171 doi "https://doi.org/10.1039/c6sc01814a" @default.
- W2516316171 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5458730" @default.
- W2516316171 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28616130" @default.
- W2516316171 hasPublicationYear "2017" @default.
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