Simultaneous Quantitation of Glycoprotein Degradation and Synthesis Rates by Integrating Isotope Labeling, Chemical Enrichment, and Multiplexed Proteomics.

ABSTRACT: Protein glycosylation is essential for cell survival and regulates many cellular events. Reversible glycosylation is also dynamic in biological systems. The functions of glycoproteins are regulated by their dynamics to adapt the ever-changing inter- and intracellular environments. Glycans on proteins not only mediate a variety of protein activities, but also creates a steric hindrance for protecting the glycoproteins from degradation by proteases. In this work, a novel strategy integrating isotopic labeling, chemical enrichment and multiplexed proteomics was developed to simultaneously quantify the degradation and synthesis rates of many glycoproteins in human cells. We quantified the synthesis rates of 847 N-glycoproteins and the degradation rates of 704 glycoproteins in biological tripli

SUBMITTER: Xiao H 

PROVIDER: S-EPMC5678942 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature