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Mapping human N-linked glycoproteins and glycosylation sites using mass spectrometry

Journal

TRAC-TRENDS IN ANALYTICAL CHEMISTRY
Volume 114, Issue -, Pages 143-150

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.trac.2019.02.009

Keywords

Glycosylation; Glycoprotein; Glycosylation site; Glycoproteome; Mass spectrometry; Human body fluids; Human tissues; Human cell lines

Funding

  1. National Natural Science Foundation of China [91853123, 21705127, 81773180, 81800655]
  2. Natural Science Foundation of Shaanxi Province [2018JM7086074]
  3. National Institutes of Health [U01CA152813, U24CA210985, P01HL107153, R21AI122382]

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N-linked glycoprotein is a highly interesting class of proteins for clinical and biological research. Over the last decade, large-scale profiling of N-linked glycoproteins and glycosylation sites from biological and clinical samples has been achieved through mass spectrometry-based glycoproteomic approaches. In this paper, we reviewed the human glycoproteomic profiles that have been reported in more than 80 individual studies, and mainly focused on the N-glycoproteins and glycosylation sites identified through their deglycosylated forms of glycosite-containing peptides. According to our analyses, more than 30,000 glycosite-containing peptides and 7000 human glycoproteins have been identified from five different body fluids, twelve human tissues (or related cell lines), and four special cell types. As the glycoproteomic data is still missing for many organs and tissues, a systematical glycoproteomic analysis of various human tissues and body fluids using a uniform platform is still needed for an integrated map of human N-glycoproteomes. (C) 2019 Elsevier B.V. All rights reserved.

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