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

Liuyi Dang, Li Jia, Yuan Zhi, Pengfei Li, Ting Zhao, Bojing Zhu, Rongxia Lan, Yingwei Hu, Hui Zhang, Shisheng Sun

Research output: Contribution to journalReview articlepeer-review

10 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)143-150
Number of pages8
JournalTrAC - Trends in Analytical Chemistry
StatePublished - May 2019


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

ASJC Scopus subject areas

  • Analytical Chemistry
  • Spectroscopy


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