Professor
Supervisor of Doctorate Candidates
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DOI number:10.1016/j.trac.2019.02.009
Key Words:Glycosylation; glycoprotein; glycoproteome; glycosylation site; human body fluids; human cell lines; human tissues; mass spectrometry.
Abstract: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 7,000 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.
Indexed by:Journal paper
Discipline:Natural Science
First-Level Discipline:Biology
Document Type:J
Translation or Not:no
Date of Publication:2019-02-13
Included Journals:SCI
Pre One:40. Liuyi Dang, Li Jia, Yuan Zhi, Pengfei Li, Ting Zhao, Bojing Zhu, Rongxia Lan, Yingwei Hu, Hui Zhang, Shisheng Sun*. Mapping human N-linked glycoproteins and glycosylation sites using mass spectrometry. Trends in Analytical Chemistry. 2019. 114: 143-150.
Next One:38. Jian Shu, Liuyi Dang, Dandan Zhang, Punit Shah, Lijun Chen, Hui Zhang, Shisheng Sun*. Dynamic analysis of proteomic alterations in response to N‐linked glycosylation inhibition in a drug‐resistant ovarian carcinoma cell line. The FEBS journal. 286, 8: 1594-1605.
