Journal
JOURNAL OF PROTEOME RESEARCH
Volume 13, Issue 3, Pages 1713-1721Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr401200h
Keywords
N-glycosylation sites; N-glycoproteins; HILIC; hydrazide chemistry; human liver
Categories
Funding
- China State Key Basic Research Program [2013CB-911202, 2012CB910101]
- NSFC [21321064, 81161120540, 21235006]
- National Key Special Program on Infection diseases [2012ZX10002009-011]
- Analytical Method Innovation Program of MOST [2012IM030900]
- Hundred Talent Young Scientist Program by DICP
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Although glycoproteomics is greatly developed in recent years, our knowledge about N-glycoproteome of human tissues is still very limited. In this study, we comprehensively mapped the N-glycosylation sites of human liver by combining click maltose-hydrophilic interaction chromatography (HILIC) and the improved hydrazide chemistry. The specificity could be as high as 90% for hydrazide chemistry and 80% for HILIC. Altogether, we identified 14 480 N-glycopeptides matched with N-!P-[SITIC] sequence motif from human liver, corresponding to 2210 N-glycoproteins and 4783 N-glycosylation sites. These N-glycoproteins are widely involved into different types of biological processes, such as hepatic stellate cell activation and acute phase response of human liver, which all highly associate with the progression of liver diseases. Moreover, the exact N-glycosylation sites of some key-regulating proteins within different human liver physiological processes were also obtained, such as E-cadherin, transforming growth factor beta receptor and 29 members of G protein coupled receptors family.
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