NDLI: Site-specific characterization of N-linked glycosylation in human urinary glycoproteins and endogenous glycopeptides

Content Provider	Springer Nature Link
Author	Kawahara, Rebeca Saad, Joyce Angeli, Claudia Blanes Palmisa, Giuseppe
Copyright Year	2016
Abstract	Glycosylation is a very important post-translational modification involved in various cellular processes, such as cell adhesion, signal transduction and immune response. Urine is a rich source of glycoproteins and attractive biological fluid for biomarker discovery, owing to its availability, ease of collection, and correlation with pathophysiology of diseases. Although the urinary proteomics have been explored previously, the urinary glycoproteome characterization remains challenging requiring the development and optimization of analytical and bioinformatics methods for protein glycoprofiling. This study describes the high confident identification of 472 unique N-glycosylation sites covering 256 urinary glycoproteins. Besides, 202 unique N-glycosylation sites were identified in low molecular weight endogenous glycopeptides, which belong to 90 glycoproteins. Global site-specific characterization of the N-linked glycan heterogeneity was achieved by intact glycopeptide analysis, revealing 303 unique glycopeptides most of them displaying complex/hybrid glycans composed by sialic acid and fucose. These datasets consist in a valuable resource of glycoproteins and N-glycosylation sites found in healthy human urine that can be further explored in different disorders, in which the N-linked glycosylation may be aberrant.
Starting Page	937
Ending Page	951
Page Count	15
File Format	PDF
ISSN	02820080
Journal	Glycoconjugate Journal
Volume Number	33
Issue Number	6
e-ISSN	15734986
Language	English
Publisher	Springer US
Publisher Date	2016-05-27
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	N-glycosylation Glycopeptides Urine Glycoforms Biochemistry Pathology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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