Tissue-specific glycosylation at the glycopeptide level

Medzihradszky F., Katalin and Kaasik, K. and Chalkley, RJ. (2015) Tissue-specific glycosylation at the glycopeptide level. MOLECULAR & CELLULAR PROTEOMICS, 14 (8). pp. 2103-2110. ISSN 1535-9476

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Abstract

This manuscript describes the enrichment and mass spectrometric analysis of intact glycopeptides from mouse liver, which yielded site-specific N- and O-glycosylation data for ∼130 proteins. Incorporation of different sialic acid variants in both N- and O-linked glycans was observed, and the importance of using both collisional activation and electron transfer dissociation for glycopeptide analysis was illustrated. The N-glycan structures of predicted lysosomal, endoplasmic reticulum (ER), secreted and transmembrane proteins were compared. The data suggest that protein N-glycosylation differs depending on cellular location. The glycosylation patterns of several mouse liver and mouse brain glycopeptides were compared. Tissue-specific differences in glycosylation were observed between sites within the same protein: Some sites displayed a similar spectrum of glycan structures in both tissues, whereas for others no overlap was observed. We present comparative brain/liver glycosylation data on 50 N-glycosylation sites from 34 proteins and 13 O-glycosylation sites from seven proteins. © 2015 by The American Society for Biochemistry and Molecular Biology, Inc.

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