title: Tissue-Specific Glycosylation at the Glycopeptide Level.
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.
authors.affiliation: From the ‡Department of Pharmaceutical Chemistry, School of Pharmacy, University of California San Francisco, 600 16th Street Genentech Hall, N474A, Box 2240, San Francisco, California 94158-2517 folkl@cgl.ucsf.edu.
authors.forename: Katalin F
authors.initials: KF
authors.lastname: Medzihradszky
authors.affiliation: From the ‡Department of Pharmaceutical Chemistry, School of Pharmacy, University of California San Francisco, 600 16th Street Genentech Hall, N474A, Box 2240, San Francisco, California 94158-2517.
authors.forename: Krista
authors.initials: K
authors.lastname: Kaasik
authors.affiliation: From the ‡Department of Pharmaceutical Chemistry, School of Pharmacy, University of California San Francisco, 600 16th Street Genentech Hall, N474A, Box 2240, San Francisco, California 94158-2517.
authors.forename: Robert J
authors.initials: RJ
authors.lastname: Chalkley
mesh_terms: D000818:Animals; D001921:Brain / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism; D006020:Glycopeptides / Q000737:chemistry / Q000378:metabolism*; D006031:Glycosylation; D008099:Liver / Q000378:metabolism; D008247:Lysosomes / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D051379:Mice; D009928:Organ Specificity
chemical_list: D006020:Glycopeptides; D008565:Membrane Proteins