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MS strategies for high throughput glycomics and glyco‐proteomics
Author(s) -
Dell Anne,
SuttonSmith Mark,
Panico Maria,
Chalabi Sara,
Wong NyetKui,
Hitchen Paul,
JangLee Jihye,
North Simon,
Ledger Victoria,
Parry Simon,
Haslam Stuart,
Morris Howard
Publication year - 2004
Publication title -
international journal of experimental pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.671
H-Index - 72
eISSN - 1365-2613
pISSN - 0959-9673
DOI - 10.1111/j.0959-9673.2004.0390e.x
Subject(s) - glycomics , glycobiology , glycome , glycosylation , glycan , proteomics , glycoprotein , biology , computational biology , glycoproteomics , biochemistry , microbiology and biotechnology , gene
Ultra‐high sensitivity mass spectrometric strategies for defining the primary structures of highly complex mixtures of glycopolymers are revolutionizing structural glycobiology in the postgenomic era. MS strategies incorporating MALDI‐MS and ES‐MS/MS enable very complex mixtures from biological extracts and/or glycopolymer digests to be screened, thereby revealing the types of glycans present and, importantly, providing clues to structures that are likely to be functionally important. This lecture will overview strategies employed in our laboratory which enable the glycome of cells, tissues and organs to be examined and the glycoforms of individual glycoproteins to be identified. The types of structural problems that can be solved with current technology will be exemplified by some of our recent research in the following areas:• Development and application of glycomics screening strategies for examining glycosylation changes in cells and tissues of knockout mice. • Defining changes in glycosylation of murine T and B cells upon cytokine activation. • Characterization of the ovarian cancer antigen, CA125. • Sequencing and site analysis of N ‐ and O ‐glycans in murine ZP3, the putative sperm receptor. • Characterization of mucin glycosylation in cystic fibrosis‐related research. • Glyco‐proteomic investigations of changes in O ‐glycosylation of CD8 during T‐cell development. • Glyco‐proteomic analyses of novel glycosylation of bacterial proteins.