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Structural characterisation of neutrophil glycans by ultra sensitive mass spectrometric glycomics methodology.

Authors
  • Babu, Ponnusamy1
  • North, Simon J
  • Jang-Lee, Jihye
  • Chalabi, Sara
  • Mackerness, Kathryn
  • Stowell, Sean R
  • Cummings, Richard D
  • Rankin, Sara
  • Dell, Anne
  • Haslam, Stuart M
  • 1 Division of Molecular Biosciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, UK.
Type
Published Article
Journal
Glycoconjugate Journal
Publisher
Springer-Verlag
Publication Date
November 2009
Volume
26
Issue
8
Pages
975–986
Identifiers
DOI: 10.1007/s10719-008-9146-4
PMID: 18587645
Source
Medline
License
Unknown

Abstract

Neutrophils are the most abundant white blood cells in humans and play a vital role in several aspects of the immune response. Numerous reports have implicated neutrophil glycosylation as an important factor in mediating these interactions. We report here the application of high sensitivity glycomics methodologies, including matrix assisted laser desorption ionisation (MALDI-TOF) and MALDI-TOF/TOF analyses, to the structural analysis of N- and O-linked carbohydrates released from two samples of neutrophils, prepared by two separate and geographically remote laboratories. The data produced demonstrates that the cells display a diverse range of sialylated and fucosylated complex glycans, with a high level of similarity between the two preparations.

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