Journal
GLYCOCONJUGATE JOURNAL
Volume 26, Issue 8, Pages 975-986Publisher
SPRINGER
DOI: 10.1007/s10719-008-9146-4
Keywords
Mass spectrometry; Neutrophil; Glycomics; Protein glycosylation
Categories
Funding
- National Institutes of Health (NIH) [RO1AI48075]
- European Community Innovative Chemokine-based Therapeutic Strategies for Autoimmunity and Chronic Inflammation (INNOCHEM)
- Wellcome Trust
- British Heart Foundation
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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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