Structural characterisation of neutrophil glycans by ultra sensitive mass spectrometric glycomics methodology.
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.
Babu
Ponnusamy
P
Division of Molecular Biosciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, UK.
North
Simon J
SJ
Jang-Lee
Jihye
J
Chalabi
Sara
S
Mackerness
Kathryn
K
Stowell
Sean R
SR
Cummings
Richard D
RD
Rankin
Sara
S
Dell
Anne
A
Haslam
Stuart M
SM
D002240:Carbohydrate Sequence; D054794:Glycomics / Q000379:methods*; D006801:Humans; D008745:Methylation; D008969:Molecular Sequence Data; D009439:Neuraminidase / Q000378:metabolism; D009504:Neutrophils / Q000737:chemistry*; D011134:Polysaccharides / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*
D011134:Polysaccharides; D009439:Neuraminidase