Document Detail


Glycomic analysis of human mast cells, eosinophils and basophils.
MedLine Citation:
PMID:  21725073     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In allergic diseases such as asthma, eosinophils, basophils and mast cells, through release of preformed and newly generated mediators, granule proteins and cytokines, are recognized as key effector cells. While their surface protein phenotypes, mediator release profiles, ontogeny, cell trafficking and genomes have been generally explored and compared, there has yet to be any thorough analysis and comparison of their glycomes. Such studies are critical to understand the contribution of carbohydrates to the induction and regulation of allergic inflammatory responses and are now possible using improved technologies for detecting and characterizing cell-derived glycans. We thus report here the application of high-sensitivity mass spectrometric-based glycomics methodologies to the analysis of N-linked glycans derived from isolated populations of human mast cells, eosinophils and basophils. The samples were subjected to matrix-assisted laser desorption ionization (MALDI) time-of-flight (TOF) screening analyses and MALDI-TOF/TOF sequencing studies. Results reveal substantive quantities of terminal N-acetylglucosamine containing structures in both the eosinophil and the basophil samples, whereas mast cells display greater relative quantities of sialylated terminal epitopes. For the first time, we characterize the cell surface glycan structures of principal allergic effector cells, which by interaction with glycan-binding proteins (e.g. lectins) have the possibility to dictate cellular functions, and might thus have important implications for the pathogenesis of inflammatory and allergic diseases.
Authors:
Simon J North; Stephan von Gunten; Aristotelis Antonopoulos; Alana Trollope; Donald W MacGlashan; Jihye Jang-Lee; Anne Dell; Dean D Metcalfe; Arnold S Kirshenbaum; Bruce S Bochner; Stuart M Haslam
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, N.I.H., Intramural; Research Support, Non-U.S. Gov't     Date:  2011-07-01
Journal Detail:
Title:  Glycobiology     Volume:  22     ISSN:  1460-2423     ISO Abbreviation:  Glycobiology     Publication Date:  2012 Jan 
Date Detail:
Created Date:  2011-12-06     Completed Date:  2012-03-28     Revised Date:  2013-06-28    
Medline Journal Info:
Nlm Unique ID:  9104124     Medline TA:  Glycobiology     Country:  England    
Other Details:
Languages:  eng     Pagination:  12-22     Citation Subset:  IM    
Affiliation:
Division of Molecular Biosciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, UK.
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MeSH Terms
Descriptor/Qualifier:
Basophils / metabolism*
Carbohydrate Conformation
Carbohydrate Sequence
Cells, Cultured
Eosinophils / metabolism*
Glycomics
Humans
Mast Cells / metabolism*
Molecular Sequence Data
N-Acetylneuraminic Acid / metabolism
Polysaccharides / metabolism*
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Grant Support
ID/Acronym/Agency:
AI 72265/AI/NIAID NIH HHS; GM 62116/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Polysaccharides; 131-48-6/N-Acetylneuraminic Acid
Comments/Corrections

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