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Updated: Mar 11, 2026

Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry
Published on: April 21, 2017
Mast cell glycosaminoglycans
B Mulloy1, R Lever2, C P Page3
1Sackler Institute of Pulmonary Pharmacology, Institute for Pharmaceutical Science, King's College London, Franklin-Wilkins Building, 150 Stamford St, London, SE1 9NN, UK. barbara.mulloy@kcl.ac.uk.
Abstract:
Mast cells contain granules packed with a mixture of proteins that are released on degranulation. The proteoglycan serglycin carries an array of glycosaminoglycan (GAG) side chains, sometimes heparin, sometimes chondroitin or dermatan sulphate. Tight packing of granule proteins is dependent on the presence of serglycin carrying these GAGs. The GAGs of mast cells were most intensively studied in the 1970s and 1980s, and though something is known about the fine structure of chondroitin sulphate and dermatan sulphate in mast cells, little is understood about the composition of the heparin/heparan sulphate chains. Recent emphasis on the analysis of mast cell heparin from different species and tissues, arising from the use of this GAG in medicine, lead to the question of whether variations within heparin structures between mast cell populations are as significant as variations in the mix of chondroitins and heparins.
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