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Different glycosphingolipid composition in human neutrophil subcellular compartments.

Journal article
Authors Anna Karlsson
Halina Miller-Podraza
P Johansson
Karl-Anders Karlsson
Claes Dahlgren
Susann Teneberg
Published in Glycoconjugate journal
Volume 18
Issue 3
Pages 231-43
ISSN 0282-0080
Publication year 2001
Published at Institute of Medical Biochemistry
Institute of Internal Medicine, Dept of Rheumatology and Inflammation Research
Pages 231-43
Language en
Keywords Antibodies, Monoclonal, metabolism, Bacterial Proteins, metabolism, Carbohydrate Sequence, Cell Fractionation, Cell Membrane, chemistry, Glycosphingolipids, analysis, chemistry, metabolism, Helicobacter pylori, metabolism, Humans, Intracellular Membranes, chemistry, Ionomycin, pharmacology, Ionophores, pharmacology, Lectins, metabolism, Mass Spectrometry, Molecular Sequence Data, Neutrophil Activation, Neutrophils, chemistry, drug effects, ultrastructure
Subject categories Immunology in the medical area, Cell and Molecular Biology


The binding of a number of carbohydrate-recognizing ligands to glycosphingolipids and polyglycosylceramides of human neutrophil subcellular fractions (plasma membranes/secretory vesicles of resting and ionomycin-stimulated cells, specific and azurophil granules) was examined using the chromatogram binding assay. Several organelle-related differences in glycosphingolipid content were observed. The most prominent difference was a decreased content of the GM3 ganglioside in plasma membranes of activated neutrophils. Gangliosides recognized by anti-VIM-2 antibodies were detected mainly in the acid fractions of azurophil and specific granules. Slow-migrating gangliosides and polyglycosylceramides with Helicobacter pylori-binding activity were found in all acid fractions. A non-acid triglycosylceramide, recognized by Gal(alpha)4Gal-binding Escherichia coli, was detected in the plasma membrane/secretory vesicles but not in the azurophil and specific granules. Although no defined roles of glycosphingolipids have yet been conclusively established with respect to neutrophil function, the fact that many of the identified glycosphingolipids are stored in granules, is in agreement with their role as receptor structures that are exposed on the neutrophil cell surface upon fusion of granules with the plasma membrane. Accordingly, we show that neutrophil granules store specific carbohydrate epitopes that are upregulated to the plasma membrane upon cell activation.

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