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Glycosylation in immune cell trafficking
Author(s) -
Sperandio Markus,
Gleissner Christian A.,
Ley Klaus
Publication year - 2009
Publication title -
immunological reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.839
H-Index - 223
eISSN - 1600-065X
pISSN - 0105-2896
DOI - 10.1111/j.1600-065x.2009.00795.x
Subject(s) - selectin , glycan , leukocyte trafficking , biology , microbiology and biotechnology , inflammation , immune system , glycosylation , cell adhesion , galectin , leukocyte extravasation , chemokine , siglec , immunology , integrin , glycobiology , cell adhesion molecule , glycome , cell , glycoprotein , biochemistry
Summary: Leukocyte recruitment encompasses cell adhesion and activation steps that enable circulating leukocytes to roll, arrest, and firmly adhere on the endothelial surface before they extravasate into distinct tissue locations. This complex sequence of events relies on adhesive interactions between surface structures on leukocytes and endothelial cells and also on signals generated during the cell–cell contacts. Cell surface glycans play a crucial role in leukocyte recruitment. Several glycosyltransferases such as α1,3 fucosyltransferases, α2,3 sialyltransferases, core 2 N ‐acetylglucosaminlytransferases, β1,4 galactosyltransferases, and polypeptide N ‐acetylgalactosaminyltransferases have been implicated in the generation of functional selectin ligands that mediate leukocyte rolling via binding to selectins. Recent evidence also suggests a role of α2,3 sialylated carbohydrate determinants in triggering chemokine‐mediated leukocyte arrest and influencing β 1 integrin function. The recent discovery of galectin‐ and siglec‐dependent processes further emphasizes the significant role of glycans for the successful recruitment of leukocytes into tissues. Advancing the knowledge on glycan function into appropriate pathology models is likely to suggest interesting new therapeutic strategies in the treatment of immune‐ and inflammation‐mediated diseases.