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Immunol Rev. 2009 Jul;230(1):97-113. doi: 10.1111/j.1600-065X.2009.00795.x.

Glycosylation in immune cell trafficking.

Author information

1
Walter Brendel Center of Experimental Medicine, Ludwig-Maximilians-Universit├Ąt, Munich, Germany. markus.sperandio@med.uni-muenchen.de

Abstract

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 alpha1,3 fucosyltransferases, alpha2,3 sialyltransferases, core 2 N-acetylglucosaminlytransferases, beta1,4 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 alpha2,3 sialylated carbohydrate determinants in triggering chemokine-mediated leukocyte arrest and influencing beta1 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.

PMID:
19594631
PMCID:
PMC2745114
DOI:
10.1111/j.1600-065X.2009.00795.x
[Indexed for MEDLINE]
Free PMC Article

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