Glycosylation in immune cell trafficking.
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TLDR
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.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.read more
Citations
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Emerging Principles for the Therapeutic Exploitation of Glycosylation
TL;DR: The current knowledge of glycans in pathogen invasion, cancer, autoimmunity, and congenital diseases is reviewed and glycan engineering will continue to deliver enhanced therapeutic glycoproteins, such as antibodies, with enhanced disease modifying properties.
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Selectins promote tumor metastasis
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Global metabolic inhibitors of sialyl- and fucosyltransferases remodel the glycome
Cory D. Rillahan,Aristotelis Antonopoulos,Craig T. Lefort,Roberto Sonon,Parastoo Azadi,Klaus Ley,Anne Dell,Stuart M. Haslam,James C. Paulson +8 more
TL;DR: It is shown that fluorinated analogs of sialic acid and fucose can be taken up and metabolized to the desired donor substrate-based inhibitors inside the cell, resulting in a global, family-wide shutdown of sIALyl- and/or fucosyltransferases and remodeling of cell-surface glycans.
References
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