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Galectins and Immune Responses—Just How Do They Do Those Things They Do?

Galectins and Immune Responses—Just How Do They Do Those Things They Do? Galectins are a family of mammalian carbohydrate-binding proteins expressed by many cell types. Galectins can function intracellularly and can also be secreted to bind to cell surface glycoconjugate counterreceptors. Some galectins are made by immune cells, whereas other galectins are secreted by different cell types, such as endothelial or epithelial cells, and bind to immune cells to regulate immune responses. Galectin binding to a single glycan ligand is a low-affinity interaction, but the multivalency of galectins and the glycan ligands presented on cell surface glycoproteins results in high-avidity binding that can reversibly scaffold or cluster these glycoproteins. Galectin binding to a specific glycoprotein counterreceptor is regulated in part by the repertoire of glycosyltransferase enzymes (which make the glycan ligands) expressed by that cell, and the effect of galectin binding results from clustering or retention of specific glycoprotein counterreceptors bearing these specific ligands. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annual Review of Immunology Annual Reviews

Galectins and Immune Responses—Just How Do They Do Those Things They Do?

Galectins and Immune Responses—Just How Do They Do Those Things They Do?


Galectins are a family of mammalian carbohydrate-binding proteins expressed by many cell types. Galectins can function intracellularly and can also be secreted to bind to cell surface glycoconjugate counterreceptors. Some galectins are made by immune cells, whereas other galectins are secreted by different cell types, such as endothelial or epithelial cells, and bind to immune cells to regulate immune responses. Galectin binding to a single glycan ligand is a low-affinity interaction, but the multivalency of galectins and the glycan ligands presented on cell surface glycoproteins results in high-avidity binding that can reversibly scaffold or cluster these glycoproteins. Galectin binding to a specific glycoprotein counterreceptor is regulated in part by the repertoire of glycosyltransferase enzymes (which make the glycan ligands) expressed by that cell, and the effect of galectin binding results from clustering or retention of specific glycoprotein counterreceptors bearing these specific ligands. INTRODUCTION As a biologist, you work with galectins every day. You may not actively think about it, but galectins are involved in virtually every process in the immune system, from holding pre-B cells in a developmental niche in the bone marrow stroma (1) to regulating the strength of T cell receptor (TCR) signaling during thymocyte selection (2) to promoting or retarding the migration of neutrophils, monocytes, and dendritic cells across endothelium and through the extracellular matrix (3, 4) to controlling cytokine secretion and cytokine receptor signaling (5, 6) to enhancing or blocking pathogen recognition and host cell attachment (7) to activating or inhibiting T and B cell death (8–10). All of these functions, for all of these cell types, in all kinds of environments—how can a family of 15 carbohydrate-binding proteins do all of this? Other lectins important for immune...
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Publisher
Annual Reviews
Copyright
Copyright © 2016 by Annual Reviews. All rights reserved
ISSN
0732-0582
eISSN
1545-3278
DOI
10.1146/annurev-immunol-041015-055402
pmid
26907217
Publisher site
See Article on Publisher Site

Abstract

Galectins are a family of mammalian carbohydrate-binding proteins expressed by many cell types. Galectins can function intracellularly and can also be secreted to bind to cell surface glycoconjugate counterreceptors. Some galectins are made by immune cells, whereas other galectins are secreted by different cell types, such as endothelial or epithelial cells, and bind to immune cells to regulate immune responses. Galectin binding to a single glycan ligand is a low-affinity interaction, but the multivalency of galectins and the glycan ligands presented on cell surface glycoproteins results in high-avidity binding that can reversibly scaffold or cluster these glycoproteins. Galectin binding to a specific glycoprotein counterreceptor is regulated in part by the repertoire of glycosyltransferase enzymes (which make the glycan ligands) expressed by that cell, and the effect of galectin binding results from clustering or retention of specific glycoprotein counterreceptors bearing these specific ligands.

Journal

Annual Review of ImmunologyAnnual Reviews

Published: May 20, 2016

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