C-Type Lectins

Richard D. Cummings; Rodger P. McEver

doi:10.1101/glycobiology.3e.034

C-Type Lectins

Review

In: Essentials of Glycobiology [Internet]. 3rd edition. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2015. Chapter 34.

2017.

Authors

Richard D. Cummings, Rodger P. McEver

Book Editors

Book Affiliations

¹ Distinguished Professor of Medicine and Cellular & Molecular Medicine, Co-Director, Glycobiology Research and Training Center, University of California, San Diego, La Jolla, California, USA
² Professor of Surgery, Director, National Center for Functional Glycomics, Harvard Medical School, Cambridge, Massachusetts, USA
³ Distinguished Professor of Cellular & Molecular Medicine, Co-Director, Glycobiology Research and Training Center, University of California, San Diego, La Jolla, California, USA
⁴ Horace W. Goldsmith Foundation Chair and Professor of Cell Biology, Albert Einstein College of Medicine, New York, New York, USA
⁵ Professor and Chairman of Biological Chemistry, Johns Hopkins University, Baltimore, Maryland, USA
⁶ Professor of Mycology, ETH Zürich, Zürich, Switzerland
⁷ Regents Professor and Director, Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia, USA
⁸ Professor, Laboratory of Immunoglycobiology, WPI Immunology Frontier Research Center, Osaka University, Osaka, Japan
⁹ Professor of Glycoproteomics and Glycomics, Macquarie University and Institute for Glycomics, Griffith University, Sydney, Australia
¹⁰ Professor and Eminent Scholar, University of Georgia, Athens, Georgia, USA
¹¹ Professor, Departments of Pharmacology and Neuroscience, Johns Hopkins University, Baltimore, Maryland, USA
¹² Director, Max-Planck-Institute of Colloids and Interfaces, Potsdam, Germany

Excerpt

C-type lectins (CTLs) are Ca⁺⁺-dependent glycan-binding proteins (GBPs) that share primary and secondary structural homology in their carbohydrate-recognition domains (CRDs). The CRD of CTLs is more generally defined as the CTL domain (CTLD), because not all proteins with this domain bind either glycans or Ca⁺⁺. CTLs include collectins, selectins, endocytic receptors, and proteoglycans, some of which are secreted and others are transmembrane proteins. They often oligomerize, which increases their avidity for multivalent ligands. CTLs differ significantly in the types of glycans that they recognize with high affinity. These proteins function as adhesion and signaling receptors in many pathways, including homeostasis and innate immunity, and are crucial in inflammatory responses and leukocyte and platelet trafficking.

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