Key regulators of galectin–glycan interactions

• Type of Material: Article
• Authors: Nourine A. Kamili, Emory University; Connie M. Arthur, Emory University; Christian Gerner-Smidt, Emory University; Eden Tafesse, Emory University; Anna Blenda, Emory University; Marcelo Dias-Baruffi, University of Sao Paulo; Sean R. Stowell, Emory University
• Language: English
• Date: 2016-12-01
• Publisher: Wiley: 12 months
• Publication Version: Author Accepted Manuscript (After Peer Review)
• Copyright Statement: © 2016 WILEY-VCH Verlag GmbH & Co.
• Final Published Version (URL): http://dx.doi.org/10.1002/pmic.201600116
• Title of Journal or Parent Work: Proteomics
• ISSN: 1615-9853
• Volume: 16
• Issue: 24
• Start Page: 3111
• End Page: 3125
• Keywords: Glycan; BLOOD-GROUP ANTIGENS; Galectin; CARBOHYDRATE-RECOGNITION DOMAIN; T-CELL DEATH; Glycoproteomics; Glycan Binding Protein; RAY CRYSTAL-STRUCTURE; Biochemical Research Methods; Science & Technology; POLY-N-ACETYLLACTOSAMINE; AMINO-ACID-SEQUENCE; PROMOTES AXONAL REGENERATION; Life Sciences & Biomedicine; GALACTOSIDE-BINDING LECTIN; HAMSTER OVARY CELLS; Biochemistry & Molecular Biology; OXIDIZED GALECTIN-1; Frontal Affinity Chromatography; Surface Plasmon Resonance
• Research Categories: Health Sciences, Medicine and Surgery; Health Sciences, General

Abstract

KGaA, Weinheim Protein–ligand interactions serve as fundamental regulators of numerous biological processes. Among protein–ligand pairs, glycan binding proteins (GBPs) and the glycans they recognize represent unique and highly complex interactions implicated in a broad range of regulatory activities. With few exceptions, cell surface receptors and secreted proteins are heavily glycosylated. As these glycans often represent highly regulatable post-translational modifications, alterations in glycosylation can fundamentally impact GBP recognition. Among GBPs, galectins in particular appear to engage a diverse set of glycan determinants to impact a broad range of biological processes. In this review, we will explore factors that impact galectin activity, including the effect of glycan modification on galectin–glycan interactions.