title: Key regulators of galectin-glycan interactions.
abstract: 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.
authors: Center for Transfusion Medicine and Cellular Therapies, Department of Laboratory Medicine and Pathology, Emory University School of Medicine, Atlanta, GA, USA.
authors: Nourine A
authors: NA
authors: Kamili
authors: Center for Transfusion Medicine and Cellular Therapies, Department of Laboratory Medicine and Pathology, Emory University School of Medicine, Atlanta, GA, USA.
authors: Connie M
authors: CM
authors: Arthur
authors: Center for Transfusion Medicine and Cellular Therapies, Department of Laboratory Medicine and Pathology, Emory University School of Medicine, Atlanta, GA, USA.
authors: Christian
authors: C
authors: Gerner-Smidt
authors: Center for Transfusion Medicine and Cellular Therapies, Department of Laboratory Medicine and Pathology, Emory University School of Medicine, Atlanta, GA, USA.
authors: Eden
authors: E
authors: Tafesse
authors: Center for Transfusion Medicine and Cellular Therapies, Department of Laboratory Medicine and Pathology, Emory University School of Medicine, Atlanta, GA, USA.|Department of Biology, Erskine College, Due West, SC, USA.
authors: Anna
authors: A
authors: Blenda
authors: Department of Clinical Analyses, Toxicology and Food Sciences, Faculty of Pharmaceutical Sciences of Ribeirao Preto, University of Sao Paulo, Ribeirao Preto, Brazil.
authors: Marcelo
authors: M
authors: Dias-Baruffi
authors: Center for Transfusion Medicine and Cellular Therapies, Department of Laboratory Medicine and Pathology, Emory University School of Medicine, Atlanta, GA, USA.|Department of Clinical Analyses, Toxicology and Food Sciences, Faculty of Pharmaceutical Sciences of Ribeirao Preto, University of Sao Paulo, Ribeirao Preto, Brazil.
authors: Sean R
authors: SR
authors: Stowell
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001789:Blood Group Antigens / Q000737:chemistry / Q000378:metabolism; D002240:Carbohydrate Sequence; D002846:Chromatography, Affinity; D037161:Galectins / Q000737:chemistry / Q000378:metabolism*; D006017:Glycolipids / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008024:Ligands; D062105:Molecular Docking Simulation; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011499:Protein Processing, Post-Translational
chemical_list: D001789:Blood Group Antigens; D037161:Galectins; D006017:Glycolipids; D008024:Ligands; D011134:Polysaccharides
keywords: Frontal Affinity Chromatography; Galectin; Glycan; Glycan Binding Protein; Glycoproteomics; Surface Plasmon Resonance