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Galectin-3 type-C self-association on neutrophil surfaces; The carbohydrate recognition domain regulates cell function

Journal article
Authors Martina Sundqvist
Amanda Welin
Jonas Elmwall
Veronica Osla
U. J. Nilsson
H. Leffler
Johan Bylund
Anna Karlsson
Published in Journal of Leukocyte Biology
Volume 103
Issue 2
Pages 341-353
ISSN 0741-5400
Publication year 2018
Published at Institute of Odontology
Institute of Medicine, Department of Rheumatology and Inflammation Research
Pages 341-353
Language en
Keywords carbohydrate recognition domain, galectin, neutrophils, priming, ROS production, calcium, fluorescein isothiocyanate, galectin 3, galectin 3c, matrix metalloproteinase, proteinase, reactive oxygen metabolite, recombinant galectin 3, recombinant galectin 3c, recombinant protein, reduced nicotinamide adenine dinucleotide phosphate oxidase, serine proteinase, unclassified drug, amino terminal sequence, Article, binding affinity, calcium cell level, calcium signaling, carboxy terminal sequence, cell interaction, cell surface, cellular distribution, circulation, competitive inhibition, controlled study, enzyme activation, ex vivo study, flow cytometry, fluorescence, human, human cell, leukocyte activation, leukocyte adherence, leukocyte function, neutrophil, nonhuman, normal human, oxidative stress, priority journal, protein assembly, protein binding, protein cleavage, protein degradation, protein protein interaction, protein structure
Subject categories Microbiology in the medical area, Rheumatology and Autoimmunity


Galectin-3 is an endogenous β-galactoside-binding lectin comprising a carbohydrate recognition domain (CRD) linked to a collagen-like N-domain. Both domains are required for galectin-3 to induce cellular effects; a C-terminal fragment of galectin-3, galectin-3C, containing the CRD but lacking the N-domain, binds cell surface glycoconjugates but does not induce cellular effects since cross-linking promoted by the N-domain is thought to be required. Instead, galectin-3C is proposed to antagonize the effects of galectin-3 by competing for binding sites. The aim of this study was to investigate the effects of galectin-3C on galectin-3 interactions with human neutrophils. Recombinant galectin-3C inhibited galectin-3-induced production of reactive oxygen species in primed neutrophils. Surprisingly, this inhibition was not due to competitive inhibition of galectin-3 binding to the cells. In contrast, galectin-3C potentiated galectin-3 binding, in line with emerging evidence that galectin-3 can aggregate not only through the N-domain but also through the CRD. The cell surface interaction between galectin-3C and galectin-3 was corroborated by colocalization of fluorescently labeled galectin-3 and galectin-3C. Galectin-3C can be generated in vivo through cleavage of galectin-3 by proteases. Indeed, in circulation, galectin-3 and galectin-3C were both attached to the cell surface of neutrophils, which displayed great capacity to bind additional galectin-3 and galectin-3C. In conclusion, galectin-3C enhances galectin-3 binding to neutrophils by nonactivating type-C self-association, in parallel to inhibiting neutrophil activation by galectin-3 (induced by type-N self-association). This implicates type-C self-association as a termination system for galectin-3-induced cell activation, with the purpose of avoiding oxidant-dependent tissue damage. ©2018 Society for Leukocyte Biology

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