Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 479, Issue 1, Pages 86-90Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2016.09.038
Keywords
Galectin-3; IgG1 immune complexes; Fc Fc gamma RIIB-Dectin-1 receptor complex; Neutrophil chemotaxis
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Funding
- Federal Ministry of Education and Research (BMBF), Germany [FZK 03Z2JN22]
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Changes in the glycosylation of immunoglobulins have been shown to modulate immune homeostasis and disease pathology. In this sense it has been shown that highly galactosylated but not agalactosylated IgG1 immune complexes (ICs) inhibit C5aR-mediated pro-inflammatory immune responses via the assembly of Fc gamma RIIB-Dectin-1 receptor complexes. In this study we demonstrated that Galectin-3, a galactose-binding lectin that is known to cross-link proteins on cell-surfaces via binding their N-glycans, bound to highly-galactosylated, but not agalactosylated IgG1. Further, Galectin-3 was essential for the IC-mediated inhibition of C5a-induced neutrophil chemotaxis in vitro. Taken together our results indicate that Galectin-3 mediates the interaction of ICs with the FcyRIIB-Dectin-1 receptor complex for delivering immunoregulatory signals to inhibit C5aR-mediated immune responses. (C) 2016 Elsevier Inc. All rights reserved.
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