Galectin-9 as a Potential Modulator of Lymphocyte Adhesion to Endothelium via Binding to Blood Group H Glycan

The recruitment of leukocytes from blood is one the most important cellular processes in response to tissue damage and inflammation. This multi-step process includes rolling their adhesion endothelial cells (EC), culminating crossing EC barrier reach inflamed tissue. Galectin-8 galectin-9 expressed on immune system are part this can induce cell via binding oligolactosamine glycans. Similarly, these galectins have an order magnitude higher affinity towards glycans ABH group system, widely represented ECs. However, roles gal-8 gal-9 as mediators antigens practically unknown. In work, we investigated whether H antigen–gal-9-mediated occurred between Jurkat (of lymphocytic origin known gal-9) EA.hy 926 (immortalized antigen). Baseline experiments showed that adhered cells; however when were defucosylated (despite unmasking lactosamine chains), adherence was abolished. Restoration fucosylation by insertion synthetic glycolipids form (type 2) trisaccharide Fucα1-2Galβ1-4GlcNAc restored adhesion. degree lymphocyte native “H-restored” (glycolipid-loaded) comparable. If gal-9/H interaction similar occur vivo, suggests only short (trisaccharide) glycan ECs required.