ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2026
Protein O-Glycosylation Shapes Lymphatic Endothelia and Lymph Node Macrophage Populations.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Endothelial cells were among the first cells identified to have a surface glycocalyx, but its functions are still elusive. Within the glycocalyx are many glycoproteins whose O-glycosylation is partly regulated by Cosmc, an essential chaperone for functional activity of T-synthase that adds galactose to O-glycans initiating their elongation. Using mice with inducible deletion of either Cosmc (C1Galt1C1) or the sialyltransferase St3Gal-1 in lymphatic endothelial cells (LEC), we discovered that loss of elongated O-glycans is accompanied by major changes in glycoprotein composition, including podoplanin, CD44, Lyve-1, and ICAM-1. These changes in the endothelial glycocalyx are sensed by adhesion molecules, such as Siglec-1, and lead to major changes in the size and phenotype of lymph node macrophage populations. Our findings demonstrate the crucial roles of O-glycosylation in regulating LEC functions and lymph node macrophage differentiation.
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