PubMed:7538131 JSONTXT

{"target":"http://pubannotation.org/docs/sourcedb/PubMed/sourceid/7538131","sourcedb":"PubMed","sourceid":"7538131","text":"Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin.\nL-selectin, the leukocyte selectin, mediates the carbohydrate-dependent attachment of circulating leukocytes to endothelium, preceding emigration into tissues. It functions in inflammatory leukocyte trafficking and in lymphocyte homing to lymph nodes. From previous work, the binding of L-selectin to endothelial-associated glycoprotein ligands, GlyCAM-1 and CD34, requires oligosaccharide sialylation, sulfation, and probably fucosylation. We have recently identified a major capping group in GlyCAM-1 as 6' sulfated sialyl Lewis x, a novel structure which potentially satisfies all of these requirements. In the present study, we define the complete structure of beta-eliminated chains of GlyCAM-1 using metabolic radiolabeling, plant lectin binding, and glycosidase digestions in conjunction with high pH anion-exchange chromatography. The majority of the O-glycans in GlyCAM-1 contain the T-antigen, i.e. Gal beta 1--\u003e3GalNAc, which is incorporated into the core-2 structure, i.e. Gal beta 1--\u003e3[GlcNAc beta 1--\u003e6]GalNAc or larger core structures with additional GlcNAc residues. The structures of two O-glycans, based on core-2, were determined to be: [sequence: see text] The implications of these structures and more complex O-glycans for binding by L-selectin are 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