Abstract
L-SELECTIN participates in the initial attachment of leukocytes to the vascular endothelium1–3. On lymphocytes, it mediates binding to high endothelial venules of lymph nodes. As a selectin4–6 it functions as a calcium-dependent lectin7,8 recognizing carbohydrate-bearing ligands on endothelial cells9–11. Two lymph node ligands for L-selectin have been identified as sulphated glycoproteins of Mr∼50K and ∼90K, called SgpSO and Sgp90 (ref. 10). The recently cloned SgpSO (ref. 12), now designated GlyCAM-1, is a high endothelial venule-associated, mucin-like glycoprotein containing predominantly O-linked carbohydrate chains. Sialylation of GlyCAM-1 is necessary for its ligand activity9,10,13 and a role for fucosylation is suspected13. We have used chlorate as a metabolic inhibitor of sulphation, and report here that GlyCAM-1 has an additional requirement for sulphate.
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lmai, Y., Lasky, L. & Rosen, S. Sulphation requirement for GlyCAM-1, an endothelial ligand for L-selectin. Nature 361, 555–557 (1993). https://doi.org/10.1038/361555a0
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DOI: https://doi.org/10.1038/361555a0
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