Sulphation requirement for GlyCAM-1, an endothelial ligand for L-selectin.
L-selectin participates in the initial attachment of leukocytes to the vascular endothelium. On lymphocytes, it mediates binding to high endothelial venules of lymph nodes. As a selectin it functions as a calcium-dependent lectin recognizing carbohydrate-bearing ligands on endothelial cells. Two lymph node ligands for L-selectin have been identified as sulphated glycoproteins of M(r) approximately 50K and approximately 90K, called Sgp50 and Sgp90 (ref. 10). The recently cloned Sgp50 (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 activity and a role for fucosylation is suspected. We have used chlorate as a metabolic inhibitor of sulphation, and report here that GlyCAM-1 has an additional requirement for sulphate.
Imai
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Y
Department of Anatomy, University of California, San Francisco 94143-0452.
Lasky
L A
LA
Rosen
S D
SD
D000818:Animals; D002448:Cell Adhesion; D015815:Cell Adhesion Molecules; D004727:Endothelium / Q000378:metabolism; D019041:L-Selectin; D008198:Lymph Nodes / Q000737:chemistry; D008562:Membrane Glycoproteins; D051379:Mice; D009077:Mucins / Q000378:metabolism*; D009924:Organ Culture Techniques; D013431:Sulfates / Q000378:metabolism*; D013912:Threonine / Q000378:metabolism
D015815:Cell Adhesion Molecules; D008562:Membrane Glycoproteins; D009077:Mucins; D013431:Sulfates; D019041:L-Selectin; C075185:sulfated glycoprotein p50; D013912:Threonine