Abstract：
:P-selectin binding to neutrophils requires a specific protein, P-selectin glycoprotein ligand 1 (PSGL-1), as well as sialyl-Lewis X (sLex) glycan determinants. We have found that a short segment near the amino terminus of PSGL-1 that contains a tyrosine sulfation consensus is essential for P-selectin adhesion and that addition of the amino-terminal segment to some but not all mucin-like molecules confers on those molecules the ability to bind P-selectin. PSGL-1 synthesized in the presence of sulfation inhibitors binds P-selectin weakly, and within the amino-terminal 20 residues, mutation of the tyrosines to phenylalanine abolishes binding. Rolling of HL-60 cells on P-selectin-coated coverslips is strongly attenuated by treatment of cells with an inhibitor of sulfation.
journal_name
Celljournal_title
Cellauthors
Pouyani T,Seed Bdoi
10.1016/0092-8674(95)90174-4subject
Has Abstractpub_date
1995-10-20 00:00:00pages
333-43issue
2eissn
0092-8674issn
1097-4172pii
0092-8674(95)90174-4journal_volume
83pub_type
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