101. Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin
- Author
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Rodger P. McEver, Patricia P. Wilkins, Kevin L. Moore, and Richard D. Cummings
- Subjects
Tyrosine sulfation ,Tyrosylprotein sulfotransferase ,Glycan ,HL-60 Cells ,Biochemistry ,Humans ,Tyrosine ,Molecular Biology ,Fucosylation ,Arylsulfatases ,chemistry.chemical_classification ,Membrane Glycoproteins ,integumentary system ,biology ,Chemistry ,Sulfates ,Cell Biology ,Ligand (biochemistry) ,Kinetics ,P-Selectin ,biology.protein ,Autoradiography ,P-selectin glycoprotein ligand-1 ,Electrophoresis, Polyacrylamide Gel ,Glycoprotein ,Protein Processing, Post-Translational - Abstract
P-selectin glycoprotein ligand-1 (PSGL-1) is a mucin-like glycoprotein on leukocytes that is a high affinity ligand for P-selectin. Previous studies have shown that sialylation and fucosylation of PSGL-1 are required for its binding to P-selectin, but other post-translational modifications of PSGL-1 may also be important. We demonstrate that PSGL-1 synthesized in human HL-60 cells can be metabolically labeled with [35S]sulfate that is incorporated primarily into tyrosine sulfate. Treatment of PSGL-1 with a bacterial arylsulfatase releases sulfate from tyrosine, resulting in a concordant decrease in binding to P-selectin. These studies demonstrate that tyrosine sulfate on PSGL-1 functions in conjunction with sialylated and fucosylated glycans to mediate high affinity binding to P-selectin.
- Published
- 1995