Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin.

@article{Wilkins1995TyrosineSO,
  title={Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin.},
  author={Patricia P. Wilkins and Kevin Lawrence Moore and Rodger P McEver and Richard D. Cummings},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 39},
  pages={22677-80}
}
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… CONTINUE READING
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