The P-selectin glycoprotein ligand from human neutrophils displays sialylated, fucosylated, O-linked poly-N-acetyllactosamine.

@article{Moore1994ThePG,
  title={The P-selectin glycoprotein ligand from human neutrophils displays sialylated, fucosylated, O-linked poly-N-acetyllactosamine.},
  author={Kevin Lawrence Moore and Scott F. Eaton and Derek Eugen Lyons and Henri S. Lichenstein and Richard D. Cummings and Rodger P McEver},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 37},
  pages={
          23318-27
        }
}
We previously demonstrated that P-selectin binds with high affinity to a trace, homodimeric glycoprotein ligand on human myeloid cells. The ligand carries the sialyl Lewis x (sLe(x)) epitope, a limited number of N-linked glycans, and clustered, sialylated O-linked glycans. In this study we demonstrate that the polypeptide component of this ligand is identical to that of P-selectin glycoprotein ligand-1 (PSGL-1), a molecule recently identified by expression cloning from a human myeloid cell cDNA… CONTINUE READING

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