Structure and function of the selectin ligand PSGL-1

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Abstract

P-selectin glycoprotein ligand-1 (PSGL-1) is a dimeric mucin-like 120-kDa glycoprotein on leukocyte surfaces that binds to P- and L-selectin and promotes cell adhesion in the inflammatory response. The extreme amino terminal extracellular domain of PSGL-1 is critical for these interactions, based on site-directed mutagenesis, blocking monoclonal antibodies, and biochemical analyses. The current hypothesis is that for high affinity interactions with P-selectin, PSGL-1 must contain O-glycans with a core-2 branched motif containing the sialyl Lewis x antigen (NeuAcα2→3Galß1→4[Fucα1→3] GlcNAcß1→R). In addition, high affinity interactions require the co-expression of tyrosine sulfate on tyrosine residues near the critical O-glycan structure. This review addresses the biochemical evidence for this hypothesis and the evidence that PSGL-1 is an important in vivo ligand for cell adhesion.

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APA

Cummings, R. D. (1999). Structure and function of the selectin ligand PSGL-1. Brazilian Journal of Medical and Biological Research, 32(5), 519–528. https://doi.org/10.1590/S0100-879X1999000500004

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