Structure and function of the selectin ligand PSGL-1
1999; Associação Brasileira de Divulgação Científica; Volume: 32; Issue: 5 Linguagem: Inglês
10.1590/s0100-879x1999000500004
ISSN1414-431X
Autores Tópico(s)Galectins and Cancer Biology
ResumoP-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 (NeuAc a 2 ® 3Galß1 ® 4[Fuc a 1 ® 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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