Structure and function of the selectin ligand PSGL-1

Brazilian Journal of Medical and Biological Research

R.d. Cummings¹ 

[1] ,University of Oklahoma Health Sciences Center

关键词: P-selectin;    L-selectin;    E-selectin;    PSGL-1;    O-glycosylation;    glycoprotein;    mucin;    tyrosine sulfate;    cell adhesion;    leukocytes;    neutrophils;   

DOI  :  10.1590/S0100-879X1999000500004

来源: SciELO

【 摘 要 】

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 (NeuAca2®3Galß1®4[Fuca1®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.

【 授权许可】

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