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• W2003148857 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 (NeuAc<FONT FACE=Symbol>a</font>2<FONT FACE=Symbol>®</font>3Galß1<FONT FACE=Symbol>®</font>4[Fuc<FONT FACE=Symbol>a</font>1<FONT FACE=Symbol>®</font>3]GlcNAcß1<FONT FACE=Symbol>®</font>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." @default.
• W2003148857 created "2016-06-24" @default.
• W2003148857 creator A5023341393 @default.
• W2003148857 date "1999-05-01" @default.
• W2003148857 modified "2023-09-24" @default.
• W2003148857 title "Structure and function of the selectin ligand PSGL-1" @default.
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• W2003148857 doi "https://doi.org/10.1590/s0100-879x1999000500004" @default.
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