Structure and function of the selectin ligand PSGL-1

• Autor(a) principal: Cummings,R.D.
• Data de Publicação: 1999
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Brazilian Journal of Medical and Biological Research
• Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999000500004
• topic: P-selectin; L-selectin; E-selectin; PSGL-1; O-glycosylation; glycoprotein; mucin; tyrosine sulfate; cell adhesion; leukocytes; neutrophils

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.