Data/hora: 10/06/2024 15:29:42

Provedor de dados: | 56
País: | Brazil
Título: | Structure and function of the selectin ligand PSGL-1
Autores: | Cummings,R.D.
Data: | 1999-05-01
Ano: | 1999
Palavras-chave: | P-selectin; L-selectin; E-selectin; PSGL-1; O-glycosylation; Glycoprotein; Mucin; Tyrosine sulfate; Cell adhesion; Leukocytes; Neutrophils.
Resumo: | 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&lt;FONT FACE="Symbol"&gt;a&lt;/font&gt;2&lt;FONT FACE="Symbol"&gt;®&lt;/font&gt;3Galß1&lt;FONT FACE="Symbol"&gt;®&lt;/font&gt;4[Fuc&lt;FONT FACE="Symbol"&gt;a&lt;/font&gt;1&lt;FONT FACE="Symbol"&gt;®&lt;/font&gt;3]GlcNAcß1&lt;FONT FACE="Symbol"&gt;®&lt;/font&gt;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.
Tipo: | Info:eu-repo/semantics/article
Idioma: | Inglês
Identificador: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999000500004
Editor: | Associação Brasileira de Divulgação Científica
Relação: | 10.1590/S0100-879X1999000500004
Formato: | text/html
Fonte: | Brazilian Journal of Medical and Biological Research  v.32 n.5 1999
Fonte: | info:eu-repo/semantics/openAccess