Data/hora: 16/06/2024 06:53:24

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