| Registro completo |
| Provedor de dados: |
BJMBR
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| País: |
Brazil
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| Título: |
Structure and function of the selectin ligand PSGL-1
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| Autores: |
Cummings,R.D.
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| Data: |
1999-05-01
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| Ano: |
1999
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| Palavras-chave: |
P-selectin
L-selectin
E-selectin
PSGL-1
O-glycosylation
Glycoprotein
Mucin
Tyrosine sulfate
Cell adhesion
Leukocytes
Neutrophils
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| 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<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.
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| Tipo: |
Info:eu-repo/semantics/article
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| Idioma: |
Inglês
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| Identificador: |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999000500004
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| Editor: |
Associação Brasileira de Divulgação Científica
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| Relação: |
10.1590/S0100-879X1999000500004
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| Formato: |
text/html
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| Fonte: |
Brazilian Journal of Medical and Biological Research v.32 n.5 1999
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| Direitos: |
info:eu-repo/semantics/openAccess
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