N-linked glycosylation of platelet P2Y12 ADP receptor is essential for signal transduction but not for ligand binding or cell surface expression.
FEBS Lett
; 562(1-3): 111-7, 2004 Mar 26.
Article
em En
| MEDLINE
| ID: mdl-15044010
ABSTRACT
P(2)Y(12) receptor is a G(i)-coupled adenosine diphosphate (ADP) receptor with a critical role in platelet aggregation. It contains two potential N-linked glycosylation sites at its extra cellular amino-terminus, which may modulate its activity. Studies of both tunicamycin treatment and site-directed mutagenesis have revealed a dispensable role of the N-linked glycosylation in the receptor's surface expression and ligand binding activity. However, the non-glycosylated P(2)Y(12) receptor is defective in the P(2)Y(12)-mediated inhibition of the adenylyl cyclase activity. Thus the study uncovers an unexpected vital role of N-linked glycans in receptor's signal transducing step but not in surface expression or ligand binding.
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Base de dados:
MEDLINE
Assunto principal:
Plaquetas
/
Transdução de Sinais
/
Membrana Celular
/
Receptores Purinérgicos P2
/
Ligantes
/
Proteínas de Membrana
Limite:
Animals
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2004
Tipo de documento:
Article
País de afiliação:
Estados Unidos