Identification and molecular characterization of fractalkine receptor CX3CR1, which mediates both leukocyte migration and adhesion.
Cell
; 91(4): 521-30, 1997 Nov 14.
Article
de En
| MEDLINE
| ID: mdl-9390561
ABSTRACT
Leukocyte trafficking at the endothelium requires both cellular adhesion molecules and chemotactic factors. Fractalkine, a novel transmembrane molecule with a CX3C-motif chemokine domain atop a mucin stalk, induces both adhesion and migration of leukocytes. Here we identify a seven-transmembrane high-affinity receptor for fractalkine and show that it mediates both the adhesive and migratory functions of fractalkine. The receptor, now termed CX3CR1, requires pertussis toxin-sensitive G protein signaling to induce migration but not to support adhesion, which also occurs without other adhesion molecules but requires the architecture of a chemokine domain atop the mucin stalk. Natural killer cells predominantly express CX3CR1 and respond to fractalkine in both migration and adhesion. Thus, fractalkine and CX3CR1 represent new types of leukocyte trafficking regulators, performing both adhesive and chemotactic functions.
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Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Adhérence cellulaire
/
Récepteur VIH
/
Mouvement cellulaire
/
Récepteurs aux cytokines
/
Chimiokines
/
Chimiokines CX3C
/
Leucocytes
/
Protéines membranaires
Type d'étude:
Diagnostic_studies
/
Prognostic_studies
Limites:
Humans
Langue:
En
Journal:
Cell
Année:
1997
Type de document:
Article
Pays d'affiliation:
Japon