Regulation of CX3CL1/fractalkine expression in endothelial cells.
CX3CL1/fractalkine is a chemokine with a unique CX3C motif. Fractalkine is synthesized in endothelial cells as a membrane protein, and the N-terminal domain containing a CX3C motif is cleaved and secreted. CX3CR1, the specific receptor for fractalkine, is expressed in monocytes and lymphocytes. Membrane-bound fractalkine works as an adhesion molecule for these leukocytes and the secreted form as a chemotactic factor. Fractalkine is produced by endothelial cells stimulated with tumor necrosis factor-alpha, interleukin-1 (IL-1), lipopolysaccharide and interferon-gamma. Expression of fractalkine in endothelial cells is inhibited by the soluble form of IL-6 receptor-alpha, 15-deoxy-Delta(12,14)-prostaglandin J(2), and hypoxia. The expression of fractalkine is tightly regulated and fractalkine plays an important role in the interaction between leukocytes and endothelial cells.
Imaizumi
Tadaatsu
T
Department of Vascular Biology, Hirosaki University School of Medicine, Aomori, Japan. timaizum@cc.hirosaki-u.ac.jp
Yoshida
Hidemi
H
Satoh
Kei
K
D054428:Chemokine CX3CL1; D020523:Chemokines, CX3C / Q000378:metabolism*; D004730:Endothelium, Vascular / Q000166:cytology / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism*
C515538:CX3CL1 protein, human; D054428:Chemokine CX3CL1; D020523:Chemokines, CX3C; D008565:Membrane Proteins