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J Biol Chem, Vol. 274, Issue 15, 10053-10058, April 9, 1999
,, and§¶
From the Fractalkine is a novel multidomain protein
expressed on the surface of activated endothelial cells. Cells
expressing the chemokine receptor CX3CR1 adhere to
fractalkine with high affinity, but it is not known if adherence
requires G-protein activation and signal transduction. To investigate
the cell adhesion properties of fractalkine, we created mutated forms
of CX3CR1 that have little or no ability to transduce
intracellular signals. Cells expressing signaling-incompetent forms of
CX3CR1 bound rapidly and with high affinity to immobilized
fractalkine in both static and flow assays. Video microscopy revealed
that CX3CR1-expressing cells bound more rapidly to
fractalkine than to VCAM-1 (60 versus 190 ms). Unlike VCAM-1, fractalkine did not mediate cell rolling, and after capture on
fractalkine, cells did not dislodge. Finally, soluble fractalkine induced intracellular calcium fluxes and chemotaxis, but it did not
activate integrins. Taken together these data provide strong evidence
that CX3CR1, a seven-transmembrane domain receptor,
mediates robust cell adhesion to fractalkine in the absence of
G-protein activation and suggest a novel role for this receptor as an
adhesion molecule.
Gladstone Institute of Cardiovascular
Disease, San Francisco, CA 94141-9100, the § Cardiovascular
Research Institute, and the ¶ Department of Medicine, University
of California, San Francisco, California 94143
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C. A. Haskell, M. D. Cleary, and I. F. Charo Unique Role of the Chemokine Domain of Fractalkine in Cell Capture. KINETICS OF RECEPTOR DISSOCIATION CORRELATE WITH CELL ADHESION J. Biol. Chem., October 27, 2000; 275(44): 34183 - 34189. [Abstract] [Full Text] [PDF]
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