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and TNF-
and Is Modulated by Metalloproteinase Activity1
Departments of
*
Vascular Biology and
Neuroscience, GlaxoSmithKline, Harlow, United Kingdom
Fractalkine/CX3C-chemokine ligand 1 is expressed as a
membrane-spanning adhesion molecule that can be cleaved from the cell
surface to produce a soluble chemoattractant. Within the vasculature,
fractalkine is known to be generated by endothelial cells, but to date
there are no reports describing its expression by smooth muscle cells
(SMC). In this study we demonstrate that IFN-
and TNF-
, but not
IL-1
, cooperate synergistically to induce fractalkine mRNA and
protein expression in cultured aortic SMC. We also report the release
of functional, soluble fractalkine from the membranes of stimulated
SMC. This release is inhibited by the zinc metalloproteinase inhibitor
batimastat, resulting in the accumulation of membrane-associated
fractalkine on the SMC surface. Therefore, an SMC-derived
metalloproteinase activity is involved in fractalkine shedding. While
soluble fractalkine present in SMC-conditioned medium is capable of
inducing calcium transients in cells expressing the fractalkine
receptor (CX3CR1), blocking experiments using neutralizing Abs reveal
that it can be inactivated without affecting the chemotactic activity
of SMC-conditioned media on monocytes. However, membrane-bound
fractalkine plays a major role in promoting adhesion of monocytic cells
to activated SMC. This fractalkine-mediated adhesion is further
enhanced in the presence of batimastat, indicating that shedding of
fractalkine from the cell surface down-regulates the adhesive
properties of SMC. Hence, during vascular inflammation, the synergistic
induction of fractalkine by IFN- and TNF- together with its
metalloproteinase-mediated cleavage may finely control the recruitment
of monocytes to SMC within the blood vessel wall.
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