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Prepublished online as a Blood First Edition Paper on April 24, 2003; DOI 10.1182/blood-2002-12-3775. This Article Full Text (PDF) All Versions of this Article: 2002-12-3775v1 102/4/1186    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Hundhausen, C. Articles by Ludwig, A. Search for Related Content PubMed PubMed Citation Articles by Hundhausen, C. Articles by Ludwig, A. Social Bookmarking                   What's this? Submitted December 12, 2002 Accepted April 15, 2003 The disintegrin-like metalloproteinase ADAM 10 is involved in constitutive cleavage of CX3CL1 (fractalkine) and regulates CX3CL1-mediated cell-cell adhesion Christian Hundhausen, Dominika Misztela, Theo A Berkhout, Neil Broadway, Paul Saftig, Karina Reiss, Dieter Hartmann, Falk Fahrenholz, Rolf Postina, Vance Matthews, Karl-Josef Kallen, Stefan Rose-John, and Andreas Ludwig* Biochemical Institute, Christian-Albrechts-University, Kiel, Germany Department of Atherosclerosis, GlaxoSmithKline, Stevenage, United Kingdom Department of Gene Expression and Protein Chemistry, GlaxoSmithKline, Stevenage, United Kingdom Center for Human Genetics, Leuven and Flanders Interuniversity (VIB 4), Leuven, Belgium Institute for Biochemistry, Johannes Gutenberg-University, Mainz, Germany * Corresponding author; email: aludwig{at}biochem.uni-kiel.de. The CX3C-chemokine fractalkine (CX3CL1) exists as a membrane-expressed protein promoting cell-cell adhesion and as a soluble molecule inducing chemotaxis. Transmembrane CX3CL1 is converted into its soluble form by defined proteolytic cleavage (shedding) which can be enhanced by stimulation with phorbol-12-N-myristate-13-acetate (PMA). PMA-induced CX3CL1 shedding has been shown to involve the TNF-converting enzyme (TACE) whereas the constitutive cleavage in unstimulated cells remains elusive. Here we demonstrate a role of the closely related disintegrin-like metalloproteinase 10 (ADAM10) in the constitutive CX3CL1 cleavage. The hydroxamate GW280264X, capable of blocking TACE as well as ADAM10, proved to be an effective inhibitor of the constitutive and the PMA-inducible CX3CL1 cleavage in CX3CL1-expressing ECV-304 cells (CX3CL1-ECV-304), whereas GI254023X, preferentially blocking ADAM10 but not TACE, reduced the constitutive cleavage only. Over-expression of ADAM10 in COS-7 cells enhanced constitutive cleavage of CX3CL1 and, more importantly, in murine fibroblasts deficient of ADAM10 constitutive CX3CL1 cleavage was markedly reduced. Thus, ADAM10 contributes to the constitutive shedding of CX3CL1 in unstimulated cells. Addressing the functional role of CX3CL1 shedding for the adhesion of monocytic cells via membrane-expressed CX3CL1, we found that THP-1 cells adhere to CX3CL1-ECV-304 cells but detach in the course of vigorous washing. Inhibition of ADAM10-mediated CX3CL1 shedding not only increased adhesive properties of CX3CL1-ECV-304 cells but also prevented de-adhesion of bound THP-1 cells. Our data demonstrate that ADAM10 is involved in the constitutive cleavage of CX3CL1 and thereby may regulate the recruitment of monocytic cells to CX3CL1-expressing cell layers. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? 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