articleBloodApr 29, 2003BRONZE OA

The disintegrin-like metalloproteinase ADAM10 is involved in constitutive cleavage of CX3CL1 (fractalkine) and regulates CX3CL1-mediated cell-cell adhesion

CHChristian HundhausenDMDominika MisztelaTATheo A. BerkhoutNBNeil BroadwayPSPaul Säftig

GlaxoSmithKline (United Kingdom) · Johannes Gutenberg University Mainz · +3 more institutions

PubMed
Indexed incrossrefpubmed

Abstract

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-myristate-13-acetate (PMA). PMA-induced CX3CL1 shedding has been shown to involve the tumor necrosis factor-alpha-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…

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Topics & keywords

Topics
Keywords
  • CX3CL1
  • Disintegrin
  • ADAM10
  • Cell biology
  • Cleavage (geology)
  • CXCL16
  • Cell adhesion
  • Metalloproteinase
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