The transmembrane CXC-chemokine ligand 16 is induced by IFN-gamma and TNF-alpha and shed by the activity of the disintegrin-like metalloproteinase ADAM10.

@article{Abel2004TheTC,
  title={The transmembrane CXC-chemokine ligand 16 is induced by IFN-gamma and TNF-alpha and shed by the activity of the disintegrin-like metalloproteinase ADAM10.},
  author={Soeren Abel and Christian Hundhausen and Rolf Mentlein and Alexander Schulte and Theo A. Berkhout and Neil M Broadway and Dieter Hartmann and Radek Sedl{\'a}cek and Sebastian Dietrich and Barbara Muetze and Bjoern Schuster and K Kallen and Paul Saftig and Stefan Rose-John and Andreas Ludwig},
  journal={Journal of immunology},
  year={2004},
  volume={172 10},
  pages={6362-72}
}
The novel CXC-chemokine ligand 16 (CXCL16) functions as transmembrane adhesion molecule on the surface of APCs and as a soluble chemoattractant for activated T cells. In this study, we elucidate the mechanism responsible for the conversion of the transmembrane molecule into a soluble chemokine and provide evidence for the expression and shedding of CXCL16 by fibroblasts and vascular cells. By transfection of human and murine CXCL16 in different cell lines, we show that soluble CXCL16 is… CONTINUE READING
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