Molecular cloning of a dendritic cell-associated transmembrane protein, DC-HIL, that promotes RGD-dependent adhesion of endothelial cells through recognition of …
S Shikano, M Bonkobara, PK Zukas… - Journal of Biological …, 2001 - jbc.org
We isolated a novel molecule (DC-HIL) expressed abundantly by the XS52 dendritic cell
(DC) line and epidermal Langerhans cells, but minimally by other cell lines. DC-HIL is a type
I transmembrane protein that contains a heparin-binding motif and an integrin-recognition
motif, RGD, in its extracellular domain (ECD). A soluble fusion protein (DC-HIL-Fc) of the
ECD and an immunoglobulin Fc bound to the surface of an endothelial cell line (SVEC). This
binding induced adhesion of SVEC to its immobilized form. Sulfated polysaccharides (eg …
(DC) line and epidermal Langerhans cells, but minimally by other cell lines. DC-HIL is a type
I transmembrane protein that contains a heparin-binding motif and an integrin-recognition
motif, RGD, in its extracellular domain (ECD). A soluble fusion protein (DC-HIL-Fc) of the
ECD and an immunoglobulin Fc bound to the surface of an endothelial cell line (SVEC). This
binding induced adhesion of SVEC to its immobilized form. Sulfated polysaccharides (eg …
