Back to Search Start Over

ADAM15 Is an Adherens Junction Molecule Whose Surface Expression Can Be Driven by VE-Cadherin

Authors :
Bodo Levkau
Barbara Herren
Claire Ham
Elaine W. Raines
Source :
Experimental Cell Research. 279:239-247
Publication Year :
2002
Publisher :
Elsevier BV, 2002.

Abstract

ADAM15 belongs to the family of proteins containing disintegrin and metalloprotease domains (ADAM) that have been implicated in cell adhesion via integrin binding and shedding of cell surface molecules. Here we provide the first report on the localization of an ADAM in adherens junctions. We show that ADAM15 colocalizes with a cell adhesion molecule, vascular endothelial (VE)-cadherin, which mediates endothelial cell adherens junction formation. In contrast, the distribution of ADAM15 correlates poorly with the localization in cell contacts of one of its proposed ligands, the β1-integrin. Furthermore, ADAM15 accumulation in cell–cell contacts is preceded by VE-cadherin-mediated adherens junction formation. To investigate the dependence of ADAM15 surface expression on adherens junction formation, we coexpressed VE-cadherin with ADAM15 and an ADAM15 green fluorescence protein (GFP) fusion protein in Chinese hamster ovary cells. VE-cadherin coexpression results in the translocation of ADAM15–GFP to the cell periphery. Analysis of cell surface levels of ADAM15 and ADAM15–GFP, with or without VE-cadherin coexpression, clearly demonstrates that VE-cadherin can drive surface expression of ADAM15. Our data suggest that ADAM15 may be a novel component of adherens junctions and thus could play a role in endothelial functions that are mediated by these cell contacts.

Details

ISSN :
00144827
Volume :
279
Database :
OpenAIRE
Journal :
Experimental Cell Research
Accession number :
edsair.doi.dedup.....d2c551aab65d035ebafece140fb4864b