ADAM9 is present at endothelial cell - cell junctions and regulates monocyte - endothelial transmigration

作者：English William R^*; Siviter Richard J; Hansen Martin; Murphy Gillian

来源：Biochemical and Biophysical Research Communications, 2017, 493(2): 1057-1062.

DOI：10.1016/j.bbrc.2017.09.089

• ADAM9
• Endothelial
• Permeability
• VE-Cadherin
• Monocyte
• Transmigration

We have found that A Disintegrin And Metalloproteinase-9 (ADAM9) localises to cell-cell junctions with VE-Cadherin in confluent endothelial monolayers. Co-cultures of cells separately transfected with ADAM9-EGFP or ADAM9-HA showed expression is required in two adjacent cells for localisation to cell cell junctions suggesting the ADAM9 ectodomain may self-associate. A direct interaction between ADAM9 ectodomains was confirmed using recombinant proteins and an ELISA based method. As the ADAM9 ectodomain can also exist as a soluble form physiologically, we examined if this could inhibit endothelial functions dependent on cell-cell junctions. The soluble ADAM9 ectodomain could not increase endothelial monolayer permeability or inhibit monocyte-endothelial adhesion, but could inhibit monocyte-endothelial transmigration. These novel findings point to ADAM9 playing an important role in endothelial cell biology that is distinct from the other ADAMs.

• 出版日期2017-11-18