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

William R. English, Richard J. Siviter, Martin Hansen, Gillian Murphy

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)1057-1062
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume493
Issue number2
DOIs
Publication statusPublished - 18 Nov 2017

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