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

English, William R. ORCID:, Siviter, Richard J., Hansen, Martin and Murphy, Gillian (2017) ADAM9 is present at endothelial cell-cell junctions and regulates monocyte–endothelial transmigration. Biochemical and Biophysical Research Communications, 493 (2). pp. 1057-1062. ISSN 0006-291X

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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.

Item Type: Article
Faculty \ School: Faculty of Medicine and Health Sciences > Norwich Medical School
Faculty of Science > School of Biological Sciences
UEA Research Groups: Faculty of Medicine and Health Sciences > Research Centres > Metabolic Health
Depositing User: LivePure Connector
Date Deposited: 15 Dec 2022 17:31
Last Modified: 19 Oct 2023 03:30
DOI: 10.1016/j.bbrc.2017.09.089


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