English, W.R. orcid.org/0000-0003-3024-2441, Siviter, S.J., Hansen, M. et al. (1 more author) (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
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.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Copyright, Publisher and Additional Information: | © 2017 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
Keywords: | ADAM9; Endothelial; Permeability; VE-Cadherin; Monocyte; Transmigration |
Dates: |
|
Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Medicine, Dentistry and Health (Sheffield) > The Medical School (Sheffield) > Division of Genomic Medicine (Sheffield) > Department of Oncology and Metabolism (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 25 Sep 2017 12:09 |
Last Modified: | 23 Nov 2017 11:37 |
Published Version: | https://doi.org/10.1016/j.bbrc.2017.09.089 |
Status: | Published |
Publisher: | Elsevier |
Refereed: | Yes |
Identification Number: | 10.1016/j.bbrc.2017.09.089 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:121461 |