CD9 controls integrin α5β1-mediated cell adhesion by modulating its association with the metalloproteinase ADAM17

Integrin α5β1 is a crucial adhesion molecule that mediates the adherence of many cell types to the extracellular matrix through recognition of its classic ligand fibronectin as well as to other cells through binding to an alternative counter-receptor, the metalloproteinase ADAM17/TACE. Interactions...

Full description

Bibliographic Details
Authors: Machado-Pineda, Yesenia, Cardeñes, Beatriz, Reyes, Raquel, López-Martín, Soraya, Toribio, Víctor, Sánchez-Organero, Paula, Suarez, Henar, Grötzinger, Joachim, Lorenzen, Inken, Yáñez Mo, María, Cabañas, Carlos
Format: article
Publication Date:2018
Country:España
Institution:Universidad Autónoma de Madrid
Repository:Biblos-e Archivo. Repositorio Institucional de la UAM
Language:English
OAI Identifier:oai:repositorio.uam.es:10486/686639
Online Access:http://hdl.handle.net/10486/686639
https://dx.doi.org/10.3389/fimmu.2018.02474
Access Level:Open access
Keyword:ADAM17
CD9
Cell adhesion
Fibronectin
Integrin
Metalloproteinase
Tetraspanin
Α5β1
Biología y Biomedicina / Biología
Description
Summary:Integrin α5β1 is a crucial adhesion molecule that mediates the adherence of many cell types to the extracellular matrix through recognition of its classic ligand fibronectin as well as to other cells through binding to an alternative counter-receptor, the metalloproteinase ADAM17/TACE. Interactions between integrin α5β1 and ADAM17 may take place both in trans (between molecules expressed on different cells) or in cis (between molecules expressed on the same cell) configurations. It has been recently reported that the cis association between α5β1 and ADAM17 keeps both molecules inactive, whereas their dissociation results in activation of their adhesive and metalloproteinase activities. Here we show that the tetraspanin CD9 negatively regulates integrin α5β1-mediated cell adhesion by enhancing the cis interaction of this integrin with ADAM17 on the cell surface. Additionally we show that, similarly to CD9, the monoclonal antibody 2A10 directed to the disintegrin domain of ADAM17 specifically inhibits integrin α5β1-mediated cell adhesion to its ligands fibronectin and ADAM17.

Similar Items