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IGDQ motogenic peptide gradient induces directional cell migration through integrin (αv)β3 activation in MDA-MB-231 metastatic breast cancer cells

Ayama-Canden, Sophie, Tondo, Rodolfo, Piñeros, Liliana, Ninane, Noëlle, Demazy, Catherine, Dieu, Marc, Fattaccioli, Antoine, Tabarrant, Tijani, Lucas, Stéphane, Bonifazi, Davide ORCID: https://orcid.org/0000-0001-5717-0121 and Michiels, Carine 2022. IGDQ motogenic peptide gradient induces directional cell migration through integrin (αv)β3 activation in MDA-MB-231 metastatic breast cancer cells. Neoplasia 31 , 100816. 10.1016/j.neo.2022.100816

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Abstract

In the context of breast cancer metastasis study, we have shown in an in vitro model of cell migration that IGDQ-exposing (IsoLeu-Gly-Asp-Glutamine type I Fibronectin motif) monolayers (SAMs) on gold sustain the adhesion of breast cancer MDA-MB-231 cells by triggering Focal Adhesion Kinase and integrin activation. Such tunable scaffolds are used to mimic the tumor extracellular environment, inducing and controlling cell migration. The observed migratory behavior induced by the IGDQ-bearing peptide gradient along the surface allows to separate cell subpopulations with a “stationary” or “migratory” phenotype. In this work, we knocked down the integrins α5(β1) and (αv)β since they are already known to be implicated in cell migration. To this aim, a whole proteomic analysis was performed in beta 3 integrin (ITGB3) or alpha 5 integrin (ITGA5) knock-down MDA-MB-231 cells, in order to highlight the pathways implied in the integrin-dependent cell migration. Our results showed that i) ITGB3 depletion influenced ITGA5 mRNA expression, ii) ITGB3 and ITGA5 were both necessary for IGDQ-mediated directional single cell migration and iii) integrin (αv)β3 was activated by IGDQ fibronectin type I motif. Finally, the proteomic analysis suggested that co-regulation of recycling transport of ITGB3 by ITGA5 is potentially necessary for directional IGDQ-mediated cell migration.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Chemistry
Additional Information: License information from Publisher: LICENSE 1: URL: http://creativecommons.org/licenses/by-nc-nd/4.0/, Start Date: 2022-06-13
Publisher: Elsevier
ISSN: 1522-8002
Date of First Compliant Deposit: 1 July 2022
Date of Acceptance: 13 June 2022
Last Modified: 06 Jan 2024 04:45
URI: https://orca.cardiff.ac.uk/id/eprint/150939

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