3ArrayExpress Uploaderarrayexpress_sidhumanBSA (control)BSA (control)BSA (control)sVEGFR-1sVEGFR-1sVEGFR-1fibronectinfibronectinfibronectin12030http://www.ebi.ac.uk/arrayexpress/experiments/E-GEOD-32560Soluble VEGFR-1 (sVEGFR-1) acts both as a decoy receptor for VEGFs and as an extracellular matrix protein for α5β1 integrin. A...24174428/profile/8773/arrayexpressuploader19cellendothelial cellfibronectinintegrinproteinDec.12, 2014Falsesvegfr-1-signaling-through-51-integrinE-GEOD-32560_A-AFFY-33sVEGFR-1 signaling through α5β1 integrinJun.18, 2014Soluble VEGFR-1 (sVEGFR-1) acts both as a decoy receptor for VEGFs and as an extracellular matrix protein for α5β1 integrin. A sVEGFR-1-derived peptide that interacts with α5β1 integrin promotes angiogenesis. However, canonical signal downstream integrin activation is not induced, resulting into lack of focal adhesion maturation. We performed a gene expression profile of endothelial cells adhering on sVEGFR-1 compared to that of cells adhering on fibronectin, the principal α5β1 integrin ligand. Three protein kinase-C substrates, adducin, MARCKS, and radixin were differently modulated. Adducin and MARCKS were less phosphorylated whereas radixin was higher phosphorylated in sVEGFR-1 adhering cells, the latter leading to prolonged small GTPase Rac1 activation and induction of a pathway involving the heterotrimeric G protein α13. Altogether, our data indicated endothelial cell acquisition of an highly motile phenotype when adherent on sVEGFR-1. Finally, we indicated radixin as accountable for the angiogenic effect of α5β1 integrin interaction with sVEGFR-1 that in turn depends on an active VEGF-A/VEGFR-2 signaling. Endothelial cells were let adhere in Petri dishes coated with fibronectin or sVEGFR-1 before RNA extraction and hybridization on Affymetrix microarrays. Endothelial cells plated on BSA-treated Petri dishes were used as non-adhesion control. Each hybridization was performed in triplicate.E-GEOD-32560http://www.ebi.ac.uk/arrayexpress/experiments/E-GEOD-32560/samples/