Santibáñez, Juan F.Frontelo, PilarMartínez, JorgeQuintanilla, MiguelIglesias Badiola, Maite2012-08-092012-08-092000-05-230006-291Xhttp://hdl.handle.net/10641/281Transformed PDV keratonocytes respond to TGF-β1 by stimulating cell motility and invasiveness concomitantly to enhancement of the urokinae-type plasmiogen activator (uPA) expression/secretion. Depletion of extracellular signal-regulated kinase (EREK1,2) proteins by treatment of PDV cells with antinese oligonucleotides reduced basal uPA production and abolished stimulation of uPA secreted levels and cell motility by TGF-β1. PD098059, an inhibitor of mitogenactivated protein kinase (MAPK) kinase (MEK), decreased TGF-β1-induced uPA mRNA expression, secreted activity in a dose-dependent manner, and abrogated TGF-β1-stimulated cell motility and invasiveness. PDV-derived dominant-negative RasN17 cell transfectants secreted similar amounts of uPA and exhibited similar invasive abilities as the parental cells or control clones, but were unable to respond to TGF-β1 for stimulation of uPA-secreted levels and invasiveness. These results suggest that a Ras/MAPK transduction pathway is involved in the invasive response ot transformed keratinocytes to TGF-β1.engAttribution-NonCommercial-NoDerivs 3.0 Spainhttp://creativecommons.org/licenses/by-nc-nd/3.0/es/TGF-β1uPAKeratinocytesRasMEKERKInvasivenessjournal article