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Nucleic Acids Research, 1993, Vol. 21, No. 15 3365-3372
© 1993

MOLECULAR BIOLOGY

Cytoskeletal reorganization and TPA differently modify AP-1 to induce the urokinase-type plasminogen activator gene in LLC-PK1 cells

Janet S. Lee+, Dietmar von der Ahe§, Birgitta Kiefer and Yoshikuni Nagamine*

Department of Genetics, University of Nottingham, Queens Medical Centre Nottingham NG7 2UH, UK

*To whom correspondence should be addressed

Received May 22, 1993. Revised June 15, 1993. Accepted June 15, 1993.

Urokinase-type plasminogen activator (uPA) is an extracellular protease and expressed in various cells that exhibit dynamic changes in cell morphology, suggesting a link between cytoskeletal reorganization (CSR) and uPA expression. CSR can be induced by pharmacological agents, such as by colchicine for microtubule cytoskeleton and by cytochalasin for microfilament cytoskeleton. Using these agents, we previously showed that CSR induced the uPA gene in LLC-PK1 cells independently of the protein kinase C and cAMP-dependent protein kinase. Here we show that the induction of the uPA gene by CSR is mediated by the activation of c-Jun which interacts with an AP-1-like site located 2kb upstream of the uPA gene. 12-O-tetradecanoylphorbol 13-acetate (TPA) induces the uPA gene through the same elements, but additionally utilizes an adjacent PEA3 element and induces c-fos. Furthermore, CSR induces a greater accumulation and a more pronounced phosphorylation of c-Jun than TPA induction. AP-1 is a positive regulator of growth and oncogenesis, and CSR is an integral part of these processes. Our results provide a view how CSR and AP-1 could be coupled in these processes. We also show that TPA and CSR act synergistically, suggesting a model where an initial activation sIgnai could be amplified by CSR.

+Present address: Institut de Chimie Biologique, Faculté de Médecine, 11 rue Humann, 67085 Strasbourg, France

§Present address: Max-Planck Institute, Kerthhoff-Klinik, Sprudelhof 11, D-6350 Bad-Nauheim, Germany


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