Staurosporine stimulates expression of the urokinase-type (u-PA) plasminogen activator in LLC-PK1 cells

✍ Scribed by Christa Dierks-Ventling; Jaromir Knesel; Yoshikuni Nagamine; Brian A. Hemmings; Gundula Pehling; Franz Fischer; Doriano Fabbro

• Publisher: John Wiley and Sons
• Year: 1989
• Tongue: French
• Weight: 959 KB
• Volume: 44
• Category: Article
• ISSN: 0020-7136
• DOI: 10.1002/ijc.2910440520

✦ Synopsis

In LLC-PK, porcine epithelial cells, the urokinase-type plasminogen activator (u-PA) mRNA and protein can be induced either by stimulation of the protein kinase C (PKC) pathway using a tumor promoter (PMA) or by stimulation of the protein kinase A (PKA) pathway with calcitonin SCT). By PKC, to LLC-PK, cells also stimulated urokinase production. In contrast to the in vitro situation (where staurosporine inhibited PKC activity), in the cell-culture system the microbial a ent caused an early translocation of PKC and inhibited PkA. Addition of staurosporine together with PMA or with SCT further increased urokinase mRNA and protein synthesis. Maximal stimulation was obtained when all 3 agents were added together. We thus assume that in LLC-PK, cells the PKA and PKC signal-transferring pathways can function independently.