Chemical Biology and Drug Design
Chemical Biology and Drug Design
5 years ago

The APE1 redox inhibitor E3330 reduces collective cell migration of human breast cancer cells and decreases chemoinvasion and colony formation when combined with docetaxel

The APE1 redox inhibitor E3330 reduces collective cell migration of human breast cancer cells and decreases chemoinvasion and colony formation when combined with docetaxel
Nuno G. Oliveira, João G. Costa, Nuno Saraiva, Patrícia S. Guerreiro, Joana P. Miranda, Eduardo Corvacho, Matilde Castro, Ana S. Fernandes
The human apurinic/apyrimidinic endonuclease 1 (APE1) is an ubiquitous multifunctional DNA repair enzyme and a redox signalling protein. Our work addressed the inhibition of APE1 redox function using E3330, as single agent or in combination with docetaxel (DTX), in human breast cancer MDA-MB-231 cells. E3330 decreased the colony formation of DTX-treated cells. In addition, E3330 alone significantly reduced the collective cell migration as assessed by the wound-healing assay, whereas the combined treatment decreased chemoinvasion. These results suggest that the inhibition of APE1 redox function might have therapeutic potential by modulating cell migration and invasion in metastatic breast cancer. The human apurinic/apyrimidinic endonuclease 1 (APE1) is a multifunctional DNA repair enzyme with relevant redox signalling functions. The quinone derivative E3330, a redox inhibitor of APE1, decreased the colony formation and chemoinvasion of docetaxel-treated MDA-MB-231 cells (represented in blue). In addition, E3330 as single agent (represented in red) significantly reduced the collective cell migration. These results suggest APE1 redox function as a potential target for the modulation of cell migration and invasion in metastatic breast cancer.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1111/cbdd.12979

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