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- W2151291231 abstract "Reactive oxygen species regulate protein functionality. Cell cycle CDC25 phosphatases are targets of such oxidative regulation in vitro. We sought to evaluate if a thioredoxin (trx)-dependent redox regulation of CDC25 exists in cancer cells. For that purpose, we used MCF7 and MDA-MB 231 breast cancer cells, which express trx1 differentially, together with two trx/thioredoxin reductase (trxR) inhibitors, Auranofin and Acrolein. Auranofin could induce a full trxR inhibition associated with ROS production in both cell lines. Acrolein could provoke similar effects only in MDA-MB 231 cells with a low trx1 expression. Simultaneous trx1 oxidation and trxR inactivation occurred only in the presence of Acrolein and resulted in a G2-M cell cycle arrest, without full CDC25 inhibition in MDA-MB 231 cells. Our data suggest that the maintenance of CDC25 activity does not fully rely on the trx system in breast cancer cells, even in the presence of a major oxidative stress." @default.
- W2151291231 created "2016-06-24" @default.
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- W2151291231 creator A5081778629 @default.
- W2151291231 creator A5089560972 @default.
- W2151291231 date "2012-03-20" @default.
- W2151291231 modified "2023-10-18" @default.
- W2151291231 title "Protection of CDC25 phosphatases against oxidative stress in breast cancer cells: Evaluation of the implication of the thioredoxin system" @default.
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- W2151291231 doi "https://doi.org/10.3109/10715762.2012.669039" @default.
- W2151291231 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22360685" @default.
- W2151291231 hasPublicationYear "2012" @default.
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