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Inhibition of reductase systems by 2-AAPA modulates peroxiredoxin oxidation and mitochondrial function in A172 glioblastoma cells.

Toxicology in vitro : an international journal published in association with BIBRA (2017-05-04)
Luiz Felipe de Souza, Ariana Ern Schmitz, Luana Caroline Schüler da Silva, Karen Andrinéia de Oliveira, Cláudia Beatriz Nedel, Carla Inês Tasca, Andreza Fabro de Bem, Marcelo Farina, Alcir Luiz Dafre
RÉSUMÉ

Thiol homeostasis has a critical role in the maintenance of proper cellular functions and survival, being coordinated by the action of several reductive enzymes, including glutathione (GSH)/glutathione reductase (GR) and thioredoxin (Trx)/thioredoxin reductase (TrxR) systems. Here, we investigated the effects of the GR inhibitor 2-acetylamino-3-[4-(2-acetylamino-2-carboxyethylsulfanylthiocarbonylamino)phenylthiocarbamoylsulfanyl]propionic acid (2-AAPA) on the activity of thiol reductases (GR and TrxR), redox balance and mitochondrial function of A172 glioblastoma cells. 2-AAPA inhibited cell GR (IC

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Cyanure de 4-(trifluorométhoxy)phénylhydrazone carbonyle, ≥98% (TLC), powder
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Cumene hydroperoxide, technical grade, 80%
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Tetramethylrhodamine ethyl ester perchlorate, suitable for fluorescence, ≥90% (HPCE)
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Thioredoxin Reductase from rat liver, buffered aqueous glycerol solution, ≥100 units/mg protein (Bradford)
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2-AAPA hydrate, ≥95% (HPLC)