Anticancer drugs for the modulation of endoplasmic reticulum stress and oxidative stressReportar como inadecuado

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Tumor Biology

, Volume 36, Issue 8, pp 5743–5752

First Online: 19 July 2015Received: 31 May 2015Accepted: 10 July 2015


Prior research has demonstrated how the endoplasmic reticulum ER functions as a multifunctional organelle and as a well-orchestrated protein-folding unit. It consists of sensors which detect stress-induced unfolded-misfolded proteins and it is the place where protein folding is catalyzed with chaperones. During this folding process, an immaculate disulfide bond formation requires an oxidized environment provided by the ER. Protein folding and the generation of reactive oxygen species ROS as a protein oxidative byproduct in ER are crosslinked. An ER stress-induced response also mediates the expression of the apoptosis-associated gene C-EBP-homologous protein CHOP and death receptor 5 DR5. ER stress induces the upregulation of tumor necrosis factor-related apoptosis inducing ligand TRAIL receptor and opening new horizons for therapeutic research. These findings can be used to maximize TRAIL-induced apoptosis in xenografted mice. This review summarizes the current understanding of the interplay between ER stress and ROS. We also discuss how damage-associated molecular patterns DAMPs function as modulators of immunogenic cell death and how natural products and drugs have shown potential in regulating ER stress and ROS in different cancer cell lines. Drugs as inducers and inhibitors of ROS modulation may respectively exert inducible and inhibitory effects on ER stress and unfolded protein response UPR. Reconceptualization of the molecular crosstalk among ROS modulating effectors, ER stress, and DAMPs will lead to advances in anticancer therapy.

KeywordsAnticancer ER stress ROS Natural products  Download fulltext PDF

Autor: Ammad Ahmad Farooqi - Kun-Tzu Li - Sundas Fayyaz - Yung-Ting Chang - Muhammad Ismail - Chih-Chuang Liaw - Shyng-Shiou F. 


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