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ROS homeostasis and metabolism: a dangerous liason in cancer cells.

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TLDR
How the mitochondria has a key role in regulating the interplay between redox homeostasis and metabolism within tumor cells is described, and the potential therapeutic use of agents that directly or indirectly block metabolism is discussed.
Abstract
Tumor cells harbor genetic alterations that promote a continuous and elevated production of reactive oxygen species. Whereas such oxidative stress conditions would be harmful to normal cells, they facilitate tumor growth in multiple ways by causing DNA damage and genomic instability, and ultimately, by reprogramming cancer cell metabolism. This review outlines the metabolic-dependent mechanisms that tumors engage in when faced with oxidative stress conditions that are critical for cancer progression by producing redox cofactors. In particular, we describe how the mitochondria has a key role in regulating the interplay between redox homeostasis and metabolism within tumor cells. Last, we will discuss the potential therapeutic use of agents that directly or indirectly block metabolism.

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Journal ArticleDOI

Reactive oxygen species (ROS) as pleiotropic physiological signalling agents.

TL;DR: This work focuses on ROS at physiological levels and their central role in redox signalling via different post-translational modifications, denoted as ‘oxidative eustress’.
Journal ArticleDOI

ROS signalling in the biology of cancer.

TL;DR: The generation and sources of ROS within tumour cells, the regulation of ROS by antioxidant defence systems, as well as the effect of elevated ROS production on their signalling targets in cancer are discussed.
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ROS in cancer therapy: the bright side of the moon

TL;DR: The review will emphasize the molecular mechanisms useful for the development of therapeutic strategies that are based on modulating ROS levels to treat cancer, and report on the growing data that highlight the role of ROS generated by different metabolic pathways as Trojan horses to eliminate cancer cells.
Journal ArticleDOI

Superoxide dismutases: Dual roles in controlling ROS damage and regulating ROS signaling.

TL;DR: Studies in model organisms and humans are discussed, which reveal the dual roles of SOD enzymes in controlling damage and regulating signaling and the need for fine local control of ROS signaling.
Journal ArticleDOI

ROS Generation and Antioxidant Defense Systems in Normal and Malignant Cells

TL;DR: This review covers the current data on the mechanisms of ROS generation and existing antioxidant systems balancing the redox state in mammalian cells that can also be related to tumors.
References
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Journal ArticleDOI

Overcoming Drug Development Bottlenecks With Repurposing: Repurposing biguanides to target energy metabolism for cancer treatment

TL;DR: Repurposing biguanides to target energy metabolism for cancer treatment and overcoming drug development bottlenecks with Repurposing is described.
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High-throughput RNAi screening for novel modulators of vimentin expression identifies MTHFD2 as a regulator of breast cancer cell migration and invasion

TL;DR: The results show that MTHFD2 is overexpressed in breast cancer, associates with poor clinical characteristics and promotes cellular features connected with metastatic disease, thus implicating MTH FD2 as a potential drug target to block breast cancer cell migration and invasion.
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Glutathionylation of the Active Site Cysteines of Peroxiredoxin 2 and Recycling by Glutaredoxin.

TL;DR: It is concluded that Prx2 glutathionylation is a favorable reaction that can occur in cells under oxidative stress and may have a role in redox signaling.
Journal ArticleDOI

Metastasis and Oxidative Stress: Are Antioxidants a Metabolic Driver of Progression?

TL;DR: It is shown that ROS limit distant metastasis: only cells with increased antioxidant capacity are able to succeed in their purpose to metastasize.
Journal ArticleDOI

Thioredoxin 1 Is Inactivated Due to Oxidation Induced by Peroxiredoxin under Oxidative Stress and Reactivated by the Glutaredoxin System

TL;DR: In this paper, a two-disulfide form of Trx1 was generated from oxidation of trx1 catalyzed by peroxiredoxin 1 in the presence of H2O2.
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