We are analyzing https://link.springer.com/article/10.1186/s12964-022-01025-9.

Title:
The Warburg effect modulates DHODH role in ferroptosis: a review | Cell Communication and Signaling
Description:
Ferroptosis is an iron-dependent regulated cell death that suppresses tumor growth. It is activated by extensive peroxidation of membrane phospholipids caused by oxidative stress. GPX4, an antioxidant enzyme, reduces these peroxidized membrane phospholipids thereby inhibiting ferroptosis. This enzyme has two distinct subcellular localization; the cytosol and mitochondria. Dihydroorotate dehydrogenase (DHODH) complements mitochondrial GPX4 in reducing peroxidized membrane phospholipids. It is the rate-limiting enzyme in de novo pyrimidine nucleotide biosynthesis. Its role in ferroptosis inhibition suggests that DHODH inhibitors could have two complementary mechanisms of action against tumors; inhibiting de novo pyrimidine nucleotide biosynthesis and enhancing ferroptosis. However, the link between mitochondrial function and ferroptosis, and the involvement of DHODH in the ETC suggests that its role in ferroptosis could be modulated by the Warburg effect. Therefore, we reviewed relevant literature to get an insight into the possible effect of this metabolic reprogramming on the role of DHODH in ferroptosis. Furthermore, an emerging link between DHODH and cellular GSH pool has also been highlighted. These insights could contribute to the rational design of ferroptosis-based anticancer drugs. Video Abstract
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28 years and 1 months (reg. 1997-05-29).

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Keywords {🔍}

complex, ferroptosis, pubmed, article, dhodh, google, scholar, mitochondrial, effect, cas, cell, iii, biosynthesis, inhibition, warburg, cancer, cells, role, study, pyrimidine, tumor, nucleotide, growth, novo, central, gpx, ros, generation, oxidative, induction, reaction, hifα, dehydrogenase, cellular, glycolysis, aspartate, suggests, tumors, gsh, mechanism, electron, membrane, mitochondria, metabolic, biochemical, result, stress, dihydroorotate, inhibit, oxygen,

Topics {✒️}

voltage-dependent anion channels 2 mutant k-ras-driven cancers oxygen-sensitive hif-1α subunit energy-demanding nucleotide biosynthesis ribonucleotide reductase oxygen-dependent degradation domain electron transport chain redox-driven proton pumps energy-generating mitochondrial catabolism n-carbamoyl-l-aspartate outer q-binding site electronic transport chain got1-dependent aspartate biosynthesis mouse skin tissues ferroptosis-based anticancer drugs got2-dependent aspartate biosynthesis respiration-deficient cancer cells article download pdf pyrimidine nucleotide biosynthesis blocking hif-1α hydroxylation silencing hif-1α gene van der heijde-mulder antioxidant α-lipoic acid bba-mol basis dis mutant kras-driven cancers glutathione-independent ferroptosis suppressor got1-catalyzed reaction reverses rate-limiting amino acid mobile electron carrier glycolysis-related gene expression literature search hif-1 prolyl-hydroxylation facilitates got1-facilitated aspartate biosynthesis synthesized de novo preserving dhodh-catalyzed reaction nadph-dependent antioxidant enzymes neurodegeneration-linked sdh deficiency dhodh-facilitated electron transfer dna-deficient cancer cells complex i-generated o2− high energy demand de novo purine nucleic acid biosynthesis inhibiting pyrimidine biosynthesis oxidative stress-mediated stabilization article amos dhodh-mediated ferroptosis defence privacy choices/manage cookies dhodh-generated coq10h2 donates ampk-dependent manner

Questions {❓}

Curbing cancer’s sweet tooth: is there a role for MnSOD in regulation of the Warburg effect?
Ras superfamily GEFs and GAPs: validated and tractable targets for cancer therapy?
The Warburg effect: how does it benefit cancer cells?
The question now arises: between oxidative stress and the inhibition of complex I activity, which of the two plays the most important role in the induction of aerobic glycolysis?

Schema {🗺️}

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         description:Ferroptosis is an iron-dependent regulated cell death that suppresses tumor growth. It is activated by extensive peroxidation of membrane phospholipids caused by oxidative stress. GPX4, an antioxidant enzyme, reduces these peroxidized membrane phospholipids thereby inhibiting ferroptosis. This enzyme has two distinct subcellular localization; the cytosol and mitochondria. Dihydroorotate dehydrogenase (DHODH) complements mitochondrial GPX4 in reducing peroxidized membrane phospholipids. It is the rate-limiting enzyme in de novo pyrimidine nucleotide biosynthesis. Its role in ferroptosis inhibition suggests that DHODH inhibitors could have two complementary mechanisms of action against tumors; inhibiting de novo pyrimidine nucleotide biosynthesis and enhancing ferroptosis. However, the link between mitochondrial function and ferroptosis, and the involvement of DHODH in the ETC suggests that its role in ferroptosis could be modulated by the Warburg effect. Therefore, we reviewed relevant literature to get an insight into the possible effect of this metabolic reprogramming on the role of DHODH in ferroptosis. Furthermore, an emerging link between DHODH and cellular GSH pool has also been highlighted. These insights could contribute to the rational design of ferroptosis-based anticancer drugs.
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         Protein-Ligand Interactions
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         Cytokines and Growth Factors
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