Redox regulation of the hypoxia-inducible factor

Pouysségur, Jacques; Mechta-Grigoriou, Fatima

doi:10.1515/bc.2006.167

Cited by 187Cancer, Hypoxia, and MetabolismRedox biology and oxidative stressNitric Oxide and Endothelin Effects

Redox regulation of the hypoxia-inducible factor

Pouysségur, Jacques, Mechta-Grigoriou, Fatima·2006·Biological Chemistry

DOI 10.1515/bc.2006.167

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Abstract

Reactive oxygen species (ROS) have long been considered only as cyto- and genotoxic. However, there is now compelling evidence that ROS also act as second messengers in response to various stimuli, such as growth factors, hormones and cytokines. The hypoxia-inducible transcription factor (HIF) is a master regulator of oxygen-sensitive gene expression. More recently, HIF has also been shown to respond to non-hypoxic stimuli. Interestingly, recent reports indicate that ROS regulate HIF stability and transcriptional activity in well-oxygenated cells, as well as under hypoxic conditions. Consequently, ROS appear to be key players in regulating HIF-dependent pathways under both normal and pathological circumstances. This review summarizes the current understanding of the role of ROS in the regulation of the mammalian HIF system.

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Moderate reductions in oxygen tension increase mitochondrial superoxide and hydrogen peroxide generation, particularly at respiratory complexes I and III.
“Subsequent studies revealed that moderate reductions in oxygen tension increase mitochondrial superoxide and hydrogen peroxide generation, particularly at respiratory complexes I and III”
From HIF inhibition: Current strategies and clinical challenges (2026) · cites this paper as [203]
These ROS inhibit prolyl hydroxylase (PHD) activity, leading to HIF-α stabilization at oxygen levels well above anoxia.
“and that these ROS inhibit prolyl hydroxylase (PHD) activity, leading to HIF-α stabilization at oxygen levels well above anoxia.”
From HIF inhibition: Current strategies and clinical challenges (2026) · cites this paper as [203]
HIF regulation by ROS is graded and redox-window-dependent, explaining how HIF signaling can be engaged under mild hypoxia or near-normoxic conditions in metabolically active or oncogenically transformed cells, rather than exhibiting a binary oxygen response.
“Importantly, this regulation is graded and redox-window–dependent, explaining how HIF signaling can be engaged under mild hypoxia or even near-normoxic conditions in metabolically active or oncogenically transformed cells, rather than exhibiting a binary oxygen response [[201], [202], [203], [204]].”
From HIF inhibition: Current strategies and clinical challenges (2026) · cites this paper as [203]
Low O2 tension in solid tumors has profound effects on tumor metabolism.
“this is recognized to have profound effects on the tumor metabolism (92)(93)(94)”
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O2 tension in the center of solid tumors may be so low that cells essentially become anoxic.
“O 2 tension in the center of solid tumors may be so low that cells essentially become anoxic”
From Adipose tissue remodeling and obesity (2011) · cites this paper as [94]

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Functional Requirement of the Hypoxia-responsive Element in the Activation of the Inducible Nitric Oxide Synthase Promoter by the Iron Chelator Desferrioxamine
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“Remarkably, desferrioxamine (DFO), an iron chelator, is known to induce accumulation of HIF-a proteins in a dose-dependent manner, showing that iron-limiting levels again modulate PHD enzymatic activity (Wang and Semenza, 1993; Semenza et al., 1994; Melillo et al., 1997).”
Background
Regulation of hypoxia-inducible factor is preserved in the absence of a functioning mitochondrial respiratory chain
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Upregulation of NAD(P)H oxidase 1 in hypoxia activates hypoxia-inducible factor 1 via increase in reactive oxygen species
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Hepatocyte growth factor signalling stimulates hypoxia inducible factor-1 (HIF-1) activity in HepG2 hepatoma cells
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Rac1 Activity Is Required for the Activation of Hypoxia-inducible Factor 1
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MAPK and Akt Act Cooperatively but Independently on Hypoxia Inducible Factor-1α in rasV12 Upregulation of VEGF
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Induction of Vascular Endothelial Growth Factor by IGF-I in Osteoblast-Like Cells Is Mediated by the PI3K Signaling Pathway through the Hypoxia-Inducible Factor-2α
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p38 Signaling-mediated Hypoxia-inducible Factor 1α and Vascular Endothelial Growth Factor Induction by Cr(VI) in DU145 Human Prostate Carcinoma Cells
Gao, N., Jiang, B., Leonard, S. S., Corum, L., Zhang, Z., Roberts, J. R., Antonini, J. M., Zheng, J. Z., Flynn, D. C., Castranova, V., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202775200 · Cited by 133 · see citing works
Regulation by Neurotransmitter Receptors of Serotonergic or Catecholaminergic Neuronal Cell Differentiation
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Inhibition of mitochondrial respiration elevates oxygen concentration but leaves regulation of hypoxia-inducible factor (HIF) intact
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Arsenite induces HIF-1α and VEGF through PI3K, Akt and reactive oxygen species in DU145 human prostate carcinoma cells
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Oxidized low-density lipoprotein (oxLDL) triggers hypoxia-inducible factor-1α (HIF-1α) accumulation via redox-dependent mechanisms
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Superoxide fluxes limit nitric oxide-induced signaling
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Up-regulation of vascular endothelial growth factor/vascular permeability factor in mouse skin carcinogenesis correlates with malignant progression state and activated H-ras expression levels.
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Antioxidant Intervention Attenuates Myocardial Neovascularization in Hypercholesterolemia
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The Transcription Factors HIF-1 and HNF-4 and the Coactivator p300 Are Involved in Insulin-regulated Glucokinase Gene Expression via the Phosphatidylinositol 3-Kinase/Protein Kinase B Pathway
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Nox4 Is Critical for Hypoxia-Inducible Factor 2-α Transcriptional Activity in von Hippel-Lindau–Deficient Renal Cell Carcinoma
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Gastric epithelial reactive oxygen species prevent normoxic degradation of hypoxia-inducible factor-1alpha in gastric cancer cells.
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Nitric Oxide Is a Factor in the Stabilization of Hypoxia-Inducible Factor-1α in Cancer: Role of Free Radical Formation
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In vitro study of HIF‐1 activation and VEGF release by bFGF in the T47D breast cancer cell line under normoxic conditions: involvement of PI‐3K/Akt and MEK1/ERK pathways
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Lack of Correlation between Expression of HIF-1α Protein and Oxygenation Status in Identical Tissue Areas of Squamous Cell Carcinomas of the Uterine Cervix
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Reactive oxygen species (ROS) as pleiotropic physiological signalling agents
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The role of reactive oxygen species and metabolism on cancer cells and their microenvironment
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Reactive oxygen species: important regulators of the oxygen sensing pathway
Wenner, J., Plate, K. H., & Acker, T. (2006) · Aktuelle Neurologie · doi:10.1055/s-2006-953496

Authors: Pouysségur, J., & Mechta-Grigoriou, F.
Affiliations: Centre National de la Recherche Scientifique (FR)
ORCID: Pouysségur, Jacques
Venue: Biological Chemistry
Publisher: Walter de Gruyter GmbH
Published: 2006-01-01
Volume: 387
Issue: 10/11
Pages: 1337-46
ISSN: 1431-6730 (ISSN-L)
1437-4315
DOI: 10.1515/bc.2006.167
OpenAlex: W2051611091
Cited by: 186
References: 144
Citations by year: 2025: 2 · 2024: 8 · 2023: 3 · 2022: 9 · 2021: 4 · 2020: 6 · 2019: 4 · 2018: 9 · 2017: 7 · 2016: 7 · 2015: 5 · 2014: 13 · 2013: 12 · 2012: 10
FWCI: 1.38
Type: journal article
Language: en
Open access: closed
Locations: Biological Chemistry (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion)
Funders: Ligue Contre le Cancer
Centre National de la Recherche Scientifique
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
Keywords: hypoxia-inducible factor, reactive oxygen species, redox regulation, second messengers, hypoxia
MeSH terms: Animals, Cytosol, Homeostasis, Humans, Mitochondria, Oxidation-Reduction, Oxygen, Basic Helix-Loop-Helix Proteins

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Redox regulation of the hypoxia-inducible factor

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