Oxygen-dependent regulation of mitochondrial respiration by hypoxia-inducible factor 1

Semenza, Gregg L.

doi:10.1042/bj20070389

Cited by 542Cancer, Hypoxia, and MetabolismMitochondrial Function and PathologyRedox biology and oxidative stress

Oxygen-dependent regulation of mitochondrial respiration by hypoxia-inducible factor 1

Semenza, Gregg L.·2007·Biochemical Journal

DOI 10.1042/bj20070389

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Abstract

The survival of metazoan organisms is dependent upon the utilization of O2 as a substrate for COX (cytochrome c oxidase), which constitutes Complex IV of the mitochondrial respiratory chain. Premature transfer of electrons, either at Complex I or at Complex III, results in the increased generation of ROS (reactive oxygen species). Recent studies have identified two critical adaptations that may function to prevent excessive ROS production in hypoxic cells. First, expression of PDK1 [PDH (pyruvate dehydrogenase) kinase 1] is induced. PDK1 phosphorylates and inactivates PDH, the mitochondrial enzyme that converts pyruvate into acetyl-CoA. In combination with the hypoxia-induced expression of LDHA (lactate dehydrogenase A), which converts pyruvate into lactate, PDK1 reduces the delivery of acetyl-CoA to the tricarboxylic acid cycle, thus reducing the levels of NADH and FADH2 delivered to the electron-transport chain. Secondly, the subunit composition of COX is altered in hypoxic cells by increased expression of the COX4-2 subunit, which optimizes COX activity under hypoxic conditions, and increased degradation of the COX4-1 subunit, which optimizes COX activity under aerobic conditions. Hypoxia-inducible factor 1 controls the metabolic adaptation of mammalian cells to hypoxia by activating transcription of the genes encoding PDK1, LDHA, COX4-2 and LON, a mitochondrial protease that is required for the degradation of COX4-1. COX subunit switching occurs in yeast, but by a completely different regulatory mechanism, suggesting that selection for O2-dependent homoeostatic regulation of mitochondrial respiration is ancient and likely to be shared by all eukaryotic organisms.

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H2O2-induced oxidation of a cysteine residue located in its catalytic site precisely and rapidly inhibits tyrosine phosphatase.
“For example, H2O2-induced oxidation of a cysteine residue located in its catalytic site precisely and rapidly inhibits tyrosine phosphatase (278, 315).”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [278]
Mitochondria are essential regulators of cellular bioenergetics that respond to changes in environmental stimuli such as hormones, nutrients, and oxygen tension.
“Mitochondria are essential regulators of cellular bioenergetics that respond to changes in environmental stimuli, such as hormones, nutrients, and oxygen tension (47, 94, 99, 109, 290, 301, 385).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [385]
HIF-1 coordinately upregulates many genes to regulate metabolism, energy production, and mitochondrial function.
“HIF-1 coordinately upregulates many genes to regulate metabolism, energy production, and mitochondrial function (385).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [385]
Enhanced ROS production is not a sustained event in hypoxia.
“Nonetheless, experimental evidence suggests that enhanced ROS production is not a sustained event in hypoxia (69, 385).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [385]

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Identification of Functional Hypoxia Response Elements in the Promoter Region of the DEC1 and DEC2 Genes
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Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the β-carbon of asparagine-803
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Hypoxia-Inducible Factor 1 Mediates Upregulation of Telomerase (hTERT)
Nishi, H., Nakada, T., Kyo, S., Inoue, M., Shay, J. W., & Isaka, K. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.13.6076-6083.2004 · Cited by 213 · see citing works
Regulation of the prolyl hydroxylase domain protein 2 (phd2/egln-1) gene: identification of a functional hypoxia-responsive element
Metzen, E., Stiehl, D. P., Doege, K., Marxsen, J. H., Hellwig‐Bürgel, T., & JELKMANN, W. E. B. (2005) · Biochemical Journal · doi:10.1042/bj20041736 · Cited by 212 · see citing works
Identification of Hypoxia-response Element in the Human Endothelial Nitric-oxide Synthase Gene Promoter
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Identification of membrane type-1 matrix metalloproteinase as a target of hypoxia-inducible factor-2α in von Hippel–Lindau renal cell carcinoma
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Selection and Analysis of a Mutant Cell Line Defective in the Hypoxia-inducible Factor-1 α-Subunit (HIF-1α)
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Mammalian subunit IV isoforms of cytochrome c oxidase
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Communication Between Mitochondria and the Nucleus in Regulation of Cytochrome Genes in the Yeast Saccharomyces cerevisiae
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Tracing Oxygen's Imprint on Earth's Metabolic Evolution
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Hypoxic Induction of Prolyl 4-Hydroxylase α(I) in Cultured Cells
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Hypoxia Regulates β-Enolase and Pyruvate Kinase-M Promoters by Modulating Sp1/Sp3 Binding to a Conserved GC Element
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Midkine Is Regulated by Hypoxia and Causes Pulmonary Vascular Remodeling
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Hypoxia Induces Transcription Factor ETS-1 via the Activity of Hypoxia-Inducible Factor-1
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Expression of Vascular Endothelial Growth Factor Receptor 1 in Bone Marrow-derived Mesenchymal Cells Is Dependent on Hypoxia-inducible Factor 1
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Genetic Analysis of Pathways Regulated by the von Hippel-Lindau Tumor Suppressor in Caenorhabditis elegans
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Extramitochondrial ATP/ADP-Ratios Regulate Cytochrome c Oxidase Activity via Binding to the Cytosolic Domain of Subunit IV
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Isoforms of Yeast Cytochrome c Oxidase Subunit V Affect the Binuclear Reaction Center and Alter the Kinetics of Interaction with the Isoforms of Yeast Cytochrome c
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Characterization of the α 1B -adrenergic receptor gene promoter region and hypoxia regulatory elements in vascular smooth muscle
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Hypoxia-induced Activation of the Retinoic Acid Receptor-related Orphan Receptor α4 Gene by an Interaction between Hypoxia-inducible Factor-1 and Sp1
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Identification and Characterization of the Hypoxia-Responsive Element of the Human Placental 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase Gene
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The gene encoding human retinoic acid-receptor-related orphan receptor α is a target for hypoxia-inducible factor 1
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Nur77 Activated by Hypoxia-Inducible Factor-1α Overproduces Proopiomelanocortin in von Hippel-Lindau-Mutated Renal Cell Carcinoma
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Transferrin receptor gene expression and transferrin-bound iron uptake are increased during postischemic rat liver reperfusion
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Up‐regulation of 94‐kDa glucose‐regulated protein by hypoxia‐inducible factor‐1 in human endothelial cells in response to hypoxia
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Hypoxia‐inducible factor‐1 and activator protein‐1 modulate the upregulation of CYP3A6 induced by hypoxia
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Reactive Oxygen Species Facilitate Oxygen Sensing
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Target validation in hypoxia-induced vascular remodeling using transcriptome/metabolome analysis
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Lactase Gene Transcription Is Activated in Response to Hypoxia in Intestinal Epithelial Cells
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Flagged first, then by citations

2 of the 113 references couldn’t be matched to a known paper.

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Mitochondria and cancer
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Mitochondrial energetics in the kidney
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Hypoxia and Adipose Tissue Function and Dysfunction in Obesity
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Mitochondrial Energetics and Therapeutics
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MicroRNA-210 Controls Mitochondrial Metabolism during Hypoxia by Repressing the Iron-Sulfur Cluster Assembly Proteins ISCU1/2
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Mitochondrial composition and function under the control of hypoxia
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Redox regulation of mitochondrial function
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Spheroid Culture of Mesenchymal Stem Cells
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Targeting Proteins for Destruction by the Ubiquitin System: Implications for Human Pathobiology
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Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function
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An integrative genomics approach identifies Hypoxia Inducible Factor-1 (HIF-1)-target genes that form the core response to hypoxia
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Aspartate is a limiting metabolite for cancer cell proliferation under hypoxia and in tumours
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Hypoxia. 2. Hypoxia regulates cellular metabolism
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miR-210 is overexpressed in late stages of lung cancer and mediates mitochondrial alterations associated with modulation of HIF-1 activity
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Molecular biology of the blood-brain and the blood-cerebrospinal fluid barriers: similarities and differences
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HIF-1-Dependent Reprogramming of Glucose Metabolic Pathway of Cancer Cells and Its Therapeutic Significance
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A Metabolic Immune Checkpoint: Adenosine in Tumor Microenvironment
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Nuclear Control of Respiratory Chain Expression by Nuclear Respiratory Factors and PGC‐1‐Related Coactivator
Scarpulla, R. C. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.006 · Cited by 389 · see citing works
Hypoxia or in situ normoxia: The stem cell paradigm
Ivanovic, Z. (2009) · Journal of Cellular Physiology · doi:10.1002/jcp.21690 · Cited by 346 · see citing works
Cross-Kingdom Comparison of Transcriptomic Adjustments to Low-Oxygen Stress Highlights Conserved and Plant-Specific Responses
Mustroph, A., Lee, S. C., Oosumi, T., Zanetti, M. E., Yang, H., Ma, K., Yaghoubi-Masihi, A., Fukao, T., & Bailey-Serres, J. N. (2010) · PLANT PHYSIOLOGY · doi:10.1104/pp.109.151845 · Cited by 374 · see citing works
MiR-210 – micromanager of the hypoxia pathway
Huang, X., Le, Q., & Giaccia, A. J. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.03.004 · Cited by 376 · see citing works
MicroRNA-210: A unique and pleiotropic hypoxamir
Chan, S. Y., & Loscalzo, J. (2010) · Cell Cycle · doi:10.4161/cc.9.6.11006 · Cited by 357 · see citing works
The transcriptional factors HIF-1 and HIF-2 and their novel inhibitors in cancer therapy
Albadari, N. G., Deng, S., & Li, W. (2019) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2019.1613370 · Cited by 351 · see citing works
The Histone Demethylases JMJD1A and JMJD2B Are Transcriptional Targets of Hypoxia-inducible Factor HIF
Beyer, S., Kristensen, M. M., Jensen, K. S., Johansen, J. V., & Staller, P. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804578200 · Cited by 341 · see citing works
MicroRNA-210 Regulates Mitochondrial Free Radical Response to Hypoxia and Krebs Cycle in Cancer Cells by Targeting Iron Sulfur Cluster Protein ISCU
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“An emerging paradigm in hypoxia is that mitochondria produce reactive oxygen species, mediated by electron transport continuing in hypoxia [3].”
Background
Sirtuins Link Inflammation and Metabolism
Vachharajani, V., Liu, T., Wang, X., Hoth, J. J., Yoza, B. K., & McCall, C. E. (2016) · Journal of Immunology Research · doi:10.1155/2016/8167273 · Cited by 326 · see citing works
Induction of HIF‐1α expression by intermittent hypoxia: Involvement of NADPH oxidase, Ca2+ signaling, prolyl hydroxylases, and mTOR
Yuan, G., Nanduri, J., Khan, S. A., Semenza, G. L., & Prabhakar, N. R. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21537 · Cited by 310 · see citing works
Self-citation
Mitochondrial gateways to cancer
Galluzzi, L., Morselli, E., Kepp, O., Vitale, I., Rigoni, A., Vacchelli, E., Michaud, M., Zischka, H., Castedo, M., & Kroemer, G. (2009) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2009.08.002 · Cited by 296 · see citing works
Impact of Oxidative Stress in Fetal Programming
Thompson, L. P., & Al-Hasan, Y. M. (2012) · Journal of Pregnancy · doi:10.1155/2012/582748 · Cited by 300 · see citing works
Mitochondria and cellular oxygen sensing in the HIF pathway
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Placental origins of adverse pregnancy outcomes: potential molecular targets: an Executive Workshop Summary of the Eunice Kennedy Shriver National Institute of Child Health and Human Development
Ilekis, J. V., Tsilou, E. T., Fisher, S. J., Abrahams, V. M., Soares, M. J., Cross, J. C., Zamudio, S., Illsley, N. P., Myatt, L., Colvis, C. M., et al. (2016) · American Journal of Obstetrics and Gynecology · doi:10.1016/j.ajog.2016.03.001 · Cited by 291 · see citing works
Cellular hypoxia and adipose tissue dysfunction in obesity
Wood, I. S., de Heredia, F. P., Wang, B., & Trayhurn, P. (2009) · Proceedings of The Nutrition Society · doi:10.1017/s0029665109990206 · Cited by 292 · see citing works
Reciprocal influence of the p53 and the hypoxic pathways
Sermeus, A., & Michiels, C. (2011) · Cell Death and Disease · doi:10.1038/cddis.2011.48 · Cited by 267 · see citing works
Structural Basis for Binding of Hypoxia-Inducible Factor to the Oxygen-Sensing Prolyl Hydroxylases
Chowdhury, R., McDonough, M. A., Mecinović, J., Loenarz, C., Flashman, E., Hewitson, K. S., Domene, C., & Schofield, C. J. (2009) · Structure · doi:10.1016/j.str.2009.06.002 · Cited by 241 · see citing works
Optical probes and techniques for O2 measurement in live cells and tissue
Dmitriev, R. I., & Papkovsky, D. B. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0914-0 · Cited by 231 · see citing works
Oxidative phosphorylation in cancer cells
Solaini, G., Sgarbi, G., & Baracca, A. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.09.003 · Cited by 231 · see citing works
Waves of gene regulation suppress and then restore oxidative phosphorylation in cancer cells
Smolková, K., Plecitá‐Hlavatá, L., Bellancé, N., Bénard, G., Rossignol, R., & Ježek, P. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.05.003 · Cited by 224 · see citing works
Regulatory mechanisms of hypoxia‐inducible factor 1 activity: Two decades of knowledge
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The Warburg effect and mitochondrial stability in cancer cells
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The role of declining adaptive homeostasis in ageing
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Oxidative Stress and MicroRNAs in Vascular Diseases
Magenta, A., Greco, S., Gaetano, C., & Martelli, F. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140917319 · Cited by 194 · see citing works
Regulation of respiration in plants: A role for alternative metabolic pathways
van Dongen, J. T., Gupta, K. J., Ramírez-Aguilar, S. J., Araújo, W. L., Nunes‐Nesi, A., & Fernie, A. R. (2010) · Journal of Plant Physiology · doi:10.1016/j.jplph.2010.11.004 · Cited by 194 · see citing works
Hypoxia and Adipocyte Physiology: Implications for Adipose Tissue Dysfunction in Obesity
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Interfering with Tumor Hypoxia for Radiotherapy Optimization
Telarović, I., Wenger, R. H., & Pruschy, M. N. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-02000-x · Cited by 196 · see citing works
Comparative analysis between plant species of transcriptional and metabolic responses to hypoxia
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Regulation of pyruvate dehydrogenase phosphorylation by hypoxia (572.4)
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Authors: Semenza, G. L.
Affiliations: Johns Hopkins University (US)
Corresponding author: Semenza, Gregg L.
ORCID: Semenza, Gregg L.
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 2007-06-13
Volume: 405
Issue: 1
Pages: 1-9
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj20070389
OpenAlex: W1799768544
Cited by: 541
References: 113
Citations by year: 2026: 8 · 2025: 9 · 2024: 15 · 2023: 16 · 2022: 19 · 2021: 37 · 2020: 25 · 2019: 27 · 2018: 29 · 2017: 27 · 2016: 29 · 2015: 29 · 2014: 29 · 2013: 36 · 2012: 37
FWCI: 3.75
Type: journal article
Language: en
Open access: closed
Locations: Biochemical Journal (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (n01hv28180-13-0-0)
National Heart, Lung, and Blood Institute (N01 HV-28180, R01HL055338)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: HIF-1, mitochondrial respiration, cytochrome c oxidase, PDK1, pyruvate dehydrogenase, LDHA, reactive oxygen species, electron transport chain, TCA cycle, Lon protease, oxygen homeostasis
MeSH terms: Pyruvate Dehydrogenase Acetyl-Transferring Kinase, Electron Transport Complex IV, Electron Transport, Gene Expression Regulation, Glucose, Glycolysis, Homeostasis, Mitochondria, Oxidative Phosphorylation, Oxygen, Protein Kinases, Protein Serine-Threonine Kinases, Cell Respiration, Hypoxia-Inducible Factor 1

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Oxygen-dependent regulation of mitochondrial respiration by hypoxia-inducible factor 1

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